GenomeNet

Database: PDB
Entry: 6I5J
LinkDB: 6I5J
Original site: 6I5J 
HEADER    SIGNALING PROTEIN                       13-NOV-18   6I5J              
TITLE     CRYSTAL STRUCTURE OF SOCS2:ELONGIN C:ELONGIN B IN COMPLEX WITH GROWTH 
TITLE    2 HORMONE RECEPTOR PEPTIDE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPPRESSOR OF CYTOKINE SIGNALING 2;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SOCS-2,CYTOKINE-INDUCIBLE SH2 PROTEIN 2,CIS-2,STAT-INDUCED  
COMPND   5 STAT INHIBITOR 2,SSI-2;                                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ELONGIN-B;                                                 
COMPND   9 CHAIN: B, E;                                                         
COMPND  10 SYNONYM: ELOB,ELONGIN 18 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  11 FACTOR SIII SUBUNIT B,SIII P18,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  12 POLYPEPTIDE 2;                                                       
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: ELONGIN-C;                                                 
COMPND  16 CHAIN: C, F;                                                         
COMPND  17 SYNONYM: ELOC,ELONGIN 15 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  18 FACTOR SIII SUBUNIT C,SIII P15,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  19 POLYPEPTIDE 1;                                                       
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 4;                                                           
COMPND  22 MOLECULE: SUPPRESSOR OF CYTOKINE SIGNALING 2;                        
COMPND  23 CHAIN: D;                                                            
COMPND  24 SYNONYM: SOCS-2,CYTOKINE-INDUCIBLE SH2 PROTEIN 2,CIS-2,STAT-INDUCED  
COMPND  25 STAT INHIBITOR 2,SSI-2;                                              
COMPND  26 ENGINEERED: YES;                                                     
COMPND  27 MOL_ID: 5;                                                           
COMPND  28 MOLECULE: GROWTH HORMONE RECEPTOR PEPTIDE;                           
COMPND  29 CHAIN: I, J, K, L;                                                   
COMPND  30 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOCS2, CIS2, SSI2, STATI2;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ELOB, TCEB2;                                                   
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 GENE: ELOC, TCEB1;                                                   
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: SOCS2, CIS2, SSI2, STATI2;                                     
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  29 MOL_ID: 5;                                                           
SOURCE  30 SYNTHETIC: YES;                                                      
SOURCE  31 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  32 ORGANISM_TAXID: 9606                                                 
KEYWDS    COMPLEX, SIGNALING PROTEIN                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.W.KUNG,S.RAMACHANDRAN,N.MAKUKHIN,E.BRUNO,A.CIULLI                   
REVDAT   5   20-NOV-19 6I5J    1       LINK                                     
REVDAT   4   21-AUG-19 6I5J    1       REMARK                                   
REVDAT   3   19-JUN-19 6I5J    1       JRNL                                     
REVDAT   2   12-JUN-19 6I5J    1       TITLE  AUTHOR                            
REVDAT   1   29-MAY-19 6I5J    0                                                
JRNL        AUTH   W.W.KUNG,S.RAMACHANDRAN,N.MAKUKHIN,E.BRUNO,A.CIULLI          
JRNL        TITL   STRUCTURAL INSIGHTS INTO SUBSTRATE RECOGNITION BY THE SOCS2  
JRNL        TITL 2 E3 UBIQUITIN LIGASE.                                         
JRNL        REF    NAT COMMUN                    V.  10  2534 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   31182716                                                     
JRNL        DOI    10.1038/S41467-019-10190-4                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.59                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 26267                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1305                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 64.6021 -  5.8231    1.00     2940   161  0.2157 0.2524        
REMARK   3     2  5.8231 -  4.6224    1.00     2813   154  0.1891 0.2565        
REMARK   3     3  4.6224 -  4.0382    1.00     2791   137  0.1636 0.2085        
REMARK   3     4  4.0382 -  3.6690    1.00     2752   140  0.1838 0.2393        
REMARK   3     5  3.6690 -  3.4060    1.00     2747   138  0.2168 0.2523        
REMARK   3     6  3.4060 -  3.2052    1.00     2726   153  0.2313 0.3239        
REMARK   3     7  3.2052 -  3.0447    1.00     2719   142  0.2554 0.2845        
REMARK   3     8  3.0447 -  2.9122    1.00     2741   140  0.2689 0.3735        
REMARK   3     9  2.9122 -  2.8001    1.00     2733   140  0.2693 0.3078        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.880           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           6235                                  
REMARK   3   ANGLE     :  0.412           8463                                  
REMARK   3   CHIRALITY :  0.036            968                                  
REMARK   3   PLANARITY :  0.003           1072                                  
REMARK   3   DIHEDRAL  :  8.044           4070                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  79.9436  27.3959  28.3844              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2419 T22:   0.2500                                     
REMARK   3      T33:   0.2452 T12:  -0.0091                                     
REMARK   3      T13:  -0.0313 T23:  -0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5339 L22:   0.1398                                     
REMARK   3      L33:   0.2453 L12:   0.0481                                     
REMARK   3      L13:  -0.1707 L23:  -0.0896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0015 S12:   0.0366 S13:  -0.0070                       
REMARK   3      S21:  -0.0404 S22:   0.0239 S23:   0.0265                       
REMARK   3      S31:   0.0669 S32:   0.0131 S33:  -0.0163                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6I5J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-APR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1200012800.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26321                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 92.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE, COBALT CHLORIDE,      
REMARK 280  MES, AMMONIUM SULPHATE, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 277.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.85350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.47200            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.85350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       78.47200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, I, K                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, J, L                         
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     THR A   138                                                      
REMARK 465     LYS E   104                                                      
REMARK 465     VLM J     6                                                      
REMARK 465     PRO K    -4                                                      
REMARK 465     PRO L    -4                                                      
REMARK 465     VAL L    -3                                                      
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  60    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  63    CE   NZ                                             
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  98    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 100    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     LYS A 117    CG   CD   CE   NZ                                   
REMARK 470     GLN A 118    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 136    CG   CD   CE   NZ                                   
REMARK 470     ARG A 144    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  19    CE   NZ                                             
REMARK 470     LYS B  55    CE   NZ                                             
REMARK 470     ASP B  82    CG   OD1  OD2                                       
REMARK 470     ASP B  83    CG   OD1  OD2                                       
REMARK 470     ASP B 101    CG   OD1  OD2                                       
REMARK 470     MET C  16    CG   SD   CE                                        
REMARK 470     LYS D  63    CE   NZ                                             
REMARK 470     ILE D 110    CG1  CG2  CD1                                       
REMARK 470     CYS D 111    SG                                                  
REMARK 470     VAL D 112    CG1  CG2                                            
REMARK 470     LYS D 113    CG   CD   CE   NZ                                   
REMARK 470     SER D 114    OG                                                  
REMARK 470     LYS D 115    CG   CD   CE   NZ                                   
REMARK 470     LYS D 117    CG   CD   CE   NZ                                   
REMARK 470     GLN D 118    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 134    CG   CD   CE   NZ                                   
REMARK 470     LYS D 136    CG   CD   CE   NZ                                   
REMARK 470     THR D 138    OG1  CG2                                            
REMARK 470     ARG D 144    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN D 145    CG   OD1  ND2                                       
REMARK 470     GLN E  65    CD   OE1  NE2                                       
REMARK 470     ASP E  82    CG   OD1  OD2                                       
REMARK 470     GLU E  98    CG   CD   OE1  OE2                                  
REMARK 470     ASP E 101    CG   OD1  OD2                                       
REMARK 470     VAL E 102    CG1  CG2                                            
REMARK 470     GLU F  56    CG   CD   OE1  OE2                                  
REMARK 470     ASN F  85    CG   OD1  ND2                                       
REMARK 470     SER F  87    OG                                                  
REMARK 470     VAL J  -3    CG1  CG2                                            
REMARK 470     THR J   1    OG1  CG2                                            
REMARK 470     HIS J   4    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL K  -3    CG1  CG2                                            
REMARK 470     ASP L  -1    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VLM I   6   C   -  N   -  CA  ANGL. DEV. =  28.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  88     -168.42   -105.03                                   
REMARK 500    THR A 153      -84.57   -130.49                                   
REMARK 500    TYR A 194       92.42   -160.87                                   
REMARK 500    HIS B  10     -118.88     53.99                                   
REMARK 500    ASP B  47     -120.02     61.06                                   
REMARK 500    ALA B  71       75.97   -153.11                                   
REMARK 500    ASP B  82     -132.30     62.67                                   
REMARK 500    SER C  47       51.23   -102.71                                   
REMARK 500    ASN C  58       35.65    -97.32                                   
REMARK 500    TYR C  83       41.09   -107.27                                   
REMARK 500    MET D  53      119.27   -162.11                                   
REMARK 500    THR D  88     -165.03   -103.99                                   
REMARK 500    ASN D 145       74.42     54.90                                   
REMARK 500    TYR D 151      117.94   -162.80                                   
REMARK 500    THR D 153      -81.49   -125.77                                   
REMARK 500    TYR D 194       91.00   -163.46                                   
REMARK 500    HIS E  10     -110.97     53.77                                   
REMARK 500    ASP E  47     -118.26     59.37                                   
REMARK 500    ALA E  71       76.33   -152.13                                   
REMARK 500    ASP E  82      -97.37   -141.14                                   
REMARK 500    ASP F 111       74.78     56.36                                   
REMARK 500    HIS J   4       48.41   -147.38                                   
REMARK 500    SER L   2      105.41    -58.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE I    5     VLM I    6                 -146.72                    
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                              CO A 201  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 149   NE2                                                    
REMARK 620 2 HIS K   4   NE2  91.0                                              
REMARK 620 3 HOH K 103   O   104.6  81.6                                        
REMARK 620 4 HOH A 301   O    80.6  86.6 167.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO D 201  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 149   NE2                                                    
REMARK 620 2 HIS L   4   NE2 119.5                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CO D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PTR I 0 and THR I 1    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ILE I 5 and VLM I 6    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ASP I -1 and PTR I 0   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PTR J 0 and THR J 1    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ASP J -1 and PTR J 0   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PTR K 0 and THR K 1    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ILE K 5 and VLM K 6    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ASP K -1 and PTR K 0   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PTR L 0 and THR L 1    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ILE L 5 and VLM L 6    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ASP L -1 and PTR L 0   
DBREF  6I5J A   30   198  UNP    O14508   SOCS2_HUMAN     30    198             
DBREF  6I5J B    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  6I5J C   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
DBREF  6I5J D   30   198  UNP    O14508   SOCS2_HUMAN     30    198             
DBREF  6I5J E    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  6I5J F   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
DBREF  6I5J I   -4     6  PDB    6I5J     6I5J            -4      6             
DBREF  6I5J J   -4     6  PDB    6I5J     6I5J            -4      6             
DBREF  6I5J K   -4     6  PDB    6I5J     6I5J            -4      6             
DBREF  6I5J L   -4     6  PDB    6I5J     6I5J            -4      6             
SEQADV 6I5J MET A   31  UNP  O14508    PRO    31 ENGINEERED MUTATION            
SEQADV 6I5J MET C   16  UNP  Q15369              INITIATING METHIONINE          
SEQADV 6I5J MET D   31  UNP  O14508    PRO    31 ENGINEERED MUTATION            
SEQADV 6I5J MET F   16  UNP  Q15369              INITIATING METHIONINE          
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 CAS 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 CAS          
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  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 B  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 B  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 B  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 B  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 B  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 B  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CAS ILE GLU          
SEQRES   8 B  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
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                                      
SEQRES   1 D  169  SER MET GLN ALA ALA ARG LEU ALA LYS ALA LEU ARG GLU          
SEQRES   2 D  169  LEU GLY GLN THR GLY TRP TYR TRP GLY SER MET THR VAL          
SEQRES   3 D  169  ASN GLU ALA LYS GLU LYS LEU LYS GLU ALA PRO GLU GLY          
SEQRES   4 D  169  THR PHE LEU ILE ARG ASP SER SER HIS SER ASP TYR LEU          
SEQRES   5 D  169  LEU THR ILE SER VAL LYS THR SER ALA GLY PRO THR ASN          
SEQRES   6 D  169  LEU ARG ILE GLU TYR GLN ASP GLY LYS PHE ARG LEU ASP          
SEQRES   7 D  169  SER ILE ILE CYS VAL LYS SER LYS LEU LYS GLN PHE ASP          
SEQRES   8 D  169  SER VAL VAL HIS LEU ILE ASP TYR TYR VAL GLN MET CAS          
SEQRES   9 D  169  LYS ASP LYS ARG THR GLY PRO GLU ALA PRO ARG ASN GLY          
SEQRES  10 D  169  THR VAL HIS LEU TYR LEU THR LYS PRO LEU TYR THR SER          
SEQRES  11 D  169  ALA PRO SER LEU GLN HIS LEU CYS ARG LEU THR ILE ASN          
SEQRES  12 D  169  LYS CYS THR GLY ALA ILE TRP GLY LEU PRO LEU PRO THR          
SEQRES  13 D  169  ARG LEU LYS ASP TYR LEU GLU GLU TYR LYS PHE GLN VAL          
SEQRES   1 E  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 E  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 E  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 E  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 E  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 E  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 E  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CAS ILE GLU          
SEQRES   8 E  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   1 F   97  MET MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU          
SEQRES   2 F   97  PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR          
SEQRES   3 F   97  ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU          
SEQRES   4 F   97  ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER          
SEQRES   5 F   97  HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS          
SEQRES   6 F   97  VAL ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE          
SEQRES   7 F   97  PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA          
SEQRES   8 F   97  ALA ASN PHE LEU ASP CYS                                      
SEQRES   1 I   11  PRO VAL PRO ASP PTR THR SER ILE HIS ILE VLM                  
SEQRES   1 J   11  PRO VAL PRO ASP PTR THR SER ILE HIS ILE VLM                  
SEQRES   1 K   11  PRO VAL PRO ASP PTR THR SER ILE HIS ILE VLM                  
SEQRES   1 L   11  PRO VAL PRO ASP PTR THR SER ILE HIS ILE VLM                  
MODRES 6I5J CAS A  111  CYS  MODIFIED RESIDUE                                   
MODRES 6I5J CAS A  133  CYS  MODIFIED RESIDUE                                   
MODRES 6I5J CAS B   89  CYS  MODIFIED RESIDUE                                   
MODRES 6I5J CAS D  133  CYS  MODIFIED RESIDUE                                   
MODRES 6I5J CAS E   89  CYS  MODIFIED RESIDUE                                   
HET    CAS  A 111       9                                                       
HET    CAS  A 133       9                                                       
HET    CAS  B  89       9                                                       
HET    CAS  D 133       9                                                       
HET    CAS  E  89       9                                                       
HET    PTR  I   0      16                                                       
HET    VLM  I   6       8                                                       
HET    PTR  J   0      16                                                       
HET    PTR  K   0      16                                                       
HET    VLM  K   6       8                                                       
HET    PTR  L   0      16                                                       
HET    VLM  L   6       8                                                       
HET     CO  A 201       1                                                       
HET     CO  D 201       1                                                       
HETNAM     CAS S-(DIMETHYLARSENIC)CYSTEINE                                      
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     VLM VALINYLAMINE                                                     
HETNAM      CO COBALT (II) ION                                                  
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  CAS    5(C5 H12 AS N O2 S)                                          
FORMUL   7  PTR    4(C9 H12 N O6 P)                                             
FORMUL   7  VLM    3(C5 H12 N2 O)                                               
FORMUL  11   CO    2(CO 2+)                                                     
FORMUL  13  HOH   *33(H2 O)                                                     
HELIX    1 AA1 MET A   31  GLY A   47  1                                  17    
HELIX    2 AA2 THR A   54  LEU A   62  1                                   9    
HELIX    3 AA3 VAL A  112  LEU A  116  5                                   5    
HELIX    4 AA4 SER A  121  CAS A  133  1                                  13    
HELIX    5 AA5 SER A  162  LYS A  173  1                                  12    
HELIX    6 AA6 ALA A  177  LEU A  181  5                                   5    
HELIX    7 AA7 PRO A  184  GLU A  193  1                                  10    
HELIX    8 AA8 THR B   23  LYS B   36  1                                  14    
HELIX    9 AA9 PRO B   38  ASP B   40  5                                   3    
HELIX   10 AB1 THR B   56  GLY B   61  1                                   6    
HELIX   11 AB2 ARG C   33  LEU C   37  1                                   5    
HELIX   12 AB3 SER C   39  SER C   47  1                                   9    
HELIX   13 AB4 PRO C   66  TYR C   83  1                                  18    
HELIX   14 AB5 ALA C   96  ASP C  111  1                                  16    
HELIX   15 AB6 MET D   31  GLY D   47  1                                  17    
HELIX   16 AB7 THR D   54  LEU D   62  1                                   9    
HELIX   17 AB8 ILE D  109  LYS D  113  5                                   5    
HELIX   18 AB9 SER D  121  CAS D  133  1                                  13    
HELIX   19 AC1 LYS D  134  LYS D  136  5                                   3    
HELIX   20 AC2 SER D  162  THR D  175  1                                  14    
HELIX   21 AC3 ALA D  177  LEU D  181  5                                   5    
HELIX   22 AC4 PRO D  184  GLU D  193  1                                  10    
HELIX   23 AC5 THR E   23  LYS E   36  1                                  14    
HELIX   24 AC6 PRO E   38  ASP E   40  5                                   3    
HELIX   25 AC7 ARG F   33  LEU F   37  1                                   5    
HELIX   26 AC8 SER F   39  SER F   47  1                                   9    
HELIX   27 AC9 PRO F   66  TYR F   83  1                                  18    
HELIX   28 AD1 ILE F   99  ASP F  111  1                                  13    
SHEET    1 AA1 4 PHE A  70  ASP A  74  0                                        
SHEET    2 AA1 4 LEU A  82  THR A  88 -1  O  SER A  85   N  LEU A  71           
SHEET    3 AA1 4 GLY A  91  GLN A 100 -1  O  LEU A  95   N  ILE A  84           
SHEET    4 AA1 4 LYS A 103  LEU A 106 -1  O  ARG A 105   N  GLU A  98           
SHEET    1 AA2 4 GLN B  49  LEU B  50  0                                        
SHEET    2 AA2 4 GLN B  42  LYS B  46 -1  N  LYS B  46   O  GLN B  49           
SHEET    3 AA2 4 ALA B  73  ALA B  81 -1  O  GLY B  76   N  TYR B  45           
SHEET    4 AA2 4 THR B  84  PHE B  85 -1  O  THR B  84   N  ALA B  81           
SHEET    1 AA3 8 GLN B  49  LEU B  50  0                                        
SHEET    2 AA3 8 GLN B  42  LYS B  46 -1  N  LYS B  46   O  GLN B  49           
SHEET    3 AA3 8 ALA B  73  ALA B  81 -1  O  GLY B  76   N  TYR B  45           
SHEET    4 AA3 8 ASP B   2  ARG B   9  1  N  MET B   6   O  ALA B  73           
SHEET    5 AA3 8 THR B  12  LYS B  19 -1  O  ALA B  18   N  VAL B   3           
SHEET    6 AA3 8 GLU C  28  LYS C  32  1  O  ILE C  30   N  THR B  13           
SHEET    7 AA3 8 TYR C  18  ILE C  22 -1  N  LEU C  21   O  PHE C  29           
SHEET    8 AA3 8 GLU C  59  ASN C  61  1  O  VAL C  60   N  ILE C  22           
SHEET    1 AA4 2 GLU C  56  THR C  57  0                                        
SHEET    2 AA4 2 ASN F  55  GLU F  56 -1  O  GLU F  56   N  GLU C  56           
SHEET    1 AA5 4 PHE D  70  ASP D  74  0                                        
SHEET    2 AA5 4 LEU D  82  THR D  88 -1  O  SER D  85   N  LEU D  71           
SHEET    3 AA5 4 GLY D  91  GLN D 100 -1  O  LEU D  95   N  ILE D  84           
SHEET    4 AA5 4 LYS D 103  LEU D 106 -1  O  ARG D 105   N  GLU D  98           
SHEET    1 AA6 3 VAL D 148  HIS D 149  0                                        
SHEET    2 AA6 3 HIS L   4  VLM L   6 -1  O  ILE L   5   N  VAL D 148           
SHEET    3 AA6 3 SER J   2  ILE J   3 -1  N  SER J   2   O  VLM L   6           
SHEET    1 AA7 8 GLN E  49  LEU E  50  0                                        
SHEET    2 AA7 8 GLN E  42  LYS E  46 -1  N  LYS E  46   O  GLN E  49           
SHEET    3 AA7 8 ALA E  73  PHE E  79 -1  O  GLY E  76   N  TYR E  45           
SHEET    4 AA7 8 ASP E   2  ARG E   9  1  N  MET E   6   O  VAL E  75           
SHEET    5 AA7 8 THR E  12  LYS E  19 -1  O  ALA E  18   N  VAL E   3           
SHEET    6 AA7 8 GLU F  28  LYS F  32  1  O  ILE F  30   N  THR E  13           
SHEET    7 AA7 8 TYR F  18  ILE F  22 -1  N  LEU F  21   O  PHE F  29           
SHEET    8 AA7 8 GLU F  59  ASN F  61  1  O  VAL F  60   N  LYS F  20           
SHEET    1 AA8 2 SER I   2  VLM I   6  0                                        
SHEET    2 AA8 2 SER K   2  VLM K   6 -1  O  HIS K   4   N  HIS I   4           
LINK         C   ILE A 110                 N   CAS A 111     1555   1555  1.33  
LINK         C   CAS A 111                 N   VAL A 112     1555   1555  1.33  
LINK         C   MET A 132                 N   CAS A 133     1555   1555  1.33  
LINK         C   CAS A 133                 N   LYS A 134     1555   1555  1.33  
LINK         NE2 HIS A 149                CO    CO A 201     1555   1555  2.08  
LINK         C   LEU B  88                 N   CAS B  89     1555   1555  1.33  
LINK         C   CAS B  89                 N   ILE B  90     1555   1555  1.33  
LINK         C   MET D 132                 N   CAS D 133     1555   1555  1.33  
LINK         C   CAS D 133                 N   LYS D 134     1555   1555  1.33  
LINK         NE2 HIS D 149                CO    CO D 201     1555   1555  2.21  
LINK         C   LEU E  88                 N   CAS E  89     1555   1555  1.33  
LINK         C   CAS E  89                 N   ILE E  90     1555   1555  1.33  
LINK         C   ASP I  -1                 N   PTR I   0     1555   1555  1.33  
LINK         C   PTR I   0                 N   THR I   1     1555   1555  1.33  
LINK         C   ILE I   5                 N   VLM I   6     1555   1555  1.33  
LINK         C   ASP J  -1                 N   PTR J   0     1555   1555  1.33  
LINK         C   PTR J   0                 N   THR J   1     1555   1555  1.33  
LINK         C   ASP K  -1                 N   PTR K   0     1555   1555  1.33  
LINK         C   PTR K   0                 N   THR K   1     1555   1555  1.33  
LINK         NE2 HIS K   4                CO    CO A 201     1555   1555  2.34  
LINK         C   ILE K   5                 N   VLM K   6     1555   1555  1.33  
LINK         C   ASP L  -1                 N   PTR L   0     1555   1555  1.33  
LINK         C   PTR L   0                 N   THR L   1     1555   1555  1.33  
LINK         NE2 HIS L   4                CO    CO D 201     1555   1555  2.40  
LINK         C   ILE L   5                 N   VLM L   6     1555   1555  1.33  
LINK        CO    CO A 201                 O   HOH K 103     1555   1555  2.22  
LINK        CO    CO A 201                 O   HOH A 301     1555   1555  2.15  
SITE     1 AC1  4 HIS A 149  HOH A 301  HIS K   4  HOH K 103                    
SITE     1 AC2  2 HIS D 149  HIS L   4                                          
SITE     1 AC3 12 ARG A  73  SER A  75  SER A  76  THR A  83                    
SITE     2 AC3 12 THR A  93  ASN A  94  LEU A  95  ARG A  96                    
SITE     3 AC3 12 ASP I  -1  PRO I  -2  SER I   2  VLM K   6                    
SITE     1 AC4  3 HIS I   4  THR K   1  SER K   2                               
SITE     1 AC5  9 ARG A  73  SER A  75  SER A  76  THR A  83                    
SITE     2 AC5  9 THR A  93  ASN A  94  ARG A  96  PRO I  -2                    
SITE     3 AC5  9 THR I   1                                                     
SITE     1 AC6 11 ARG D  73  SER D  75  SER D  76  THR D  83                    
SITE     2 AC6 11 ASN D  94  LEU D  95  ARG D  96  ASP J  -1                    
SITE     3 AC6 11 PRO J  -2  SER J   2  VLM L   6                               
SITE     1 AC7 11 VAL D  55  ARG D  73  SER D  75  SER D  76                    
SITE     2 AC7 11 THR D  83  THR D  93  ASN D  94  ARG D  96                    
SITE     3 AC7 11 VAL J  -3  PRO J  -2  THR J   1                               
SITE     1 AC8 11 MET A 132  CAS A 133  ARG A 137  HIS A 149                    
SITE     2 AC8 11 ILE I   5  PRO K  -2  ASP K  -1  SER K   2                    
SITE     3 AC8 11 ILE K   3  HOH K 101  HOH K 102                               
SITE     1 AC9  6 THR A  88  ILE A 109  VAL A 148  THR I   1                    
SITE     2 AC9  6 SER I   2  HIS K   4                                          
SITE     1 AD1 10 MET A 132  ARG A 137  HIS A 149  LYS E  36                    
SITE     2 AD1 10 PRO K  -2  VAL K  -3  THR K   1  SER K   2                    
SITE     3 AD1 10 HOH K 101  HOH K 102                                          
SITE     1 AD2  8 MET D 132  CAS D 133  LYS D 136  ARG D 137                    
SITE     2 AD2  8 ASP L  -1  PRO L  -2  SER L   2  ILE L   3                    
SITE     1 AD3  5 VAL D 148  THR J   1  SER J   2  ILE J   3                    
SITE     2 AD3  5 HIS L   4                                                     
SITE     1 AD4  7 MET D 132  CAS D 133  LYS D 136  ARG D 137                    
SITE     2 AD4  7 PRO L  -2  THR L   1  SER L   2                               
CRYST1   57.835  113.707  156.944  90.00  90.00  90.00 P 2 21 21    16          
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      0.017291  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008795  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006372        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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