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Database: PDB
Entry: 4K24
LinkDB: 4K24
Original site: 4K24 
HEADER    IMMUNE SYSTEM                           08-APR-13   4K24              
TITLE     STRUCTURE OF ANTI-UPAR FAB ATN-658 IN COMPLEX WITH UPAR               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 21-153;                                       
COMPND   5 SYNONYM: U-PLASMINOGEN ACTIVATOR, UPA, UROKINASE-TYPE PLASMINOGEN    
COMPND   6 ACTIVATOR LONG CHAIN A, UROKINASE-TYPE PLASMINOGEN ACTIVATOR SHORT   
COMPND   7 CHAIN A, UROKINASE-TYPE PLASMINOGEN ACTIVATOR CHAIN B;               
COMPND   8 EC: 3.4.21.73;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: VITRONECTIN;                                               
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: UNP RESIDUES 21-60;                                        
COMPND  14 SYNONYM: VN, S-PROTEIN, SERUM-SPREADING FACTOR, V75, VITRONECTIN V65 
COMPND  15 SUBUNIT, VITRONECTIN V10 SUBUNIT, SOMATOMEDIN-B;                     
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: ANTI-UPAR ANTIBODY, HEAVY CHAIN;                           
COMPND  19 CHAIN: H;                                                            
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: ANTI-UPAR ANTIBODY, LIGHT CHAIN;                           
COMPND  22 CHAIN: L;                                                            
COMPND  23 MOL_ID: 5;                                                           
COMPND  24 MOLECULE: UROKINASE PLASMINOGEN ACTIVATOR SURFACE RECEPTOR;          
COMPND  25 CHAIN: U;                                                            
COMPND  26 FRAGMENT: UNP RESIDUES 23-303;                                       
COMPND  27 SYNONYM: U-PAR, UPAR, MONOCYTE ACTIVATION ANTIGEN MO3;               
COMPND  28 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: PLAU;                                                          
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SCHNEIDER 2;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMT/BIP;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: VTN;                                                           
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 MOL_ID: 3;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  25 ORGANISM_TAXID: 10090;                                               
SOURCE  26 MOL_ID: 5;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  28 ORGANISM_COMMON: HUMAN;                                              
SOURCE  29 ORGANISM_TAXID: 9606;                                                
SOURCE  30 GENE: MO3, PLAUR, UPAR;                                              
SOURCE  31 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  33 EXPRESSION_SYSTEM_STRAIN: SCHNEIDER 2;                               
SOURCE  34 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  35 EXPRESSION_SYSTEM_PLASMID: PMT/BIP                                   
KEYWDS    IMMUNE SYSTEM                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.D.HUANG,X.XU,C.YUAN                                                 
REVDAT   4   29-JUL-20 4K24    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   11-DEC-19 4K24    1       REMARK SEQADV SSBOND LINK                
REVDAT   2   05-MAR-14 4K24    1       EXPDTA                                   
REVDAT   1   26-FEB-14 4K24    0                                                
JRNL        AUTH   X.XU,Y.CAI,Y.WEI,F.DONATE,J.JUAREZ,G.PARRY,L.CHEN,           
JRNL        AUTH 2 E.J.MEEHAN,R.W.AHN,A.UGOLKOV,O.DUBROVSKYI,T.V.O'HALLORAN,    
JRNL        AUTH 3 M.HUANG,A.P.MAZAR                                            
JRNL        TITL   IDENTIFICATION OF A NEW EPITOPE IN UPAR AS A TARGET FOR THE  
JRNL        TITL 2 CANCER THERAPEUTIC MONOCLONAL ANTIBODY ATN-658, A STRUCTURAL 
JRNL        TITL 3 HOMOLOG OF THE UPAR BINDING INTEGRIN CD11B ( ALPHA M)        
JRNL        REF    PLOS ONE                      V.   9 85349 2014              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   24465541                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0085349                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.1_1168                                    
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) : 4.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 12432                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.840                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 602                             
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 26.9029 -  7.0874    0.99     3039   150  0.2000 0.2666        
REMARK   3     2  7.0874 -  5.6425    1.00     2971   139  0.2246 0.2762        
REMARK   3     3  5.6425 -  4.9343    1.00     2940   155  0.2405 0.2991        
REMARK   3     4  4.9343 -  4.5000    0.99     2880   158  0.2535 0.2792        
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)     : 0.510            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.960           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 284.9                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 13.44000                                             
REMARK   3    B22 (A**2) : 13.44000                                             
REMARK   3    B33 (A**2) : -26.88000                                            
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      :  0.013           6948                                  
REMARK   3   ANGLE     :  2.017           9371                                  
REMARK   3   CHIRALITY :  0.132           1034                                  
REMARK   3   PLANARITY :  0.008           1208                                  
REMARK   3   DIHEDRAL  : 20.414           2544                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6697  29.6905  52.7353              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1128 T22:   1.9723                                     
REMARK   3      T33:   2.4258 T12:  -0.3301                                     
REMARK   3      T13:   0.0829 T23:   0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3627 L22:  -0.6560                                     
REMARK   3      L33:   3.6246 L12:   0.9741                                     
REMARK   3      L13:   1.6251 L23:   2.9948                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0501 S12:  -0.5488 S13:  -0.6942                       
REMARK   3      S21:  -0.6807 S22:   0.0290 S23:   0.1128                       
REMARK   3      S31:   0.7341 S32:  -0.6133 S33:   0.3410                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8113  25.7080  82.1740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3569 T22:   3.4422                                     
REMARK   3      T33:   2.4535 T12:  -0.0374                                     
REMARK   3      T13:  -0.3173 T23:   0.1099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1548 L22:   0.4658                                     
REMARK   3      L33:   9.2023 L12:  -1.2400                                     
REMARK   3      L13:  -8.1171 L23:   1.3574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -2.6771 S12:  -3.1627 S13:   1.3568                       
REMARK   3      S21:   0.4839 S22:   0.6504 S23:  -0.0612                       
REMARK   3      S31:   0.6322 S32:   0.1250 S33:   2.2204                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'U'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.2660  29.3461  54.0831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7406 T22:   2.0830                                     
REMARK   3      T33:   2.3148 T12:  -0.1827                                     
REMARK   3      T13:   0.1030 T23:  -0.2058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8017 L22:   0.0348                                     
REMARK   3      L33:   4.8272 L12:  -1.6905                                     
REMARK   3      L13:   0.0782 L23:  -1.5974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1036 S12:  -0.0306 S13:   0.4133                       
REMARK   3      S21:  -0.2336 S22:   0.7136 S23:  -0.1370                       
REMARK   3      S31:  -0.5576 S32:  -0.3305 S33:  -0.6051                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'H'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -41.9119  13.1353  16.8476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.4315 T22:   3.4216                                     
REMARK   3      T33:   2.4659 T12:  -0.2213                                     
REMARK   3      T13:   0.1944 T23:   0.2833                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -1.0037 L22:  -0.0041                                     
REMARK   3      L33:   9.9394 L12:  -1.1663                                     
REMARK   3      L13:   0.3460 L23:   0.3374                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7267 S12:   1.3586 S13:   0.7132                       
REMARK   3      S21:  -0.4628 S22:  -0.5035 S23:  -0.6677                       
REMARK   3      S31:   0.5711 S32:  -0.1993 S33:   0.2034                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'L'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -46.0106  29.5362   9.3293              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.0456 T22:   3.6272                                     
REMARK   3      T33:   2.6696 T12:  -0.2477                                     
REMARK   3      T13:  -0.2211 T23:   0.0905                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1690 L22:   1.5560                                     
REMARK   3      L33:   2.7252 L12:  -0.8838                                     
REMARK   3      L13:   4.4172 L23:   0.3648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.3838 S12:   1.3198 S13:   0.6265                       
REMARK   3      S21:  -1.2440 S22:  -0.1814 S23:   0.9262                       
REMARK   3      S31:  -2.0766 S32:   1.0930 S33:   0.2170                       
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 4K24 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-APR-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000078794.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JAN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.04                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12451                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.13900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.84100                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 3BT2(CHAIN A, B, U), 4K23(CHAIN H, L)                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 55%(V/V) TACSIMATE,   
REMARK 280  2%(V/V) 2-METHYL-1,3-PROPANEDIOL, VAPOR DIFFUSION, SITTING DROP,    
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       82.32950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       47.53296            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      130.52733            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       82.32950            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       47.53296            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      130.52733            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       82.32950            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       47.53296            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      130.52733            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       82.32950            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       47.53296            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      130.52733            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       82.32950            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       47.53296            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      130.52733            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       82.32950            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       47.53296            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      130.52733            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       95.06592            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      261.05467            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       95.06592            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      261.05467            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       95.06592            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      261.05467            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       95.06592            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      261.05467            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       95.06592            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      261.05467            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       95.06592            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      261.05467            
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, U, C, D                   
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     ARG A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     ASP A   133                                                      
REMARK 465     SER H   128                                                      
REMARK 465     ALA H   129                                                      
REMARK 465     ALA H   130                                                      
REMARK 465     GLN H   131                                                      
REMARK 465     THR H   132                                                      
REMARK 465     ASN H   133                                                      
REMARK 465     ARG H   213                                                      
REMARK 465     ASP H   214                                                      
REMARK 465     CYS H   215                                                      
REMARK 465     GLY H   216                                                      
REMARK 465     CYS H   217                                                      
REMARK 465     LYS H   218                                                      
REMARK 465     PRO H   219                                                      
REMARK 465     CYS H   220                                                      
REMARK 465     ILE H   221                                                      
REMARK 465     CYS H   222                                                      
REMARK 465     CYS L   214                                                      
REMARK 465     ARG U    -1                                                      
REMARK 465     SER U     0                                                      
REMARK 465     ARG U    83                                                      
REMARK 465     ALA U    84                                                      
REMARK 465     LEU U   276                                                      
REMARK 465     ASP U   277                                                      
REMARK 465     VAL U   278                                                      
REMARK 465     GLN U   279                                                      
REMARK 465     TYR U   280                                                      
REMARK 465     ARG U   281                                                      
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   O4   NAG C     2     C1   MAN U   303              1.09            
REMARK 500   ND2  ASN U    52     C1   NAG C     1              1.60            
REMARK 500   NE2  HIS U   203     O5   NAG D     1              1.68            
REMARK 500   CB   CYS A    13     SG   CYS A    31              1.68            
REMARK 500   CB   CYS U   266     SG   CYS U   271              1.73            
REMARK 500   O4   NAG C     1     O5   NAG C     2              1.76            
REMARK 500   N    THR H    83     OD2  ASP H    86              1.77            
REMARK 500   NH1  ARG H    66     O    SER H    82B             1.83            
REMARK 500   ND2  ASN U   172     C2   NAG U   304              1.85            
REMARK 500   OH   TYR A    58     O    LYS A    61              1.85            
REMARK 500   CB   CYS U     3     SG   CYS U    24              1.85            
REMARK 500   O    HIS A    56     NH2  ARG A    59              1.90            
REMARK 500   O    TYR H    97     CD2  HIS H    99              1.93            
REMARK 500   O    LEU U   184     N    LEU U   187              1.93            
REMARK 500   OG   SER H   178     OG   SER L   176              1.96            
REMARK 500   O    LEU U   184     N    ASN U   186              1.98            
REMARK 500   O    VAL A    79     N    GLN A    82              1.98            
REMARK 500   NZ   LYS H    13     O    SER H   113              1.99            
REMARK 500   CD2  HIS U   203     O6   NAG D     1              2.00            
REMARK 500   ND2  ASN U   200     C2   NAG D     1              2.00            
REMARK 500   OE1  GLN B     2     OG   SER B     4              2.02            
REMARK 500   OE2  GLU L   105     OH   TYR L   173              2.02            
REMARK 500   OD1  ASP B    22     N    LEU B    24              2.03            
REMARK 500   O    SER B    26     N    GLN B    29              2.03            
REMARK 500   SG   CYS U     3     SG   CYS U    24              2.03            
REMARK 500   NH1  ARG A    88     OD2  ASP A    90              2.04            
REMARK 500   ND2  ASN U   200     O5   NAG D     1              2.04            
REMARK 500   SG   CYS B     5     SG   CYS B    32              2.05            
REMARK 500   OG   SER U   100     OE1  GLU U   106              2.06            
REMARK 500   NE2  GLN L    90     OG1  THR L    97              2.08            
REMARK 500   O    SER H    95     O    VAL H   100A             2.08            
REMARK 500   N    THR H   117     O    PHE H   146              2.09            
REMARK 500   O    TYR U   195     ND2  ASN U   272              2.10            
REMARK 500   O4   NAG D     1     O5   NAG D     2              2.11            
REMARK 500   O    GLY U    99     N    SER U   104              2.12            
REMARK 500   O    GLY B     7     N    CYS B     9              2.12            
REMARK 500   O    LYS U   198     O    GLY U   204              2.14            
REMARK 500   OG1  THR U   243     OG   SER U   245              2.14            
REMARK 500   NE2  HIS U   203     C5   NAG D     1              2.16            
REMARK 500   ND2  ASN U   172     N2   NAG U   304              2.18            
REMARK 500   OD1  ASN L    34     O    TRP L    89              2.19            
REMARK 500   O4   NAG C     2     O5   MAN U   303              2.19            
REMARK 500   OE1  GLN L     6     N    GLY L   101              2.19            
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   OE1  GLN A    93     O    GLY H    55     3555     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A  59   N   -  CA  -  C   ANGL. DEV. = -17.2 DEGREES          
REMARK 500    LEU A  94   CA  -  CB  -  CG  ANGL. DEV. = -15.3 DEGREES          
REMARK 500    CYS B  32   CA  -  CB  -  SG  ANGL. DEV. =   8.0 DEGREES          
REMARK 500    PRO B  41   C   -  N   -  CA  ANGL. DEV. =  12.8 DEGREES          
REMARK 500    TYR H  33   CA  -  CB  -  CG  ANGL. DEV. =  12.9 DEGREES          
REMARK 500    PRO H  52A  C   -  N   -  CA  ANGL. DEV. =  20.6 DEGREES          
REMARK 500    PRO H  52A  C   -  N   -  CD  ANGL. DEV. = -20.5 DEGREES          
REMARK 500    VAL H 111   CB  -  CA  -  C   ANGL. DEV. = -11.7 DEGREES          
REMARK 500    PRO H 167   C   -  N   -  CA  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    PRO H 167   C   -  N   -  CD  ANGL. DEV. = -15.6 DEGREES          
REMARK 500    LEU L  27C  CA  -  CB  -  CG  ANGL. DEV. = -15.8 DEGREES          
REMARK 500    VAL U  41   CB  -  CA  -  C   ANGL. DEV. = -11.9 DEGREES          
REMARK 500    PRO U 118   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    PRO U 218   C   -  N   -  CA  ANGL. DEV. =  12.6 DEGREES          
REMARK 500    PRO U 218   C   -  N   -  CD  ANGL. DEV. = -13.5 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    CYS A  11     -152.69     43.52                                   
REMARK 500    SER A  26       19.80     43.90                                   
REMARK 500    LYS A  35     -102.46     54.21                                   
REMARK 500    LYS A  36      -11.99    -43.70                                   
REMARK 500    SER A  47      -63.30   -148.82                                   
REMARK 500    THR A  49      -71.49    -72.06                                   
REMARK 500    ASN A  54      -14.93     68.29                                   
REMARK 500    TYR A  58      101.99    -48.53                                   
REMARK 500    LYS A  61     -154.80    -75.28                                   
REMARK 500    ALA A  62       77.55     77.46                                   
REMARK 500    ARG A  69     -171.17    -63.59                                   
REMARK 500    PRO A  70     -169.67    -76.67                                   
REMARK 500    ALA A  77      -74.59    -47.78                                   
REMARK 500    THR A  78       -6.81    -59.40                                   
REMARK 500    LEU A  80       -9.53    -58.47                                   
REMARK 500    GLN A  82     -169.50    -75.89                                   
REMARK 500    THR A  83      -79.08    -73.09                                   
REMARK 500    SER A  89     -102.56     38.87                                   
REMARK 500    LYS A  98       -1.91    -59.82                                   
REMARK 500    PRO A 105       53.26   -101.56                                   
REMARK 500    ARG A 109      -77.37    -48.67                                   
REMARK 500    PRO A 111     -171.71    -60.29                                   
REMARK 500    TRP A 112     -176.79   -172.27                                   
REMARK 500    PRO A 121      151.30    -47.93                                   
REMARK 500    GLU B   3      -75.91    -88.74                                   
REMARK 500    SER B   4       66.99     38.67                                   
REMARK 500    ARG B   8      -17.23     55.75                                   
REMARK 500    CYS B   9      -17.91     57.44                                   
REMARK 500    LYS B  17      164.91    170.75                                   
REMARK 500    ALA B  37      -72.80    -56.36                                   
REMARK 500    TYR H  27      178.47    175.98                                   
REMARK 500    THR H  30       -7.71    -57.37                                   
REMARK 500    LYS H  43      -70.63   -135.38                                   
REMARK 500    ASN H  52       84.20   -151.78                                   
REMARK 500    PRO H  52A     -48.63    -11.33                                   
REMARK 500    TYR H  53      -76.17    -78.05                                   
REMARK 500    THR H  70      168.32    176.01                                   
REMARK 500    SER H  82B     114.08     32.81                                   
REMARK 500    ALA H  88     -169.03   -171.05                                   
REMARK 500    SER H  95      -77.63    -84.61                                   
REMARK 500    HIS H  99       28.97     42.50                                   
REMARK 500    SER H 100     -143.75     32.38                                   
REMARK 500    VAL H 100A      96.47     63.50                                   
REMARK 500    ASP H 101      -68.13   -134.46                                   
REMARK 500    SER H 112     -168.49   -165.79                                   
REMARK 500    SER H 113      -73.78    -80.31                                   
REMARK 500    PHE H 146      142.17   -176.54                                   
REMARK 500    SER H 160      -74.82   -123.94                                   
REMARK 500    GLN H 171      162.73    173.35                                   
REMARK 500    SER H 190      -72.29    -70.96                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      91 RAMACHANDRAN OUTLIERS.                        
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 ARG A   88     SER A   89                  139.79                    
REMARK 500 THR B   10     GLU B   11                  144.91                    
REMARK 500 ILE H   51     ASN H   52                 -148.93                    
REMARK 500 GLU U   37     LEU U   38                 -145.72                    
REMARK 500 GLU U  230     PRO U  231                 -130.29                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG C    1                                                       
REMARK 610     MAN U  303                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4K23   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 A SEQUENCE DATABASE REFERENCE FOR ENTITY 3 AND 4 DOES NOT CURRENTLY  
REMARK 999 EXIST.                                                               
DBREF  4K24 A    1   133  UNP    P00749   UROK_HUMAN      21    153             
DBREF  4K24 B    2    41  UNP    P04004   VTNC_HUMAN      21     60             
DBREF  4K24 U    1   281  UNP    Q03405   UPAR_HUMAN      23    303             
DBREF  4K24 H    1   222  PDB    4K24     4K24             1    222             
DBREF  4K24 L    1   214  PDB    4K24     4K24             1    214             
SEQADV 4K24 ARG A   -1  UNP  P00749              EXPRESSION TAG                 
SEQADV 4K24 SER A    0  UNP  P00749              EXPRESSION TAG                 
SEQADV 4K24 ARG U   -1  UNP  Q03405              EXPRESSION TAG                 
SEQADV 4K24 SER U    0  UNP  Q03405              EXPRESSION TAG                 
SEQRES   1 A  135  ARG SER SER ASN GLU LEU HIS GLN VAL PRO SER ASN CYS          
SEQRES   2 A  135  ASP CYS LEU ASN GLY GLY THR CYS VAL SER ASN LYS TYR          
SEQRES   3 A  135  PHE SER ASN ILE HIS TRP CYS ASN CYS PRO LYS LYS PHE          
SEQRES   4 A  135  GLY GLY GLN HIS CYS GLU ILE ASP LYS SER LYS THR CYS          
SEQRES   5 A  135  TYR GLU GLY ASN GLY HIS PHE TYR ARG GLY LYS ALA SER          
SEQRES   6 A  135  THR ASP THR MET GLY ARG PRO CYS LEU PRO TRP ASN SER          
SEQRES   7 A  135  ALA THR VAL LEU GLN GLN THR TYR HIS ALA HIS ARG SER          
SEQRES   8 A  135  ASP ALA LEU GLN LEU GLY LEU GLY LYS HIS ASN TYR CYS          
SEQRES   9 A  135  ARG ASN PRO ASP ASN ARG ARG ARG PRO TRP CYS TYR VAL          
SEQRES  10 A  135  GLN VAL GLY LEU LYS PRO LEU VAL GLN GLU CYS MET VAL          
SEQRES  11 A  135  HIS ASP CYS ALA ASP                                          
SEQRES   1 B   40  GLN GLU SER CYS LYS GLY ARG CYS THR GLU GLY PHE ASN          
SEQRES   2 B   40  VAL ASP LYS LYS CYS GLN CYS ASP GLU LEU CYS SER TYR          
SEQRES   3 B   40  TYR GLN SER CYS CYS THR ASP TYR THR ALA GLU CYS LYS          
SEQRES   4 B   40  PRO                                                          
SEQRES   1 H  228  GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS          
SEQRES   2 H  228  THR GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY          
SEQRES   3 H  228  TYR SER PHE THR SER TYR TYR MET HIS TRP VAL LYS GLN          
SEQRES   4 H  228  SER HIS GLY LYS SER LEU GLU TRP ILE GLY GLU ILE ASN          
SEQRES   5 H  228  PRO TYR ASN GLY GLY ALA SER TYR ASN GLN LYS ILE LYS          
SEQRES   6 H  228  GLY ARG ALA THR PHE THR VAL ASP THR SER SER ARG THR          
SEQRES   7 H  228  ALA TYR MET GLN PHE ASN SER LEU THR SER GLU ASP SER          
SEQRES   8 H  228  ALA VAL TYR TYR CYS ALA ARG SER ILE TYR GLY HIS SER          
SEQRES   9 H  228  VAL LEU ASP TYR TRP GLY GLN GLY THR SER VAL SER VAL          
SEQRES  10 H  228  SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU          
SEQRES  11 H  228  ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR          
SEQRES  12 H  228  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  228  THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  228  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  228  LEU SER SER SER VAL THR VAL PRO SER SER THR TRP PRO          
SEQRES  16 H  228  SER GLN THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  228  SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS          
SEQRES  18 H  228  GLY CYS LYS PRO CYS ILE CYS                                  
SEQRES   1 L  219  ASP VAL VAL MET THR GLN THR PRO LEU THR LEU SER VAL          
SEQRES   2 L  219  THR ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER          
SEQRES   3 L  219  GLN SER LEU LEU ASP SER ASP GLY LYS THR TYR LEU ASN          
SEQRES   4 L  219  TRP LEU LEU GLN ARG PRO GLY GLN SER PRO LYS ARG LEU          
SEQRES   5 L  219  ILE TYR LEU VAL SER LYS LEU ASP SER GLY VAL PRO ASP          
SEQRES   6 L  219  ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR LEU          
SEQRES   7 L  219  LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR          
SEQRES   8 L  219  TYR CYS TRP GLN GLY THR HIS PHE PRO LEU THR PHE GLY          
SEQRES   9 L  219  ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA ALA          
SEQRES  10 L  219  PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU          
SEQRES  11 L  219  THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN          
SEQRES  12 L  219  PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP          
SEQRES  13 L  219  GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR          
SEQRES  14 L  219  ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER          
SEQRES  15 L  219  THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN          
SEQRES  16 L  219  SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER          
SEQRES  17 L  219  PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS                  
SEQRES   1 U  283  ARG SER LEU ARG CYS MET GLN CYS LYS THR ASN GLY ASP          
SEQRES   2 U  283  CYS ARG VAL GLU GLU CYS ALA LEU GLY GLN ASP LEU CYS          
SEQRES   3 U  283  ARG THR THR ILE VAL ARG LEU TRP GLU GLU GLY GLU GLU          
SEQRES   4 U  283  LEU GLU LEU VAL GLU LYS SER CYS THR HIS SER GLU LYS          
SEQRES   5 U  283  THR ASN ARG THR LEU SER TYR ARG THR GLY LEU LYS ILE          
SEQRES   6 U  283  THR SER LEU THR GLU VAL VAL CYS GLY LEU ASP LEU CYS          
SEQRES   7 U  283  ASN GLN GLY ASN SER GLY ARG ALA VAL THR TYR SER ARG          
SEQRES   8 U  283  SER ARG TYR LEU GLU CYS ILE SER CYS GLY SER SER ASP          
SEQRES   9 U  283  MET SER CYS GLU ARG GLY ARG HIS GLN SER LEU GLN CYS          
SEQRES  10 U  283  ARG SER PRO GLU GLU GLN CYS LEU ASP VAL VAL THR HIS          
SEQRES  11 U  283  TRP ILE GLN GLU GLY GLU GLU GLY ARG PRO LYS ASP ASP          
SEQRES  12 U  283  ARG HIS LEU ARG GLY CYS GLY TYR LEU PRO GLY CYS PRO          
SEQRES  13 U  283  GLY SER ASN GLY PHE HIS ASN ASN ASP THR PHE HIS PHE          
SEQRES  14 U  283  LEU LYS CYS CYS ASN THR THR LYS CYS ASN GLU GLY PRO          
SEQRES  15 U  283  ILE LEU GLU LEU GLU ASN LEU PRO GLN ASN GLY ARG GLN          
SEQRES  16 U  283  CYS TYR SER CYS LYS GLY ASN SER THR HIS GLY CYS SER          
SEQRES  17 U  283  SER GLU GLU THR PHE LEU ILE ASP CYS ARG GLY PRO MET          
SEQRES  18 U  283  ASN GLN CYS LEU VAL ALA THR GLY THR HIS GLU PRO LYS          
SEQRES  19 U  283  ASN GLN SER TYR MET VAL ARG GLY CYS ALA THR ALA SER          
SEQRES  20 U  283  MET CYS GLN HIS ALA HIS LEU GLY ASP ALA PHE SER MET          
SEQRES  21 U  283  ASN HIS ILE ASP VAL SER CYS CYS THR LYS SER GLY CYS          
SEQRES  22 U  283  ASN HIS PRO ASP LEU ASP VAL GLN TYR ARG                      
MODRES 4K24 ASN U  172  ASN  GLYCOSYLATION SITE                                 
MODRES 4K24 ASN U  200  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    MAN  U 303      11                                                       
HET    NAG  U 304      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
FORMUL   6  NAG    5(C8 H15 N O6)                                               
FORMUL   8  MAN    C6 H12 O6                                                    
HELIX    1   1 GLU A   52  HIS A   56  5                                   5    
HELIX    2   2 SER A   76  GLN A   81  1                                   6    
HELIX    3   3 ASP A   90  GLY A   95  5                                   6    
HELIX    4   4 LEU B   24  GLN B   29  5                                   6    
HELIX    5   5 ASP B   34  CYS B   39  1                                   6    
HELIX    6   6 SER H   28  TYR H   32  5                                   5    
HELIX    7   7 ASN H   60  LYS H   64  5                                   5    
HELIX    8   8 THR H   83  SER H   87  5                                   5    
HELIX    9   9 VAL L   51  LYS L   53  5                                   3    
HELIX   10  10 SER L  121  GLY L  128  1                                   8    
HELIX   11  11 THR L  182  GLU L  187  1                                   6    
HELIX   12  12 HIS U  229  ASN U  233  5                                   5    
HELIX   13  13 THR U  243  GLN U  248  1                                   6    
HELIX   14  14 HIS U  251  PHE U  256  1                                   6    
SHEET    1   A 2 THR A  18  SER A  21  0                                        
SHEET    2   A 2 HIS A  29  ASN A  32 -1  O  ASN A  32   N  THR A  18           
SHEET    1   B 2 PHE A  37  GLY A  38  0                                        
SHEET    2   B 2 ILE A  44  ASP A  45 -1  O  ILE A  44   N  GLY A  38           
SHEET    1   C 2 TRP A 112  TYR A 114  0                                        
SHEET    2   C 2 VAL A 123  GLU A 125 -1  O  GLN A 124   N  CYS A 113           
SHEET    1   D 4 GLN H   3  GLN H   6  0                                        
SHEET    2   D 4 CYS H  22  SER H  25 -1  O  SER H  25   N  GLN H   3           
SHEET    3   D 4 THR H  77  ALA H  78 -1  O  ALA H  78   N  CYS H  22           
SHEET    4   D 4 VAL H  71  ASP H  72 -1  N  ASP H  72   O  THR H  77           
SHEET    1   E 6 GLU H  10  VAL H  12  0                                        
SHEET    2   E 6 SER H 108  VAL H 111  1  O  SER H 108   N  GLU H  10           
SHEET    3   E 6 ALA H  88  TYR H  91 -1  N  ALA H  88   O  VAL H 109           
SHEET    4   E 6 MET H  34  SER H  40 -1  N  GLN H  39   O  VAL H  89           
SHEET    5   E 6 SER H  44  ASN H  52 -1  O  GLU H  46   N  LYS H  38           
SHEET    6   E 6 GLY H  56  ALA H  57 -1  O  GLY H  56   N  ASN H  52           
SHEET    1   F 3 VAL H  18  LYS H  19  0                                        
SHEET    2   F 3 GLN H  81  PHE H  82 -1  O  PHE H  82   N  VAL H  18           
SHEET    3   F 3 ALA H  67  THR H  68 -1  N  THR H  68   O  GLN H  81           
SHEET    1   G 4 SER H 120  TYR H 122  0                                        
SHEET    2   G 4 CYS H 140  TYR H 145 -1  O  LEU H 141   N  TYR H 122           
SHEET    3   G 4 LEU H 174  SER H 180 -1  O  TYR H 175   N  TYR H 145           
SHEET    4   G 4 HIS H 164  GLN H 171 -1  N  PHE H 166   O  SER H 178           
SHEET    1   H 2 MET H 135  THR H 137  0                                        
SHEET    2   H 2 THR H 182  PRO H 184 -1  O  VAL H 183   N  VAL H 136           
SHEET    1   I 3 THR H 151  TRP H 154  0                                        
SHEET    2   I 3 THR H 194  HIS H 199 -1  O  ASN H 196   N  THR H 153           
SHEET    3   I 3 THR H 204  LYS H 209 -1  O  LYS H 208   N  CYS H 195           
SHEET    1   J 4 MET L   4  THR L   7  0                                        
SHEET    2   J 4 SER L  22  SER L  25 -1  O  SER L  22   N  THR L   7           
SHEET    3   J 4 ASP L  70  ILE L  75 -1  O  PHE L  71   N  CYS L  23           
SHEET    4   J 4 PHE L  62  SER L  67 -1  N  THR L  63   O  LYS L  74           
SHEET    1   K 5 THR L  10  THR L  14  0                                        
SHEET    2   K 5 THR L 102  LYS L 107  1  O  LYS L 107   N  VAL L  13           
SHEET    3   K 5 GLY L  84  TYR L  87 -1  N  TYR L  86   O  THR L 102           
SHEET    4   K 5 ASN L  34  GLN L  38 -1  N  GLN L  38   O  VAL L  85           
SHEET    5   K 5 LYS L  45  TYR L  49 -1  O  LYS L  45   N  LEU L  37           
SHEET    1   L 2 TRP L  89  GLN L  90  0                                        
SHEET    2   L 2 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1   M 3 ALA L 130  PHE L 139  0                                        
SHEET    2   M 3 TYR L 173  LEU L 181 -1  O  LEU L 181   N  ALA L 130           
SHEET    3   M 3 VAL L 159  TRP L 163 -1  N  LEU L 160   O  THR L 178           
SHEET    1   N 4 SER L 153  ARG L 155  0                                        
SHEET    2   N 4 ASN L 145  ILE L 150 -1  N  ILE L 150   O  SER L 153           
SHEET    3   N 4 TYR L 192  THR L 197 -1  O  GLU L 195   N  LYS L 147           
SHEET    4   N 4 VAL L 206  LYS L 207 -1  O  LYS L 207   N  CYS L 194           
SHEET    1   O 2 CYS U   3  CYS U   6  0                                        
SHEET    2   O 2 CYS U  12  GLU U  15 -1  O  ARG U  13   N  GLN U   5           
SHEET    1   P 7 GLU U  37  THR U  46  0                                        
SHEET    2   P 7 LEU U  23  GLU U  33 -1  N  LEU U  23   O  THR U  46           
SHEET    3   P 7 LYS U  62  SER U  65 -1  O  SER U  65   N  ARG U  30           
SHEET    4   P 7 SER U  56  ARG U  58 -1  N  TYR U  57   O  THR U  64           
SHEET    5   P 7 LEU U 144  GLY U 148 -1  O  CYS U 147   N  SER U  56           
SHEET    6   P 7 ILE U  96  GLY U  99 -1  N  CYS U  98   O  ARG U 145           
SHEET    7   P 7 GLN U 111  SER U 112 -1  O  GLN U 111   N  SER U  97           
SHEET    1   Q 6 GLU U  68  CYS U  71  0                                        
SHEET    2   Q 6 LEU U  23  GLU U  33 -1  N  THR U  26   O  VAL U  69           
SHEET    3   Q 6 LYS U  62  SER U  65 -1  O  SER U  65   N  ARG U  30           
SHEET    4   Q 6 SER U  56  ARG U  58 -1  N  TYR U  57   O  THR U  64           
SHEET    5   Q 6 LEU U 144  GLY U 148 -1  O  CYS U 147   N  SER U  56           
SHEET    6   Q 6 GLN U 121  LEU U 123 -1  N  GLN U 121   O  GLY U 148           
SHEET    1   R 6 VAL U 126  HIS U 128  0                                        
SHEET    2   R 6 THR U 164  LEU U 168 -1  O  PHE U 165   N  HIS U 128           
SHEET    3   R 6 ASN U 157  ASN U 161 -1  N  ASN U 157   O  LEU U 168           
SHEET    4   R 6 MET U 237  ALA U 242 -1  O  CYS U 241   N  HIS U 160           
SHEET    5   R 6 GLN U 189  GLY U 199 -1  N  CYS U 197   O  ARG U 239           
SHEET    6   R 6 PHE U 211  ARG U 216 -1  O  CYS U 215   N  ARG U 192           
SHEET    1   S 6 VAL U 126  HIS U 128  0                                        
SHEET    2   S 6 THR U 164  LEU U 168 -1  O  PHE U 165   N  HIS U 128           
SHEET    3   S 6 ASN U 157  ASN U 161 -1  N  ASN U 157   O  LEU U 168           
SHEET    4   S 6 MET U 237  ALA U 242 -1  O  CYS U 241   N  HIS U 160           
SHEET    5   S 6 GLN U 221  THR U 228 -1  N  GLN U 221   O  ALA U 242           
SHEET    6   S 6 ASN U 259  CYS U 266 -1  O  ASN U 259   N  THR U 228           
SSBOND   1 CYS A   11    CYS A   19                          1555   1555  2.05  
SSBOND   2 CYS A   13    CYS A   31                          1555   1555  2.03  
SSBOND   3 CYS A   33    CYS A   42                          1555   1555  2.03  
SSBOND   4 CYS A   50    CYS A  131                          1555   1555  2.03  
SSBOND   5 CYS A   71    CYS A  113                          1555   1555  2.05  
SSBOND   6 CYS A  102    CYS A  126                          1555   1555  2.03  
SSBOND   7 CYS B    5    CYS B   21                          1555   1555  2.04  
SSBOND   8 CYS B    9    CYS B   39                          1555   1555  2.03  
SSBOND   9 CYS B   19    CYS B   32                          1555   1555  2.04  
SSBOND  10 CYS B   25    CYS B   31                          1555   1555  2.02  
SSBOND  11 CYS H   22    CYS H   92                          1555   1555  2.04  
SSBOND  12 CYS H  140    CYS H  195                          1555   1555  2.04  
SSBOND  13 CYS L   23    CYS L   88                          1555   1555  2.03  
SSBOND  14 CYS L  134    CYS L  194                          1555   1555  2.04  
SSBOND  15 CYS U    3    CYS U   17                          1555   1555  2.03  
SSBOND  16 CYS U    6    CYS U   12                          1555   1555  2.04  
SSBOND  17 CYS U   17    CYS U   45                          1555   1555  2.03  
SSBOND  18 CYS U   71    CYS U   76                          1555   1555  2.03  
SSBOND  19 CYS U   95    CYS U  122                          1555   1555  2.02  
SSBOND  20 CYS U   98    CYS U  105                          1555   1555  2.03  
SSBOND  21 CYS U  115    CYS U  147                          1555   1555  2.04  
SSBOND  22 CYS U  153    CYS U  170                          1555   1555  2.04  
SSBOND  23 CYS U  171    CYS U  176                          1555   1555  2.04  
SSBOND  24 CYS U  194    CYS U  222                          1555   1555  2.02  
SSBOND  25 CYS U  197    CYS U  205                          1555   1555  2.04  
SSBOND  26 CYS U  215    CYS U  241                          1555   1555  2.05  
SSBOND  27 CYS U  247    CYS U  265                          1555   1555  2.03  
SSBOND  28 CYS U  266    CYS U  271                          1555   1555  2.03  
LINK         ND2 ASN U 172                 C1  NAG U 304     1555   1555  1.36  
LINK         ND2 ASN U 200                 C1  NAG D   1     1555   1555  1.52  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.28  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.53  
CISPEP   1 SER H   95    ILE H   96          0       -16.93                     
CISPEP   2 ILE H   96    TYR H   97          0        -5.43                     
CISPEP   3 PHE H  146    PRO H  147          0        -1.11                     
CISPEP   4 GLU H  148    PRO H  149          0         2.87                     
CISPEP   5 TRP H  188    PRO H  189          0        -6.57                     
CISPEP   6 THR L    7    PRO L    8          0        -1.01                     
CISPEP   7 PHE L   94    PRO L   95          0         0.15                     
CISPEP   8 TYR L  140    PRO L  141          0         0.21                     
CRYST1  164.659  164.659  391.582  90.00  90.00 120.00 H 3 2        18          
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      0.006073  0.003506  0.000000        0.00000                         
SCALE2      0.000000  0.007013  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002554        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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