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Entry: 2ZCK
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HEADER    IMMUNE SYSTEM                           09-NOV-07   2ZCK              
TITLE     CRYSTAL STRUCTURE OF A TERNARY COMPLEX BETWEEN PSA, A SUBSTRAT-ACYL   
TITLE    2 INTERMEDIATE AND AN ACTIVATING ANTIBODY                              
CAVEAT     2ZCK    LEU P 67 HAS WRONG CHIRALITY AT ATOM CA ASP L 28 HAS WRONG   
CAVEAT   2 2ZCK    CHIRALITY AT ATOM CA TRP H 188 HAS WRONG CHIRALITY AT ATOM   
CAVEAT   3 2ZCK    CA NAG A 1 HAS WRONG CHIRALITY AT ATOM C1 MAN A 2 HAS WRONG  
CAVEAT   4 2ZCK    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTATE-SPECIFIC ANTIGEN;                                 
COMPND   3 CHAIN: P;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 25-261;                                       
COMPND   5 SYNONYM: PSA, KALLIKREIN- 3, SEMENOGELASE, GAMMA-SEMINOPROTEIN,      
COMPND   6 SEMININ, P-30 ANTIGEN;                                               
COMPND   7 EC: 3.4.21.77;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: KGISSQY;                                                   
COMPND  10 CHAIN: S;                                                            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: MONOCLONAL ANTIBODY 8G8F5 FAB;                             
COMPND  14 CHAIN: L;                                                            
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: MONOCLONAL ANTIBODY 8G8F5 FAB;                             
COMPND  17 CHAIN: H                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 OTHER_DETAILS: SEMINAL FLUIDS;                                       
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 SYNTHETIC: YES;                                                      
SOURCE   8 OTHER_DETAILS: PEPTIDE SYNTHESIS;                                    
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 STRAIN: BALB/CJYCO;                                                  
SOURCE  14 OTHER_DETAILS: ASCITIC FLUIDS;                                       
SOURCE  15 MOL_ID: 4;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  17 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  18 ORGANISM_TAXID: 10090;                                               
SOURCE  19 STRAIN: BALB/CJYCO;                                                  
SOURCE  20 OTHER_DETAILS: ASCITIC FLUIDS                                        
KEYWDS    HUMAN PSA, ANTIBODIES, KALLIKREIN RELATED PEPTIDASES, PROSTATE        
KEYWDS   2 CANCER, GLYCOPROTEIN, HYDROLASE, PROTEASE, SECRETED, SERINE          
KEYWDS   3 PROTEASE, ZYMOGEN, IMMUNE SYSTEM                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.MENEZ,E.STURA,C.JOLIVET-REYNAUD                                     
REVDAT   5   29-JUL-20 2ZCK    1       CAVEAT COMPND REMARK DBREF               
REVDAT   5 2                   1       HETNAM LINK   SITE   ATOM                
REVDAT   4   13-JUL-11 2ZCK    1       VERSN                                    
REVDAT   3   24-FEB-09 2ZCK    1       VERSN                                    
REVDAT   2   18-MAR-08 2ZCK    1       JRNL                                     
REVDAT   1   29-JAN-08 2ZCK    0                                                
JRNL        AUTH   S.MICHEL,B.H.MULLER,M.BOSSUS,F.DUCANCEL,C.JOLIVET-REYNAUD,   
JRNL        AUTH 2 E.A.STURA                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF A TERNARY COMPLEX BETWEEN HUMAN         
JRNL        TITL 2 PROSTATE-SPECIFIC ANTIGEN, ITS SUBSTRATE ACYL INTERMEDIATE   
JRNL        TITL 3 AND AN ACTIVATING ANTIBODY                                   
JRNL        REF    J.MOL.BIOL.                   V. 376  1021 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18187150                                                     
JRNL        DOI    10.1016/J.JMB.2007.11.052                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 16217                          
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) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 870                             
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1143                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.37                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 61                           
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5273                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 31                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.11000                                              
REMARK   3    B22 (A**2) : 1.11000                                              
REMARK   3    B33 (A**2) : -2.22000                                             
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): 0.500         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.377         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.086        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.906                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.862                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5437 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4732 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7414 ; 1.733 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11094 ; 0.974 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   688 ; 8.335 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   214 ;35.733 ;24.533       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   863 ;18.849 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;16.009 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   835 ; 0.241 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6031 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1035 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1199 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5134 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2578 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3066 ; 0.091 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   130 ; 0.166 ; 0.200       
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):    22 ; 0.178 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    62 ; 0.161 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.173 ; 0.200       
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):  4338 ; 1.136 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1403 ; 0.064 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5586 ; 1.149 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2318 ; 1.578 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1828 ; 2.342 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER 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 : BABINET MODEL WITH 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 ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2ZCK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000027800.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM, XFIT                       
REMARK 200  DATA SCALING SOFTWARE          : PROCESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17100                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.11500                            
REMARK 200  R SYM                      (I) : 0.12700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.58300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: XFIT                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2ZCH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTAL GROWN IN 14% MPEG550, 100MM      
REMARK 280  HEPES (PH7.2), THEN SOAKED IN PEG400, 100MM TRIS-HCL (PH7.3),       
REMARK 280  10MM ZNCL2, 0.28 MG/ML MU-KGISSQY-AFC, VAPOR DIFFUSION, SITTING     
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      119.09000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.38250            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.38250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       59.54500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.38250            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.38250            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      178.63500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.38250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.38250            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       59.54500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.38250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.38250            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      178.63500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      119.09000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, S, L, H, A                         
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 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    SER P   195     O    THR P   213              1.85            
REMARK 500   O    HOH L   221     O    HOH L   223              1.91            
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    LEU P  67   N   -  CA  -  C   ANGL. DEV. =  18.6 DEGREES          
REMARK 500    ARG H  94   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    PRO H 219   C   -  N   -  CA  ANGL. DEV. =  22.3 DEGREES          
REMARK 500    PRO H 219   C   -  N   -  CD  ANGL. DEV. = -19.1 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    VAL P  41      -75.38    161.17                                   
REMARK 500    LEU P  67      -65.09    -92.82                                   
REMARK 500    HIS P  70      -55.65   -124.09                                   
REMARK 500    SER P  99       31.42    -86.99                                   
REMARK 500    ASP P 102       79.19    -66.22                                   
REMARK 500    GLU P 148      106.54     78.15                                   
REMARK 500    GLN P 210      -35.34   -133.30                                   
REMARK 500    SER P 214     -118.20    146.46                                   
REMARK 500    ASN P 246       56.77   -140.56                                   
REMARK 500    ASP L  28      -37.45     61.39                                   
REMARK 500    LEU L  47      -61.32    -94.54                                   
REMARK 500    ALA L  51      -47.58     69.96                                   
REMARK 500    ALA L  60       -5.09    -55.40                                   
REMARK 500    GLN L  76      119.71   -178.92                                   
REMARK 500    ALA L 111      139.03   -175.35                                   
REMARK 500    ALA L 130      116.43   -161.34                                   
REMARK 500    ASP L 151      108.52     49.58                                   
REMARK 500    SER L 153       78.17    -57.67                                   
REMARK 500    ARG L 155       84.54    176.61                                   
REMARK 500    ASN L 157       82.02    101.41                                   
REMARK 500    GLN L 166      109.29    -45.00                                   
REMARK 500    GLU L 187       32.20    -81.31                                   
REMARK 500    ASN L 190     -115.29    -81.92                                   
REMARK 500    LYS L 199        0.74    -42.80                                   
REMARK 500    SER L 201      -95.44   -129.47                                   
REMARK 500    ARG L 211       72.91     48.73                                   
REMARK 500    ASN L 212       74.49     43.63                                   
REMARK 500    GLU L 213       97.33      4.63                                   
REMARK 500    GLN H   6     -112.51    -85.16                                   
REMARK 500    PRO H  41      -53.63    -29.27                                   
REMARK 500    GLU H  61       81.55    -69.81                                   
REMARK 500    MET H  62      -42.99    168.43                                   
REMARK 500    SER H  82A     -89.99   -100.83                                   
REMARK 500    SER H  84      119.89     60.65                                   
REMARK 500    ASP H  86      -34.47    171.29                                   
REMARK 500    ASN H 100       19.51     59.23                                   
REMARK 500    GLU H 100C      51.39     32.38                                   
REMARK 500    SER H 113      -74.23    -21.92                                   
REMARK 500    ALA H 114       16.11   -159.00                                   
REMARK 500    LYS H 115     -131.91     16.58                                   
REMARK 500    THR H 116       81.41   -150.97                                   
REMARK 500    LEU H 124       77.26   -113.77                                   
REMARK 500    PRO H 126      150.60    -39.37                                   
REMARK 500    VAL H 127      -88.55    -16.76                                   
REMARK 500    CYS H 128     -171.83     64.96                                   
REMARK 500    LEU H 138     -168.50   -114.25                                   
REMARK 500    SER H 149       68.16    102.73                                   
REMARK 500    SER H 161       51.42   -109.53                                   
REMARK 500    GLN H 171      -36.81   -150.18                                   
REMARK 500    TRP H 188     -141.02    -30.32                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA P   39     VAL P   41                  -73.07                    
REMARK 500 THR P  213     SER P  214                  -63.58                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZCH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PSA COMPLEXED WITH ANTIBODY 8G8F5 AT      
REMARK 900 PH7.2                                                                
REMARK 900 RELATED ID: 2ZCL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PSA COMPLEXED WITH ANTIBODY 8G8F5 AT      
REMARK 900 PH5.5                                                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 A SEQUENCE DATABASE REFERENCE FOR CHAIN L AND H DOES NOT CURRENTLY   
REMARK 999 EXIST.                                                               
DBREF  2ZCK P   16   247  UNP    P07288   KLK3_HUMAN      25    261             
DBREF  2ZCK S  498   504  PDB    2ZCK     2ZCK           498    504             
DBREF  2ZCK L    1   214  PDB    2ZCK     2ZCK             1    214             
DBREF  2ZCK H    1   221  PDB    2ZCK     2ZCK             1    221             
SEQRES   1 P  237  ILE VAL GLY GLY TRP GLU CYS GLU LYS HIS SER GLN PRO          
SEQRES   2 P  237  TRP GLN VAL LEU VAL ALA SER ARG GLY ARG ALA VAL CYS          
SEQRES   3 P  237  GLY GLY VAL LEU VAL HIS PRO GLN TRP VAL LEU THR ALA          
SEQRES   4 P  237  ALA HIS CYS ILE ARG ASN LYS SER VAL ILE LEU LEU GLY          
SEQRES   5 P  237  ARG HIS SER LEU PHE HIS PRO GLU ASP THR GLY GLN VAL          
SEQRES   6 P  237  PHE GLN VAL SER HIS SER PHE PRO HIS PRO LEU TYR ASP          
SEQRES   7 P  237  MET SER LEU LEU LYS ASN ARG PHE LEU ARG PRO GLY ASP          
SEQRES   8 P  237  ASP SER SER HIS ASP LEU MET LEU LEU ARG LEU SER GLU          
SEQRES   9 P  237  PRO ALA GLU LEU THR ASP ALA VAL LYS VAL MET ASP LEU          
SEQRES  10 P  237  PRO THR GLN GLU PRO ALA LEU GLY THR THR CYS TYR ALA          
SEQRES  11 P  237  SER GLY TRP GLY SER ILE GLU PRO GLU GLU PHE LEU THR          
SEQRES  12 P  237  PRO LYS LYS LEU GLN CYS VAL ASP LEU HIS VAL ILE SER          
SEQRES  13 P  237  ASN ASP VAL CYS ALA GLN VAL HIS PRO GLN LYS VAL THR          
SEQRES  14 P  237  LYS PHE MET LEU CYS ALA GLY ARG TRP THR GLY GLY LYS          
SEQRES  15 P  237  SER THR CYS SER GLY ASP SER GLY GLY PRO LEU VAL CYS          
SEQRES  16 P  237  ASN GLY VAL LEU GLN GLY ILE THR SER TRP GLY SER GLU          
SEQRES  17 P  237  PRO CYS ALA LEU PRO GLU ARG PRO SER LEU TYR THR LYS          
SEQRES  18 P  237  VAL VAL HIS TYR ARG LYS TRP ILE LYS ASP THR ILE VAL          
SEQRES  19 P  237  ALA ASN PRO                                                  
SEQRES   1 S    7  LYS GLY ILE SER SER GLN TYR                                  
SEQRES   1 L  218  ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL          
SEQRES   2 L  218  SER LEU GLY GLN ARG ALA THR ILE SER CYS LYS ALA SER          
SEQRES   3 L  218  GLN SER VAL ASP PHE ASP GLY ASP SER TYR MET ASN TRP          
SEQRES   4 L  218  TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE          
SEQRES   5 L  218  PHE ALA ALA SER ASN LEU ALA SER GLY ILE PRO ALA ARG          
SEQRES   6 L  218  LEU SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN          
SEQRES   7 L  218  ILE GLN PRO VAL GLU GLU GLU ASP ALA ALA THR TYR TYR          
SEQRES   8 L  218  CYS GLN GLN SER ASN GLU ASP PRO TYR THR PHE GLY GLY          
SEQRES   9 L  218  GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO          
SEQRES  10 L  218  THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR          
SEQRES  11 L  218  SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE          
SEQRES  12 L  218  TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY          
SEQRES  13 L  218  SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP          
SEQRES  14 L  218  GLN ASP SER LYS ASP SER THR TYR SER MET SER SER THR          
SEQRES  15 L  218  LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER          
SEQRES  16 L  218  TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO          
SEQRES  17 L  218  ILE VAL LYS SER PHE ASN ARG ASN GLU CYS                      
SEQRES   1 H  230  GLN VAL GLN LEU GLN GLN SER GLY ASP ASP LEU VAL LYS          
SEQRES   2 H  230  PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY          
SEQRES   3 H  230  TYR THR PHE THR THR TYR TYR ILE ASN TRP MET ARG GLN          
SEQRES   4 H  230  ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ARG ILE ALA          
SEQRES   5 H  230  PRO ALA SER GLY THR THR TYR SER SER GLU MET PHE LYS          
SEQRES   6 H  230  ASP LYS ALA THR LEU THR VAL ASP THR SER SER ASN THR          
SEQRES   7 H  230  ALA TYR ILE GLN LEU SER SER LEU SER SER GLU ASP SER          
SEQRES   8 H  230  ALA VAL TYR PHE CYS ALA ARG ALA ASP TYR GLY PHE ASN          
SEQRES   9 H  230  SER GLY GLU ALA MET ASP TYR TRP GLY GLN GLY THR SER          
SEQRES  10 H  230  VAL THR VAL SER SER ALA LYS THR THR ALA PRO PRO VAL          
SEQRES  11 H  230  TYR PRO LEU ALA PRO VAL CYS GLY ASP THR THR GLY SER          
SEQRES  12 H  230  SER VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO          
SEQRES  13 H  230  GLU SER VAL THR LEU LEU TRP ASN SER GLY SER LEU SER          
SEQRES  14 H  230  SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP          
SEQRES  15 H  230  LEU TYR THR LEU SER SER SER VAL THR VAL THR SER SER          
SEQRES  16 H  230  THR TRP PRO SER GLN SER ILE THR CYS ASN VAL ALA HIS          
SEQRES  17 H  230  PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO          
SEQRES  18 H  230  ARG ASP CYS GLY CYS LYS PRO CYS ILE                          
MODRES 2ZCK ASN P   61  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A   1      14                                                       
HET    MAN  A   2      11                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
FORMUL   5  NAG    C8 H15 N O6                                                  
FORMUL   5  MAN    C6 H12 O6                                                    
FORMUL   6  HOH   *31(H2 O)                                                     
HELIX    1   1 ALA P   55  ILE P   59  5                                   5    
HELIX    2   2 ASP P   95  LYS P   95E 5                                   6    
HELIX    3   3 SER P  164  HIS P  172  1                                   9    
HELIX    4   4 TYR P  235  ALA P  245  1                                  11    
HELIX    5   5 GLU L   79  ALA L   83  5                                   5    
HELIX    6   6 SER L  121  THR L  126  1                                   6    
HELIX    7   7 LYS L  183  GLU L  187  1                                   5    
HELIX    8   8 THR H   28  TYR H   32  5                                   5    
HELIX    9   9 THR H   73  SER H   75  5                                   3    
SHEET    1   A 6 TRP P  20  GLU P  21  0                                        
SHEET    2   A 6 GLN P 156  VAL P 162 -1  O  CYS P 157   N  TRP P  20           
SHEET    3   A 6 THR P 135  GLY P 140 -1  N  CYS P 136   O  LEU P 160           
SHEET    4   A 6 PRO P 198  CYS P 201 -1  O  VAL P 200   N  TYR P 137           
SHEET    5   A 6 VAL P 208  SER P 217 -1  O  VAL P 208   N  CYS P 201           
SHEET    6   A 6 SER S 501  GLN S 503 -1  O  SER S 502   N  GLY P 216           
SHEET    1   B 6 TRP P  20  GLU P  21  0                                        
SHEET    2   B 6 GLN P 156  VAL P 162 -1  O  CYS P 157   N  TRP P  20           
SHEET    3   B 6 MET P 180  GLY P 184 -1  O  GLY P 184   N  HIS P 161           
SHEET    4   B 6 SER P 227  LYS P 231 -1  O  TYR P 229   N  LEU P 181           
SHEET    5   B 6 VAL P 208  SER P 217 -1  N  ILE P 212   O  THR P 230           
SHEET    6   B 6 SER S 501  GLN S 503 -1  O  SER S 502   N  GLY P 216           
SHEET    1   C 7 GLN P  30  SER P  35  0                                        
SHEET    2   C 7 ARG P  38  HIS P  48 -1  O  CYS P  42   N  VAL P  33           
SHEET    3   C 7 TRP P  51  THR P  54 -1  O  LEU P  53   N  VAL P  45           
SHEET    4   C 7 MET P 104  LEU P 108 -1  O  MET P 104   N  THR P  54           
SHEET    5   C 7 VAL P  82  PRO P  90 -1  N  PHE P  89   O  LEU P 105           
SHEET    6   C 7 VAL P  64  LEU P  66 -1  N  ILE P  65   O  PHE P  83           
SHEET    7   C 7 GLN P  30  SER P  35 -1  N  ALA P  34   O  VAL P  64           
SHEET    1   D 4 LEU L   4  SER L   7  0                                        
SHEET    2   D 4 ALA L  19  ALA L  25 -1  O  LYS L  24   N  THR L   5           
SHEET    3   D 4 ASP L  70  ILE L  75 -1  O  ILE L  75   N  ALA L  19           
SHEET    4   D 4 LEU L  62  SER L  67 -1  N  SER L  63   O  ASN L  74           
SHEET    1   E 6 SER L  10  VAL L  13  0                                        
SHEET    2   E 6 LYS L 103  ILE L 106  1  O  GLU L 105   N  LEU 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  TYR L  36   O  TYR L  87           
SHEET    5   E 6 LYS L  45  PHE L  49 -1  O  LYS L  45   N  GLN L  37           
SHEET    6   E 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  PHE L  49           
SHEET    1   F 4 SER L  10  VAL L  13  0                                        
SHEET    2   F 4 LYS L 103  ILE L 106  1  O  GLU L 105   N  LEU L  11           
SHEET    3   F 4 ALA L  84  GLN L  90 -1  N  ALA L  84   O  LEU L 104           
SHEET    4   F 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1   G 2 ASP L  27C PHE L  27D 0                                        
SHEET    2   G 2 ASP L  30  SER L  31 -1  O  ASP L  30   N  PHE L  27D          
SHEET    1   H 4 THR L 114  PHE L 118  0                                        
SHEET    2   H 4 GLY L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3   H 4 TYR L 173  THR L 182 -1  O  MET L 175   N  LEU L 136           
SHEET    4   H 4 VAL L 159  LEU L 160 -1  N  LEU L 160   O  THR L 178           
SHEET    1   I 3 ILE L 144  TRP L 148  0                                        
SHEET    2   I 3 TYR L 192  HIS L 198 -1  O  GLU L 195   N  LYS L 147           
SHEET    3   I 3 VAL L 206  PHE L 209 -1  O  PHE L 209   N  TYR L 192           
SHEET    1   J 4 GLN H   3  GLN H   5  0                                        
SHEET    2   J 4 VAL H  18  SER H  25 -1  O  LYS H  23   N  GLN H   5           
SHEET    3   J 4 THR H  77  LEU H  82 -1  O  ALA H  78   N  CYS H  22           
SHEET    4   J 4 ALA H  67  ASP H  72 -1  N  THR H  70   O  TYR H  79           
SHEET    1   K 6 ASP H  10  VAL H  12  0                                        
SHEET    2   K 6 SER H 108  VAL H 111  1  O  SER H 108   N  ASP H  10           
SHEET    3   K 6 ALA H  88  ALA H  95 -1  N  ALA H  88   O  VAL H 109           
SHEET    4   K 6 TYR H  33  GLN H  39 -1  N  ASN H  35   O  ALA H  93           
SHEET    5   K 6 LEU H  45  ILE H  51 -1  O  ILE H  48   N  TRP H  36           
SHEET    6   K 6 THR H  57  SER H  59 -1  O  TYR H  58   N  ARG H  50           
SHEET    1   L 4 ASP H  10  VAL H  12  0                                        
SHEET    2   L 4 SER H 108  VAL H 111  1  O  SER H 108   N  ASP H  10           
SHEET    3   L 4 ALA H  88  ALA H  95 -1  N  ALA H  88   O  VAL H 109           
SHEET    4   L 4 MET H 100E TRP H 103 -1  O  TYR H 102   N  ARG H  94           
SHEET    1   M 4 VAL H 121  PRO H 123  0                                        
SHEET    2   M 4 SER H 135  TYR H 145 -1  O  LEU H 141   N  TYR H 122           
SHEET    3   M 4 TYR H 175  THR H 184 -1  O  TYR H 175   N  TYR H 145           
SHEET    4   M 4 VAL H 163  THR H 165 -1  N  HIS H 164   O  SER H 180           
SHEET    1   N 4 VAL H 121  PRO H 123  0                                        
SHEET    2   N 4 SER H 135  TYR H 145 -1  O  LEU H 141   N  TYR H 122           
SHEET    3   N 4 TYR H 175  THR H 184 -1  O  TYR H 175   N  TYR H 145           
SHEET    4   N 4 VAL H 169  LEU H 170 -1  N  VAL H 169   O  THR H 176           
SHEET    1   O 3 THR H 151  TRP H 154  0                                        
SHEET    2   O 3 THR H 194  ALA H 198 -1  O  ALA H 198   N  THR H 151           
SHEET    3   O 3 LYS H 205  LYS H 209 -1  O  VAL H 206   N  VAL H 197           
SSBOND   1 CYS P   22    CYS P  157                          1555   1555  2.04  
SSBOND   2 CYS P   42    CYS P   58                          1555   1555  2.03  
SSBOND   3 CYS P  136    CYS P  201                          1555   1555  2.06  
SSBOND   4 CYS P  168    CYS P  182                          1555   1555  2.03  
SSBOND   5 CYS P  191    CYS P  220                          1555   1555  2.07  
SSBOND   6 CYS L   23    CYS L   88                          1555   1555  2.06  
SSBOND   7 CYS L  134    CYS L  194                          1555   1555  2.05  
SSBOND   8 CYS H   22    CYS H   92                          1555   1555  2.05  
SSBOND   9 CYS H  140    CYS H  195                          1555   1555  2.03  
LINK         ND2 ASN P  61                 C1  NAG A   1     1555   1555  1.46  
LINK         O4  NAG A   1                 C1  MAN A   2     1555   1555  1.47  
CISPEP   1 GLU P  218    PRO P  219          0         0.80                     
CISPEP   2 SER L    7    PRO L    8          0        -1.35                     
CISPEP   3 GLN L   76    PRO L   77          0        -1.50                     
CISPEP   4 ASP L   94    PRO L   95          0         0.32                     
CISPEP   5 TYR L  140    PRO L  141          0        -3.69                     
CISPEP   6 GLN L  156    ASN L  157          0        -6.57                     
CISPEP   7 THR L  200    SER L  201          0       -11.19                     
CISPEP   8 THR L  202    SER L  203          0       -17.80                     
CISPEP   9 GLU L  213    CYS L  214          0         6.41                     
CISPEP  10 SER H   83    SER H   84          0        27.63                     
CISPEP  11 SER H  113    ALA H  114          0       -22.61                     
CISPEP  12 VAL H  127    CYS H  128          0       -13.68                     
CISPEP  13 CYS H  128    GLY H  129          0        -2.14                     
CISPEP  14 GLY H  129    ASP H  130          0         3.57                     
CISPEP  15 THR H  132    GLY H  133          0        -5.53                     
CISPEP  16 PHE H  146    PRO H  147          0        -0.83                     
CISPEP  17 SER H  203    THR H  204          0         6.70                     
CISPEP  18 ARG H  213    ASP H  214          0         7.07                     
CISPEP  19 ASP H  214    CYS H  215          0         5.99                     
CISPEP  20 LYS H  218    PRO H  219          0        -2.88                     
CRYST1   86.765   86.765  238.180  90.00  90.00  90.00 P 41 21 2     8          
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      0.011525  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011525  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004199        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system