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Database: PDB
Entry: 4WWY
LinkDB: 4WWY
Original site: 4WWY 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           12-NOV-14   4WWY              
TITLE     HUMAN CATIONIC TRYPSIN G193R MUTANT IN COMPLEX WITH BOVINE PANCREATIC 
TITLE    2 TRYPSIN INHIBITOR                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN-1;                                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 24-247;                                       
COMPND   5 SYNONYM: BETA-TRYPSIN,CATIONIC TRYPSINOGEN,SERINE PROTEASE 1,TRYPSIN 
COMPND   6 I;                                                                   
COMPND   7 EC: 3.4.21.4;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;                              
COMPND  12 CHAIN: C, I;                                                         
COMPND  13 FRAGMENT: UNP RESIDUES 36-93;                                        
COMPND  14 SYNONYM: APROTININ,BASIC PROTEASE INHIBITOR,BPTI;                    
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: PANCREAS;                                                     
SOURCE   6 GENE: PRSS1, TRP1, TRY1, TRYP1;                                      
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTRAP-T7;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  13 ORGANISM_COMMON: BOVINE;                                             
SOURCE  14 ORGANISM_TAXID: 9913;                                                
SOURCE  15 ORGAN: PANCREAS;                                                     
SOURCE  16 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: X-33;                                      
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PPICZA                                    
KEYWDS    TRYPSIN INHIBITORS, COMPLEX, BPTI, HYDROLASE-HYDROLASE INHIBITOR      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ALLOY,O.KAYODE,A.S.SOARES,R.WANG,E.S.RADISKY                        
REVDAT   6   04-DEC-19 4WWY    1       REMARK                                   
REVDAT   5   13-SEP-17 4WWY    1       JRNL   REMARK                            
REVDAT   4   09-SEP-15 4WWY    1       JRNL                                     
REVDAT   3   19-AUG-15 4WWY    1       REMARK                                   
REVDAT   2   29-JUL-15 4WWY    1       JRNL                                     
REVDAT   1   22-JUL-15 4WWY    0                                                
JRNL        AUTH   A.P.ALLOY,O.KAYODE,R.WANG,A.HOCKLA,A.S.SOARES,E.S.RADISKY    
JRNL        TITL   MESOTRYPSIN HAS EVOLVED FOUR UNIQUE RESIDUES TO CLEAVE       
JRNL        TITL 2 TRYPSIN INHIBITORS AS SUBSTRATES.                            
JRNL        REF    J.BIOL.CHEM.                  V. 290 21523 2015              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   26175157                                                     
JRNL        DOI    10.1074/JBC.M115.662429                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 59179                          
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) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3029                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2157                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 46.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 108                          
REMARK   3   BIN FREE R VALUE                    : 0.4410                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4278                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 390                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.03000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.110         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.108         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.069         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.130         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4488 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4147 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6108 ; 1.957 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9515 ; 0.902 ; 3.007       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   576 ; 6.659 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   195 ;34.779 ;24.564       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   719 ;12.642 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;14.887 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   652 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5219 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1045 ; 0.001 ; 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   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4WWY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204359.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 1                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59179                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 45.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.210                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 2RA3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M SODIUM       
REMARK 280  CACODYLATE TRIHYDRATE, 30% PEG-8000, PH 6.5, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       31.61350            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I                                  
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  23    CD   OE1  OE2                                       
REMARK 470     HIS A  71    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS A 117    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 236    NZ                                                  
REMARK 470     HIS B  71    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS B 117    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  96   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP A 153   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASP B 189   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 115     -165.38   -161.32                                   
REMARK 500    ARG A 193       -8.68     86.71                                   
REMARK 500    SER A 214      -73.31   -131.70                                   
REMARK 500    SER B  37       63.77   -150.34                                   
REMARK 500    HIS B  71      -68.65   -109.40                                   
REMARK 500    ASN B 115     -163.49   -163.03                                   
REMARK 500    ARG B 193       -8.85     91.45                                   
REMARK 500    SER B 214      -71.49   -122.62                                   
REMARK 500    ASN C  44      110.33   -160.77                                   
REMARK 500    ASN I  44      106.95   -160.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  70   OE2                                                    
REMARK 620 2 ILE B  73   O   112.4                                              
REMARK 620 3 HOH B 533   O   111.1  85.9                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 102                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4WXV   RELATED DB: PDB                                   
DBREF  4WWY A   16   246  UNP    P07477   TRY1_HUMAN      24    247             
DBREF  4WWY B   16   246  UNP    P07477   TRY1_HUMAN      24    247             
DBREF  4WWY C    1    58  UNP    P00974   BPT1_BOVIN      36     93             
DBREF  4WWY I    1    58  UNP    P00974   BPT1_BOVIN      36     93             
SEQADV 4WWY HIS A  117  UNP  P07477    ARG   122 ENGINEERED MUTATION            
SEQADV 4WWY ARG A  193  UNP  P07477    GLY   198 ENGINEERED MUTATION            
SEQADV 4WWY HIS B  117  UNP  P07477    ARG   122 ENGINEERED MUTATION            
SEQADV 4WWY ARG B  193  UNP  P07477    GLY   198 ENGINEERED MUTATION            
SEQRES   1 A  224  ILE VAL GLY GLY TYR ASN CYS GLU GLU ASN SER VAL PRO          
SEQRES   2 A  224  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 A  224  GLY SER LEU ILE ASN GLU GLN TRP VAL VAL SER ALA GLY          
SEQRES   4 A  224  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  224  HIS ASN ILE GLU VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  224  ASN ALA ALA LYS ILE ILE ARG HIS PRO GLN TYR ASP ARG          
SEQRES   7 A  224  LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  224  SER ARG ALA VAL ILE ASN ALA HIS VAL SER THR ILE SER          
SEQRES   9 A  224  LEU PRO THR ALA PRO PRO ALA THR GLY THR LYS CYS LEU          
SEQRES  10 A  224  ILE SER GLY TRP GLY ASN THR ALA SER SER GLY ALA ASP          
SEQRES  11 A  224  TYR PRO ASP GLU LEU GLN CYS LEU ASP ALA PRO VAL LEU          
SEQRES  12 A  224  SER GLN ALA LYS CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 A  224  THR SER ASN MET PHE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 A  224  LYS ASP SER CYS GLN ARG ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  224  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY ASP          
SEQRES  16 A  224  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  224  VAL TYR ASN TYR VAL LYS TRP ILE LYS ASN THR ILE ALA          
SEQRES  18 A  224  ALA ASN SER                                                  
SEQRES   1 B  224  ILE VAL GLY GLY TYR ASN CYS GLU GLU ASN SER VAL PRO          
SEQRES   2 B  224  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 B  224  GLY SER LEU ILE ASN GLU GLN TRP VAL VAL SER ALA GLY          
SEQRES   4 B  224  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 B  224  HIS ASN ILE GLU VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 B  224  ASN ALA ALA LYS ILE ILE ARG HIS PRO GLN TYR ASP ARG          
SEQRES   7 B  224  LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 B  224  SER ARG ALA VAL ILE ASN ALA HIS VAL SER THR ILE SER          
SEQRES   9 B  224  LEU PRO THR ALA PRO PRO ALA THR GLY THR LYS CYS LEU          
SEQRES  10 B  224  ILE SER GLY TRP GLY ASN THR ALA SER SER GLY ALA ASP          
SEQRES  11 B  224  TYR PRO ASP GLU LEU GLN CYS LEU ASP ALA PRO VAL LEU          
SEQRES  12 B  224  SER GLN ALA LYS CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 B  224  THR SER ASN MET PHE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 B  224  LYS ASP SER CYS GLN ARG ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 B  224  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY ASP          
SEQRES  16 B  224  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 B  224  VAL TYR ASN TYR VAL LYS TRP ILE LYS ASN THR ILE ALA          
SEQRES  18 B  224  ALA ASN SER                                                  
SEQRES   1 C   58  ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO          
SEQRES   2 C   58  CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS          
SEQRES   3 C   58  ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG          
SEQRES   4 C   58  ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET          
SEQRES   5 C   58  ARG THR CYS GLY GLY ALA                                      
SEQRES   1 I   58  ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO          
SEQRES   2 I   58  CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS          
SEQRES   3 I   58  ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG          
SEQRES   4 I   58  ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET          
SEQRES   5 I   58  ARG THR CYS GLY GLY ALA                                      
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HET    SO4  A 303       5                                                       
HET     CA  B 301       1                                                       
HET    SO4  B 302       5                                                       
HET    SO4  C 101      10                                                       
HET    SO4  C 102       5                                                       
HET    SO4  I 101       5                                                       
HET    SO4  I 102      10                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
FORMUL   5  SO4    8(O4 S 2-)                                                   
FORMUL   8   CA    CA 2+                                                        
FORMUL  14  HOH   *390(H2 O)                                                    
HELIX    1 AA1 ALA A   55  TYR A   59  5                                   5    
HELIX    2 AA2 SER A  164  TYR A  172  1                                   9    
HELIX    3 AA3 TYR A  234  ASN A  245  1                                  12    
HELIX    4 AA4 ALA B   55  TYR B   59  5                                   5    
HELIX    5 AA5 SER B  164  TYR B  172  1                                   9    
HELIX    6 AA6 TYR B  234  ASN B  245  1                                  12    
HELIX    7 AA7 PRO C    2  GLU C    7  5                                   6    
HELIX    8 AA8 SER C   47  CYS C   55  1                                   9    
HELIX    9 AA9 PRO I    2  GLU I    7  5                                   6    
HELIX   10 AB1 SER I   47  GLY I   56  1                                  10    
SHEET    1 AA1 7 TYR A  20  ASN A  21  0                                        
SHEET    2 AA1 7 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3 AA1 7 LYS A 135  GLY A 140 -1  N  ILE A 138   O  LEU A 158           
SHEET    4 AA1 7 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5 AA1 7 GLN A 204  TRP A 215 -1  O  GLN A 204   N  CYS A 201           
SHEET    6 AA1 7 GLY A 226  LYS A 230 -1  O  VAL A 227   N  TRP A 215           
SHEET    7 AA1 7 MET A 180  VAL A 183 -1  N  PHE A 181   O  TYR A 228           
SHEET    1 AA2 7 GLN A  30  ASN A  34  0                                        
SHEET    2 AA2 7 HIS A  40  ASN A  48 -1  O  CYS A  42   N  LEU A  33           
SHEET    3 AA2 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4 AA2 7 MET A 104  LEU A 108 -1  O  ILE A 106   N  VAL A  52           
SHEET    5 AA2 7 GLN A  81  ARG A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    6 AA2 7 GLN A  64  LEU A  67 -1  N  LEU A  67   O  GLN A  81           
SHEET    7 AA2 7 GLN A  30  ASN A  34 -1  N  SER A  32   O  ARG A  66           
SHEET    1 AA3 7 TYR B  20  ASN B  21  0                                        
SHEET    2 AA3 7 GLN B 156  PRO B 161 -1  O  CYS B 157   N  TYR B  20           
SHEET    3 AA3 7 LYS B 135  GLY B 140 -1  N  ILE B 138   O  LEU B 158           
SHEET    4 AA3 7 PRO B 198  CYS B 201 -1  O  VAL B 200   N  LEU B 137           
SHEET    5 AA3 7 GLN B 204  TRP B 215 -1  O  GLN B 204   N  CYS B 201           
SHEET    6 AA3 7 GLY B 226  LYS B 230 -1  O  VAL B 227   N  TRP B 215           
SHEET    7 AA3 7 MET B 180  VAL B 183 -1  N  PHE B 181   O  TYR B 228           
SHEET    1 AA4 7 GLN B  30  ASN B  34  0                                        
SHEET    2 AA4 7 HIS B  40  ASN B  48 -1  O  CYS B  42   N  LEU B  33           
SHEET    3 AA4 7 TRP B  51  SER B  54 -1  O  VAL B  53   N  SER B  45           
SHEET    4 AA4 7 MET B 104  LEU B 108 -1  O  ILE B 106   N  VAL B  52           
SHEET    5 AA4 7 GLN B  81  ARG B  90 -1  N  ILE B  89   O  LEU B 105           
SHEET    6 AA4 7 GLN B  64  LEU B  67 -1  N  VAL B  65   O  ILE B  83           
SHEET    7 AA4 7 GLN B  30  ASN B  34 -1  N  ASN B  34   O  GLN B  64           
SHEET    1 AA5 2 ILE C  18  ASN C  24  0                                        
SHEET    2 AA5 2 LEU C  29  TYR C  35 -1  O  GLN C  31   N  PHE C  22           
SHEET    1 AA6 2 ILE I  18  ASN I  24  0                                        
SHEET    2 AA6 2 LEU I  29  TYR I  35 -1  O  GLN I  31   N  PHE I  22           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.05  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.01  
SSBOND   3 CYS A  136    CYS A  201                          1555   1555  1.99  
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  2.04  
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.16  
SSBOND   6 CYS B   22    CYS B  157                          1555   1555  2.03  
SSBOND   7 CYS B   42    CYS B   58                          1555   1555  2.00  
SSBOND   8 CYS B  136    CYS B  201                          1555   1555  2.06  
SSBOND   9 CYS B  168    CYS B  182                          1555   1555  2.05  
SSBOND  10 CYS B  191    CYS B  220                          1555   1555  2.12  
SSBOND  11 CYS C    5    CYS C   55                          1555   1555  2.06  
SSBOND  12 CYS C   14    CYS C   38                          1555   1555  2.08  
SSBOND  13 CYS C   30    CYS C   51                          1555   1555  2.17  
SSBOND  14 CYS I    5    CYS I   55                          1555   1555  2.07  
SSBOND  15 CYS I   14    CYS I   38                          1555   1555  2.09  
SSBOND  16 CYS I   30    CYS I   51                          1555   1555  2.16  
LINK         OE2 GLU B  70                CA    CA B 301     1555   1555  2.63  
LINK         O   ILE B  73                CA    CA B 301     1555   1555  2.95  
LINK        CA    CA B 301                 O   HOH B 533     1555   1555  3.10  
SITE     1 AC1  4 LYS A  60  SER A  61  HOH A 489  LYS C  46                    
SITE     1 AC2  3 THR A 177  SER A 178  HOH A 526                               
SITE     1 AC3  3 ARG A 111  HOH A 433  HOH A 536                               
SITE     1 AC4  4 HIS B  40  ARG B  66  GLU B  70  ILE B  73                    
SITE     1 AC5  6 LYS B  97  LEU B  99  LYS B 175  TRP B 215                    
SITE     2 AC5  6 HOH B 422  ARG I  39                                          
SITE     1 AC6 11 ARG A  96  HOH A 429  ARG C  20  TYR C  35                    
SITE     2 AC6 11 GLY C  37  ARG C  39  ALA C  40  HOH C 201                    
SITE     3 AC6 11 HOH C 202  HOH C 209  HOH C 233                               
SITE     1 AC7  5 GLU C   7  ARG C  42  HOH C 210  HOH C 214                    
SITE     2 AC7  5 HOH C 215                                                     
SITE     1 AC8  4 GLU I   7  LYS I  41  ARG I  42  HOH I 222                    
SITE     1 AC9  9 ARG B  96  HOH B 452  ARG I  20  TYR I  35                    
SITE     2 AC9  9 GLY I  37  ARG I  39  ALA I  40  HOH I 202                    
SITE     3 AC9  9 HOH I 206                                                     
CRYST1   52.952   63.227   90.535  90.00  94.74  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018885  0.000000  0.001567        0.00000                         
SCALE2      0.000000  0.015816  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011083        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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