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Database: PDB
Entry: 1AN1
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Original site: 1AN1 
HEADER    COMPLEX (SERINE PROTEASE/INHIBITOR)     26-JUN-97   1AN1              
TITLE     LEECH-DERIVED TRYPTASE INHIBITOR/TRYPSIN COMPLEX                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: E;                                                            
COMPND   4 SYNONYM: LDTI;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TRYPTASE INHIBITOR;                                        
COMPND   8 CHAIN: I;                                                            
COMPND   9 EC: 3.4.21.4;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: PANCREAS;                                                     
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;                             
SOURCE   8 ORGANISM_COMMON: MEDICINAL LEECH;                                    
SOURCE   9 ORGANISM_TAXID: 6421;                                                
SOURCE  10 ORGAN: SALIVARY GLANDS;                                              
SOURCE  11 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  12 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: H449;                                      
SOURCE  15 EXPRESSION_SYSTEM_VARIANT: TR1376, TR1417;                           
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PDP34                                     
KEYWDS    SERINE PROTEINASE INHIBITOR, TRYPTASE INHIBITION, NON-                
KEYWDS   2 CLASSICAL KAZAL-TYPE INHIBITOR, COMPLEX (SERINE                      
KEYWDS   3 PROTEASE/INHIBITOR)                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.PRIESTLE,S.DI MARCO                                               
REVDAT   2   24-FEB-09 1AN1    1       VERSN                                    
REVDAT   1   01-JUL-98 1AN1    0                                                
JRNL        AUTH   S.DI MARCO,J.P.PRIESTLE                                      
JRNL        TITL   STRUCTURE OF THE COMPLEX OF LEECH-DERIVED TRYPTASE           
JRNL        TITL 2 INHIBITOR (LDTI) WITH TRYPSIN AND MODELING OF THE            
JRNL        TITL 3 LDTI-TRYPTASE SYSTEM.                                        
JRNL        REF    STRUCTURE                     V.   5  1465 1997              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   9384562                                                      
JRNL        DOI    10.1016/S0969-2126(97)00296-7                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.POHLIG,G.FENDRICH,R.KNECHT,B.EDER,G.PIECHOTTKA,            
REMARK   1  AUTH 2 C.P.SOMMERHOFF,J.HEIM                                        
REMARK   1  TITL   PURIFICATION, CHARACTERIZATION AND BIOLOGICAL                
REMARK   1  TITL 2 EVALUATION OF RECOMBINANT LEECH-DERIVED TRYPTASE             
REMARK   1  TITL 3 INHIBITOR (RLDTI) EXPRESSED AT HIGH LEVEL IN THE             
REMARK   1  TITL 4 YEAST SACCHAROMYCES CEREVISIAE                               
REMARK   1  REF    EUR.J.BIOCHEM.                V. 241   619 1996              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.P.SOMMERHOFF,C.SOLLNER,R.MENTELE,G.P.PIECHOTTKA,           
REMARK   1  AUTH 2 E.A.AUERSWALD,H.FRITZ                                        
REMARK   1  TITL   A KAZAL-TYPE INHIBITOR OF HUMAN MAST CELL                    
REMARK   1  TITL 2 TRYPTASE: ISOLATION FROM THE MEDICAL LEECH HIRUDO            
REMARK   1  TITL 3 MEDICINALIS, CHARACTERIZATION, AND SEQUENCE                  
REMARK   1  TITL 4 ANALYSIS                                                     
REMARK   1  REF    BIOL.CHEM.HOPPE-SEYLER        V. 375   685 1994              
REMARK   1  REFN                   ISSN 0177-3593                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.03 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 16406                          
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 SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 909                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 12                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.03                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.09                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 15497                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2670                       
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 68                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.036                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1924                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 138                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.98                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.75                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.48                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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  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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : PARAM19X.SUP                                   
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSXD.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.ASD                                     
REMARK   3  TOPOLOGY FILE  3   : TOPH19.WAT                                     
REMARK   3  TOPOLOGY FILE  4   : TOPH19.CAL                                     
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUE 115 WAS REFINED AS D-             
REMARK   3  ASPARTIC ACID. WATER MOLECULE 98 IS LOCATED ON A                    
REMARK   3  CRYSTALLOGRAPHIC 2-FOLD AXIS AND THEREFORE HAS AN OCCUPANCY OF      
REMARK   3  0.5                                                                 
REMARK   4                                                                      
REMARK   4 1AN1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JAN-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 294                                
REMARK 200  PH                             : 8.5                                
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          : ENRAF-NONIUS FR591                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : MARSCALE                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17213                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.030                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : 8.730                              
REMARK 200  R MERGE                    (I) : 0.11540                            
REMARK 200  R SYM                      (I) : 0.11540                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.8200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48460                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48460                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PORCINE PANCREATIC BETA-TRYPSIN (PDB ENTRY 1EPT)     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% V/V 2-PROPANOL, 0.2M AMMONIUM        
REMARK 280  ACETATE, 0.1M TRIS-HCL, PH 8.5 ROOM TEMPERATURE 27 MONTHS FOR       
REMARK 280  GROWTH.                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.43000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.85000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       98.14500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.85000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.85000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       32.71500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.85000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.85000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       98.14500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.85000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.85000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       32.71500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       65.43000            
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: 1440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH E 393  LIES ON A SPECIAL POSITION.                          
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     LYS I     1                                                      
REMARK 465     THR I    42                                                      
REMARK 465     GLY I    43                                                      
REMARK 465     ILE I    44                                                      
REMARK 465     LEU I    45                                                      
REMARK 465     ASN I    46                                                      
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    SER E  37       56.53   -151.15                                   
REMARK 500    HIS E  71      -62.57   -123.65                                   
REMARK 500    SER E 214      -68.76   -126.51                                   
REMARK 500    LYS I   8       37.79    -90.96                                   
REMARK 500    LYS I  11       73.01   -150.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E 409        DISTANCE =  9.87 ANGSTROMS                       
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 E 300  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  70   OE1                                                    
REMARK 620 2 ASN E  72   O    88.2                                              
REMARK 620 3 VAL E  75   O   157.2  85.3                                        
REMARK 620 4 HOH E 355   O    71.3  86.5  86.5                                  
REMARK 620 5 GLU E  77   OE1 100.6  83.6 100.3 167.4                            
REMARK 620 6 GLU E  80   OE2  98.4 167.4  92.3 105.7  84.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: P1                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: BINDING LOOP OF LDTI. LYS I 8 IS THE PRIMARY       
REMARK 800  SPECIFICITY.                                                        
REMARK 800 SITE_IDENTIFIER: CA                                                  
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CALCIUM+2 ION BINDING SITE IN TRYPSIN. BOUND       
REMARK 800  THROUGH SIDE CHAINS OF GLUE 70, GLU E 77, GLU E 80, PEPTIDE         
REMARK 800  CARBONYLS OF ASN E 72 AND VAL E 75 AND HOH 75.                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 300                  
DBREF  1AN1 E   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  1AN1 I    1    46  UNP    P80424   LDTI_HIRME       1     46             
SEQADV 1AN1 DAS E  115  UNP  P00761    ASN   105 MODIFIED RESIDUE               
SEQRES   1 E  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 E  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 E  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 E  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 E  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 E  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 E  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 E  223  SER PRO ALA THR LEU DAS SER ARG VAL ALA THR VAL SER          
SEQRES   9 E  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 E  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 E  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 E  223  SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 E  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 E  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 E  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 E  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 E  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 E  223  ALA ASN                                                      
SEQRES   1 I   46  LYS LYS VAL CYS ALA CYS PRO LYS ILE LEU LYS PRO VAL          
SEQRES   2 I   46  CYS GLY SER ASP GLY ARG THR TYR ALA ASN SER CYS ILE          
SEQRES   3 I   46  ALA ARG CYS ASN GLY VAL SER ILE LYS SER GLU GLY SER          
SEQRES   4 I   46  CYS PRO THR GLY ILE LEU ASN                                  
HET    DAS  E 115       8                                                       
HET     CA  E 300       1                                                       
HETNAM     DAS D-ASPARTIC ACID                                                  
HETNAM      CA CALCIUM ION                                                      
FORMUL   1  DAS    C4 H7 N O4                                                   
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *138(H2 O)                                                    
HELIX    1   1 ALA E   56  CYS E   58  5                                   3    
HELIX    2   2 ASP E  165  SER E  171  1                                   7    
HELIX    3   3 VAL E  231  ALA E  243  5                                  13    
HELIX    4   4 SER I   24  ASN I   30  1                                   7    
SHEET    1   A 7 GLN E  81  ASN E  84  0                                        
SHEET    2   A 7 GLN E  64  LEU E  67 -1  N  LEU E  67   O  GLN E  81           
SHEET    3   A 7 GLN E  30  ASN E  34 -1  N  ASN E  34   O  GLN E  64           
SHEET    4   A 7 HIS E  40  ASN E  48 -1  N  GLY E  44   O  VAL E  31           
SHEET    5   A 7 TRP E  51  SER E  54 -1  N  VAL E  53   O  SER E  45           
SHEET    6   A 7 MET E 104  LEU E 108 -1  N  ILE E 106   O  VAL E  52           
SHEET    7   A 7 ALA E  85  THR E  90 -1  N  ILE E  89   O  LEU E 105           
SHEET    1   B 2 GLU E 135  GLY E 140  0                                        
SHEET    2   B 2 GLN E 156  PRO E 161 -1  N  ALA E 160   O  CYS E 136           
SHEET    1   C 4 MET E 180  VAL E 183  0                                        
SHEET    2   C 4 GLY E 226  LYS E 230 -1  N  TYR E 228   O  ILE E 181           
SHEET    3   C 4 GLN E 204  TRP E 215 -1  N  TRP E 215   O  VAL E 227           
SHEET    4   C 4 PRO E 198  CYS E 201 -1  N  CYS E 201   O  GLN E 204           
SHEET    1   D 2 VAL I  13  GLY I  15  0                                        
SHEET    2   D 2 ILE I  34  GLU I  37 -1  N  SER I  36   O  CYS I  14           
SSBOND   1 CYS E   22    CYS E  157                          1555   1555  2.03  
SSBOND   2 CYS E   42    CYS E   58                          1555   1555  2.03  
SSBOND   3 CYS E  128    CYS E  232                          1555   1555  2.02  
SSBOND   4 CYS E  136    CYS E  201                          1555   1555  2.03  
SSBOND   5 CYS E  168    CYS E  182                          1555   1555  2.04  
SSBOND   6 CYS E  191    CYS E  220                          1555   1555  2.04  
SSBOND   7 CYS I    4    CYS I   29                          1555   1555  2.03  
SSBOND   8 CYS I    6    CYS I   25                          1555   1555  2.01  
SSBOND   9 CYS I   14    CYS I   40                          1555   1555  2.03  
LINK         C   LEU E 114                 N   DAS E 115     1555   1555  1.33  
LINK         C   DAS E 115                 N   SER E 116     1555   1555  1.33  
LINK        CA    CA E 300                 OE1 GLU E  70     1555   1555  2.40  
LINK        CA    CA E 300                 O   ASN E  72     1555   1555  2.34  
LINK        CA    CA E 300                 O   VAL E  75     1555   1555  2.22  
LINK        CA    CA E 300                 O   HOH E 355     1555   1555  2.33  
LINK        CA    CA E 300                 OE1 GLU E  77     1555   1555  2.50  
LINK        CA    CA E 300                 OE2 GLU E  80     1555   1555  2.44  
SLTBRG       OD1 ASP E 189                 NZ  LYS I   8   1555    1555         
SITE     1  P1  1 LYS I   8                                                     
SITE     1  CA  1  CA E 300                                                     
SITE     1 AC1  6 GLU E  70  ASN E  72  VAL E  75  GLU E  77                    
SITE     2 AC1  6 GLU E  80  HOH E 355                                          
CRYST1   63.700   63.700  130.860  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015699  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015699  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007642        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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