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Database: PDB
Entry: 4MWS
LinkDB: 4MWS
Original site: 4MWS 
HEADER    HYDROLASE                               25-SEP-13   4MWS              
TITLE     CRYSTAL STRUCTURE OF HUMAN PPCA (TRIGONAL CRYSTAL FORM 1)             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSOSOMAL PROTECTIVE PROTEIN;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CARBOXYPEPTIDASE C, CARBOXYPEPTIDASE L, CATHEPSIN A,        
COMPND   5 PROTECTIVE PROTEIN CATHEPSIN A, PPCA, PROTECTIVE PROTEIN FOR BETA-   
COMPND   6 GALACTOSIDASE;                                                       
COMPND   7 EC: 3.4.16.5;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CTSA, PPGB;                                                    
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HI-FIVE;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE CELL LINE;                     
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PIB/V5-HIS-TOPO TA                        
KEYWDS    CATHEPSIN A, GLYCOPROTEIN, SERINE PROTEASE, CARBOXYPEPTIDASE,         
KEYWDS   2 PROTECTIVE PROTEIN, N-LINKED GLYCOSYLATION, PROTEOLYTICALLY          
KEYWDS   3 ACTIVATED FORM, LYSOSOMAL ENZYME, HYDROLASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.KOLLI,S.C.GARMAN                                                    
REVDAT   4   29-JUL-20 4MWS    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   23-AUG-17 4MWS    1       REMARK                                   
REVDAT   2   15-APR-15 4MWS    1       JRNL                                     
REVDAT   1   12-MAR-14 4MWS    0                                                
JRNL        AUTH   N.KOLLI,S.C.GARMAN                                           
JRNL        TITL   PROTEOLYTIC ACTIVATION OF HUMAN CATHEPSIN A.                 
JRNL        REF    J.BIOL.CHEM.                  V. 289 11592 2014              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   24599961                                                     
JRNL        DOI    10.1074/JBC.M113.524280                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 25868                          
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) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1258                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1781                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.38                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 98                           
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6596                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 149                                     
REMARK   3   SOLVENT ATOMS            : 4                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 75.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.87                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -19.15000                                            
REMARK   3    B22 (A**2) : -19.15000                                            
REMARK   3    B33 (A**2) : 38.29000                                             
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): 0.062         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.186         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.907        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6950 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  6309 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9466 ; 1.164 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14475 ; 0.785 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   822 ; 6.186 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   340 ;38.429 ;24.824       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1076 ;14.270 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;15.916 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1017 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7916 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1670 ; 0.002 ; 0.020       
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   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     1    452       B     1    452   25478 0.040 0.050     
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.530                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : -H,-K,L                                         
REMARK   3      TWIN FRACTION : 0.470                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   182                          
REMARK   3    RESIDUE RANGE :   A   183        A   303                          
REMARK   3    RESIDUE RANGE :   A   304        A   452                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9560 -26.5930  -6.4880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1246 T22:   0.2069                                     
REMARK   3      T33:   0.0045 T12:  -0.0033                                     
REMARK   3      T13:  -0.0040 T23:   0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2639 L22:   1.0286                                     
REMARK   3      L33:   0.3084 L12:  -0.0568                                     
REMARK   3      L13:  -0.1089 L23:  -0.0344                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0010 S12:   0.0322 S13:  -0.0077                       
REMARK   3      S21:  -0.0365 S22:   0.0185 S23:  -0.0310                       
REMARK   3      S31:  -0.0376 S32:  -0.0617 S33:  -0.0175                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   182                          
REMARK   3    RESIDUE RANGE :   B   183        B   303                          
REMARK   3    RESIDUE RANGE :   B   304        B   452                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.7210 -62.8870 -10.2820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1834 T22:   0.1815                                     
REMARK   3      T33:   0.0210 T12:   0.0428                                     
REMARK   3      T13:   0.0385 T23:   0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9145 L22:   0.9212                                     
REMARK   3      L33:   0.3251 L12:  -0.6097                                     
REMARK   3      L13:  -0.4171 L23:   0.1581                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1472 S12:  -0.1046 S13:  -0.0456                       
REMARK   3      S21:   0.0448 S22:   0.0782 S23:  -0.0383                       
REMARK   3      S31:   0.1546 S32:   0.0931 S33:   0.0690                       
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 ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 4MWS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000082463.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : FOCUSING MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PILATUS CBF                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25989                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.14900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.88400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1IVY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 3350, 0.1M SODIUM FORMATE, PH    
REMARK 280  7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.26833            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       66.53667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       66.53667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       33.26833            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 20.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   289                                                      
REMARK 465     HIS A   290                                                      
REMARK 465     PHE A   291                                                      
REMARK 465     ARG A   292                                                      
REMARK 465     SER A   293                                                      
REMARK 465     GLY A   294                                                      
REMARK 465     ASP A   295                                                      
REMARK 465     LYS A   296                                                      
REMARK 465     VAL A   297                                                      
REMARK 465     HIS A   453                                                      
REMARK 465     HIS A   454                                                      
REMARK 465     HIS A   455                                                      
REMARK 465     HIS A   456                                                      
REMARK 465     HIS A   457                                                      
REMARK 465     HIS A   458                                                      
REMARK 465     SER B   289                                                      
REMARK 465     HIS B   290                                                      
REMARK 465     PHE B   291                                                      
REMARK 465     ARG B   292                                                      
REMARK 465     SER B   293                                                      
REMARK 465     GLY B   294                                                      
REMARK 465     ASP B   295                                                      
REMARK 465     LYS B   296                                                      
REMARK 465     VAL B   297                                                      
REMARK 465     HIS B   453                                                      
REMARK 465     HIS B   454                                                      
REMARK 465     HIS B   455                                                      
REMARK 465     HIS B   456                                                      
REMARK 465     HIS B   457                                                      
REMARK 465     HIS B   458                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A   8      -79.48    -86.28                                   
REMARK 500    ASP A  44       75.34     59.76                                   
REMARK 500    HIS A  70       23.34   -144.33                                   
REMARK 500    LYS A 112       16.21     59.56                                   
REMARK 500    PHE A 136       64.68   -119.90                                   
REMARK 500    SER A 150     -131.88     61.63                                   
REMARK 500    ASN A 170       59.61    -91.06                                   
REMARK 500    ASN A 178       59.94     34.02                                   
REMARK 500    GLN A 215       85.20     35.23                                   
REMARK 500    ASN A 216       13.52     83.27                                   
REMARK 500    SER A 242       13.66   -144.68                                   
REMARK 500    ASN A 248      100.09   -161.67                                   
REMARK 500    ASN A 388       74.51     47.32                                   
REMARK 500    GLU A 392      -83.37   -108.27                                   
REMARK 500    ASP A 404      -48.71     79.58                                   
REMARK 500    HIS A 418       -6.21     76.67                                   
REMARK 500    GLN B   8      -78.93    -85.61                                   
REMARK 500    ASP B  44       75.86     58.31                                   
REMARK 500    HIS B  70       23.77   -144.61                                   
REMARK 500    LYS B 112       17.43     59.39                                   
REMARK 500    SER B 150     -131.94     61.86                                   
REMARK 500    ASN B 170       59.09    -90.33                                   
REMARK 500    ASN B 178       60.95     33.38                                   
REMARK 500    SER B 242       13.69   -144.25                                   
REMARK 500    ASN B 248       99.99   -161.45                                   
REMARK 500    ASN B 388       74.44     48.16                                   
REMARK 500    GLU B 392      -83.48   -108.77                                   
REMARK 500    ASP B 404      -47.40     78.75                                   
REMARK 500    HIS B 418       -3.08     73.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1IVY   RELATED DB: PDB                                   
REMARK 900 ZYMOGEN FORM                                                         
REMARK 900 RELATED ID: 4MWT   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AN UNIDENTIFIED PROTEASE CONVERTED THE ZYMOGEN INTO ACTIVE ENZYME.   
REMARK 999 PUTATIVE TERMINI ASSUME PROTEOLYTIC REMOVAL OF 263-292, CONSISTENT   
REMARK 999 WITH MASS SPECTROMETRY AND N-TERMINAL SEQUENCING DATA.               
DBREF  4MWS A    1   452  UNP    P10619   PPGB_HUMAN      29    480             
DBREF  4MWS B    1   452  UNP    P10619   PPGB_HUMAN      29    480             
SEQADV 4MWS     A       UNP  P10619    TYR   291 DELETION                       
SEQADV 4MWS     A       UNP  P10619    GLU   292 DELETION                       
SEQADV 4MWS     A       UNP  P10619    LYS   293 DELETION                       
SEQADV 4MWS     A       UNP  P10619    ASP   294 DELETION                       
SEQADV 4MWS     A       UNP  P10619    THR   295 DELETION                       
SEQADV 4MWS     A       UNP  P10619    VAL   296 DELETION                       
SEQADV 4MWS     A       UNP  P10619    VAL   297 DELETION                       
SEQADV 4MWS     A       UNP  P10619    VAL   298 DELETION                       
SEQADV 4MWS     A       UNP  P10619    GLN   299 DELETION                       
SEQADV 4MWS     A       UNP  P10619    ASP   300 DELETION                       
SEQADV 4MWS     A       UNP  P10619    LEU   301 DELETION                       
SEQADV 4MWS     A       UNP  P10619    GLY   302 DELETION                       
SEQADV 4MWS     A       UNP  P10619    ASN   303 DELETION                       
SEQADV 4MWS     A       UNP  P10619    ILE   304 DELETION                       
SEQADV 4MWS     A       UNP  P10619    PHE   305 DELETION                       
SEQADV 4MWS     A       UNP  P10619    THR   306 DELETION                       
SEQADV 4MWS     A       UNP  P10619    ARG   307 DELETION                       
SEQADV 4MWS     A       UNP  P10619    LEU   308 DELETION                       
SEQADV 4MWS     A       UNP  P10619    PRO   309 DELETION                       
SEQADV 4MWS     A       UNP  P10619    LEU   310 DELETION                       
SEQADV 4MWS     A       UNP  P10619    LYS   311 DELETION                       
SEQADV 4MWS     A       UNP  P10619    ARG   312 DELETION                       
SEQADV 4MWS     A       UNP  P10619    MET   313 DELETION                       
SEQADV 4MWS     A       UNP  P10619    TRP   314 DELETION                       
SEQADV 4MWS     A       UNP  P10619    HIS   315 DELETION                       
SEQADV 4MWS     A       UNP  P10619    GLN   316 DELETION                       
SEQADV 4MWS     A       UNP  P10619    ALA   317 DELETION                       
SEQADV 4MWS     A       UNP  P10619    LEU   318 DELETION                       
SEQADV 4MWS     A       UNP  P10619    LEU   319 DELETION                       
SEQADV 4MWS     A       UNP  P10619    ARG   320 DELETION                       
SEQADV 4MWS HIS A  453  UNP  P10619              EXPRESSION TAG                 
SEQADV 4MWS HIS A  454  UNP  P10619              EXPRESSION TAG                 
SEQADV 4MWS HIS A  455  UNP  P10619              EXPRESSION TAG                 
SEQADV 4MWS HIS A  456  UNP  P10619              EXPRESSION TAG                 
SEQADV 4MWS HIS A  457  UNP  P10619              EXPRESSION TAG                 
SEQADV 4MWS HIS A  458  UNP  P10619              EXPRESSION TAG                 
SEQADV 4MWS     B       UNP  P10619    TYR   291 DELETION                       
SEQADV 4MWS     B       UNP  P10619    GLU   292 DELETION                       
SEQADV 4MWS     B       UNP  P10619    LYS   293 DELETION                       
SEQADV 4MWS     B       UNP  P10619    ASP   294 DELETION                       
SEQADV 4MWS     B       UNP  P10619    THR   295 DELETION                       
SEQADV 4MWS     B       UNP  P10619    VAL   296 DELETION                       
SEQADV 4MWS     B       UNP  P10619    VAL   297 DELETION                       
SEQADV 4MWS     B       UNP  P10619    VAL   298 DELETION                       
SEQADV 4MWS     B       UNP  P10619    GLN   299 DELETION                       
SEQADV 4MWS     B       UNP  P10619    ASP   300 DELETION                       
SEQADV 4MWS     B       UNP  P10619    LEU   301 DELETION                       
SEQADV 4MWS     B       UNP  P10619    GLY   302 DELETION                       
SEQADV 4MWS     B       UNP  P10619    ASN   303 DELETION                       
SEQADV 4MWS     B       UNP  P10619    ILE   304 DELETION                       
SEQADV 4MWS     B       UNP  P10619    PHE   305 DELETION                       
SEQADV 4MWS     B       UNP  P10619    THR   306 DELETION                       
SEQADV 4MWS     B       UNP  P10619    ARG   307 DELETION                       
SEQADV 4MWS     B       UNP  P10619    LEU   308 DELETION                       
SEQADV 4MWS     B       UNP  P10619    PRO   309 DELETION                       
SEQADV 4MWS     B       UNP  P10619    LEU   310 DELETION                       
SEQADV 4MWS     B       UNP  P10619    LYS   311 DELETION                       
SEQADV 4MWS     B       UNP  P10619    ARG   312 DELETION                       
SEQADV 4MWS     B       UNP  P10619    MET   313 DELETION                       
SEQADV 4MWS     B       UNP  P10619    TRP   314 DELETION                       
SEQADV 4MWS     B       UNP  P10619    HIS   315 DELETION                       
SEQADV 4MWS     B       UNP  P10619    GLN   316 DELETION                       
SEQADV 4MWS     B       UNP  P10619    ALA   317 DELETION                       
SEQADV 4MWS     B       UNP  P10619    LEU   318 DELETION                       
SEQADV 4MWS     B       UNP  P10619    LEU   319 DELETION                       
SEQADV 4MWS     B       UNP  P10619    ARG   320 DELETION                       
SEQADV 4MWS HIS B  453  UNP  P10619              EXPRESSION TAG                 
SEQADV 4MWS HIS B  454  UNP  P10619              EXPRESSION TAG                 
SEQADV 4MWS HIS B  455  UNP  P10619              EXPRESSION TAG                 
SEQADV 4MWS HIS B  456  UNP  P10619              EXPRESSION TAG                 
SEQADV 4MWS HIS B  457  UNP  P10619              EXPRESSION TAG                 
SEQADV 4MWS HIS B  458  UNP  P10619              EXPRESSION TAG                 
SEQRES   1 A  428  ALA PRO ASP GLN ASP GLU ILE GLN ARG LEU PRO GLY LEU          
SEQRES   2 A  428  ALA LYS GLN PRO SER PHE ARG GLN TYR SER GLY TYR LEU          
SEQRES   3 A  428  LYS GLY SER GLY SER LYS HIS LEU HIS TYR TRP PHE VAL          
SEQRES   4 A  428  GLU SER GLN LYS ASP PRO GLU ASN SER PRO VAL VAL LEU          
SEQRES   5 A  428  TRP LEU ASN GLY GLY PRO GLY CYS SER SER LEU ASP GLY          
SEQRES   6 A  428  LEU LEU THR GLU HIS GLY PRO PHE LEU VAL GLN PRO ASP          
SEQRES   7 A  428  GLY VAL THR LEU GLU TYR ASN PRO TYR SER TRP ASN LEU          
SEQRES   8 A  428  ILE ALA ASN VAL LEU TYR LEU GLU SER PRO ALA GLY VAL          
SEQRES   9 A  428  GLY PHE SER TYR SER ASP ASP LYS PHE TYR ALA THR ASN          
SEQRES  10 A  428  ASP THR GLU VAL ALA GLN SER ASN PHE GLU ALA LEU GLN          
SEQRES  11 A  428  ASP PHE PHE ARG LEU PHE PRO GLU TYR LYS ASN ASN LYS          
SEQRES  12 A  428  LEU PHE LEU THR GLY GLU SER TYR ALA GLY ILE TYR ILE          
SEQRES  13 A  428  PRO THR LEU ALA VAL LEU VAL MET GLN ASP PRO SER MET          
SEQRES  14 A  428  ASN LEU GLN GLY LEU ALA VAL GLY ASN GLY LEU SER SER          
SEQRES  15 A  428  TYR GLU GLN ASN ASP ASN SER LEU VAL TYR PHE ALA TYR          
SEQRES  16 A  428  TYR HIS GLY LEU LEU GLY ASN ARG LEU TRP SER SER LEU          
SEQRES  17 A  428  GLN THR HIS CYS CYS SER GLN ASN LYS CYS ASN PHE TYR          
SEQRES  18 A  428  ASP ASN LYS ASP LEU GLU CYS VAL THR ASN LEU GLN GLU          
SEQRES  19 A  428  VAL ALA ARG ILE VAL GLY ASN SER GLY LEU ASN ILE TYR          
SEQRES  20 A  428  ASN LEU TYR ALA PRO CYS ALA GLY GLY VAL PRO SER HIS          
SEQRES  21 A  428  PHE ARG SER GLY ASP LYS VAL ARG MET ASP PRO PRO CYS          
SEQRES  22 A  428  THR ASN THR THR ALA ALA SER THR TYR LEU ASN ASN PRO          
SEQRES  23 A  428  TYR VAL ARG LYS ALA LEU ASN ILE PRO GLU GLN LEU PRO          
SEQRES  24 A  428  GLN TRP ASP MET CYS ASN PHE LEU VAL ASN LEU GLN TYR          
SEQRES  25 A  428  ARG ARG LEU TYR ARG SER MET ASN SER GLN TYR LEU LYS          
SEQRES  26 A  428  LEU LEU SER SER GLN LYS TYR GLN ILE LEU LEU TYR ASN          
SEQRES  27 A  428  GLY ASP VAL ASP MET ALA CYS ASN PHE MET GLY ASP GLU          
SEQRES  28 A  428  TRP PHE VAL ASP SER LEU ASN GLN LYS MET GLU VAL GLN          
SEQRES  29 A  428  ARG ARG PRO TRP LEU VAL LYS TYR GLY ASP SER GLY GLU          
SEQRES  30 A  428  GLN ILE ALA GLY PHE VAL LYS GLU PHE SER HIS ILE ALA          
SEQRES  31 A  428  PHE LEU THR ILE LYS GLY ALA GLY HIS MET VAL PRO THR          
SEQRES  32 A  428  ASP LYS PRO LEU ALA ALA PHE THR MET PHE SER ARG PHE          
SEQRES  33 A  428  LEU ASN LYS GLN PRO TYR HIS HIS HIS HIS HIS HIS              
SEQRES   1 B  428  ALA PRO ASP GLN ASP GLU ILE GLN ARG LEU PRO GLY LEU          
SEQRES   2 B  428  ALA LYS GLN PRO SER PHE ARG GLN TYR SER GLY TYR LEU          
SEQRES   3 B  428  LYS GLY SER GLY SER LYS HIS LEU HIS TYR TRP PHE VAL          
SEQRES   4 B  428  GLU SER GLN LYS ASP PRO GLU ASN SER PRO VAL VAL LEU          
SEQRES   5 B  428  TRP LEU ASN GLY GLY PRO GLY CYS SER SER LEU ASP GLY          
SEQRES   6 B  428  LEU LEU THR GLU HIS GLY PRO PHE LEU VAL GLN PRO ASP          
SEQRES   7 B  428  GLY VAL THR LEU GLU TYR ASN PRO TYR SER TRP ASN LEU          
SEQRES   8 B  428  ILE ALA ASN VAL LEU TYR LEU GLU SER PRO ALA GLY VAL          
SEQRES   9 B  428  GLY PHE SER TYR SER ASP ASP LYS PHE TYR ALA THR ASN          
SEQRES  10 B  428  ASP THR GLU VAL ALA GLN SER ASN PHE GLU ALA LEU GLN          
SEQRES  11 B  428  ASP PHE PHE ARG LEU PHE PRO GLU TYR LYS ASN ASN LYS          
SEQRES  12 B  428  LEU PHE LEU THR GLY GLU SER TYR ALA GLY ILE TYR ILE          
SEQRES  13 B  428  PRO THR LEU ALA VAL LEU VAL MET GLN ASP PRO SER MET          
SEQRES  14 B  428  ASN LEU GLN GLY LEU ALA VAL GLY ASN GLY LEU SER SER          
SEQRES  15 B  428  TYR GLU GLN ASN ASP ASN SER LEU VAL TYR PHE ALA TYR          
SEQRES  16 B  428  TYR HIS GLY LEU LEU GLY ASN ARG LEU TRP SER SER LEU          
SEQRES  17 B  428  GLN THR HIS CYS CYS SER GLN ASN LYS CYS ASN PHE TYR          
SEQRES  18 B  428  ASP ASN LYS ASP LEU GLU CYS VAL THR ASN LEU GLN GLU          
SEQRES  19 B  428  VAL ALA ARG ILE VAL GLY ASN SER GLY LEU ASN ILE TYR          
SEQRES  20 B  428  ASN LEU TYR ALA PRO CYS ALA GLY GLY VAL PRO SER HIS          
SEQRES  21 B  428  PHE ARG SER GLY ASP LYS VAL ARG MET ASP PRO PRO CYS          
SEQRES  22 B  428  THR ASN THR THR ALA ALA SER THR TYR LEU ASN ASN PRO          
SEQRES  23 B  428  TYR VAL ARG LYS ALA LEU ASN ILE PRO GLU GLN LEU PRO          
SEQRES  24 B  428  GLN TRP ASP MET CYS ASN PHE LEU VAL ASN LEU GLN TYR          
SEQRES  25 B  428  ARG ARG LEU TYR ARG SER MET ASN SER GLN TYR LEU LYS          
SEQRES  26 B  428  LEU LEU SER SER GLN LYS TYR GLN ILE LEU LEU TYR ASN          
SEQRES  27 B  428  GLY ASP VAL ASP MET ALA CYS ASN PHE MET GLY ASP GLU          
SEQRES  28 B  428  TRP PHE VAL ASP SER LEU ASN GLN LYS MET GLU VAL GLN          
SEQRES  29 B  428  ARG ARG PRO TRP LEU VAL LYS TYR GLY ASP SER GLY GLU          
SEQRES  30 B  428  GLN ILE ALA GLY PHE VAL LYS GLU PHE SER HIS ILE ALA          
SEQRES  31 B  428  PHE LEU THR ILE LYS GLY ALA GLY HIS MET VAL PRO THR          
SEQRES  32 B  428  ASP LYS PRO LEU ALA ALA PHE THR MET PHE SER ARG PHE          
SEQRES  33 B  428  LEU ASN LYS GLN PRO TYR HIS HIS HIS HIS HIS HIS              
MODRES 4MWS ASN B  305  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWS ASN A  117  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWS ASN B  117  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWS ASN A  305  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET    MAN  C   4      11                                                       
HET    FUC  C   5      10                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    BMA  D   3      11                                                       
HET    FUC  D   4      10                                                       
HET    NAG  A 506      14                                                       
HET    GOL  A 507       6                                                       
HET    NAG  B 505      14                                                       
HET    GOL  B 506       6                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    6(C8 H15 N O6)                                               
FORMUL   3  BMA    2(C6 H12 O6)                                                 
FORMUL   3  MAN    C6 H12 O6                                                    
FORMUL   3  FUC    2(C6 H12 O5)                                                 
FORMUL   6  GOL    2(C3 H8 O3)                                                  
FORMUL   9  HOH   *4(H2 O)                                                      
HELIX    1   1 PRO A    2  GLU A    6  5                                   5    
HELIX    2   2 ASP A   44  SER A   48  5                                   5    
HELIX    3   3 SER A   62  GLU A   69  1                                   8    
HELIX    4   4 SER A   88  ILE A   92  5                                   5    
HELIX    5   5 ASN A  117  PHE A  136  1                                  20    
HELIX    6   6 PRO A  137  LYS A  140  5                                   4    
HELIX    7   7 TYR A  151  GLN A  165  1                                  15    
HELIX    8   8 SER A  182  HIS A  197  1                                  16    
HELIX    9   9 LEU A  200  CYS A  213  1                                  14    
HELIX   10  10 ASP A  225  ASN A  241  1                                  17    
HELIX   11  11 THR A  306  ASN A  315  1                                  10    
HELIX   12  12 ASN A  315  LEU A  322  1                                   8    
HELIX   13  13 ASN A  335  GLN A  341  1                                   7    
HELIX   14  14 MET A  349  GLN A  360  1                                  12    
HELIX   15  15 ASN A  376  SER A  386  1                                  11    
HELIX   16  16 MET A  430  LYS A  435  1                                   6    
HELIX   17  17 LYS A  435  ASN A  448  1                                  14    
HELIX   18  18 PRO B    2  GLU B    6  5                                   5    
HELIX   19  19 ASP B   44  SER B   48  5                                   5    
HELIX   20  20 SER B   62  GLU B   69  1                                   8    
HELIX   21  21 SER B   88  ILE B   92  5                                   5    
HELIX   22  22 ASN B  117  PHE B  136  1                                  20    
HELIX   23  23 PRO B  137  LYS B  140  5                                   4    
HELIX   24  24 TYR B  151  GLN B  165  1                                  15    
HELIX   25  25 SER B  182  HIS B  197  1                                  16    
HELIX   26  26 GLY B  201  CYS B  212  1                                  12    
HELIX   27  27 ASP B  225  ASN B  241  1                                  17    
HELIX   28  28 THR B  306  ASN B  315  1                                  10    
HELIX   29  29 ASN B  315  LEU B  322  1                                   8    
HELIX   30  30 ASN B  335  GLN B  341  1                                   7    
HELIX   31  31 MET B  349  GLN B  360  1                                  12    
HELIX   32  32 ASN B  376  SER B  386  1                                  11    
HELIX   33  33 MET B  430  LYS B  435  1                                   6    
HELIX   34  34 LYS B  435  ASN B  448  1                                  14    
SHEET    1   A 3 GLN A  21  LYS A  27  0                                        
SHEET    2   A 3 LYS A  32  VAL A  39 -1  O  TYR A  36   N  GLY A  24           
SHEET    3   A 3 TYR A 108  SER A 109 -1  O  TYR A 108   N  HIS A  33           
SHEET    1   B10 GLN A  21  LYS A  27  0                                        
SHEET    2   B10 LYS A  32  VAL A  39 -1  O  TYR A  36   N  GLY A  24           
SHEET    3   B10 ASN A  94  LEU A  98 -1  O  TYR A  97   N  TRP A  37           
SHEET    4   B10 VAL A  50  LEU A  54  1  N  VAL A  51   O  LEU A  96           
SHEET    5   B10 LEU A 144  GLU A 149  1  O  PHE A 145   N  VAL A  50           
SHEET    6   B10 LEU A 171  GLY A 177  1  O  GLN A 172   N  LEU A 144           
SHEET    7   B10 GLN A 363  GLY A 369  1  O  LEU A 365   N  VAL A 176           
SHEET    8   B10 ILE A 419  ILE A 424  1  O  ILE A 424   N  ASN A 368           
SHEET    9   B10 GLY A 406  PHE A 416 -1  N  PHE A 412   O  THR A 423           
SHEET   10   B10 ARG A 396  TYR A 402 -1  N  ARG A 396   O  VAL A 413           
SHEET    1   C 2 PHE A  73  VAL A  75  0                                        
SHEET    2   C 2 LEU A  82  TYR A  84 -1  O  GLU A  83   N  LEU A  74           
SHEET    1   D 3 GLN B  21  LYS B  27  0                                        
SHEET    2   D 3 LYS B  32  VAL B  39 -1  O  TYR B  36   N  GLY B  24           
SHEET    3   D 3 TYR B 108  SER B 109 -1  O  TYR B 108   N  HIS B  33           
SHEET    1   E10 GLN B  21  LYS B  27  0                                        
SHEET    2   E10 LYS B  32  VAL B  39 -1  O  TYR B  36   N  GLY B  24           
SHEET    3   E10 ASN B  94  LEU B  98 -1  O  TYR B  97   N  TRP B  37           
SHEET    4   E10 VAL B  50  LEU B  54  1  N  VAL B  51   O  LEU B  96           
SHEET    5   E10 LEU B 144  GLU B 149  1  O  PHE B 145   N  VAL B  50           
SHEET    6   E10 LEU B 171  GLY B 177  1  O  GLN B 172   N  LEU B 144           
SHEET    7   E10 GLN B 363  GLY B 369  1  O  LEU B 365   N  VAL B 176           
SHEET    8   E10 ILE B 419  ILE B 424  1  O  ILE B 424   N  ASN B 368           
SHEET    9   E10 GLY B 406  PHE B 416 -1  N  LYS B 414   O  PHE B 421           
SHEET   10   E10 ARG B 396  TYR B 402 -1  N  ARG B 396   O  VAL B 413           
SHEET    1   F 2 PHE B  73  VAL B  75  0                                        
SHEET    2   F 2 LEU B  82  TYR B  84 -1  O  GLU B  83   N  LEU B  74           
SHEET    1   G 2 CYS B 213  SER B 214  0                                        
SHEET    2   G 2 LYS B 217  CYS B 218 -1  O  LYS B 217   N  SER B 214           
SSBOND   1 CYS A   60    CYS A  334                          1555   1555  2.06  
SSBOND   2 CYS A  212    CYS A  228                          1555   1555  2.02  
SSBOND   3 CYS A  213    CYS A  218                          1555   1555  2.05  
SSBOND   4 CYS A  253    CYS A  303                          1555   1555  2.06  
SSBOND   5 CYS B   60    CYS B  334                          1555   1555  2.05  
SSBOND   6 CYS B  212    CYS B  228                          1555   1555  2.05  
SSBOND   7 CYS B  213    CYS B  218                          1555   1555  2.05  
SSBOND   8 CYS B  253    CYS B  303                          1555   1555  2.05  
LINK         ND2 ASN A 117                 C1  NAG C   1     1555   1555  1.44  
LINK         ND2 ASN A 305                 C1  NAG A 506     1555   1555  1.47  
LINK         ND2 ASN B 117                 C1  NAG D   1     1555   1555  1.44  
LINK         ND2 ASN B 305                 C1  NAG B 505     1555   1555  1.44  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.43  
LINK         O3  NAG C   1                 C1  FUC C   5     1555   1555  1.44  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.44  
LINK         O3  BMA C   3                 C1  MAN C   4     1555   1555  1.44  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.44  
LINK         O3  NAG D   1                 C1  FUC D   4     1555   1555  1.45  
LINK         O4  NAG D   2                 C1  BMA D   3     1555   1555  1.46  
CISPEP   1 GLY A   57    PRO A   58          0        -8.07                     
CISPEP   2 SER A  100    PRO A  101          0        -0.41                     
CISPEP   3 GLY B   57    PRO B   58          0        -7.97                     
CISPEP   4 SER B  100    PRO B  101          0        -2.78                     
CRYST1  134.889  134.889   99.805  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007414  0.004280  0.000000        0.00000                         
SCALE2      0.000000  0.008560  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010020        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system