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Database: PDB
Entry: 3EJH
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Original site: 3EJH 
HEADER    CELL ADHESION                           18-SEP-08   3EJH              
TITLE     CRYSTAL STRUCTURE OF THE FIBRONECTIN 8-9FNI DOMAIN PAIR IN COMPLEX    
TITLE    2 WITH A TYPE-I COLLAGEN PEPTIDE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBRONECTIN;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: 8-9FNI;                                                    
COMPND   5 SYNONYM: FN, COLD-INSOLUBLE GLOBULIN, CIG, UGL-Y1, UGL-Y2, UGL-Y3;   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: COLLAGEN TYPE-I A1 CHAIN;                                  
COMPND  10 CHAIN: E, F;                                                         
COMPND  11 FRAGMENT: COLLAGENASE SITE C-TERMINAL PEPTIDE;                       
COMPND  12 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: FN, FN1;                                                       
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: X-33;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: GENOMIC INTEGRATION;                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE  
SOURCE  13 OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN) TYPE-I     
SOURCE  14 COLLAGEN A1 CHAIN.                                                   
KEYWDS    FIBRONECTIN, COLLAGEN, PROTEIN COMPLEX, COLLAGENASE SITE, ACUTE       
KEYWDS   2 PHASE, CELL ADHESION, DISEASE MUTATION, EXTRACELLULAR MATRIX,        
KEYWDS   3 GLYCOPROTEIN, HEPARIN-BINDING, PHOSPHOPROTEIN, PYRROLIDONE           
KEYWDS   4 CARBOXYLIC ACID, SECRETED, SULFATION                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.ERAT,E.D.LOWE,I.D.CAMPBELL,I.VAKONAKIS                            
REVDAT   5   14-MAR-12 3EJH    1       MTRIX1 MTRIX2 MTRIX3 REMARK              
REVDAT   4   16-NOV-11 3EJH    1       HETATM                                   
REVDAT   3   13-JUL-11 3EJH    1       VERSN                                    
REVDAT   2   28-APR-09 3EJH    1       JRNL                                     
REVDAT   1   03-FEB-09 3EJH    0                                                
JRNL        AUTH   M.C.ERAT,D.A.SLATTER,E.D.LOWE,C.J.MILLARD,R.W.FARNDALE,      
JRNL        AUTH 2 I.D.CAMPBELL,I.VAKONAKIS                                     
JRNL        TITL   IDENTIFICATION AND STRUCTURAL ANALYSIS OF TYPE I COLLAGEN    
JRNL        TITL 2 SITES IN COMPLEX WITH FIBRONECTIN FRAGMENTS.                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106  4195 2009              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19251642                                                     
JRNL        DOI    10.1073/PNAS.0812516106                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.400                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 17126                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.260                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1229                            
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 49.2380 -  5.2900    0.98     1817   138  0.1970 0.2240        
REMARK   3     2  5.2900 -  4.1990    1.00     1840   143  0.1660 0.2020        
REMARK   3     3  4.1990 -  3.6690    1.00     1818   152  0.1660 0.1700        
REMARK   3     4  3.6690 -  3.3330    1.00     1839   148  0.1840 0.1820        
REMARK   3     5  3.3330 -  3.0950    1.00     1837   145  0.2010 0.2730        
REMARK   3     6  3.0950 -  2.9120    1.00     1830   138  0.2340 0.3090        
REMARK   3     7  2.9120 -  2.7660    1.00     1871   146  0.2140 0.2830        
REMARK   3     8  2.7660 -  2.6460    1.00     1831   138  0.2230 0.2420        
REMARK   3     9  2.6460 -  2.5440    1.00     1845   147  0.2440 0.3010        
REMARK   3    10  2.5440 -  2.4560    1.00     1808   136  0.2360 0.3180        
REMARK   3    11  2.4560 -  2.3790    1.00     1857   144  0.2470 0.3240        
REMARK   3    12  2.3790 -  2.3110    1.00     1825   144  0.2470 0.3020        
REMARK   3    13  2.3110 -  2.2500    1.00     1841   148  0.2320 0.2950        
REMARK   3    14  2.2500 -  2.1960    1.00     1808   147  0.2340 0.3030        
REMARK   3    15  2.1960 -  2.1460    1.00     1864   147  0.2260 0.2790        
REMARK   3    16  2.1460 -  2.1000    1.00     1803   136  0.2350 0.2760        
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              : 0.38                                          
REMARK   3   B_SOL              : 59.31                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.43100                                              
REMARK   3    B22 (A**2) : 4.43100                                              
REMARK   3    B33 (A**2) : -8.86100                                             
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      :  0.008           1916                                  
REMARK   3   ANGLE     :  1.297           2579                                  
REMARK   3   CHIRALITY :  0.081            247                                  
REMARK   3   PLANARITY :  0.004            339                                  
REMARK   3   DIHEDRAL  : 17.760            682                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A): -28.2235  18.3287  -2.6364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2446 T22:   0.3252                                     
REMARK   3      T33:   0.2801 T12:  -0.0348                                     
REMARK   3      T13:  -0.0761 T23:   0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5445 L22:   2.0750                                     
REMARK   3      L33:   0.7547 L12:   1.6166                                     
REMARK   3      L13:  -0.9621 L23:  -0.2491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1307 S12:   0.1639 S13:   0.3137                       
REMARK   3      S21:  -0.4053 S22:   0.2066 S23:   0.1369                       
REMARK   3      S31:  -0.1953 S32:  -0.3866 S33:  -0.0437                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A): -26.4682  30.8614  23.0860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2097 T22:   0.2629                                     
REMARK   3      T33:   0.2604 T12:  -0.0720                                     
REMARK   3      T13:   0.0443 T23:  -0.0670                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0588 L22:   2.2181                                     
REMARK   3      L33:   0.6133 L12:   1.3970                                     
REMARK   3      L13:   0.0836 L23:  -0.0397                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3234 S12:   0.1193 S13:   0.3005                       
REMARK   3      S21:   0.5483 S22:  -0.3371 S23:   0.1529                       
REMARK   3      S31:   0.2519 S32:  -0.1134 S33:   0.0025                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9905  24.6195  -8.9458              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3440 T22:   0.1088                                     
REMARK   3      T33:   0.2934 T12:   0.0630                                     
REMARK   3      T13:   0.0031 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4602 L22:  -1.9579                                     
REMARK   3      L33:   2.2544 L12:   1.9997                                     
REMARK   3      L13:   0.1434 L23:   0.4425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0337 S12:   0.1807 S13:  -0.0656                       
REMARK   3      S21:  -0.0794 S22:  -0.0197 S23:  -0.2658                       
REMARK   3      S31:   0.4285 S32:   0.0835 S33:  -0.0149                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A): -26.0306  47.4004  -9.2038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4013 T22:   0.2936                                     
REMARK   3      T33:   0.6233 T12:   0.2205                                     
REMARK   3      T13:  -0.2164 T23:  -0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0902 L22:   5.9771                                     
REMARK   3      L33:   0.3359 L12:  -5.0061                                     
REMARK   3      L13:   1.7787 L23:  -1.0255                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6949 S12:  -0.6203 S13:   0.6559                       
REMARK   3      S21:   0.0853 S22:   0.1408 S23:  -0.1602                       
REMARK   3      S31:  -0.6814 S32:  -0.5103 S33:   0.5790                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A): -31.2925  10.3237   2.0042              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3761 T22:   0.4296                                     
REMARK   3      T33:   0.3401 T12:  -0.1177                                     
REMARK   3      T13:  -0.0333 T23:  -0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2051 L22:   0.5963                                     
REMARK   3      L33:   1.9948 L12:   0.8030                                     
REMARK   3      L13:   1.3855 L23:   1.5480                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2487 S12:  -0.1166 S13:   0.2539                       
REMARK   3      S21:   0.1447 S22:  -0.4582 S23:   0.1018                       
REMARK   3      S31:   0.9980 S32:  -1.2237 S33:   0.6111                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A): -21.3315  20.6247  -9.0467              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3262 T22:   0.2141                                     
REMARK   3      T33:   0.2425 T12:  -0.0838                                     
REMARK   3      T13:   0.1093 T23:   0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0260 L22:   5.0761                                     
REMARK   3      L33:   1.2189 L12:   0.1451                                     
REMARK   3      L13:  -0.5141 L23:   1.3462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0363 S12:   0.5125 S13:   0.2831                       
REMARK   3      S21:   0.2633 S22:   0.1525 S23:  -0.6404                       
REMARK   3      S31:   0.1609 S32:  -0.1359 S33:  -0.1292                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (chain A and not (resseq 546:552 or         
REMARK   3                          resseq 558 or resseq 578:587 or resseq      
REMARK   3                          592:594 or resseq 598:603)) or chain C      
REMARK   3     SELECTION          : (chain B and not (resseq 546:552 or         
REMARK   3                          resseq 558 or resseq 578:587 or resseq      
REMARK   3                          592:594 or resseq 598:603)) or chain D      
REMARK   3     ATOM PAIRS NUMBER  : 477                                         
REMARK   3     RMSD               : 0.108                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain E and resseq 961:973 and not          
REMARK   3                          (resname HXP or resname HYP)                
REMARK   3     SELECTION          : chain F and resseq 961:973 and not          
REMARK   3                          (resname HXP or resname HYP)                
REMARK   3     ATOM PAIRS NUMBER  : 71                                          
REMARK   3     RMSD               : 0.053                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ONE TLS GROUP PER FNI DOMAIN AND          
REMARK   3  PEPTIDE CHAIN                                                       
REMARK   4                                                                      
REMARK   4 3EJH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049399.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUL-08                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9796                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
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   : 19940                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.225                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : 0.06500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.0230                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.57100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 2CG6, 2CG7                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M NACL, 0.1 M BISTRIS PH 6.5 ,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.07333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      100.14667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      100.14667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       50.07333            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 650  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   607                                                      
REMARK 465     SER A   608                                                      
REMARK 465     GLY E   956                                                      
REMARK 465     GLN E   957                                                      
REMARK 465     ARG E   958                                                      
REMARK 465     GLY E   959                                                      
REMARK 465     LEU E   975                                                      
REMARK 465     HYP E   976                                                      
REMARK 465     GLY E   977                                                      
REMARK 465     TYR E   978                                                      
REMARK 465     GLN B   603                                                      
REMARK 465     THR B   604                                                      
REMARK 465     TYR B   605                                                      
REMARK 465     PRO B   606                                                      
REMARK 465     SER B   607                                                      
REMARK 465     SER B   608                                                      
REMARK 465     GLY F   959                                                      
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   O    HOH A   638     O    HOH E   105              2.10            
REMARK 500   NE2  HIS A   581     O    HOH A   646              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    TYR F   978     O    HOH A   627     4455     2.06            
REMARK 500   CE1  HIS B   598     CE1  HIS B   598     4465     2.19            
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    GLN A 528       -6.83     83.34                                   
REMARK 500    HIS A 581     -136.78     43.57                                   
REMARK 500    GLU E 969      165.62    176.94                                   
REMARK 500    HYP E 973      -70.39    -73.26                                   
REMARK 500    ASP B 521     -106.42     57.36                                   
REMARK 500    GLN B 528       -2.81     81.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1                   
DBREF  3EJH A  516   608  UNP    P02751   FINC_HUMAN     516    608             
DBREF  3EJH B  516   608  UNP    P02751   FINC_HUMAN     516    608             
SEQADV 3EJH GLN A  528  UNP  P02751    ASN   528 ENGINEERED                     
SEQADV 3EJH LYS A  534  UNP  P02751    ARG   534 ENGINEERED                     
SEQADV 3EJH GLN B  528  UNP  P02751    ASN   528 ENGINEERED                     
SEQADV 3EJH LYS B  534  UNP  P02751    ARG   534 ENGINEERED                     
SEQRES   1 A   93  ASP GLN CYS ILE VAL ASP ASP ILE THR TYR ASN VAL GLN          
SEQRES   2 A   93  ASP THR PHE HIS LYS LYS HIS GLU GLU GLY HIS MET LEU          
SEQRES   3 A   93  ASN CYS THR CYS PHE GLY GLN GLY ARG GLY ARG TRP LYS          
SEQRES   4 A   93  CYS ASP PRO VAL ASP GLN CYS GLN ASP SER GLU THR GLY          
SEQRES   5 A   93  THR PHE TYR GLN ILE GLY ASP SER TRP GLU LYS TYR VAL          
SEQRES   6 A   93  HIS GLY VAL ARG TYR GLN CYS TYR CYS TYR GLY ARG GLY          
SEQRES   7 A   93  ILE GLY GLU TRP HIS CYS GLN PRO LEU GLN THR TYR PRO          
SEQRES   8 A   93  SER SER                                                      
SEQRES   1 E   23  GLY GLN ARG GLY VAL VAL GLY LEU HYP GLY GLN ARG GLY          
SEQRES   2 E   23  GLU ARG GLY PHE HYP GLY LEU HYP GLY TYR                      
SEQRES   1 B   93  ASP GLN CYS ILE VAL ASP ASP ILE THR TYR ASN VAL GLN          
SEQRES   2 B   93  ASP THR PHE HIS LYS LYS HIS GLU GLU GLY HIS MET LEU          
SEQRES   3 B   93  ASN CYS THR CYS PHE GLY GLN GLY ARG GLY ARG TRP LYS          
SEQRES   4 B   93  CYS ASP PRO VAL ASP GLN CYS GLN ASP SER GLU THR GLY          
SEQRES   5 B   93  THR PHE TYR GLN ILE GLY ASP SER TRP GLU LYS TYR VAL          
SEQRES   6 B   93  HIS GLY VAL ARG TYR GLN CYS TYR CYS TYR GLY ARG GLY          
SEQRES   7 B   93  ILE GLY GLU TRP HIS CYS GLN PRO LEU GLN THR TYR PRO          
SEQRES   8 B   93  SER SER                                                      
SEQRES   1 F   23  GLY GLN ARG GLY VAL VAL GLY LEU HYP GLY GLN ARG GLY          
SEQRES   2 F   23  GLU ARG GLY PHE HYP GLY LEU HYP GLY TYR                      
MODRES 3EJH ASN A  542  ASN  GLYCOSYLATION SITE                                 
MODRES 3EJH ASN B  542  ASN  GLYCOSYLATION SITE                                 
MODRES 3EJH HYP E  964  PRO  4-HYDROXYPROLINE                                   
MODRES 3EJH HYP E  973  PRO  4-HYDROXYPROLINE                                   
MODRES 3EJH HYP F  964  PRO  4-HYDROXYPROLINE                                   
MODRES 3EJH HYP F  973  PRO  4-HYDROXYPROLINE                                   
MODRES 3EJH HYP F  976  PRO  4-HYDROXYPROLINE                                   
HET    HYP  E 964       8                                                       
HET    HYP  E 973       8                                                       
HET    HYP  F 964       8                                                       
HET    HYP  F 973       8                                                       
HET    HYP  F 976       8                                                       
HET    NAG  A   1      14                                                       
HET    NAG  B   1      14                                                       
HET    GOL  B 609       6                                                       
HETNAM     HYP 4-HYDROXYPROLINE                                                 
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     GOL GLYCEROL                                                         
HETSYN     HYP HYDROXYPROLINE                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  HYP    5(C5 H9 N O3)                                                
FORMUL   5  NAG    2(C8 H15 N O6)                                               
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL   8  HOH   *105(H2 O)                                                    
SHEET    1   A 2 GLN A 517  VAL A 520  0                                        
SHEET    2   A 2 ILE A 523  ASN A 526 -1  O  TYR A 525   N  CYS A 518           
SHEET    1   B 8 GLN E 966  GLY E 968  0                                        
SHEET    2   B 8 ARG A 552  PRO A 557 -1  N  CYS A 555   O  GLN E 966           
SHEET    3   B 8 MET A 540  GLY A 547 -1  N  ASN A 542   O  ASP A 556           
SHEET    4   B 8 ASP A 529  LYS A 534 -1  N  PHE A 531   O  CYS A 543           
SHEET    5   B 8 GLY F 965  GLY F 968 -1  O  GLY F 965   N  THR A 530           
SHEET    6   B 8 ARG B 552  PRO B 557 -1  N  CYS B 555   O  GLN F 966           
SHEET    7   B 8 MET B 540  GLY B 547 -1  N  ASN B 542   O  ASP B 556           
SHEET    8   B 8 THR B 530  LYS B 534 -1  N  PHE B 531   O  CYS B 543           
SHEET    1   C 2 GLN A 560  GLN A 562  0                                        
SHEET    2   C 2 PHE A 569  GLN A 571 -1  O  TYR A 570   N  CYS A 561           
SHEET    1   D 3 SER A 575  LYS A 578  0                                        
SHEET    2   D 3 TYR A 585  GLY A 591 -1  O  CYS A 587   N  TRP A 576           
SHEET    3   D 3 GLU A 596  PRO A 601 -1  O  GLN A 600   N  GLN A 586           
SHEET    1   E 2 GLN B 517  VAL B 520  0                                        
SHEET    2   E 2 ILE B 523  ASN B 526 -1  O  TYR B 525   N  CYS B 518           
SHEET    1   F 2 GLN B 560  GLN B 562  0                                        
SHEET    2   F 2 PHE B 569  GLN B 571 -1  O  TYR B 570   N  CYS B 561           
SHEET    1   G 3 SER B 575  VAL B 580  0                                        
SHEET    2   G 3 VAL B 583  GLY B 591 -1  O  TYR B 585   N  LYS B 578           
SHEET    3   G 3 GLU B 596  PRO B 601 -1  O  GLN B 600   N  GLN B 586           
SSBOND   1 CYS A  518    CYS A  545                          1555   1555  2.03  
SSBOND   2 CYS A  543    CYS A  555                          1555   1555  2.08  
SSBOND   3 CYS A  561    CYS A  589                          1555   1555  2.03  
SSBOND   4 CYS A  587    CYS A  599                          1555   1555  2.06  
SSBOND   5 CYS B  518    CYS B  545                          1555   1555  2.03  
SSBOND   6 CYS B  543    CYS B  555                          1555   1555  2.07  
SSBOND   7 CYS B  561    CYS B  589                          1555   1555  2.04  
SSBOND   8 CYS B  587    CYS B  599                          1555   1555  2.04  
LINK         C   LEU E 963                 N   HYP E 964     1555   1555  1.32  
LINK         C   HYP E 964                 N   GLY E 965     1555   1555  1.33  
LINK         C   PHE E 972                 N   HYP E 973     1555   1555  1.32  
LINK         C   HYP E 973                 N   GLY E 974     1555   1555  1.33  
LINK         C   LEU F 963                 N   HYP F 964     1555   1555  1.33  
LINK         C   HYP F 964                 N   GLY F 965     1555   1555  1.33  
LINK         C   PHE F 972                 N   HYP F 973     1555   1555  1.33  
LINK         C   HYP F 973                 N   GLY F 974     1555   1555  1.34  
LINK         C   LEU F 975                 N   HYP F 976     1555   1555  1.32  
LINK         C   HYP F 976                 N   GLY F 977     1555   1555  1.33  
LINK         ND2 ASN A 542                 C1  NAG A   1     1555   1555  1.45  
LINK         ND2 ASN B 542                 C1  NAG B   1     1555   1555  1.45  
SITE     1 AC1  7 ASN A 542  CYS A 543  THR A 544  LYS A 554                    
SITE     2 AC1  7 ASP A 556  HOH A 610  ARG F 967                               
SITE     1 AC2  9 HOH B  11  HOH B  33  HOH B 102  ASN B 542                    
SITE     2 AC2  9 CYS B 543  THR B 544  LYS B 554  ASP B 556                    
SITE     3 AC2  9 ARG E 967                                                     
CRYST1   56.840   56.840  150.220  90.00  90.00 120.00 P 31 2 1     12          
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      0.017593  0.010157  0.000000        0.00000                         
SCALE2      0.000000  0.020315  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006657        0.00000                         
MTRIX1   1  0.261943  0.313324  0.912805      -25.46090    1                    
MTRIX2   1  0.476324  0.780628 -0.404642        0.76632    1                    
MTRIX3   1 -0.839346  0.540784  0.055237      -25.16250    1                    
MTRIX1   2  0.247755  0.367001  0.896620      -27.25420    1                    
MTRIX2   2  0.482008  0.756112 -0.442677        1.15435    1                    
MTRIX3   2 -0.840408  0.541854  0.010433      -25.59050    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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