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Database: PDB
Entry: 1D4T
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Original site: 1D4T 
HEADER    SIGNALING PROTEIN                       06-OCT-99   1D4T              
TITLE     CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP IN COMPLEX WITH A SLAM       
TITLE    2 PEPTIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: T CELL SIGNAL TRANSDUCTION MOLECULE SAP;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SH2 DOMAIN (RESIDUES 1-104);                               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE;                 
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: SLAM TAIL PEPTIDE (RESIDUES 276 TO 286);                   
COMPND  10 SYNONYM: SLAM;                                                       
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BLOOD;                                                       
SOURCE   6 CELL: T CELL;                                                        
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: T7-PRSET;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE 
SOURCE  14 OF THIS PEPTIDE NATURALLY OCCURS IN HUMANS (HOMO SAPIENS)            
KEYWDS    SH2 DOMAIN, TYROSINE KINASE, SIGNAL TRANSDUCTION, PEPTIDE             
KEYWDS   2 RECOGNITION, SIGNALING PROTEIN                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.POY,M.B.YAFFE,J.SAYOS,K.SAXENA,M.J.ECK                              
REVDAT   4   31-JAN-18 1D4T    1       REMARK                                   
REVDAT   3   24-FEB-09 1D4T    1       VERSN                                    
REVDAT   2   10-APR-00 1D4T    1       JRNL                                     
REVDAT   1   14-OCT-99 1D4T    0                                                
JRNL        AUTH   F.POY,M.B.YAFFE,J.SAYOS,K.SAXENA,M.MORRA,J.SUMEGI,           
JRNL        AUTH 2 L.C.CANTLEY,C.TERHORST,M.J.ECK                               
JRNL        TITL   CRYSTAL STRUCTURES OF THE XLP PROTEIN SAP REVEAL A CLASS OF  
JRNL        TITL 2 SH2 DOMAINS WITH EXTENDED, PHOSPHOTYROSINE-INDEPENDENT       
JRNL        TITL 3 SEQUENCE RECOGNITION.                                        
JRNL        REF    MOL.CELL                      V.   4   555 1999              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   10549287                                                     
JRNL        DOI    10.1016/S1097-2765(00)80206-3                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.SAYOS,C.WU,M.MORRA,N.WANG,C.TERHOSRT                       
REMARK   1  TITL   THE X-LINKED LYMPHOPROLIFERATIVE DISEASE GENE PRODUCT SAP    
REMARK   1  TITL 2 REGULATES SIGNALS INDUCED THROUGH THE CO-RECEPTOR SLAM       
REMARK   1  REF    NATURE                        V. 395   462 1998              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  DOI    10.1038/26683                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.9                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.127                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.130                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.165                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 171                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.115                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.117                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.152                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 149                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 2809                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 915                                           
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 0                                             
REMARK   3   SOLVENT ATOMS      : 236                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1147.0                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 957.00                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 1032                    
REMARK   3   NUMBER OF RESTRAINTS                     : 1219                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.010                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.030                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.031                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.080                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.130                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.070                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.040                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.080                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1D4T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000009793.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : .9                                 
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : PRINCETON 2K                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04300                            
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO                    
REMARK 200 SOFTWARE USED: ARP                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 20% GLYCEROL, 100 MM       
REMARK 280  HEPES PH 8.0, AND 100 MM DTT, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 22K, TEMPERATURE 295.0K                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       21.45500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6500 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LEU B 278   CG    LEU B 278   CD2     0.234                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  13   NH1 -  CZ  -  NH2 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG A  13   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A  55   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG A  75   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A  78   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    LYS B 276   CA  -  CB  -  CG  ANGL. DEV. =  20.8 DEGREES          
REMARK 500    LEU B 278   CB  -  CG  -  CD1 ANGL. DEV. = -10.4 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    LYS A  10       43.45    -91.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D1Z   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE UNLIGANDED SAP SH2 DOMAIN                           
REMARK 900 RELATED ID: 1D4W   RELATED DB: PDB                                   
REMARK 900 SAP SH2 DOMAIN IN COMPLEX WITH SYNTHETIC PHOSPHOPEPTIDE              
DBREF  1D4T A    1   104  UNP    O60880   SH21A_HUMAN      1    104             
DBREF  1D4T B  276   286  UNP    Q13291   SLAF1_HUMAN    276    286             
SEQRES   1 A  104  MET ASP ALA VAL ALA VAL TYR HIS GLY LYS ILE SER ARG          
SEQRES   2 A  104  GLU THR GLY GLU LYS LEU LEU LEU ALA THR GLY LEU ASP          
SEQRES   3 A  104  GLY SER TYR LEU LEU ARG ASP SER GLU SER VAL PRO GLY          
SEQRES   4 A  104  VAL TYR CYS LEU CYS VAL LEU TYR HIS GLY TYR ILE TYR          
SEQRES   5 A  104  THR TYR ARG VAL SER GLN THR GLU THR GLY SER TRP SER          
SEQRES   6 A  104  ALA GLU THR ALA PRO GLY VAL HIS LYS ARG TYR PHE ARG          
SEQRES   7 A  104  LYS ILE LYS ASN LEU ILE SER ALA PHE GLN LYS PRO ASP          
SEQRES   8 A  104  GLN GLY ILE VAL ILE PRO LEU GLN TYR PRO VAL GLU LYS          
SEQRES   1 B   11  LYS SER LEU THR ILE TYR ALA GLN VAL GLN LYS                  
FORMUL   3  HOH   *236(H2 O)                                                    
HELIX    1   1 SER A   12  GLY A   24  1                                  13    
HELIX    2   2 LYS A   79  GLN A   88  1                                  10    
SHEET    1   A 5 TYR A 100  PRO A 101  0                                        
SHEET    2   A 5 SER A  28  ASP A  33  1  N  TYR A  29   O  TYR A 100           
SHEET    3   A 5 TYR A  41  TYR A  47 -1  N  CYS A  42   O  ARG A  32           
SHEET    4   A 5 TYR A  50  GLN A  58 -1  O  TYR A  50   N  TYR A  47           
SHEET    5   A 5 TRP A  64  ALA A  66 -1  O  SER A  65   N  SER A  57           
SHEET    1  A1 5 TYR A 100  PRO A 101  0                                        
SHEET    2  A1 5 SER A  28  ASP A  33  1  N  TYR A  29   O  TYR A 100           
SHEET    3  A1 5 TYR A  41  TYR A  47 -1  N  CYS A  42   O  ARG A  32           
SHEET    4  A1 5 TYR A  50  GLN A  58 -1  O  TYR A  50   N  TYR A  47           
SHEET    5  A1 5 THR B 279  TYR B 281  1  O  ILE B 280   N  THR A  53           
CRYST1   25.870   42.910   44.950  90.00  98.26  90.00 P 1 21 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      0.038655  0.000000  0.005612        0.00000                         
SCALE2      0.000000  0.023305  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022480        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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