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Database: PDB
Entry: 2A31
LinkDB: 2A31
Original site: 2A31 
HEADER    HYDROLASE                               23-JUN-05   2A31              
TITLE     TRYPSIN IN COMPLEX WITH BORATE                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.4                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: PANCREAS                                                      
KEYWDS    HYDROLASE, TRYPSIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.R.TRANSUE,S.A.GABEL,R.E.LONDON                                      
REVDAT   2   24-FEB-09 2A31    1       VERSN                                    
REVDAT   1   04-JUL-06 2A31    0                                                
JRNL        AUTH   T.R.TRANSUE,S.A.GABEL,R.E.LONDON                             
JRNL        TITL   NMR AND CRYSTALLOGRAPHIC CHARACTERIZATION OF                 
JRNL        TITL 2 ADVENTITIOUS BORATE BINDING BY TRYPSIN.                      
JRNL        REF    BIOCONJUG.CHEM.               V.  17   300 2006              
JRNL        REFN                   ISSN 1043-1802                               
JRNL        PMID   16536459                                                     
JRNL        DOI    10.1021/BC0502210                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.R.TRANSUE,J.M.KRAHN,S.A.GABEL,E.F.DEROSE,                  
REMARK   1  AUTH 2 R.E.LONDON                                                   
REMARK   1  TITL   X-RAY AND NMR CHARACTERIZATION OF COVALENT                   
REMARK   1  TITL 2 COMPLEXES OF TRYPSIN, BORATE, AND ALCOHOLS                   
REMARK   1  REF    BIOCHEMISTRY                  V.  43  2829 2004              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : AMBER                                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 46307                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : 5 % RANDOM                      
REMARK   3   R VALUE            (WORKING SET) : 0.140                           
REMARK   3   FREE R VALUE                     : 0.162                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2347                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3489                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 1239                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.57400                                             
REMARK   3    B22 (A**2) : 0.54500                                              
REMARK   3    B33 (A**2) : 0.02900                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.91                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : 0.47                                                 
REMARK   3   BSOL        : 61.80                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2A31 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033427.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47257                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.6                               
REMARK 200  DATA REDUNDANCY                : 12.300                             
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.31000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1S5S                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MGSO4, HEPES, CACL2, PH 8.0, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 300K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.15200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.23300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.72300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       23.23300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.15200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.72300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     SER A  153   CB    OG                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 220   CB    CYS A 220   SG     -0.104                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A  22   CA  -  CB  -  SG  ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ARG A  66   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    PHE A  82   CB  -  CG  -  CD2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    PHE A  82   CB  -  CG  -  CD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TYR A 217   CB  -  CG  -  CD2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    CYS A 220   CB  -  CA  -  C   ANGL. DEV. =   8.6 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    HIS A  71      -68.24   -122.38                                   
REMARK 500    ASN A 115     -167.15   -160.80                                   
REMARK 500    SER A 214      -71.70   -124.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     BO4 A  901                                                       
REMARK 610     BO4 A  512                                                       
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 A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE1                                                    
REMARK 620 2 ASN A  72   O    92.0                                              
REMARK 620 3 VAL A  75   O   176.5  87.4                                        
REMARK 620 4 GLU A  80   OE2  93.1 160.8  88.7                                  
REMARK 620 5 HOH A1215   O    80.7  88.9 102.7  73.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 503  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE1                                                    
REMARK 620 2 ASN A  72   O    85.7                                              
REMARK 620 3 VAL A  75   O   151.5  77.9                                        
REMARK 620 4 GLU A  77   OE1  96.8  91.1 106.6                                  
REMARK 620 5 GLU A  80   OE2 103.0 170.7  92.8  91.1                            
REMARK 620 6 HOH A 975   O    78.2  86.7  77.7 174.7  91.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 504  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1159   O                                                      
REMARK 620 2 HOH A1161   O    87.4                                              
REMARK 620 3 HOH A1162   O    97.2  87.0                                        
REMARK 620 4 HOH A1158   O    92.0 179.0  92.3                                  
REMARK 620 5 HOH A1115   O    96.7  84.1 163.1  96.7                            
REMARK 620 6 HOH A1160   O   178.1  93.9  84.3  86.7  82.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 505  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1233   O                                                      
REMARK 620 2 HOH A1170   O    90.5                                              
REMARK 620 3 HOH A1138   O    87.6  83.5                                        
REMARK 620 4 HOH A1168   O   175.2  90.3  87.8                                  
REMARK 620 5 HOH A1167   O    99.9 169.2  99.6  79.6                            
REMARK 620 6 HOH A1169   O   103.1  75.9 156.8  81.7  98.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 506  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1014   O                                                      
REMARK 620 2 HOH A1151   O    97.7                                              
REMARK 620 3 HOH A 944   O    69.4 107.1                                        
REMARK 620 4 HOH A1152   O   106.2 153.2  92.9                                  
REMARK 620 5 GLU A  80   O   146.7  80.8  79.2  85.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 503                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 504                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 505                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 506                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 511                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 A 901                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG3 A 501                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO4 A 512                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1S5S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1S6F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1S6H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1S81   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1S82   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1S83   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1S84   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1S85   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2A32   RELATED DB: PDB                                   
DBREF  2A31 A   16   245  UNP    P00761   TRYP_PIG         9    231             
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 A  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 A  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 A  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 A  223  SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 A  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 A  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 A  223  ALA ASN                                                      
HET     CA  A 502       1                                                       
HET     MG  A 503       1                                                       
HET     MG  A 504       1                                                       
HET     MG  A 505       1                                                       
HET     NA  A 506       1                                                       
HET    SO4  A 511       5                                                       
HET    BO4  A 901       5                                                       
HET    PG3  A 501      40                                                       
HET    BO4  A 512       7                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     BO4 BORATE ION                                                       
HETNAM     PG3 GUANIDINE-3-PROPANOL                                             
FORMUL   2   CA    CA 2+                                                        
FORMUL   3   MG    3(MG 2+)                                                     
FORMUL   6   NA    NA 1+                                                        
FORMUL   7  SO4    O4 S 2-                                                      
FORMUL   8  BO4    2(B H4 O4 1-)                                                
FORMUL   9  PG3    C4 H12 N3 O 1+                                               
FORMUL  11  HOH   *339(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 SER A  164  TYR A  172  1                                   9    
HELIX    3   3 TYR A  234  ASN A  245  1                                  12    
SHEET    1   A 7 TYR A  20  THR A  21  0                                        
SHEET    2   A 7 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3   A 7 GLU A 135  GLY A 140 -1  N  ILE A 138   O  LEU A 158           
SHEET    4   A 7 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5   A 7 GLN A 204  TRP A 215 -1  O  GLN A 204   N  CYS A 201           
SHEET    6   A 7 VAL A 227  LYS A 230 -1  O  VAL A 227   N  TRP A 215           
SHEET    7   A 7 MET A 180  CYS A 182 -1  N  ILE A 181   O  TYR A 228           
SHEET    1   B 7 GLN A  30  ASN A  34  0                                        
SHEET    2   B 7 HIS A  40  ASN A  48 -1  O  CYS A  42   N  LEU A  33           
SHEET    3   B 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   B 7 MET A 104  LEU A 108 -1  O  MET A 104   N  SER A  54           
SHEET    5   B 7 GLN A  81  THR A  90 -1  N  ALA A  86   O  LYS A 107           
SHEET    6   B 7 GLN A  64  LEU A  67 -1  N  LEU A  67   O  GLN A  81           
SHEET    7   B 7 GLN A  30  ASN A  34 -1  N  SER A  32   O  ARG A  66           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.03  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.06  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.04  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.01  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.11  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.14  
LINK         OE1 GLU A  70                CA  A CA A 502     1555   1555  2.14  
LINK         OE1 GLU A  70                MG  B MG A 503     1555   1555  2.13  
LINK         O   ASN A  72                CA  A CA A 502     1555   1555  2.10  
LINK         O   ASN A  72                MG  B MG A 503     1555   1555  2.35  
LINK         O   VAL A  75                CA  A CA A 502     1555   1555  2.06  
LINK         O   VAL A  75                MG  B MG A 503     1555   1555  2.21  
LINK         OE1BGLU A  77                MG  B MG A 503     1555   1555  2.14  
LINK         OE2 GLU A  80                CA  A CA A 502     1555   1555  2.25  
LINK         OE2 GLU A  80                MG  B MG A 503     1555   1555  1.95  
LINK        CA  A CA A 502                 O  AHOH A1215     1555   1555  2.25  
LINK        MG  B MG A 503                 O   HOH A 975     1555   1555  2.36  
LINK        MG    MG A 504                 O   HOH A1159     1555   1555  2.29  
LINK        MG    MG A 504                 O   HOH A1161     1555   1555  2.14  
LINK        MG    MG A 504                 O   HOH A1162     1555   1555  2.19  
LINK        MG    MG A 504                 O   HOH A1158     1555   1555  2.01  
LINK        MG    MG A 504                 O   HOH A1115     1555   1555  2.27  
LINK        MG    MG A 504                 O   HOH A1160     1555   1555  2.32  
LINK        MG    MG A 505                 O  BHOH A1233     1555   1555  2.04  
LINK        MG    MG A 505                 O   HOH A1170     1555   1555  2.09  
LINK        MG    MG A 505                 O  BHOH A1138     1555   1555  2.14  
LINK        MG    MG A 505                 O   HOH A1168     1555   1555  2.18  
LINK        MG    MG A 505                 O   HOH A1167     1555   1555  2.19  
LINK        NA    NA A 506                 O   HOH A1014     1555   1555  2.76  
LINK        NA    NA A 506                 O   HOH A1151     1555   1555  2.50  
LINK        NA    NA A 506                 O   HOH A 944     1555   1555  2.36  
LINK        NA    NA A 506                 O   HOH A1152     1555   1555  2.42  
LINK         OG ASER A 164                 B  ABO4 A 901     1555   1555  1.40  
LINK         OG ASER A 167                 B  ABO4 A 901     1555   1555  1.41  
LINK        MG    MG A 505                 O   HOH A1169     1555   1555  2.61  
LINK        NA    NA A 506                 O   GLU A  80     1555   1556  2.27  
SITE     1 AC1  7 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC1  7 GLU A  80  HOH A 975  HOH A1215                               
SITE     1 AC2  7 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC2  7 GLU A  80  HOH A 975  HOH A1215                               
SITE     1 AC3  6 HOH A1115  HOH A1158  HOH A1159  HOH A1160                    
SITE     2 AC3  6 HOH A1161  HOH A1162                                          
SITE     1 AC4  7 HOH A1138  HOH A1165  HOH A1167  HOH A1168                    
SITE     2 AC4  7 HOH A1169  HOH A1170  HOH A1233                               
SITE     1 AC5  6 GLY A  78  GLU A  80  HOH A 944  HOH A1014                    
SITE     2 AC5  6 HOH A1151  HOH A1152                                          
SITE     1 AC6  5 ARG A  66  HOH A1009  HOH A1086  HOH A1179                    
SITE     2 AC6  5 HOH A1183                                                     
SITE     1 AC7  4 SER A 164  SER A 167  HOH A1092  HOH A1234                    
SITE     1 AC8 17 HIS A  57  SER A 127  ASP A 189  SER A 190                    
SITE     2 AC8 17 CYS A 191  GLN A 192  SER A 195  VAL A 213                    
SITE     3 AC8 17 SER A 214  TRP A 215  GLY A 216  GLY A 219                    
SITE     4 AC8 17 GLY A 226  HOH A 940  HOH A 983  HOH A1067                    
SITE     5 AC8 17 HOH A1214                                                     
SITE     1 AC9 10 SER A  37  LYS A  60  SER A  61  ARG A  62                    
SITE     2 AC9 10 SER A 164  ASP A 165  SER A 166  HOH A1011                    
SITE     3 AC9 10 HOH A1230  HOH A1235                                          
CRYST1   76.304   53.446   46.466  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013105  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018710  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021521        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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