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Database: PDB
Entry: 4DW2
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Original site: 4DW2 
HEADER    HYDROLASE/IMMUNE SYSTEM                 24-FEB-12   4DW2              
TITLE     THE CRYSTAL STRUCTURE OF UPA IN COMPLEX WITH THE FAB FRAGMENT OF MAB- 
TITLE    2 112                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND   3 CHAIN: U;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 179-424;                    
COMPND   5 SYNONYM: UROKINASE-TYPE PLASMINOGEN ACTIVATOR CHAIN B;               
COMPND   6 EC: 3.4.21.73;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: FAB FRAGMENT OF PRO-UPA ANTIBODY MAB-112;                  
COMPND  11 CHAIN: H;                                                            
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: FAB FRAGMENT OF PRO-UPA ANTIBODY MAB-112;                  
COMPND  14 CHAIN: L                                                             
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: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: X33;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPICZAA;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 MOL_ID: 3;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  16 ORGANISM_TAXID: 10090                                                
KEYWDS    UROKINASE-TYPE PLASMINOGEN ACTIVATOR, ANTIBODY, SERINE PROTEASE,      
KEYWDS   2 ZYMOGEN, HYDROLASE-IMMUNE SYSTEM COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.JIANG,K.A.BOTKJAER,L.M.ANDERSEN,C.YUAN,P.A.ANDREASEN,M.HUANG        
REVDAT   1   16-JAN-13 4DW2    0                                                
JRNL        AUTH   L.JIANG,K.A.BOTKJAER,L.M.ANDERSEN,C.YUAN,P.A.ANDREASEN,      
JRNL        AUTH 2 M.HUANG                                                      
JRNL        TITL   REZYMOGENATION OF ACTIVE UROKINASE INDUCED BY AN INHIBITORY  
JRNL        TITL 2 ANTIBODY.                                                    
JRNL        REF    BIOCHEM.J.                    V. 449   161 2013              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   23016918                                                     
JRNL        DOI    10.1042/BJ20121132                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 80.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 10825                          
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 + TEST SET) : 0.243                           
REMARK   3   R VALUE            (WORKING SET) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.300                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 554                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.97                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.04                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 651                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 34                           
REMARK   3   BIN FREE R VALUE                    : 0.3600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5007                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.58000                                              
REMARK   3    B22 (A**2) : -1.21000                                             
REMARK   3    B33 (A**2) : 0.63000                                              
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.637         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.467         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.279        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.884                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.815                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5114 ; 0.014 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6920 ; 1.875 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   619 ; 8.646 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   204 ;34.615 ;23.529       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   839 ;24.942 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;21.879 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   778 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3753 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4DW2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070854.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11462                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.970                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) PEG 2000 MME, 100MM TRIS-HCL   
REMARK 280  (PH 8.0), 0.21M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,    
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
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       19.48050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.38000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.47750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.38000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.48050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.47750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, H, L                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ILE U    16                                                      
REMARK 465     ILE U    17                                                      
REMARK 465     GLY U    18                                                      
REMARK 465     GLY U    19                                                      
REMARK 465     GLU U    20                                                      
REMARK 465     HIS U    37                                                      
REMARK 465     ARG U    37A                                                     
REMARK 465     GLY U    37B                                                     
REMARK 465     GLY U    37C                                                     
REMARK 465     SER U    37D                                                     
REMARK 465     GLN U   169                                                      
REMARK 465     GLN U   170                                                      
REMARK 465     PRO U   170A                                                     
REMARK 465     HIS U   170B                                                     
REMARK 465     LYS U   187                                                      
REMARK 465     THR U   188                                                      
REMARK 465     ASP U   189                                                      
REMARK 465     SER U   190                                                      
REMARK 465     CYS U   191                                                      
REMARK 465     GLY U   218                                                      
REMARK 465     CYS U   219                                                      
REMARK 465     ALA U   220                                                      
REMARK 465     LEU U   221                                                      
REMARK 465     LYS U   222                                                      
REMARK 465     ASP U   223                                                      
REMARK 465     GLY H   127                                                      
REMARK 465     SER H   128                                                      
REMARK 465     HIS L   198                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL U   176     N    THR U   178              1.08            
REMARK 500   O    GLU U   175     N    THR U   177              1.34            
REMARK 500   CD   PRO L     8     CE   MET L    11              1.60            
REMARK 500   OE1  GLN H    39     NE2  GLN L    38              1.67            
REMARK 500   NE   ARG H    94     OD2  ASP H   101              1.69            
REMARK 500   O    TYR U   171     O    TYR U   172              1.79            
REMARK 500   O    PRO H   178     OG1  THR H   181              1.82            
REMARK 500   O    VAL U   159     OD2  ASP U   185              1.82            
REMARK 500   NH2  ARG H    94     OD2  ASP H   101              1.89            
REMARK 500   CG   PRO L     8     CE   MET L    11              1.90            
REMARK 500   O    TYR L   186     OH   TYR L   192              1.95            
REMARK 500   CZ   ARG H    94     OD2  ASP H   101              1.98            
REMARK 500   O    VAL L    28     OH   TYR L    71              2.02            
REMARK 500   OD2  ASP L   151     ND1  HIS L   189              2.03            
REMARK 500   O    GLN U   131     OG1  THR U   134              2.07            
REMARK 500   OG   SER H   196     OG1  THR H   198              2.08            
REMARK 500   NH1  ARG H    38     OH   TYR H    90              2.09            
REMARK 500   N    SER U   164     OE1  GLU U   167              2.11            
REMARK 500   O    LEU U   155     NE2  HIS L    31              2.12            
REMARK 500   CD1  ILE L     2     O    SER L    26              2.12            
REMARK 500   OG   SER U   164     OE1  GLU U   167              2.13            
REMARK 500   N    PRO H   178     OG1  THR H   181              2.14            
REMARK 500   O    LEU U   181     N    TYR U   228              2.14            
REMARK 500   NH1  ARG U    72     OG   SER U    75              2.15            
REMARK 500   O    VAL U   176     CA   THR U   178              2.16            
REMARK 500   N    LEU H   132     O    VAL H   175              2.17            
REMARK 500   NE2  GLN H    39     OE1  GLN L    38              2.18            
REMARK 500   O    ASP L     1     O    TYR L    94              2.18            
REMARK 500   OE2  GLU H    46     NH2  ARG L    96              2.19            
REMARK 500   N    GLY H    15     O    LEU H    82C             2.19            
REMARK 500   O    ASP L   184     N    GLU L   187              2.19            
REMARK 500   O    LEU U   150     CA   PRO U   152              2.19            
REMARK 500   OG   SER H    35     OG   SER H    50              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   OH   TYR U   151     OG   SER U   164     1655     1.37            
REMARK 500   OG   SER L    67     O    THR L   200     4445     2.08            
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    SER H  82A  C     SER H  82B  N       0.147                       
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 U  60C  C   -  N   -  CD  ANGL. DEV. = -18.4 DEGREES          
REMARK 500    PRO U 185A  C   -  N   -  CD  ANGL. DEV. = -18.9 DEGREES          
REMARK 500    CYS L  23   CA  -  CB  -  SG  ANGL. DEV. = -10.9 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    PRO U  28       31.29    -93.38                                   
REMARK 500    LEU U  97B     -84.53   -109.23                                   
REMARK 500    TYR U 127       59.79     32.71                                   
REMARK 500    THR U 134      155.04    -49.39                                   
REMARK 500    SER U 146        1.48    111.52                                   
REMARK 500    THR U 147       77.63     50.12                                   
REMARK 500    ASP U 148     -176.20    -63.37                                   
REMARK 500    TYR U 172      152.07     46.98                                   
REMARK 500    VAL U 176        4.10      6.25                                   
REMARK 500    THR U 177       -7.73    -17.81                                   
REMARK 500    THR U 178      -16.64     66.13                                   
REMARK 500    LYS H  43        0.51     85.11                                   
REMARK 500    VAL H  63       -1.40   -141.72                                   
REMARK 500    ALA H  88      155.02    179.30                                   
REMARK 500    ALA H 100      166.04     88.12                                   
REMARK 500    SER H 184     -116.76     40.28                                   
REMARK 500    SER H 197       -2.32     66.90                                   
REMARK 500    ILE L   2       77.51     42.09                                   
REMARK 500    ALA L  13      178.24     88.40                                   
REMARK 500    THR L  27A     130.42     32.81                                   
REMARK 500    THR L  51      -64.23     84.12                                   
REMARK 500    ALA L  60      -31.82    -38.47                                   
REMARK 500    ASN L 138       72.11     48.77                                   
REMARK 500    SER L 171       18.28     59.36                                   
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 LEU U  150     TYR U  151                 -133.59                    
REMARK 500 ALA L   13     SER L   14                 -126.60                    
REMARK 500 ALA L   25     SER L   26                  147.67                    
REMARK 500 SER L   26     SER L   27                 -148.89                    
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 U 149        22.4      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 L 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DVB   RELATED DB: PDB                                   
DBREF  4DW2 U   16   243  UNP    P00749   UROK_HUMAN     179    424             
DBREF  4DW2 H    1   208  PDB    4DW2     4DW2             1    208             
DBREF  4DW2 L    1   214  PDB    4DW2     4DW2             1    214             
SEQADV 4DW2 ALA U  122  UNP  P00749    CYS   299 ENGINEERED MUTATION            
SEQADV 4DW2 GLN U  145  UNP  P00749    ASN   322 ENGINEERED MUTATION            
SEQRES   1 U  246  ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO          
SEQRES   2 U  246  TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER          
SEQRES   3 U  246  VAL THR TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS          
SEQRES   4 U  246  TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO          
SEQRES   5 U  246  LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG          
SEQRES   6 U  246  LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL          
SEQRES   7 U  246  GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR          
SEQRES   8 U  246  LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG          
SEQRES   9 U  246  SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE          
SEQRES  10 U  246  GLN THR ILE ALA LEU PRO SER MET TYR ASN ASP PRO GLN          
SEQRES  11 U  246  PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU          
SEQRES  12 U  246  GLN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET          
SEQRES  13 U  246  THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN          
SEQRES  14 U  246  PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU          
SEQRES  15 U  246  CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN          
SEQRES  16 U  246  GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY          
SEQRES  17 U  246  ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY          
SEQRES  18 U  246  CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL          
SEQRES  19 U  246  SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR LYS              
SEQRES   1 H  212  GLN VAL LYS LEU GLN GLU SER GLY GLY ASP LEU VAL LYS          
SEQRES   2 H  212  PRO GLY GLY SER LEU LYS LEU SER CYS SER ALA SER GLY          
SEQRES   3 H  212  PHE THR PHE SER ARG TYR ALA MET SER TRP VAL ARG GLN          
SEQRES   4 H  212  THR PRO GLU LYS ARG LEU GLU TRP VAL ALA SER ILE THR          
SEQRES   5 H  212  ASN GLY GLY SER THR TYR TYR SER ASP SER VAL LYS GLY          
SEQRES   6 H  212  ARG PHE ILE ILE SER ARG ASP ASN ALA ARG ASN ILE LEU          
SEQRES   7 H  212  SER LEU GLN MET SER SER LEU ARG SER GLU ASP THR ALA          
SEQRES   8 H  212  MET TYR TYR CYS GLU ARG GLY GLU LEU THR TYR ALA MET          
SEQRES   9 H  212  ASP TYR TRP GLY GLN GLY THR THR VAL THR VAL SER SER          
SEQRES  10 H  212  ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO          
SEQRES  11 H  212  GLY SER MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR          
SEQRES  12 H  212  PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY SER          
SEQRES  13 H  212  LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN          
SEQRES  14 H  212  SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL PRO          
SEQRES  15 H  212  SER SER THR TRP PRO SER GLU THR VAL THR CYS ASN VAL          
SEQRES  16 H  212  ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE          
SEQRES  17 H  212  VAL VAL LYS GLY                                              
SEQRES   1 L  215  ASP ILE GLU LEU THR GLN SER PRO ALA ILE MET SER ALA          
SEQRES   2 L  215  SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER          
SEQRES   3 L  215  SER THR VAL SER PHE HIS TYR LEU HIS TRP TYR GLN GLN          
SEQRES   4 L  215  LYS SER GLY ALA SER PRO LYS LEU TRP ILE TYR ALA THR          
SEQRES   5 L  215  SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY          
SEQRES   6 L  215  SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER          
SEQRES   7 L  215  VAL GLU THR GLU ASP ALA ALA THR TYR TYR CYS GLN HIS          
SEQRES   8 L  215  TYR SER ALA TYR PRO ARG THR PHE GLY GLY GLY THR LYS          
SEQRES   9 L  215  LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER          
SEQRES  10 L  215  ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY          
SEQRES  11 L  215  ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS          
SEQRES  12 L  215  ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG          
SEQRES  13 L  215  GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER          
SEQRES  14 L  215  LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU          
SEQRES  15 L  215  THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS          
SEQRES  16 L  215  GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS          
SEQRES  17 L  215  SER PHE ASN ARG ASN GLU CYS                                  
HET    SO4  L 301       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  HOH   *10(H2 O)                                                     
HELIX    1   1 THR U   56  ASP U   60A 1                                   6    
HELIX    2   2 VAL U  231  LYS U  243  1                                  13    
HELIX    3   3 THR H   28  TYR H   32  5                                   5    
HELIX    4   4 ARG H   83  THR H   87  5                                   5    
HELIX    5   5 GLU L   79  ALA L   83  5                                   5    
HELIX    6   6 SER L  121  GLY L  128  1                                   8    
HELIX    7   7 LYS L  183  ARG L  188  1                                   6    
SHEET    1   A 7 THR U  39  CYS U  42  0                                        
SHEET    2   A 7 ALA U  32  ARG U  35 -1  N  ARG U  35   O  THR U  39           
SHEET    3   A 7 TYR U  64  LEU U  68 -1  O  ILE U  65   N  TYR U  34           
SHEET    4   A 7 MET U  81  LEU U  90 -1  O  PHE U  83   N  VAL U  66           
SHEET    5   A 7 ILE U 103  SER U 110 -1  O  ARG U 109   N  GLU U  84           
SHEET    6   A 7 TRP U  51  ALA U  55 -1  N  SER U  54   O  ALA U 104           
SHEET    7   A 7 SER U  45  LEU U  46 -1  N  SER U  45   O  ILE U  53           
SHEET    1   B 2 SER U  95  ALA U  96  0                                        
SHEET    2   B 2 HIS U  99  HIS U 100 -1  O  HIS U 100   N  SER U  95           
SHEET    1   C 7 ARG U 206  LEU U 209  0                                        
SHEET    2   C 7 VAL U 200  LEU U 203 -1  N  LEU U 203   O  ARG U 206           
SHEET    3   C 7 SER U 135  ILE U 138 -1  N  GLU U 137   O  VAL U 200           
SHEET    4   C 7 THR U 158  LEU U 162 -1  O  THR U 158   N  ILE U 138           
SHEET    5   C 7 MET U 180  ALA U 184 -1  O  ALA U 184   N  LYS U 161           
SHEET    6   C 7 GLY U 226  ARG U 230 -1  O  TYR U 228   N  LEU U 181           
SHEET    7   C 7 GLY U 211  TRP U 215 -1  N  TRP U 215   O  VAL U 227           
SHEET    1   D 4 LEU H   4  SER H   7  0                                        
SHEET    2   D 4 LEU H  18  ALA H  24 -1  O  SER H  23   N  GLN H   5           
SHEET    3   D 4 ILE H  77  MET H  82 -1  O  MET H  82   N  LEU H  18           
SHEET    4   D 4 PHE H  67  ASP H  72 -1  N  SER H  70   O  SER H  79           
SHEET    1   E 5 THR H  57  TYR H  59  0                                        
SHEET    2   E 5 LEU H  45  ILE H  51 -1  N  SER H  50   O  TYR H  58           
SHEET    3   E 5 MET H  34  GLN H  39 -1  N  TRP H  36   O  ALA H  49           
SHEET    4   E 5 ALA H  88  ARG H  94 -1  O  TYR H  91   N  VAL H  37           
SHEET    5   E 5 THR H 107  VAL H 109 -1  O  THR H 107   N  TYR H  90           
SHEET    1   F 4 SER H 120  LEU H 124  0                                        
SHEET    2   F 4 THR H 131  TYR H 139 -1  O  LEU H 135   N  TYR H 122           
SHEET    3   F 4 LEU H 168  THR H 176 -1  O  VAL H 175   N  LEU H 132           
SHEET    4   F 4 VAL H 163  GLN H 165 -1  N  GLN H 165   O  LEU H 168           
SHEET    1   G 3 THR H 145  TRP H 148  0                                        
SHEET    2   G 3 THR H 188  ALA H 192 -1  O  ASN H 190   N  THR H 147           
SHEET    3   G 3 LYS H 199  LYS H 203 -1  O  VAL H 200   N  VAL H 191           
SHEET    1   H 4 LEU L   4  SER L   7  0                                        
SHEET    2   H 4 VAL L  19  ALA L  25 -1  O  ARG L  24   N  THR L   5           
SHEET    3   H 4 SER L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4   H 4 PHE L  62  SER L  67 -1  N  SER L  65   O  SER L  72           
SHEET    1   I 6 ILE L  10  SER L  12  0                                        
SHEET    2   I 6 THR L 102  GLU L 105  1  O  GLU L 105   N  MET L  11           
SHEET    3   I 6 ALA L  84  HIS L  90 -1  N  ALA L  84   O  LEU L 104           
SHEET    4   I 6 LEU L  33  GLN L  38 -1  N  TYR L  36   O  TYR L  87           
SHEET    5   I 6 PRO L  44  TYR L  49 -1  O  ILE L  48   N  TRP L  35           
SHEET    6   I 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1   J 4 THR L 114  PHE L 118  0                                        
SHEET    2   J 4 GLY L 129  PHE L 139 -1  O  ASN L 137   N  THR L 114           
SHEET    3   J 4 TYR L 173  THR L 182 -1  O  SER L 177   N  CYS L 134           
SHEET    4   J 4 VAL L 159  TRP L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1   K 4 SER L 153  ARG L 155  0                                        
SHEET    2   K 4 ASN L 145  ILE L 150 -1  N  ILE L 150   O  SER L 153           
SHEET    3   K 4 SER L 191  THR L 197 -1  O  THR L 193   N  LYS L 149           
SHEET    4   K 4 ILE L 205  ASN L 210 -1  O  PHE L 209   N  TYR L 192           
SSBOND   1 CYS U   42    CYS U   58                          1555   1555  2.03  
SSBOND   2 CYS U   50    CYS U  111                          1555   1555  2.00  
SSBOND   3 CYS U  136    CYS U  201                          1555   1555  1.90  
SSBOND   4 CYS U  168    CYS U  182                          1555   1555  2.04  
SSBOND   5 CYS H   22    CYS H   92                          1555   1555  2.02  
SSBOND   6 CYS H  134    CYS H  189                          1555   1555  1.97  
SSBOND   7 CYS L   23    CYS L   88                          1555   1555  1.99  
SSBOND   8 CYS L  134    CYS L  194                          1555   1555  2.03  
CISPEP   1 TYR U  151    PRO U  152          0        -1.05                     
CISPEP   2 PRO U  185A   GLN U  185B         0        18.58                     
CISPEP   3 PHE H  140    PRO H  141          0        -5.51                     
CISPEP   4 GLU H  142    PRO H  143          0         2.93                     
CISPEP   5 TRP H  182    PRO H  183          0        -4.53                     
CISPEP   6 SER L    7    PRO L    8          0        -5.85                     
CISPEP   7 TYR L   94    PRO L   95          0       -14.64                     
CISPEP   8 TYR L  140    PRO L  141          0        -5.21                     
SITE     1 AC1  5 GLN H  81  THR L 182  ASP L 184  GLU L 185                    
SITE     2 AC1  5 ARG L 188                                                     
CRYST1   38.961   94.955  154.760  90.00  90.00  90.00 P 21 21 21    4          
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      0.025667  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010531  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006462        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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