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Database: PDB
Entry: 3URF
LinkDB: 3URF
Original site: 3URF 
HEADER    CYTOKINE                                22-NOV-11   3URF              
TITLE     HUMAN RANKL/OPG COMPLEX                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 11, SOLUBLE
COMPND   3 FORM;                                                                
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 162-317;                                      
COMPND   6 SYNONYM: OSTEOCLAST DIFFERENTIATION FACTOR, ODF, OSTEOPROTEGERIN     
COMPND   7 LIGAND, OPGL, RECEPTOR ACTIVATOR OF NUCLEAR FACTOR KAPPA-B LIGAND,   
COMPND   8 RANKL, TNF-RELATED ACTIVATION-INDUCED CYTOKINE, TRANCE;              
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 11B;     
COMPND  12 CHAIN: Z;                                                            
COMPND  13 FRAGMENT: UNP RESIDUES 22-186;                                       
COMPND  14 SYNONYM: OSTEOCLASTOGENESIS INHIBITORY FACTOR, OSTEOPROTEGERIN;      
COMPND  15 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: TNFSF11, OPGL, RANKL, TRANCE;                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: TNFRSF11B, OCIF, OPG;                                          
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    CYSTEIN-RICH DOMAIN, BETA-SANDWICH, CYTOKINE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.Q.WANG,X.D.LUAN,Q.Y.LU                                              
REVDAT   2   29-JUL-20 3URF    1       COMPND REMARK SEQADV HETNAM              
REVDAT   2 2                   1       LINK   SITE                              
REVDAT   1   11-JUL-12 3URF    0                                                
JRNL        AUTH   X.D.LUAN,Q.Y.LU,Y.N.JIANG,S.Y.ZHANG,Q.WANG,H.H.YUAN,         
JRNL        AUTH 2 W.M.ZHAO,J.W.WANG,X.Q.WANG                                   
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN RANKL COMPLEXED WITH ITS DECOY    
JRNL        TITL 2 RECEPTOR OSTEOPROTEGERIN                                     
JRNL        REF    J.IMMUNOL.                    V. 189   245 2012              
JRNL        REFN                   ISSN 0022-1767                               
JRNL        PMID   22664871                                                     
JRNL        DOI    10.4049/JIMMUNOL.1103387                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.16                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 14783                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 748                             
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 40.1647 -  4.6168    0.99     2995   130  0.2127 0.2522        
REMARK   3     2  4.6168 -  3.6653    1.00     2808   151  0.1539 0.1986        
REMARK   3     3  3.6653 -  3.2022    1.00     2751   163  0.1879 0.2488        
REMARK   3     4  3.2022 -  2.9095    1.00     2743   157  0.2405 0.3226        
REMARK   3     5  2.9095 -  2.7010    1.00     2738   147  0.3358 0.3984        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 59.41                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.860           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.009           2654                                  
REMARK   3   ANGLE     :  1.232           3585                                  
REMARK   3   CHIRALITY :  0.085            377                                  
REMARK   3   PLANARITY :  0.005            460                                  
REMARK   3   DIHEDRAL  : 18.708            955                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   8.8381  -0.6075  17.2613              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2779 T22:   0.3548                                     
REMARK   3      T33:   0.2878 T12:  -0.0074                                     
REMARK   3      T13:  -0.0451 T23:   0.0706                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7691 L22:   2.7247                                     
REMARK   3      L33:   3.2350 L12:  -0.2399                                     
REMARK   3      L13:   0.0892 L23:   0.0124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0803 S12:  -0.5201 S13:  -0.2886                       
REMARK   3      S21:   0.4776 S22:  -0.0488 S23:  -0.0401                       
REMARK   3      S31:   0.2055 S32:  -0.0806 S33:  -0.0035                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN Z                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0164  -6.4273  29.8520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3243 T22:   0.5155                                     
REMARK   3      T33:   0.3708 T12:  -0.0246                                     
REMARK   3      T13:   0.1191 T23:   0.1734                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8755 L22:   0.8659                                     
REMARK   3      L33:   1.0451 L12:  -0.4491                                     
REMARK   3      L13:   0.1119 L23:  -0.3756                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3391 S12:  -0.4917 S13:  -0.4886                       
REMARK   3      S21:   0.2077 S22:   0.2705 S23:   0.1241                       
REMARK   3      S31:   0.0246 S32:  -0.3981 S33:  -0.0045                       
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 3URF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-DEC-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000069115.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14783                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.160                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
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   (%): 62.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NACL, 100MM MES PH 6.5, 100MM         
REMARK 280  SODIUM PHOSPHATE MONOBASIC MONOHYDRATE, 100MM POTASSIUM             
REMARK 280  PHOSPHATE MONOBASIC, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   Y+3/4,X+1/4,-Z+1/4                                      
REMARK 290      14555   -Y+3/4,-X+3/4,-Z+3/4                                    
REMARK 290      15555   Y+1/4,-X+1/4,Z+3/4                                      
REMARK 290      16555   -Y+1/4,X+3/4,Z+1/4                                      
REMARK 290      17555   X+3/4,Z+1/4,-Y+1/4                                      
REMARK 290      18555   -X+1/4,Z+3/4,Y+1/4                                      
REMARK 290      19555   -X+3/4,-Z+3/4,-Y+3/4                                    
REMARK 290      20555   X+1/4,-Z+1/4,Y+3/4                                      
REMARK 290      21555   Z+3/4,Y+1/4,-X+1/4                                      
REMARK 290      22555   Z+1/4,-Y+1/4,X+3/4                                      
REMARK 290      23555   -Z+1/4,Y+3/4,X+1/4                                      
REMARK 290      24555   -Z+3/4,-Y+3/4,-X+3/4                                    
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       72.40000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.40000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.40000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.40000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       72.40000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.40000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       72.40000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       72.40000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       72.40000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       72.40000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       72.40000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       72.40000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       72.40000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       72.40000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       72.40000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       72.40000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       72.40000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       72.40000            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000      108.60000            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       36.20000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       36.20000            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000      108.60000            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000      108.60000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      108.60000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       36.20000            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       36.20000            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      108.60000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       36.20000            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000      108.60000            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       36.20000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000      108.60000            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       36.20000            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       36.20000            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       36.20000            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000      108.60000            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       36.20000            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000      108.60000            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000      108.60000            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000      108.60000            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       36.20000            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       36.20000            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000      108.60000            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000      108.60000            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       36.20000            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       36.20000            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       36.20000            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       36.20000            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000      108.60000            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       36.20000            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000      108.60000            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       36.20000            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000      108.60000            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000      108.60000            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000      108.60000            
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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, Z                                  
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   BIOMT1   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000        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     HIS A   318                                                      
REMARK 465     HIS A   319                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     GLU Z     1                                                      
REMARK 465     THR Z     2                                                      
REMARK 465     PHE Z     3                                                      
REMARK 465     PRO Z     4                                                      
REMARK 465     HIS Z   169                                                      
REMARK 465     HIS Z   170                                                      
REMARK 465     HIS Z   171                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS Z   145     CB   CYS Z   164              1.67            
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    HIS A 180     -148.02   -137.08                                   
REMARK 500    ASP A 190       56.58   -147.70                                   
REMARK 500    ARG A 191      136.31   -173.10                                   
REMARK 500    ASN A 198       27.71     48.67                                   
REMARK 500    ASN A 203       36.61     34.95                                   
REMARK 500    ASP A 211      154.39    -47.56                                   
REMARK 500    SER A 228      149.85   -176.83                                   
REMARK 500    LYS A 248      -48.09    131.11                                   
REMARK 500    ILE A 249       74.89   -107.11                                   
REMARK 500    TYR Z   7      126.57    101.00                                   
REMARK 500    ASP Z  11      -54.60   -129.29                                   
REMARK 500    GLU Z  12       71.61     76.50                                   
REMARK 500    GLU Z  13     -175.02    -67.84                                   
REMARK 500    SER Z  15      -92.65    -65.87                                   
REMARK 500    THR Z  34       19.28   -149.93                                   
REMARK 500    ALA Z  35      106.43     66.72                                   
REMARK 500    LYS Z  36      -15.88     81.93                                   
REMARK 500    HIS Z  54     -172.30   -176.79                                   
REMARK 500    THR Z  55       -1.57   -142.18                                   
REMARK 500    ILE Z  94     -102.57     62.79                                   
REMARK 500    PRO Z 105       -3.17    -53.12                                   
REMARK 500    PRO Z 125      172.11    -51.38                                   
REMARK 500    SER Z 146      -65.81    -27.36                                   
REMARK 500    VAL Z 147     -112.80    -82.13                                   
REMARK 500    LEU Z 150     -149.23   -116.12                                   
REMARK 500    THR Z 153      -32.96   -134.35                                   
REMARK 500    ASN Z 157     -154.94    -86.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3URF A  162   317  UNP    O14788   TNF11_HUMAN    162    317             
DBREF  3URF Z    1   165  UNP    O00300   TR11B_HUMAN     22    186             
SEQADV 3URF HIS A  318  UNP  O14788              EXPRESSION TAG                 
SEQADV 3URF HIS A  319  UNP  O14788              EXPRESSION TAG                 
SEQADV 3URF HIS A  320  UNP  O14788              EXPRESSION TAG                 
SEQADV 3URF HIS A  321  UNP  O14788              EXPRESSION TAG                 
SEQADV 3URF HIS A  322  UNP  O14788              EXPRESSION TAG                 
SEQADV 3URF HIS A  323  UNP  O14788              EXPRESSION TAG                 
SEQADV 3URF HIS Z  166  UNP  O00300              EXPRESSION TAG                 
SEQADV 3URF HIS Z  167  UNP  O00300              EXPRESSION TAG                 
SEQADV 3URF HIS Z  168  UNP  O00300              EXPRESSION TAG                 
SEQADV 3URF HIS Z  169  UNP  O00300              EXPRESSION TAG                 
SEQADV 3URF HIS Z  170  UNP  O00300              EXPRESSION TAG                 
SEQADV 3URF HIS Z  171  UNP  O00300              EXPRESSION TAG                 
SEQRES   1 A  162  ALA GLN PRO PHE ALA HIS LEU THR ILE ASN ALA THR ASP          
SEQRES   2 A  162  ILE PRO SER GLY SER HIS LYS VAL SER LEU SER SER TRP          
SEQRES   3 A  162  TYR HIS ASP ARG GLY TRP ALA LYS ILE SER ASN MET THR          
SEQRES   4 A  162  PHE SER ASN GLY LYS LEU ILE VAL ASN GLN ASP GLY PHE          
SEQRES   5 A  162  TYR TYR LEU TYR ALA ASN ILE CYS PHE ARG HIS HIS GLU          
SEQRES   6 A  162  THR SER GLY ASP LEU ALA THR GLU TYR LEU GLN LEU MET          
SEQRES   7 A  162  VAL TYR VAL THR LYS THR SER ILE LYS ILE PRO SER SER          
SEQRES   8 A  162  HIS THR LEU MET LYS GLY GLY SER THR LYS TYR TRP SER          
SEQRES   9 A  162  GLY ASN SER GLU PHE HIS PHE TYR SER ILE ASN VAL GLY          
SEQRES  10 A  162  GLY PHE PHE LYS LEU ARG SER GLY GLU GLU ILE SER ILE          
SEQRES  11 A  162  GLU VAL SER ASN PRO SER LEU LEU ASP PRO ASP GLN ASP          
SEQRES  12 A  162  ALA THR TYR PHE GLY ALA PHE LYS VAL ARG ASP ILE ASP          
SEQRES  13 A  162  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 Z  171  GLU THR PHE PRO PRO LYS TYR LEU HIS TYR ASP GLU GLU          
SEQRES   2 Z  171  THR SER HIS GLN LEU LEU CYS ASP LYS CYS PRO PRO GLY          
SEQRES   3 Z  171  THR TYR LEU LYS GLN HIS CYS THR ALA LYS TRP LYS THR          
SEQRES   4 Z  171  VAL CYS ALA PRO CYS PRO ASP HIS TYR TYR THR ASP SER          
SEQRES   5 Z  171  TRP HIS THR SER ASP GLU CYS LEU TYR CYS SER PRO VAL          
SEQRES   6 Z  171  CYS LYS GLU LEU GLN TYR VAL LYS GLN GLU CYS ASN ARG          
SEQRES   7 Z  171  THR HIS ASN ARG VAL CYS GLU CYS LYS GLU GLY ARG TYR          
SEQRES   8 Z  171  LEU GLU ILE GLU PHE CYS LEU LYS HIS ARG SER CYS PRO          
SEQRES   9 Z  171  PRO GLY PHE GLY VAL VAL GLN ALA GLY THR PRO GLU ARG          
SEQRES  10 Z  171  ASN THR VAL CYS LYS ARG CYS PRO ASP GLY PHE PHE SER          
SEQRES  11 Z  171  ASN GLU THR SER SER LYS ALA PRO CYS ARG LYS HIS THR          
SEQRES  12 Z  171  ASN CYS SER VAL PHE GLY LEU LEU LEU THR GLN LYS GLY          
SEQRES  13 Z  171  ASN ALA THR HIS ASP ASN ILE CYS SER HIS HIS HIS HIS          
SEQRES  14 Z  171  HIS HIS                                                      
MODRES 3URF ASN Z  157  ASN  GLYCOSYLATION SITE                                 
HET    NAG  Z 201      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   3  NAG    C8 H15 N O6                                                  
FORMUL   4  HOH   *36(H2 O)                                                     
HELIX    1   1 ASN A  295  LEU A  299  5                                   5    
SHEET    1   A 3 TRP A 187  TYR A 188  0                                        
SHEET    2   A 3 PHE A 165  ILE A 170 -1  N  THR A 169   O  TYR A 188           
SHEET    3   A 3 LYS A 195  SER A 197 -1  O  SER A 197   N  PHE A 165           
SHEET    1   B 5 TRP A 187  TYR A 188  0                                        
SHEET    2   B 5 PHE A 165  ILE A 170 -1  N  THR A 169   O  TYR A 188           
SHEET    3   B 5 TYR A 307  ARG A 314 -1  O  PHE A 308   N  LEU A 168           
SHEET    4   B 5 GLY A 212  HIS A 225 -1  N  PHE A 213   O  VAL A 313           
SHEET    5   B 5 PHE A 270  LEU A 283 -1  O  GLY A 279   N  LEU A 216           
SHEET    1   C 4 VAL A 182  LEU A 184  0                                        
SHEET    2   C 4 GLU A 287  VAL A 293 -1  O  ILE A 291   N  LEU A 184           
SHEET    3   C 4 LYS A 205  VAL A 208 -1  N  VAL A 208   O  GLU A 287           
SHEET    4   C 4 MET A 199  SER A 202 -1  N  THR A 200   O  ILE A 207           
SHEET    1   D 4 VAL A 182  LEU A 184  0                                        
SHEET    2   D 4 GLU A 287  VAL A 293 -1  O  ILE A 291   N  LEU A 184           
SHEET    3   D 4 TYR A 235  SER A 246 -1  N  THR A 243   O  SER A 290           
SHEET    4   D 4 HIS A 253  TYR A 263 -1  O  LEU A 255   N  VAL A 242           
SHEET    1   E 2 LEU Z   8  TYR Z  10  0                                        
SHEET    2   E 2 LEU Z  19  ASP Z  21 -1  O  CYS Z  20   N  HIS Z   9           
SHEET    1   F 2 THR Z  27  GLN Z  31  0                                        
SHEET    2   F 2 VAL Z  40  PRO Z  43 -1  O  VAL Z  40   N  LYS Z  30           
SHEET    1   G 2 TYR Z  48  TYR Z  49  0                                        
SHEET    2   G 2 LEU Z  60  TYR Z  61 -1  O  LEU Z  60   N  TYR Z  49           
SHEET    1   H 2 GLN Z  70  GLN Z  74  0                                        
SHEET    2   H 2 VAL Z  83  CYS Z  86 -1  O  VAL Z  83   N  GLN Z  74           
SHEET    1   I 2 ARG Z  90  GLU Z  93  0                                        
SHEET    2   I 2 PHE Z  96  LYS Z  99 -1  O  PHE Z  96   N  GLU Z  93           
SHEET    1   J 2 PHE Z 107  GLN Z 111  0                                        
SHEET    2   J 2 VAL Z 120  ARG Z 123 -1  O  VAL Z 120   N  VAL Z 110           
SHEET    1   K 2 PHE Z 128  PHE Z 129  0                                        
SHEET    2   K 2 ARG Z 140  LYS Z 141 -1  O  ARG Z 140   N  PHE Z 129           
SSBOND   1 CYS Z   20    CYS Z   33                          1555   1555  2.03  
SSBOND   2 CYS Z   23    CYS Z   41                          1555   1555  2.04  
SSBOND   3 CYS Z   44    CYS Z   59                          1555   1555  2.05  
SSBOND   4 CYS Z   62    CYS Z   76                          1555   1555  2.03  
SSBOND   5 CYS Z   66    CYS Z   84                          1555   1555  2.04  
SSBOND   6 CYS Z   86    CYS Z   97                          1555   1555  2.03  
SSBOND   7 CYS Z  103    CYS Z  121                          1555   1555  2.04  
SSBOND   8 CYS Z  124    CYS Z  139                          1555   1555  2.05  
SSBOND   9 CYS Z  145    CYS Z  164                          1555   1555  2.03  
LINK         ND2 ASN Z 157                 C1  NAG Z 201     1555   1555  1.45  
CISPEP   1 SER Z   63    PRO Z   64          0        -9.55                     
CRYST1  144.800  144.800  144.800  90.00  90.00  90.00 P 41 3 2     24          
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      0.006906  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006906  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006906        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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