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Database: PDB
Entry: 2FD6
LinkDB: 2FD6
Original site: 2FD6 
HEADER    IMMUNE SYSTEM, HYDROLASE                13-DEC-05   2FD6              
TITLE     STRUCTURE OF HUMAN UROKINASE PLASMINOGEN ACTIVATOR IN COMPLEX WITH    
TITLE    2 UROKINASE RECEPTOR AND AN ANTI-UPAR ANTIBODY AT 1.9 A                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: AMINO TERMINAL RESIDUES 31-152;                            
COMPND   5 EC: 3.4.21.73;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: L CHAIN OF FAB OF ATN-615 ANTI-UPAR ANTIBODY;              
COMPND   9 CHAIN: L;                                                            
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: H CHAIN OF FAB OF ATN-615 ANTI-UPAR ANTIBODY;              
COMPND  12 CHAIN: H;                                                            
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: UROKINASE PLASMINOGEN ACTIVATOR SURFACE RECEPTOR;          
COMPND  15 CHAIN: U;                                                            
COMPND  16 FRAGMENT: RESIDUES 23-297;                                           
COMPND  17 SYNONYM: UPAR, U-PAR, MONOCYTE ACTIVATION ANTIGEN MO3, CD87 ANTIGEN; 
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7215;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: S2 CELLS;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PMT-BIP-V5-HIS;                            
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 SECRETION: ASCITE LIQUID;                                            
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  17 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  18 ORGANISM_TAXID: 10090;                                               
SOURCE  19 SECRETION: ASCITE LIQUID;                                            
SOURCE  20 MOL_ID: 4;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  22 ORGANISM_COMMON: HUMAN;                                              
SOURCE  23 ORGANISM_TAXID: 9606;                                                
SOURCE  24 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE  25 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;                               
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 7215;                                       
SOURCE  27 EXPRESSION_SYSTEM_CELL_LINE: S2 CELLS;                               
SOURCE  28 EXPRESSION_SYSTEM_VECTOR: PMT-BIP-V5-HIS                             
KEYWDS    UPAR, ATF, ATN-615 ANTIBODY, FAB, TERNARY COMPLEX, IMMUNE SYSTEM,     
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.HUANG,Q.HUAI,Y.LI                                                   
REVDAT   4   18-JUL-12 2FD6    1       LINK                                     
REVDAT   3   13-JUL-11 2FD6    1       VERSN                                    
REVDAT   2   24-FEB-09 2FD6    1       VERSN                                    
REVDAT   1   21-FEB-06 2FD6    0                                                
JRNL        AUTH   Q.HUAI,A.P.MAZAR,A.KUO,G.C.PARRY,D.E.SHAW,J.CALLAHAN,Y.LI,   
JRNL        AUTH 2 C.YUAN,C.BIAN,L.CHEN,B.FURIE,B.C.FURIE,D.B.CINES,M.HUANG     
JRNL        TITL   STRUCTURE OF HUMAN UROKINASE PLASMINOGEN ACTIVATOR IN        
JRNL        TITL 2 COMPLEX WITH ITS RECEPTOR                                    
JRNL        REF    SCIENCE                       V. 311   656 2006              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   16456079                                                     
JRNL        DOI    10.1126/SCIENCE.1121143                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.36                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1755432.420                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 83101                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4228                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10624                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4030                       
REMARK   3   BIN FREE R VALUE                    : 0.4100                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 559                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6139                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 125                                     
REMARK   3   SOLVENT ATOMS            : 336                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.31000                                             
REMARK   3    B22 (A**2) : 4.95000                                              
REMARK   3    B33 (A**2) : -4.64000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -3.70000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.36                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.43                                                 
REMARK   3   BSOL        : 300.00                                               
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : TEMP.DUMMY                                     
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2FD6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-DEC-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB035735.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-APR-05; NULL; NULL; NULL        
REMARK 200  TEMPERATURE           (KELVIN) : 90; NULL; NULL; NULL               
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y; Y                         
REMARK 200  RADIATION SOURCE               : APS; NSLS; NSLS; APS               
REMARK 200  BEAMLINE                       : 22-ID; X25; X12C; 17-ID            
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL; NULL             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL; NULL; NULL                
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00; 1.00; 1.0; NULL              
REMARK 200  MONOCHROMATOR                  : NULL; NULL; NULL; NULL             
REMARK 200  OPTICS                         : NULL; NULL; NULL; NULL             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD; CCD; NULL                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH; NULL; NULL; NULL      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 86852                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.360                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.970                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL; NULL; NULL            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2FAT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG4000, 5% ETHYLENE GLYCOL, 5%       
REMARK 280  METHANOL, 0.05% SODIUM AZIDE, 50 MM CACODYLATE, PH 6.5,             
REMARK 280  MICRODIALYSIS, TEMPERATURE 298K                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       43.40250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, H, U                            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, U                                  
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 APPLY THE FOLLOWING TO CHAINS: L, H                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       51.79200            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -43.40250            
REMARK 350   BIOMT3   2  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     GLY H   127                                                      
REMARK 465     GLU U    34                                                      
REMARK 465     GLY U    35                                                      
REMARK 465     GLU U    36                                                      
REMARK 465     SER U    81                                                      
REMARK 465     GLY U    82                                                      
REMARK 465     ARG U    83                                                      
REMARK 465     ALA U    84                                                      
REMARK 465     VAL U    85                                                      
REMARK 465     THR U    86                                                      
REMARK 465     TYR U    87                                                      
REMARK 465     SER U    88                                                      
REMARK 465     ARG U    89                                                      
REMARK 465     SER U    90                                                      
REMARK 465     ARG U    91                                                      
REMARK 465     ILE U   130                                                      
REMARK 465     GLN U   131                                                      
REMARK 465     GLU U   132                                                      
REMARK 465     GLY U   133                                                      
REMARK 465     GLU U   134                                                      
REMARK 465     GLU U   135                                                      
REMARK 465     GLY U   136                                                      
REMARK 465     ARG U   137                                                      
REMARK 465     PRO U   138                                                      
REMARK 465     LYS U   139                                                      
REMARK 465     HIS U   249                                                      
REMARK 465     ALA U   250                                                      
REMARK 465     HIS U   251                                                      
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   O6   NAG U   452     O1   FUC U   453              0.65            
REMARK 500   ND2  ASN U   172     O1   NAG U   472              0.79            
REMARK 500   C6   NAG U   452     O1   FUC U   453              0.82            
REMARK 500   CG   ASN U   172     O1   NAG U   472              1.26            
REMARK 500   O6   NAG U   452     O5   FUC U   453              1.73            
REMARK 500   OD1  ASN U   172     O1   NAG U   472              1.78            
REMARK 500   NE2  HIS U   143     O    HOH U   545              1.87            
REMARK 500   O    ASN H   128     OG   SER H   180              1.95            
REMARK 500   NE2  HIS U   128     O    HOH U   545              1.96            
REMARK 500   NE2  HIS A    41     O    HOH A   523              1.97            
REMARK 500   ND2  ASN U    52     O1   NAG U   452              2.00            
REMARK 500   O4   NAG U   472     O5   NAG U   473              2.00            
REMARK 500   ND2  ASN U   172     O7   NAG U   472              2.01            
REMARK 500   C5   NAG U   452     O1   FUC U   453              2.03            
REMARK 500   NE2  HIS A    29     O    HOH A   523              2.06            
REMARK 500   C6   NAG U   452     C1   FUC U   453              2.15            
REMARK 500   OE1  GLU U   183     O    HOH U   545              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLY H 134   C     CYS H 135   N      -0.197                       
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    PRO L  94   C   -  N   -  CA  ANGL. DEV. = -14.0 DEGREES          
REMARK 500    GLY H 134   C   -  N   -  CA  ANGL. DEV. = -15.2 DEGREES          
REMARK 500    CYS H 135   CA  -  CB  -  SG  ANGL. DEV. =   7.8 DEGREES          
REMARK 500    GLY H 134   CA  -  C   -  N   ANGL. DEV. = -17.2 DEGREES          
REMARK 500    GLY H 134   O   -  C   -  N   ANGL. DEV. =  10.4 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    ASN A  15     -126.71     61.77                                   
REMARK 500    PHE A  25       60.58   -117.39                                   
REMARK 500    SER A  26       13.72     54.31                                   
REMARK 500    GLU A  52     -136.01    -64.77                                   
REMARK 500    ALA A  62       50.69    167.26                                   
REMARK 500    MET A  67       54.73   -112.16                                   
REMARK 500    TRP A  74       -5.84    -55.11                                   
REMARK 500    ASN A 107       90.79    -67.85                                   
REMARK 500    ARG A 109        7.83    -46.69                                   
REMARK 500    TRP A 112     -158.14   -136.17                                   
REMARK 500    CYS A 113      162.49    179.27                                   
REMARK 500    VAL A 128      127.72    -39.02                                   
REMARK 500    CYS A 131       22.67    -73.97                                   
REMARK 500    ILE L  51      -46.87     64.82                                   
REMARK 500    ALA L  84     -171.97    179.56                                   
REMARK 500    TYR L  93      -57.80     -4.40                                   
REMARK 500    PRO L 140     -178.62    -68.79                                   
REMARK 500    ALA L 213      122.98    174.58                                   
REMARK 500    LYS L 214     -172.60     52.94                                   
REMARK 500    HIS H  52A     -56.20     69.58                                   
REMARK 500    THR H  83     -169.20   -119.02                                   
REMARK 500    ALA H  88     -177.81   -172.78                                   
REMARK 500    LEU H 133      139.31   -178.55                                   
REMARK 500    CYS H 135      127.46    175.61                                   
REMARK 500    SER U  44      178.36    172.65                                   
REMARK 500    LEU U  75       18.70     50.84                                   
REMARK 500    PRO U 118       -4.02    -59.54                                   
REMARK 500    CYS U 153      -70.08    -65.01                                   
REMARK 500    PRO U 154       94.18    -38.07                                   
REMARK 500    ASN U 162      -15.47    -44.38                                   
REMARK 500    ASP U 163       21.16   -157.21                                   
REMARK 500    THR U 174      124.58    -37.28                                   
REMARK 500    CYS U 197      171.47    178.12                                   
REMARK 500    HIS U 229     -155.58   -128.41                                   
REMARK 500    GLU U 230     -162.38     48.71                                   
REMARK 500    LYS U 232     -158.29    -79.30                                   
REMARK 500    ASN U 233       41.51    -85.49                                   
REMARK 500    CYS U 247       38.97    -97.83                                   
REMARK 500    ASN U 259      -97.95   -111.72                                   
REMARK 500    THR U 267       57.10   -116.36                                   
REMARK 500    PRO U 274       66.38    -62.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TYR L  93        22.8      L          L   OUTSIDE RANGE           
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 SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETX L 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETX L 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETX H 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE H 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG U 452                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC U 453                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG U 472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG U 473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG U 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 U 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FAT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ATN-615                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE AMINOACID SEQUENCE DATABASE REFERENCE IS CURRENTLY NOT           
REMARK 999 AVAILABLE FOR FAB ATN-615 ANTI-UPAR ANTIBODY, LIGHT AND              
REMARK 999 HEAVY CHAINS                                                         
DBREF  2FD6 A   11   132  UNP    P00749   UROK_HUMAN      31    152             
DBREF  2FD6 L   26   212  UNP    Q52L64   Q52L64_MOUSE    46    239             
DBREF  2FD6 H    2   192  UNP    Q4V9V8   Q4V9V8_MOUSE    21    223             
DBREF  2FD6 U    2   275  UNP    Q03405   UPAR_HUMAN      23    297             
SEQADV 2FD6 SER U    1A UNP  Q03405              CLONING ARTIFACT               
SEQRES   1 A  122  CYS ASP CYS LEU ASN GLY GLY THR CYS VAL SER ASN LYS          
SEQRES   2 A  122  TYR PHE SER ASN ILE HIS TRP CYS ASN CYS PRO LYS LYS          
SEQRES   3 A  122  PHE GLY GLY GLN HIS CYS GLU ILE ASP LYS SER LYS THR          
SEQRES   4 A  122  CYS TYR GLU GLY ASN GLY HIS PHE TYR ARG GLY LYS ALA          
SEQRES   5 A  122  SER THR ASP THR MET GLY ARG PRO CYS LEU PRO TRP ASN          
SEQRES   6 A  122  SER ALA THR VAL LEU GLN GLN THR TYR HIS ALA HIS ARG          
SEQRES   7 A  122  SER ASP ALA LEU GLN LEU GLY LEU GLY LYS HIS ASN TYR          
SEQRES   8 A  122  CYS ARG ASN PRO ASP ASN ARG ARG ARG PRO TRP CYS TYR          
SEQRES   9 A  122  VAL GLN VAL GLY LEU LYS PRO LEU VAL GLN GLU CYS MET          
SEQRES  10 A  122  VAL HIS ASP CYS ALA                                          
SEQRES   1 L  214  ASP ILE VAL LEU THR GLN SER PRO ASP ILE THR ALA ALA          
SEQRES   2 L  214  SER LEU GLY GLN LYS VAL THR ILE THR CYS SER ALA SER          
SEQRES   3 L  214  SER SER VAL SER TYR MET HIS TRP TYR GLN GLN LYS SER          
SEQRES   4 L  214  GLY THR SER PRO LYS PRO TRP ILE PHE GLU ILE SER LYS          
SEQRES   5 L  214  LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY          
SEQRES   6 L  214  SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU          
SEQRES   7 L  214  ALA GLU ASP ALA ALA ILE TYR TYR CYS GLN GLN TRP ASN          
SEQRES   8 L  214  TYR PRO PHE THR PHE GLY GLY GLY THR LYS LEU GLU ILE          
SEQRES   9 L  214  LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE PRO          
SEQRES  10 L  214  PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER VAL          
SEQRES  11 L  214  VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE ASN          
SEQRES  12 L  214  VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN GLY          
SEQRES  13 L  214  VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SER          
SEQRES  14 L  214  THR TYR SER MET SER SER THR LEU THR LEU THR LYS ASP          
SEQRES  15 L  214  GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA THR          
SEQRES  16 L  214  HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE ASN          
SEQRES  17 L  214  ARG ASN GLU ALA LYS ALA                                      
SEQRES   1 H  213  GLY VAL LYS LEU GLN GLN SER GLY PRO GLU VAL VAL LYS          
SEQRES   2 H  213  PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY          
SEQRES   3 H  213  TYR SER PHE THR ASN PHE TYR ILE HIS TRP VAL LYS GLN          
SEQRES   4 H  213  ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP ILE PHE          
SEQRES   5 H  213  HIS GLY SER ASP ASN THR GLU TYR ASN GLU LYS PHE LYS          
SEQRES   6 H  213  ASP LYS ALA THR LEU THR ALA ASP THR SER SER SER THR          
SEQRES   7 H  213  ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER          
SEQRES   8 H  213  ALA VAL TYR PHE CYS ALA ARG TRP GLY PRO HIS TRP TYR          
SEQRES   9 H  213  PHE ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER          
SEQRES  10 H  213  SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA          
SEQRES  11 H  213  PRO GLY ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS          
SEQRES  12 H  213  GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER          
SEQRES  13 H  213  GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL          
SEQRES  14 H  213  LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR          
SEQRES  15 H  213  VAL PRO SER SER THR TRP PRO SER GLU THR VAL THR CYS          
SEQRES  16 H  213  ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS          
SEQRES  17 H  213  LYS ILE ALA ALA ALA                                          
SEQRES   1 U  276  SER LEU ARG CYS MET GLN CYS LYS THR ASN GLY ASP CYS          
SEQRES   2 U  276  ARG VAL GLU GLU CYS ALA LEU GLY GLN ASP LEU CYS ARG          
SEQRES   3 U  276  THR THR ILE VAL ARG LEU TRP GLU GLU GLY GLU GLU LEU          
SEQRES   4 U  276  GLU LEU VAL GLU LYS SER CYS THR HIS SER GLU LYS THR          
SEQRES   5 U  276  ASN ARG THR LEU SER TYR ARG THR GLY LEU LYS ILE THR          
SEQRES   6 U  276  SER LEU THR GLU VAL VAL CYS GLY LEU ASP LEU CYS ASN          
SEQRES   7 U  276  GLN GLY ASN SER GLY ARG ALA VAL THR TYR SER ARG SER          
SEQRES   8 U  276  ARG TYR LEU GLU CYS ILE SER CYS GLY SER SER ASP MET          
SEQRES   9 U  276  SER CYS GLU ARG GLY ARG HIS GLN SER LEU GLN CYS ARG          
SEQRES  10 U  276  SER PRO GLU GLU GLN CYS LEU ASP VAL VAL THR HIS TRP          
SEQRES  11 U  276  ILE GLN GLU GLY GLU GLU GLY ARG PRO LYS ASP ASP ARG          
SEQRES  12 U  276  HIS LEU ARG GLY CYS GLY TYR LEU PRO GLY CYS PRO GLY          
SEQRES  13 U  276  SER ASN GLY PHE HIS ASN ASN ASP THR PHE HIS PHE LEU          
SEQRES  14 U  276  LYS CYS CYS ASN THR THR LYS CYS ASN GLU GLY PRO ILE          
SEQRES  15 U  276  LEU GLU LEU GLU ASN LEU PRO GLN ASN GLY ARG GLN CYS          
SEQRES  16 U  276  TYR SER CYS LYS GLY ASN SER THR HIS GLY CYS SER SER          
SEQRES  17 U  276  GLU GLU THR PHE LEU ILE ASP CYS ARG GLY PRO MET ASN          
SEQRES  18 U  276  GLN CYS LEU VAL ALA THR GLY THR HIS GLU PRO LYS ASN          
SEQRES  19 U  276  GLN SER TYR MET VAL ARG GLY CYS ALA THR ALA SER MET          
SEQRES  20 U  276  CYS GLN HIS ALA HIS LEU GLY ASP ALA PHE SER MET ASN          
SEQRES  21 U  276  HIS ILE ASP VAL SER CYS CYS THR LYS SER GLY CYS ASN          
SEQRES  22 U  276  HIS PRO ASP                                                  
MODRES 2FD6 ASN U   52  ASN  GLYCOSYLATION SITE                                 
MODRES 2FD6 ASN U  172  ASN  GLYCOSYLATION SITE                                 
HET    SO4  A 501       5                                                       
HET    ETX  L 401       6                                                       
HET    EDO  L 405       4                                                       
HET    ETX  L 407       6                                                       
HET    ETX  H 403       6                                                       
HET    EDO  H 404       4                                                       
HET    PGE  H 406      10                                                       
HET    NAG  U 452      15                                                       
HET    FUC  U 453      11                                                       
HET    NAG  U 472      15                                                       
HET    NAG  U 473      15                                                       
HET    NDG  U 400      15                                                       
HET    PG4  U 402      13                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ETX 2-ETHOXYETHANOL                                                  
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  ETX    3(C4 H10 O2)                                                 
FORMUL   7  EDO    2(C2 H6 O2)                                                  
FORMUL  11  PGE    C6 H14 O4                                                    
FORMUL  12  NAG    3(C8 H15 N O6)                                               
FORMUL  12  FUC    C6 H12 O5                                                    
FORMUL  15  NDG    C8 H15 N O6                                                  
FORMUL  16  PG4    C8 H18 O5                                                    
FORMUL  17  HOH   *336(H2 O)                                                    
HELIX    1   1 THR A   78  GLN A   82  5                                   5    
HELIX    2   2 ASP A   90  GLY A   95  1                                   6    
HELIX    3   3 GLU L   79  ALA L   83  5                                   5    
HELIX    4   4 SER L  120  SER L  126  1                                   7    
HELIX    5   5 LYS L  182  ARG L  187  1                                   6    
HELIX    6   6 SER H   28  ASN H   31  5                                   4    
HELIX    7   7 GLU H   61  LYS H   64  5                                   4    
HELIX    8   8 THR H   73  SER H   75  5                                   3    
HELIX    9   9 THR H   83  SER H   87  5                                   5    
HELIX   10  10 SER H  151  SER H  153  5                                   3    
HELIX   11  11 PRO H  195  SER H  198  5                                   4    
HELIX   12  12 GLU U  183  LEU U  187  5                                   5    
HELIX   13  13 ALA U  244  CYS U  247  5                                   4    
HELIX   14  14 LEU U  252  SER U  257  5                                   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  VAL A 117  0                                        
SHEET    2   C 2 LYS A 120  GLU A 125 -1  O  LEU A 122   N  VAL A 115           
SHEET    1   D 4 LEU L   4  SER L   7  0                                        
SHEET    2   D 4 VAL L  19  ALA L  25 -1  O  SER L  24   N  THR L   5           
SHEET    3   D 4 SER L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4   D 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1   E 6 ILE L  10  ALA L  13  0                                        
SHEET    2   E 6 THR L 102  ILE L 106  1  O  GLU L 105   N  THR L  11           
SHEET    3   E 6 ALA L  84  GLN L  90 -1  N  ALA L  84   O  LEU L 104           
SHEET    4   E 6 MET L  33  GLN L  38 -1  N  GLN L  38   O  ILE L  85           
SHEET    5   E 6 LYS L  45  PHE L  49 -1  O  ILE L  48   N  TRP L  35           
SHEET    6   E 6 LYS L  53  LEU L  54 -1  O  LYS L  53   N  PHE L  49           
SHEET    1   F 4 THR L 113  PHE L 117  0                                        
SHEET    2   F 4 GLY L 128  PHE L 138 -1  O  VAL L 132   N  PHE L 117           
SHEET    3   F 4 TYR L 172  THR L 181 -1  O  LEU L 178   N  VAL L 131           
SHEET    4   F 4 VAL L 158  TRP L 162 -1  N  LEU L 159   O  THR L 177           
SHEET    1   G 4 SER L 152  ARG L 154  0                                        
SHEET    2   G 4 ASN L 144  ILE L 149 -1  N  ILE L 149   O  SER L 152           
SHEET    3   G 4 SER L 190  THR L 196 -1  O  THR L 196   N  ASN L 144           
SHEET    4   G 4 ILE L 204  ASN L 209 -1  O  LYS L 206   N  CYS L 193           
SHEET    1   H 4 LYS H   3  GLN H   6  0                                        
SHEET    2   H 4 VAL H  18  SER H  25 -1  O  LYS H  23   N  GLN H   5           
SHEET    3   H 4 THR H  77  LEU H  82 -1  O  LEU H  82   N  VAL H  18           
SHEET    4   H 4 ALA H  67  ASP H  72 -1  N  ASP H  72   O  THR H  77           
SHEET    1   I 6 GLU H  10  VAL H  12  0                                        
SHEET    2   I 6 THR H 107  VAL H 111  1  O  THR H 110   N  GLU H  10           
SHEET    3   I 6 ALA H  88  TRP H  95 -1  N  ALA H  88   O  VAL H 109           
SHEET    4   I 6 TYR H  33  GLN H  39 -1  N  HIS H  35   O  ALA H  93           
SHEET    5   I 6 GLU H  46  PHE H  52 -1  O  ILE H  48   N  TRP H  36           
SHEET    6   I 6 THR H  57  TYR H  59 -1  O  GLU H  58   N  TRP H  50           
SHEET    1   J 4 GLU H  10  VAL H  12  0                                        
SHEET    2   J 4 THR H 107  VAL H 111  1  O  THR H 110   N  GLU H  10           
SHEET    3   J 4 ALA H  88  TRP H  95 -1  N  ALA H  88   O  VAL H 109           
SHEET    4   J 4 PHE H 100A TRP H 103 -1  O  VAL H 102   N  ARG H  94           
SHEET    1   K 4 SER H 120  PRO H 123  0                                        
SHEET    2   K 4 CYS H 135  TYR H 140 -1  O  LEU H 136   N  TYR H 122           
SHEET    3   K 4 LEU H 169  VAL H 176 -1  O  LEU H 172   N  VAL H 137           
SHEET    4   K 4 VAL H 158  THR H 160 -1  N  HIS H 159   O  SER H 175           
SHEET    1   L 4 SER H 120  PRO H 123  0                                        
SHEET    2   L 4 CYS H 135  TYR H 140 -1  O  LEU H 136   N  TYR H 122           
SHEET    3   L 4 LEU H 169  VAL H 176 -1  O  LEU H 172   N  VAL H 137           
SHEET    4   L 4 VAL H 164  GLN H 166 -1  N  GLN H 166   O  LEU H 169           
SHEET    1   M 3 THR H 146  TRP H 149  0                                        
SHEET    2   M 3 THR H 189  HIS H 194 -1  O  ASN H 191   N  THR H 148           
SHEET    3   M 3 THR H 199  LYS H 204 -1  O  VAL H 201   N  VAL H 192           
SHEET    1   N 2 ARG U   2  CYS U   6  0                                        
SHEET    2   N 2 CYS U  12  GLU U  16 -1  O  ARG U  13   N  GLN U   5           
SHEET    1   O11 LEU U  38  THR U  46  0                                        
SHEET    2   O11 LEU U  23  TRP U  32 -1  N  LEU U  23   O  THR U  46           
SHEET    3   O11 LYS U  62  CYS U  71 -1  O  CYS U  71   N  CYS U  24           
SHEET    4   O11 ARG U  53  THR U  59 -1  N  LEU U  55   O  LEU U  66           
SHEET    5   O11 HIS U 143  TYR U 149 -1  O  CYS U 147   N  SER U  56           
SHEET    6   O11 GLN U 121  HIS U 128 -1  N  GLN U 121   O  GLY U 148           
SHEET    7   O11 THR U 164  CYS U 171 -1  O  PHE U 167   N  VAL U 126           
SHEET    8   O11 GLY U 155  ASN U 161 -1  N  GLY U 155   O  CYS U 170           
SHEET    9   O11 GLN U 234  ALA U 242 -1  O  CYS U 241   N  HIS U 160           
SHEET   10   O11 GLN U 189  GLY U 199 -1  N  GLY U 199   O  MET U 237           
SHEET   11   O11 PHE U 211  ARG U 216 -1  O  CYS U 215   N  ARG U 192           
SHEET    1   P 9 GLN U 111  GLN U 114  0                                        
SHEET    2   P 9 GLU U  94  GLY U  99 -1  N  SER U  97   O  GLN U 111           
SHEET    3   P 9 HIS U 143  TYR U 149 -1  O  ARG U 145   N  CYS U  98           
SHEET    4   P 9 GLN U 121  HIS U 128 -1  N  GLN U 121   O  GLY U 148           
SHEET    5   P 9 THR U 164  CYS U 171 -1  O  PHE U 167   N  VAL U 126           
SHEET    6   P 9 GLY U 155  ASN U 161 -1  N  GLY U 155   O  CYS U 170           
SHEET    7   P 9 GLN U 234  ALA U 242 -1  O  CYS U 241   N  HIS U 160           
SHEET    8   P 9 GLN U 221  HIS U 229 -1  N  ALA U 225   O  VAL U 238           
SHEET    9   P 9 ASP U 262  CYS U 266 -1  O  CYS U 266   N  CYS U 222           
SSBOND   1 CYS A   13    CYS A   31                          1555   1555  2.03  
SSBOND   2 CYS A   33    CYS A   42                          1555   1555  2.03  
SSBOND   3 CYS A   50    CYS A  131                          1555   1555  2.03  
SSBOND   4 CYS A   71    CYS A  113                          1555   1555  2.04  
SSBOND   5 CYS A  102    CYS A  126                          1555   1555  2.03  
SSBOND   6 CYS L   23    CYS L   88                          1555   1555  2.04  
SSBOND   7 CYS L  133    CYS L  193                          1555   1555  2.03  
SSBOND   8 CYS H   22    CYS H   92                          1555   1555  2.04  
SSBOND   9 CYS H  135    CYS H  190                          1555   1555  2.04  
SSBOND  10 CYS U    3    CYS U   24                          1555   1555  2.03  
SSBOND  11 CYS U    6    CYS U   12                          1555   1555  2.05  
SSBOND  12 CYS U   17    CYS U   45                          1555   1555  2.03  
SSBOND  13 CYS U   71    CYS U   76                          1555   1555  2.04  
SSBOND  14 CYS U   95    CYS U  122                          1555   1555  2.03  
SSBOND  15 CYS U   98    CYS U  105                          1555   1555  2.04  
SSBOND  16 CYS U  115    CYS U  147                          1555   1555  2.04  
SSBOND  17 CYS U  153    CYS U  170                          1555   1555  2.04  
SSBOND  18 CYS U  171    CYS U  176                          1555   1555  2.04  
SSBOND  19 CYS U  194    CYS U  222                          1555   1555  2.03  
SSBOND  20 CYS U  197    CYS U  205                          1555   1555  2.05  
SSBOND  21 CYS U  215    CYS U  241                          1555   1555  2.03  
SSBOND  22 CYS U  247    CYS U  265                          1555   1555  2.03  
SSBOND  23 CYS U  266    CYS U  271                          1555   1555  2.03  
LINK         ND2 ASN U  52                 C1  NAG U 452     1555   1555  1.68  
LINK         O4  NAG U 472                 C1  NAG U 473     1555   1555  1.55  
LINK         ND2 ASN U 172                 C1  NAG U 472     1555   1555  1.99  
LINK         O6  NAG U 452                 C1  FUC U 453     1555   1555  1.14  
CISPEP   1 SER L    7    PRO L    8          0         0.04                     
CISPEP   2 TYR L  139    PRO L  140          0         0.00                     
CISPEP   3 PHE H  141    PRO H  142          0        -0.04                     
CISPEP   4 GLU H  143    PRO H  144          0        -0.41                     
CISPEP   5 TRP H  183    PRO H  184          0        -0.23                     
SITE     1 AC1  6 ASP A  12  HIS A  29  HIS A  41  HOH A 511                    
SITE     2 AC1  6 HOH A 523  HOH U 501                                          
SITE     1 AC2  6 ASP L   1  ILE L   2  GLN L  90  ASN L  92                    
SITE     2 AC2  6 PRO L  94  HOH L 444                                          
SITE     1 AC3  2 PRO L  46  SER L  56                                          
SITE     1 AC4  4 TYR L  93  HOH L 489  GLY U 191  GLN U 193                    
SITE     1 AC5  5 LYS H  23  SER H  75  THR H  77  HOH H 410                    
SITE     2 AC5  5 HOH H 427                                                     
SITE     1 AC6  3 LYS H  19  THR H  70  ALA H  71                               
SITE     1 AC7  8 ASN H  31  PHE H  32  TYR H  33  TRP H  95                    
SITE     2 AC7  8 TRP H  99  LEU U 187  PRO U 218  PG4 U 402                    
SITE     1 AC8  4 ASN U  52  VAL U  70  FUC U 453  HOH U 530                    
SITE     1 AC9  1 NAG U 452                                                     
SITE     1 BC1  2 ASN U 172  NAG U 473                                          
SITE     1 BC2  1 NAG U 472                                                     
SITE     1 BC3  3 ASN U 200  THR U 202  HIS U 203                               
SITE     1 BC4 12 ASN H  31  PHE H  52  HIS H  52A ASN H  56                    
SITE     2 BC4 12 PGE H 406  PRO U 218  ASN U 220  GLN U 221                    
SITE     3 BC4 12 THR U 243  ALA U 244  HOH U 475  HOH U 486                    
CRYST1   51.792   86.805  124.690  90.00  94.54  90.00 P 1 21 1      2          
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      0.019308  0.000000  0.001533        0.00000                         
SCALE2      0.000000  0.011520  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008045        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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