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Database: PDB
Entry: 1CWE
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Original site: 1CWE 
HEADER    TRANSFERASE/PEPTIDE                     06-SEP-95   1CWE              
TITLE     HUMAN P56LCK TYROSINE KINASE COMPLEXED WITH PHOSPHOPEPTIDE            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: P56LCK TYROSINE KINASE;                                    
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: PHOSPHOTYROSINE RECOGNITION DOMAIN SH2;                    
COMPND   5 EC: 2.7.1.112;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PHOSPHOPEPTIDE ACQ-PMP-GLU-GLU-ILE-PRO;                    
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 ORGANISM_TAXID: 32630;                                               
SOURCE  10 OTHER_DETAILS: SYNTHESIZED USING STEP-WISE NA-FMOC STRATEGY          
KEYWDS    PHOSPHOTRANSFERASE, TRANSFERASE-PEPTIDE COMPLEX                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.MIKOL                                                               
REVDAT   4   17-AUG-11 1CWE    1       SOURCE                                   
REVDAT   3   03-AUG-11 1CWE    1       COMPND HEADER KEYWDS SEQRES              
REVDAT   2   24-FEB-09 1CWE    1       VERSN                                    
REVDAT   1   07-DEC-96 1CWE    0                                                
JRNL        AUTH   V.MIKOL,G.BAUMANN,T.H.KELLER,U.MANNING,M.G.ZURINI            
JRNL        TITL   THE CRYSTAL STRUCTURES OF THE SH2 DOMAIN OF P56LCK COMPLEXED 
JRNL        TITL 2 WITH TWO PHOSPHOPEPTIDES SUGGEST A GATED PEPTIDE BINDING     
JRNL        TITL 3 SITE.                                                        
JRNL        REF    J.MOL.BIOL.                   V. 246   344 1995              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   7532720                                                      
JRNL        DOI    10.1006/JMBI.1994.0089                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
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             : NULL                           
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) : 0.192                           
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            : 1677                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 216                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.80                            
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 1CWE 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        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10015                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.000                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: THE COMPLEX CRYSTALLIZES AS A DIMER IN WHICH THE TWO         
REMARK 300 MOLECULES ARE RELATED BY APPROXIMATE TWO-FOLD SYMMETRY.              
REMARK 300 THE TWO MOLECULES HAVE BEEN ASSIGNED CHAIN IDENTIFIERS A             
REMARK 300 AND C.  RESIDUES 201 TO 205 COMPRISE THE PHOSPHOPEPTIDE.             
REMARK 300 THE TWO MOLECULES HAVE BEEN ASSIGNED CHAIN IDENTIFIERS B             
REMARK 300 AND D.                                                               
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ACE B   200                                                      
REMARK 465     ACE D   200                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 100    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 100    CB   CG   CD   NE   CZ   NH1  NH2                   
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    PRO C  22   C   -  N   -  CA  ANGL. DEV. =  10.5 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    SER A   4      -46.97   -170.47                                   
REMARK 500    ASP A  92       52.56     39.29                                   
REMARK 500    SER A  99     -120.88    -79.74                                   
REMARK 500    SER C   4      -89.93     27.86                                   
REMARK 500    TYR C  70      145.99   -175.45                                   
REMARK 500    ALA C  90      139.46   -175.39                                   
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 ANGLE, 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    GLU A  54         10.16                                           
REMARK 500    ILE A  75         10.65                                           
REMARK 500    SER C   4        -10.29                                           
REMARK 500    ILE C  61         10.73                                           
REMARK 500    THR C  96         10.22                                           
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 A 126        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH A 177        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH A 195        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH A 201        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH C 137        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH C 144        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH C 172        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH C 182        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH D 207        DISTANCE =  6.18 ANGSTROMS                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE REGION BETWEEN RESIDUES 3 AND 100 CORRESPONDS TO THE             
REMARK 999 REGION OF THE P56LCK TYROSINE KINASE BETWEEN RESIDUES 124            
REMARK 999 AND 221.                                                             
DBREF  1CWE A    5   100  UNP    P06239   LCK_HUMAN      126    221             
DBREF  1CWE C    5   100  UNP    P06239   LCK_HUMAN      126    221             
DBREF  1CWE B  201   206  PDB    1CWE     1CWE           201    206             
DBREF  1CWE D  201   206  PDB    1CWE     1CWE           201    206             
SEQRES   1 A   98  GLY SER TRP PHE PHE LYS ASN LEU SER ARG LYS ASP ALA          
SEQRES   2 A   98  GLU ARG GLN LEU LEU ALA PRO GLY ASN THR HIS GLY SER          
SEQRES   3 A   98  PHE LEU ILE ARG GLU SER GLU SER THR ALA GLY SER PHE          
SEQRES   4 A   98  SER LEU SER VAL ARG ASP PHE ASP GLN ASN GLN GLY GLU          
SEQRES   5 A   98  VAL VAL LYS HIS TYR LYS ILE ARG ASN LEU ASP ASN GLY          
SEQRES   6 A   98  GLY PHE TYR ILE SER PRO ARG ILE THR PHE PRO GLY LEU          
SEQRES   7 A   98  HIS GLU LEU VAL ARG HIS TYR THR ASN ALA SER ASP GLY          
SEQRES   8 A   98  LEU CYS THR ARG LEU SER ARG                                  
SEQRES   1 B    7  ACE GLN PM3 GLU GLU ILE PRO                                  
SEQRES   1 C   98  GLY SER TRP PHE PHE LYS ASN LEU SER ARG LYS ASP ALA          
SEQRES   2 C   98  GLU ARG GLN LEU LEU ALA PRO GLY ASN THR HIS GLY SER          
SEQRES   3 C   98  PHE LEU ILE ARG GLU SER GLU SER THR ALA GLY SER PHE          
SEQRES   4 C   98  SER LEU SER VAL ARG ASP PHE ASP GLN ASN GLN GLY GLU          
SEQRES   5 C   98  VAL VAL LYS HIS TYR LYS ILE ARG ASN LEU ASP ASN GLY          
SEQRES   6 C   98  GLY PHE TYR ILE SER PRO ARG ILE THR PHE PRO GLY LEU          
SEQRES   7 C   98  HIS GLU LEU VAL ARG HIS TYR THR ASN ALA SER ASP GLY          
SEQRES   8 C   98  LEU CYS THR ARG LEU SER ARG                                  
SEQRES   1 D    7  ACE GLN PM3 GLU GLU ILE PRO                                  
MODRES 1CWE PM3 B  202  PHE                                                     
MODRES 1CWE PM3 D  202  PHE                                                     
HET    PM3  B 202      16                                                       
HET    PM3  D 202      16                                                       
HETNAM     PM3 2-AMINO-3-(4-PHOSPHONOMETHYL-PHENYL)-PROPIONIC ACID              
FORMUL   2  PM3    2(C10 H14 N O5 P)                                            
FORMUL   5  HOH   *216(H2 O)                                                    
HELIX    1   1 ARG A   12  LEU A   19  1                                   8    
HELIX    2   2 LEU A   80  TYR A   87  1                                   8    
HELIX    3   3 ARG C   12  LEU C   19  1                                   8    
HELIX    4   4 LEU C   80  THR C   88  1                                   9    
SHEET    1   A 4 PHE A   6  LYS A   8  0                                        
SHEET    2   A 4 PHE A  29  GLU A  33  1  N  ILE A  31   O  PHE A   7           
SHEET    3   A 4 PHE A  41  ASP A  49 -1  N  SER A  44   O  LEU A  30           
SHEET    4   A 4 GLY A  53  LYS A  60 -1  N  TYR A  59   O  LEU A  43           
SHEET    1   B 4 PHE C   6  LYS C   8  0                                        
SHEET    2   B 4 PHE C  29  GLU C  33  1  N  ILE C  31   O  PHE C   7           
SHEET    3   B 4 PHE C  41  ASP C  49 -1  N  SER C  44   O  LEU C  30           
SHEET    4   B 4 GLY C  53  LYS C  60 -1  N  TYR C  59   O  LEU C  43           
LINK         C   GLN B 201                 N   PM3 B 202     1555   1555  1.35  
LINK         C   PM3 B 202                 N   GLU B 203     1555   1555  1.32  
LINK         C   GLN D 201                 N   PM3 D 202     1555   1555  1.34  
LINK         C   PM3 D 202                 N   GLU D 203     1555   1555  1.32  
CRYST1   35.170   41.840   45.520  68.71  82.94  87.36 P 1           2          
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      0.028433 -0.001311 -0.003269        0.00000                         
SCALE2      0.000000  0.023926 -0.009248        0.00000                         
SCALE3      0.000000  0.000000  0.023732        0.00000                         
MTRIX1   1 -0.414900  0.440100 -0.796400       17.88140    1                    
MTRIX2   1  0.513200 -0.609600 -0.604200       59.77560    1                    
MTRIX3   1 -0.751400 -0.659300  0.027100       64.71060    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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