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Database: PDB
Entry: 2ELA
LinkDB: 2ELA
Original site: 2ELA 
HEADER    CELL CYCLE                              27-MAR-07   2ELA              
TITLE     CRYSTAL STRUCTURE OF THE PTB DOMAIN OF HUMAN APPL1                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADAPTER PROTEIN CONTAINING PH DOMAIN, PTB DOMAIN           
COMPND   3 AND LEUCINE ZIPPER MOTIF 1;                                          
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: PTB DOMAIN;                                                
COMPND   6 SYNONYM: APPL1, DIP13 ALPHA, DCC-INTERACTING PROTEIN 13              
COMPND   7 ALPHA;                                                               
COMPND   8 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 BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    APPL, PTB DOMAIN, CELL CYCLE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LI,X.MAO,L.Q.DONG,F.LIU,L.TONG                                      
REVDAT   2   24-FEB-09 2ELA    1       VERSN                                    
REVDAT   1   29-MAY-07 2ELA    0                                                
JRNL        AUTH   J.LI,X.MAO,L.Q.DONG,F.LIU,L.TONG                             
JRNL        TITL   CRYSTAL STRUCTURES OF THE BAR-PH AND PTB DOMAINS             
JRNL        TITL 2 OF HUMAN APPL1                                               
JRNL        REF    STRUCTURE                     V.  15   525 2007              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   17502098                                                     
JRNL        DOI    10.1016/J.STR.2007.03.011                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 435558.130                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 21359                          
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) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1557                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1782                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2620                       
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 133                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2182                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 236                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 8.90                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.74000                                              
REMARK   3    B22 (A**2) : 0.07000                                              
REMARK   3    B33 (A**2) : -8.81000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.81000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.70                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.580 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.520 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.470 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.690 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 45.61                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ELA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB026804.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUN-05; 24-JUL-05               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : NSLS; NSLS                         
REMARK 200  BEAMLINE                       : X4A; X4C                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97641; 0.97950                   
REMARK 200  MONOCHROMATOR                  : MIRRORS; MIRRORS                   
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; IMAGE PLATE                   
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; MAR SCANNER        
REMARK 200                                   180 MM PLATE                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23819                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.7400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.917                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SNB                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE (PH 5.6), 10%        
REMARK 280  (W/V) PEG 10K, 10% (V/V) ISOPROPANOL, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 277.0K                                            
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       30.79650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 BIOLOGICAL ASSEMBLY IS A MONOMER.                        
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     MET A   472                                                      
REMARK 465     GLY A   473                                                      
REMARK 465     SER A   474                                                      
REMARK 465     SER A   475                                                      
REMARK 465     HIS A   476                                                      
REMARK 465     HIS A   477                                                      
REMARK 465     HIS A   478                                                      
REMARK 465     HIS A   479                                                      
REMARK 465     HIS A   480                                                      
REMARK 465     HIS A   481                                                      
REMARK 465     SER A   482                                                      
REMARK 465     SER A   483                                                      
REMARK 465     GLY A   484                                                      
REMARK 465     LEU A   485                                                      
REMARK 465     VAL A   486                                                      
REMARK 465     PRO A   487                                                      
REMARK 465     ARG A   488                                                      
REMARK 465     GLY A   489                                                      
REMARK 465     SER A   490                                                      
REMARK 465     HIS A   491                                                      
REMARK 465     MET A   492                                                      
REMARK 465     THR A   493                                                      
REMARK 465     GLU A   494                                                      
REMARK 465     ASP A   495                                                      
REMARK 465     SER A   592                                                      
REMARK 465     GLY A   593                                                      
REMARK 465     ARG A   594                                                      
REMARK 465     SER A   595                                                      
REMARK 465     GLU A   596                                                      
REMARK 465     SER A   597                                                      
REMARK 465     ASN A   598                                                      
REMARK 465     ARG A   634                                                      
REMARK 465     ALA A   635                                                      
REMARK 465     SER A   636                                                      
REMARK 465     GLU A   637                                                      
REMARK 465     LYS A   638                                                      
REMARK 465     GLN A   639                                                      
REMARK 465     LYS A   640                                                      
REMARK 465     GLU A   641                                                      
REMARK 465     ILE A   642                                                      
REMARK 465     GLU A   643                                                      
REMARK 465     ARG A   644                                                      
REMARK 465     VAL A   645                                                      
REMARK 465     LYS A   646                                                      
REMARK 465     MET B   472                                                      
REMARK 465     GLY B   473                                                      
REMARK 465     SER B   474                                                      
REMARK 465     SER B   475                                                      
REMARK 465     HIS B   476                                                      
REMARK 465     HIS B   477                                                      
REMARK 465     HIS B   478                                                      
REMARK 465     HIS B   479                                                      
REMARK 465     HIS B   480                                                      
REMARK 465     HIS B   481                                                      
REMARK 465     SER B   482                                                      
REMARK 465     SER B   483                                                      
REMARK 465     GLY B   484                                                      
REMARK 465     LEU B   485                                                      
REMARK 465     VAL B   486                                                      
REMARK 465     PRO B   487                                                      
REMARK 465     ARG B   488                                                      
REMARK 465     GLY B   489                                                      
REMARK 465     SER B   490                                                      
REMARK 465     HIS B   491                                                      
REMARK 465     MET B   492                                                      
REMARK 465     THR B   493                                                      
REMARK 465     GLU B   494                                                      
REMARK 465     ASP B   495                                                      
REMARK 465     SER B   496                                                      
REMARK 465     ILE B   497                                                      
REMARK 465     LEU B   498                                                      
REMARK 465     GLY B   593                                                      
REMARK 465     ARG B   594                                                      
REMARK 465     SER B   595                                                      
REMARK 465     GLU B   596                                                      
REMARK 465     SER B   597                                                      
REMARK 465     ASN B   598                                                      
REMARK 465     LYS B   646                                                      
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    HIS A 499       85.18   -156.33                                   
REMARK 500    ASP A 515     -114.68    -77.56                                   
REMARK 500    ASP A 516        7.63    172.40                                   
REMARK 500    PRO A 518      -15.08    -49.58                                   
REMARK 500    ASN A 580       93.93   -166.40                                   
REMARK 500    LYS A 581        1.54    -68.07                                   
REMARK 500    SER B 514       98.19     59.43                                   
REMARK 500    ASP B 516       35.78    -98.96                                   
REMARK 500    ASN B 580       92.57   -163.78                                   
REMARK 500    LYS B 581        0.80    -68.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ELB   RELATED DB: PDB                                   
DBREF  2ELA A  493   646  UNP    Q9UKG1   DP13A_HUMAN    493    646             
DBREF  2ELA B  493   646  UNP    Q9UKG1   DP13A_HUMAN    493    646             
SEQADV 2ELA MET A  472  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA GLY A  473  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA SER A  474  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA SER A  475  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS A  476  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS A  477  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS A  478  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS A  479  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS A  480  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS A  481  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA SER A  482  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA SER A  483  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA GLY A  484  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA LEU A  485  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA VAL A  486  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA PRO A  487  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA ARG A  488  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA GLY A  489  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA SER A  490  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS A  491  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA MET A  492  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA MET B  472  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA GLY B  473  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA SER B  474  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA SER B  475  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS B  476  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS B  477  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS B  478  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS B  479  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS B  480  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS B  481  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA SER B  482  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA SER B  483  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA GLY B  484  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA LEU B  485  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA VAL B  486  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA PRO B  487  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA ARG B  488  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA GLY B  489  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA SER B  490  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA HIS B  491  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELA MET B  492  UNP  Q9UKG1              CLONING ARTIFACT               
SEQRES   1 A  175  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  175  LEU VAL PRO ARG GLY SER HIS MET THR GLU ASP SER ILE          
SEQRES   3 A  175  LEU HIS GLN LEU PHE ILE VAL ARG PHE LEU GLY SER MET          
SEQRES   4 A  175  GLU VAL LYS SER ASP ASP HIS PRO ASP VAL VAL TYR GLU          
SEQRES   5 A  175  THR MET ARG GLN ILE LEU ALA ALA ARG ALA ILE HIS ASN          
SEQRES   6 A  175  ILE PHE ARG MET THR GLU SER HIS LEU LEU VAL THR CYS          
SEQRES   7 A  175  ASP CYS LEU LYS LEU ILE ASP PRO GLN THR GLN VAL THR          
SEQRES   8 A  175  ARG LEU THR PHE PRO LEU PRO CYS VAL VAL LEU TYR ALA          
SEQRES   9 A  175  THR HIS GLN GLU ASN LYS ARG LEU PHE GLY PHE VAL LEU          
SEQRES  10 A  175  ARG THR SER SER GLY ARG SER GLU SER ASN LEU SER SER          
SEQRES  11 A  175  VAL CYS TYR ILE PHE GLU SER ASN ASN GLU GLY GLU LYS          
SEQRES  12 A  175  ILE CYS ASP SER VAL GLY LEU ALA LYS GLN ILE ALA LEU          
SEQRES  13 A  175  HIS ALA GLU LEU ASP ARG ARG ALA SER GLU LYS GLN LYS          
SEQRES  14 A  175  GLU ILE GLU ARG VAL LYS                                      
SEQRES   1 B  175  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  175  LEU VAL PRO ARG GLY SER HIS MET THR GLU ASP SER ILE          
SEQRES   3 B  175  LEU HIS GLN LEU PHE ILE VAL ARG PHE LEU GLY SER MET          
SEQRES   4 B  175  GLU VAL LYS SER ASP ASP HIS PRO ASP VAL VAL TYR GLU          
SEQRES   5 B  175  THR MET ARG GLN ILE LEU ALA ALA ARG ALA ILE HIS ASN          
SEQRES   6 B  175  ILE PHE ARG MET THR GLU SER HIS LEU LEU VAL THR CYS          
SEQRES   7 B  175  ASP CYS LEU LYS LEU ILE ASP PRO GLN THR GLN VAL THR          
SEQRES   8 B  175  ARG LEU THR PHE PRO LEU PRO CYS VAL VAL LEU TYR ALA          
SEQRES   9 B  175  THR HIS GLN GLU ASN LYS ARG LEU PHE GLY PHE VAL LEU          
SEQRES  10 B  175  ARG THR SER SER GLY ARG SER GLU SER ASN LEU SER SER          
SEQRES  11 B  175  VAL CYS TYR ILE PHE GLU SER ASN ASN GLU GLY GLU LYS          
SEQRES  12 B  175  ILE CYS ASP SER VAL GLY LEU ALA LYS GLN ILE ALA LEU          
SEQRES  13 B  175  HIS ALA GLU LEU ASP ARG ARG ALA SER GLU LYS GLN LYS          
SEQRES  14 B  175  GLU ILE GLU ARG VAL LYS                                      
FORMUL   3  HOH   *236(H2 O)                                                    
HELIX    1   1 PRO A  518  HIS A  535  1                                  18    
HELIX    2   2 GLU A  611  ASP A  632  1                                  22    
HELIX    3   3 PRO B  518  HIS B  535  1                                  18    
HELIX    4   4 GLU B  611  ARG B  644  1                                  34    
SHEET    1   A 7 THR A 562  PRO A 567  0                                        
SHEET    2   A 7 CYS A 551  ILE A 555 -1  N  LEU A 552   O  PHE A 566           
SHEET    3   A 7 THR A 541  VAL A 547 -1  N  HIS A 544   O  ILE A 555           
SHEET    4   A 7 GLN A 500  VAL A 512 -1  N  PHE A 502   O  LEU A 545           
SHEET    5   A 7 SER A 600  SER A 608 -1  O  CYS A 603   N  MET A 510           
SHEET    6   A 7 ASN A 580  THR A 590 -1  N  PHE A 584   O  PHE A 606           
SHEET    7   A 7 VAL A 571  HIS A 577 -1  N  ALA A 575   O  GLY A 585           
SHEET    1   B 7 THR B 562  PRO B 567  0                                        
SHEET    2   B 7 CYS B 551  ILE B 555 -1  N  LEU B 552   O  PHE B 566           
SHEET    3   B 7 THR B 541  VAL B 547 -1  N  HIS B 544   O  ILE B 555           
SHEET    4   B 7 GLN B 500  VAL B 512 -1  N  PHE B 502   O  LEU B 545           
SHEET    5   B 7 SER B 600  SER B 608 -1  O  ILE B 605   N  LEU B 507           
SHEET    6   B 7 ASN B 580  THR B 590 -1  N  PHE B 584   O  PHE B 606           
SHEET    7   B 7 VAL B 571  HIS B 577 -1  N  ALA B 575   O  GLY B 585           
CRYST1   45.533   61.593   60.745  90.00 101.22  90.00 P 1 21 1      4          
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      0.021962  0.000000  0.004357        0.00000                         
SCALE2      0.000000  0.016236  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016783        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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