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Database: PDB
Entry: 2OQ1
LinkDB: 2OQ1
Original site: 2OQ1 
HEADER    TRANSFERASE                             30-JAN-07   2OQ1              
TITLE     TANDEM SH2 DOMAINS OF ZAP-70 WITH 19-MER ZETA1 PEPTIDE                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE ZAP-70;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 3-256;                                            
COMPND   5 SYNONYM: 70 KDA ZETA-ASSOCIATED PROTEIN, SYK-RELATED TYROSINE KINASE;
COMPND   6 EC: 2.7.10.2;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD3 ZETA CHAIN;                
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: RESIDUES 69-87;                                            
COMPND  12 SYNONYM: T-CELL RECEPTOR T3 ZETA CHAIN, CD247 ANTIGEN;               
COMPND  13 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 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HOMO SAPIENS        
SOURCE  10 (HUMANS)                                                             
KEYWDS    TANDEM SH2 DOMAINS, ZAP-70, TYROSINE KINASE, TRANSFERASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.H.HATADA,E.R.LAIRD,J.GREEN,J.MORGENSTERN,M.K.RAM                    
REVDAT   3   24-JUL-19 2OQ1    1       REMARK LINK                              
REVDAT   2   24-FEB-09 2OQ1    1       VERSN                                    
REVDAT   1   06-MAR-07 2OQ1    0                                                
JRNL        AUTH   M.H.HATADA,X.LU,E.R.LAIRD,J.GREEN,J.P.MORGENSTERN,M.LOU,     
JRNL        AUTH 2 C.MARR,T.B.PHILLIPS,M.K.RAM,K.THERIAULT                      
JRNL        TITL   MOLECULAR BASIS FOR THE INTERACTION OF ZAP-70 WITH THE       
JRNL        TITL 2 T-CELL RECEPTOR                                              
JRNL        REF    NATURE                        V. 377    32 1995              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   7659156                                                      
JRNL        DOI    10.1038/377032A0                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.843                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
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             : 23697                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2369                            
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            : 2197                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 114                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.99                          
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) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.580                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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 2OQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000041445.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : GRAPHITE MONOCHROMATOR             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23978                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04900                            
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: MIR                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%PEG 4000, 50MM SODIUM CITRATE,100     
REMARK 280  MM AMMONIUM ACETATE, 20MM DTT, PH 6.2, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 298K                                              
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       31.68500            
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: 2540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500  PB     PB A  1119     O    HOH A   582     2647     1.63            
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    LEU A 204   CA  -  CB  -  CG  ANGL. DEV. =  14.8 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 102      104.73     72.90                                   
REMARK 500    LYS A 253      -95.65   -122.84                                   
REMARK 500    PRO A 257      174.11    -52.85                                   
REMARK 500    GLN B 302     -146.90   -165.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 CYSTEINE 119 IS MODIFIED WITH TRIMETHYL LEAD ACETATE.                
REMARK 600 CARBONS OF METHYLS ARE MISSING FROM THE MODEL                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 1119                 
DBREF  2OQ1 A    5   258  UNP    P43403   ZAP70_HUMAN      3    256             
DBREF  2OQ1 B  301   319  UNP    P20963   CD3Z_HUMAN      69     87             
SEQADV 2OQ1 MSE A   31  UNP  P43403    MET    29 MODIFIED RESIDUE               
SEQADV 2OQ1 MSE A  124  UNP  P43403    MET   122 MODIFIED RESIDUE               
SEQADV 2OQ1 MSE A  163  UNP  P43403    MET   161 MODIFIED RESIDUE               
SEQADV 2OQ1 PTR B  304  UNP  P20963    TYR    72 MODIFIED RESIDUE               
SEQADV 2OQ1 PTR B  315  UNP  P20963    TYR    83 MODIFIED RESIDUE               
SEQRES   1 A  254  ASP PRO ALA ALA HIS LEU PRO PHE PHE TYR GLY SER ILE          
SEQRES   2 A  254  SER ARG ALA GLU ALA GLU GLU HIS LEU LYS LEU ALA GLY          
SEQRES   3 A  254  MSE ALA ASP GLY LEU PHE LEU LEU ARG GLN CYS LEU ARG          
SEQRES   4 A  254  SER LEU GLY GLY TYR VAL LEU SER LEU VAL HIS ASP VAL          
SEQRES   5 A  254  ARG PHE HIS HIS PHE PRO ILE GLU ARG GLN LEU ASN GLY          
SEQRES   6 A  254  THR TYR ALA ILE ALA GLY GLY LYS ALA HIS CYS GLY PRO          
SEQRES   7 A  254  ALA GLU LEU CYS GLU PHE TYR SER ARG ASP PRO ASP GLY          
SEQRES   8 A  254  LEU PRO CYS ASN LEU ARG LYS PRO CYS ASN ARG PRO SER          
SEQRES   9 A  254  GLY LEU GLU PRO GLN PRO GLY VAL PHE ASP CYS LEU ARG          
SEQRES  10 A  254  ASP ALA MSE VAL ARG ASP TYR VAL ARG GLN THR TRP LYS          
SEQRES  11 A  254  LEU GLU GLY GLU ALA LEU GLU GLN ALA ILE ILE SER GLN          
SEQRES  12 A  254  ALA PRO GLN VAL GLU LYS LEU ILE ALA THR THR ALA HIS          
SEQRES  13 A  254  GLU ARG MSE PRO TRP TYR HIS SER SER LEU THR ARG GLU          
SEQRES  14 A  254  GLU ALA GLU ARG LYS LEU TYR SER GLY ALA GLN THR ASP          
SEQRES  15 A  254  GLY LYS PHE LEU LEU ARG PRO ARG LYS GLU GLN GLY THR          
SEQRES  16 A  254  TYR ALA LEU SER LEU ILE TYR GLY LYS THR VAL TYR HIS          
SEQRES  17 A  254  TYR LEU ILE SER GLN ASP LYS ALA GLY LYS TYR CYS ILE          
SEQRES  18 A  254  PRO GLU GLY THR LYS PHE ASP THR LEU TRP GLN LEU VAL          
SEQRES  19 A  254  GLU TYR LEU LYS LEU LYS ALA ASP GLY LEU ILE TYR CYS          
SEQRES  20 A  254  LEU LYS GLU ALA CYS PRO ASN                                  
SEQRES   1 B   19  ASN GLN LEU PTR ASN GLU LEU ASN LEU GLY ARG ARG GLU          
SEQRES   2 B   19  GLU PTR ASP VAL LEU ASP                                      
MODRES 2OQ1 MSE A   31  MET  SELENOMETHIONINE                                   
MODRES 2OQ1 MSE A  124  MET  SELENOMETHIONINE                                   
MODRES 2OQ1 MSE A  163  MET  SELENOMETHIONINE                                   
MODRES 2OQ1 PTR B  304  TYR  O-PHOSPHOTYROSINE                                  
MODRES 2OQ1 PTR B  315  TYR  O-PHOSPHOTYROSINE                                  
HET    MSE  A  31       8                                                       
HET    MSE  A 124       8                                                       
HET    MSE  A 163       8                                                       
HET    PTR  B 304      16                                                       
HET    PTR  B 315      16                                                       
HET     PB  A1119       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM      PB LEAD (II) ION                                                    
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  MSE    3(C5 H11 N O2 SE)                                            
FORMUL   2  PTR    2(C9 H12 N O6 P)                                             
FORMUL   3   PB    PB 2+                                                        
FORMUL   4  HOH   *114(H2 O)                                                    
HELIX    1   1 SER A   18  ALA A   29  1                                  12    
HELIX    2   2 GLY A   81  ASP A   92  1                                  12    
HELIX    3   3 GLY A  115  LYS A  134  1                                  20    
HELIX    4   4 GLU A  136  ALA A  159  1                                  24    
HELIX    5   5 HIS A  160  MSE A  163  5                                   4    
HELIX    6   6 THR A  171  SER A  181  1                                  11    
HELIX    7   7 THR A  233  LYS A  244  1                                  12    
HELIX    8   8 ASN B  308  ARG B  312  5                                   5    
SHEET    1   A 4 PHE A  36  GLN A  40  0                                        
SHEET    2   A 4 TYR A  48  HIS A  54 -1  O  SER A  51   N  LEU A  37           
SHEET    3   A 4 ARG A  57  ARG A  65 -1  O  ILE A  63   N  TYR A  48           
SHEET    4   A 4 TYR A  71  ILE A  73 -1  O  ALA A  72   N  GLU A  64           
SHEET    1   B 4 LYS A 188  PRO A 193  0                                        
SHEET    2   B 4 THR A 199  TYR A 206 -1  O  ALA A 201   N  ARG A 192           
SHEET    3   B 4 THR A 209  GLN A 217 -1  O  TYR A 211   N  LEU A 204           
SHEET    4   B 4 TYR A 223  CYS A 224 -1  O  CYS A 224   N  SER A 216           
LINK         SG  CYS A 119                PB    PB A1119     1555   1555  2.62  
LINK         C   GLY A  30                 N   MSE A  31     1555   1555  1.33  
LINK         C   MSE A  31                 N   ALA A  32     1555   1555  1.33  
LINK         C   ALA A 123                 N   MSE A 124     1555   1555  1.33  
LINK         C   MSE A 124                 N   VAL A 125     1555   1555  1.33  
LINK         C   ARG A 162                 N   MSE A 163     1555   1555  1.33  
LINK         C   MSE A 163                 N   PRO A 164     1555   1555  1.34  
LINK         C   LEU B 303                 N   PTR B 304     1555   1555  1.33  
LINK         C   PTR B 304                 N   ASN B 305     1555   1555  1.32  
LINK         C   GLU B 314                 N   PTR B 315     1555   1555  1.33  
LINK         C   PTR B 315                 N   ASP B 316     1555   1555  1.32  
SITE     1 AC1  1 CYS A 119                                                     
CRYST1   50.110   63.370   54.000  90.00 114.44  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      0.019956  0.000000  0.009069        0.00000                         
SCALE2      0.000000  0.015780  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020341        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system