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Database: PDB
Entry: 1TRN
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Original site: 1TRN 
HEADER    HYDROLASE (SERINE PROTEINASE)           16-MAR-95   1TRN              
TITLE     CRYSTAL STRUCTURE OF HUMAN TRYPSIN 1: UNEXPECTED                      
TITLE    2 PHOSPHORYLATION OF TYROSINE 151                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    HUMAN TRYPSIN, DFP INHIBITED, HYDROLASE (SERINE PROTEINASE)           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.GABORIAUD,J.C.FONTECILLA-CAMPS                                      
REVDAT   2   24-FEB-09 1TRN    1       VERSN                                    
REVDAT   1   03-JUN-95 1TRN    0                                                
JRNL        AUTH   C.GABORIAUD,L.SERRE,O.GUY-CROTTE,E.FOREST,                   
JRNL        AUTH 2 J.C.FONTECILLA-CAMPS                                         
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN TRYPSIN 1: UNEXPECTED             
JRNL        TITL 2 PHOSPHORYLATION OF TYR151.                                   
JRNL        REF    J.MOL.BIOL.                   V. 259   995 1996              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8683601                                                      
JRNL        DOI    10.1006/JMBI.1996.0376                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
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)   (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 22613                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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            : 3382                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 301                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.50                          
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) : 0.25                            
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) : NULL                            
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  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 1TRN 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        : OCT-92                             
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : LURE                               
REMARK 200  BEAMLINE                       : DW32                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22989                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.04400                            
REMARK 200  R SYM                      (I) : NULL                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
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 300 REMARK: MTRIX                                                        
REMARK 300  THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW                
REMARK 300  DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE               
REMARK 300  VARIOUS DOMAINS IN THIS ENTRY.  APPLYING THE APPROPRIATE            
REMARK 300  MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL              
REMARK 300  YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED               
REMARK 300  SECOND.                                                             
REMARK 300                                                                      
REMARK 300            APPLIED TO           TRANSFORMED TO                       
REMARK 300  MTRIX      RESIDUES               RESIDUES         RMSD             
REMARK 300    M1   B   16  ..  B  302     A   16  ..  A  302   0.311            
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     GLU A   23   OE1                                                 
REMARK 480     GLU A   24   CB    CG    CD    OE1   OE2                         
REMARK 480     ASN A   25   CB    OD1                                           
REMARK 480     TYR A   39   CD1   CE1                                           
REMARK 480     ARG A   62   CG    CD    NE                                      
REMARK 480     GLN A   93   NE2                                                 
REMARK 480     ASP A   95   CB                                                  
REMARK 480     ARG A   96   CG    CD    NH1   NH2                               
REMARK 480     LYS A   97   NZ                                                  
REMARK 480     ARG A  117   NH1   NH2                                           
REMARK 480     GLN A  165   CG    OE1                                           
REMARK 480     PRO A  173   CD                                                  
REMARK 480     LYS A  222   CG    CD                                            
REMARK 480     GLU B   24   C     O     OE2                                     
REMARK 480     ASN B   25   CB    OD1                                           
REMARK 480     SER B   37   CB    OG                                            
REMARK 480     GLY B   38   O                                                   
REMARK 480     TYR B   39   CE1                                                 
REMARK 480     LYS B   60   NZ                                                  
REMARK 480     ILE B   88   CD1                                                 
REMARK 480     LYS B   97   N     CD                                            
REMARK 480     ALA B  145   CB                                                  
REMARK 480     SER B  147   CB    OG                                            
REMARK 480     GLY B  148   O                                                   
REMARK 480     GLN B  165   CG    OE1                                           
REMARK 480     TYR B  172   C     O                                             
REMARK 480     LYS B  175   CB    CG    CD    CE    NZ                          
REMARK 480     GLN B  221   N     CA    O     CB    OE1   NE2                   
REMARK 480     LYS B  222   CG    CD                                            
REMARK 480     LYS B  224   CE                                                  
REMARK 480     PRO B  225   CD                                                  
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  25       44.51     36.54                                   
REMARK 500    ASN A 115     -154.58   -148.57                                   
REMARK 500    SER A 214      -72.09   -108.64                                   
REMARK 500    ASN B 115     -159.08   -145.43                                   
REMARK 500    SER B 214      -64.82   -120.47                                   
REMARK 500    ALA B 221A      19.79     59.89                                   
REMARK 500    ASN B 223       -0.08     66.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B  59         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    SER B  37         10.19                                           
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 B 682        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH B 739        DISTANCE =  5.00 ANGSTROMS                       
REMARK 525    HOH B 751        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH A 743        DISTANCE =  5.73 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAT                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ISP A 301                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ISP B 301                 
DBREF  1TRN A   16   246  UNP    P07477   TRY1_HUMAN      24    247             
DBREF  1TRN B   16   246  UNP    P07477   TRY1_HUMAN      24    247             
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 ARG 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  PTR 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 GLY 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 ARG 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  PTR 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 GLY 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                                                  
MODRES 1TRN PTR A  151  TYR  O-PHOSPHOTYROSINE                                  
MODRES 1TRN PTR B  151  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A 151      16                                                       
HET    PTR  B 151      16                                                       
HET    ISP  A 301       7                                                       
HET    ISP  B 301       7                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     ISP PHOSPHORYLISOPROPANE                                             
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   3  ISP    2(C3 H9 O4 P)                                                
FORMUL   5  HOH   *301(H2 O)                                                    
HELIX    1   2 GLN A  165  SER A  171  1                                   7    
HELIX    2   3 VAL A  231  ASN A  245  5C-TERMINAL HELIX                  15    
HELIX    3   5 GLN B  165  SER B  171  1                                   7    
HELIX    4   6 VAL B  231  ASN B  245  5C-TERMINAL HELIX                  15    
SHEET    1   A 7 GLN A  81  ALA A  85  0                                        
SHEET    2   A 7 GLN A  64  LEU A  67 -1  N  LEU A  67   O  GLN A  81           
SHEET    3   A 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  GLN A  64           
SHEET    4   A 7 PHE A  41  ASN A  48 -1  N  GLY A  44   O  VAL A  31           
SHEET    5   A 7 TRP A  51  SER A  54 -1  N  VAL A  53   O  SER A  45           
SHEET    6   A 7 MET A 104  LEU A 108 -1  N  ILE A 106   O  VAL A  52           
SHEET    7   A 7 ALA A  86  HIS A  91 -1  N  ILE A  89   O  LEU A 105           
SHEET    1   B 7 GLN A 156  ASP A 159  0                                        
SHEET    2   B 7 LYS A 135  GLY A 140 -1  N  GLY A 140   O  GLN A 156           
SHEET    3   B 7 GLY A 197  CYS A 201 -1  N  VAL A 200   O  LEU A 137           
SHEET    4   B 7 GLN A 210  TRP A 215 -1  N  GLY A 211   O  VAL A 199           
SHEET    5   B 7 GLY A 226  LYS A 230 -1  N  THR A 229   O  VAL A 212           
SHEET    6   B 7 MET A 180  GLY A 184A-1  N  VAL A 183   O  GLY A 226           
SHEET    7   B 7 ALA A 160  LEU A 163 -1  N  LEU A 163   O  CYS A 182           
SHEET    1   C 7 GLN B  81  ALA B  85  0                                        
SHEET    2   C 7 GLN B  64  LEU B  67 -1  N  LEU B  67   O  GLN B  81           
SHEET    3   C 7 GLN B  30  ASN B  34 -1  N  ASN B  34   O  GLN B  64           
SHEET    4   C 7 PHE B  41  ASN B  48 -1  N  GLY B  44   O  VAL B  31           
SHEET    5   C 7 TRP B  51  SER B  54 -1  N  VAL B  53   O  SER B  45           
SHEET    6   C 7 MET B 104  LEU B 108 -1  N  ILE B 106   O  VAL B  52           
SHEET    7   C 7 ALA B  86  HIS B  91 -1  N  ILE B  89   O  LEU B 105           
SHEET    1   D 7 GLN B 156  ASP B 159  0                                        
SHEET    2   D 7 LYS B 135  GLY B 140 -1  N  GLY B 140   O  GLN B 156           
SHEET    3   D 7 GLY B 197  CYS B 201 -1  N  VAL B 200   O  LEU B 137           
SHEET    4   D 7 GLN B 210  TRP B 215 -1  N  GLY B 211   O  VAL B 199           
SHEET    5   D 7 GLY B 226  LYS B 230 -1  N  THR B 229   O  VAL B 212           
SHEET    6   D 7 MET B 180  GLY B 184A-1  N  VAL B 183   O  GLY B 226           
SHEET    7   D 7 ALA B 160  LEU B 163 -1  N  LEU B 163   O  CYS B 182           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.05  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.08  
SSBOND   3 CYS A  136    CYS A  201                          1555   1555  2.04  
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  2.04  
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.03  
SSBOND   6 CYS B   22    CYS B  157                          1555   1555  2.03  
SSBOND   7 CYS B   42    CYS B   58                          1555   1555  2.03  
SSBOND   8 CYS B  136    CYS B  201                          1555   1555  2.03  
SSBOND   9 CYS B  168    CYS B  182                          1555   1555  2.03  
SSBOND  10 CYS B  191    CYS B  220                          1555   1555  2.03  
LINK         C   ASP A 150                 N   PTR A 151     1555   1555  1.33  
LINK         C   PTR A 151                 N   PRO A 152     1555   1555  1.35  
LINK         OG  SER A 195                 P   ISP A 301     1555   1555  1.59  
LINK         C   ASP B 150                 N   PTR B 151     1555   1555  1.33  
LINK         C   PTR B 151                 N   PRO B 152     1555   1555  1.33  
LINK         OG  SER B 195                 P   ISP B 301     1555   1555  1.58  
SITE     1 CAT  6 SER A 195  HIS A  57  ASP A 102  SER B 195                    
SITE     2 CAT  6 HIS B  57  ASP B 102                                          
SITE     1 AC1  7 HIS A  57  CYS A 191  GLN A 192  GLY A 193                    
SITE     2 AC1  7 ASP A 194  SER A 195  VAL A 213                               
SITE     1 AC2  8 HIS B  57  CYS B 191  GLN B 192  GLY B 193                    
SITE     2 AC2  8 ASP B 194  SER B 195  VAL B 213  SER B 214                    
CRYST1  107.120  107.120   39.920  90.00  90.00  90.00 P 4           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      0.009335  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009335  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025050        0.00000                         
MTRIX1   1  0.683235 -0.730181  0.005026        2.47110    1                    
MTRIX2   1 -0.730173 -0.683252 -0.003589       75.82290    1                    
MTRIX3   1  0.006055 -0.001218 -0.999981       24.09780    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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