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Database: PDB
Entry: 2F8Y
LinkDB: 2F8Y
Original site: 2F8Y 
HEADER    TRANSCRIPTION                           04-DEC-05   2F8Y              
TITLE     CRYSTAL STRUCTURE OF HUMAN NOTCH1 ANKYRIN REPEATS TO 1.55A            
TITLE    2 RESOLUTION.                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NOTCH HOMOLOG 1, TRANSLOCATION-ASSOCIATED                  
COMPND   3 (DROSOPHILA);                                                        
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: ANKYRIN REPEAT DOMAIN, REPEATS 1-7;                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NOTCH1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST15                                   
KEYWDS    NOTCH, ANKYRIN REPEATS, TRANSCRIPTION                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.NAM,P.SLIZ,S.C.BLACKLOW                                             
REVDAT   2   24-FEB-09 2F8Y    1       VERSN                                    
REVDAT   1   04-APR-06 2F8Y    0                                                
JRNL        AUTH   Y.NAM,P.SLIZ,L.SONG,J.C.ASTER,S.C.BLACKLOW                   
JRNL        TITL   STRUCTURAL BASIS FOR COOPERATIVITY IN RECRUITMENT            
JRNL        TITL 2 OF MAML COACTIVATORS TO NOTCH TRANSCRIPTION                  
JRNL        TITL 3 COMPLEXES.                                                   
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 124   973 2006              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   16530044                                                     
JRNL        DOI    10.1016/J.CELL.2005.12.037                                   
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1901493.440                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 82.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 70977                          
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) : 0.150                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4762                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.61                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 45.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4981                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE                    : 0.2790                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 247                          
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            : 3282                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 404                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.79000                                              
REMARK   3    B22 (A**2) : 2.79000                                              
REMARK   3    B33 (A**2) : -5.58000                                             
REMARK   3    B12 (A**2) : 2.24000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.20                            
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) : 0.18                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.16                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.75                            
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) : 1.180 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.940 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.960 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.090 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.41                                                 
REMARK   3   BSOL        : 71.50                                                
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2F8Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB035599.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JAN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70977                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.7                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 45.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.37500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1OT8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.71200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.35600            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       54.53400            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       18.17800            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.89000            
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 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     GLY A  1905                                                      
REMARK 465     ASP A  1906                                                      
REMARK 465     ALA A  1907                                                      
REMARK 465     PRO A  1908                                                      
REMARK 465     GLN A  2124                                                      
REMARK 465     LEU A  2125                                                      
REMARK 465     HIS A  2126                                                      
REMARK 465     GLY A  2127                                                      
REMARK 465     GLY B  1905                                                      
REMARK 465     ASP B  1906                                                      
REMARK 465     ALA B  1907                                                      
REMARK 465     PRO B  1908                                                      
REMARK 465     ASN B  2118                                                      
REMARK 465     LEU B  2119                                                      
REMARK 465     VAL B  2120                                                      
REMARK 465     ARG B  2121                                                      
REMARK 465     SER B  2122                                                      
REMARK 465     PRO B  2123                                                      
REMARK 465     GLN B  2124                                                      
REMARK 465     LEU B  2125                                                      
REMARK 465     HIS B  2126                                                      
REMARK 465     GLY B  2127                                                      
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    PHE A1914       -3.57     70.17                                   
REMARK 500    GLN A1917      114.63    -24.54                                   
REMARK 500    VAL A2008       77.68   -100.98                                   
REMARK 500    HIS A2107       68.70   -109.21                                   
REMARK 500    ARG A2121       -3.19     57.65                                   
REMARK 500    THR B1925       58.17   -165.25                                   
REMARK 500    ASP B1926      -77.39   -107.36                                   
REMARK 500    VAL B2008       66.48   -109.96                                   
REMARK 500    GLU B2009      -53.98    -28.50                                   
REMARK 500    HIS B2019       27.41     84.27                                   
REMARK 500    ASP B2026     -169.45    -77.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 292        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH A 312        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH A 352        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A 359        DISTANCE =  6.14 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503                 
DBREF  2F8Y A 1906  2127  UNP    P46531   NOTC1_HUMAN   1906   2127             
DBREF  2F8Y B 1906  2127  UNP    P46531   NOTC1_HUMAN   1906   2127             
SEQADV 2F8Y GLY A 1905  UNP  P46531              CLONING ARTIFACT               
SEQADV 2F8Y GLY B 1905  UNP  P46531              CLONING ARTIFACT               
SEQRES   1 A  223  GLY ASP ALA PRO ALA VAL ILE SER ASP PHE ILE TYR GLN          
SEQRES   2 A  223  GLY ALA SER LEU HIS ASN GLN THR ASP ARG THR GLY GLU          
SEQRES   3 A  223  THR ALA LEU HIS LEU ALA ALA ARG TYR SER ARG SER ASP          
SEQRES   4 A  223  ALA ALA LYS ARG LEU LEU GLU ALA SER ALA ASP ALA ASN          
SEQRES   5 A  223  ILE GLN ASP ASN MET GLY ARG THR PRO LEU HIS ALA ALA          
SEQRES   6 A  223  VAL SER ALA ASP ALA GLN GLY VAL PHE GLN ILE LEU ILE          
SEQRES   7 A  223  ARG ASN ARG ALA THR ASP LEU ASP ALA ARG MET HIS ASP          
SEQRES   8 A  223  GLY THR THR PRO LEU ILE LEU ALA ALA ARG LEU ALA VAL          
SEQRES   9 A  223  GLU GLY MET LEU GLU ASP LEU ILE ASN SER HIS ALA ASP          
SEQRES  10 A  223  VAL ASN ALA VAL ASP ASP LEU GLY LYS SER ALA LEU HIS          
SEQRES  11 A  223  TRP ALA ALA ALA VAL ASN ASN VAL ASP ALA ALA VAL VAL          
SEQRES  12 A  223  LEU LEU LYS ASN GLY ALA ASN LYS ASP MET GLN ASN ASN          
SEQRES  13 A  223  ARG GLU GLU THR PRO LEU PHE LEU ALA ALA ARG GLU GLY          
SEQRES  14 A  223  SER TYR GLU THR ALA LYS VAL LEU LEU ASP HIS PHE ALA          
SEQRES  15 A  223  ASN ARG ASP ILE THR ASP HIS MET ASP ARG LEU PRO ARG          
SEQRES  16 A  223  ASP ILE ALA GLN GLU ARG MET HIS HIS ASP ILE VAL ARG          
SEQRES  17 A  223  LEU LEU ASP GLU TYR ASN LEU VAL ARG SER PRO GLN LEU          
SEQRES  18 A  223  HIS GLY                                                      
SEQRES   1 B  223  GLY ASP ALA PRO ALA VAL ILE SER ASP PHE ILE TYR GLN          
SEQRES   2 B  223  GLY ALA SER LEU HIS ASN GLN THR ASP ARG THR GLY GLU          
SEQRES   3 B  223  THR ALA LEU HIS LEU ALA ALA ARG TYR SER ARG SER ASP          
SEQRES   4 B  223  ALA ALA LYS ARG LEU LEU GLU ALA SER ALA ASP ALA ASN          
SEQRES   5 B  223  ILE GLN ASP ASN MET GLY ARG THR PRO LEU HIS ALA ALA          
SEQRES   6 B  223  VAL SER ALA ASP ALA GLN GLY VAL PHE GLN ILE LEU ILE          
SEQRES   7 B  223  ARG ASN ARG ALA THR ASP LEU ASP ALA ARG MET HIS ASP          
SEQRES   8 B  223  GLY THR THR PRO LEU ILE LEU ALA ALA ARG LEU ALA VAL          
SEQRES   9 B  223  GLU GLY MET LEU GLU ASP LEU ILE ASN SER HIS ALA ASP          
SEQRES  10 B  223  VAL ASN ALA VAL ASP ASP LEU GLY LYS SER ALA LEU HIS          
SEQRES  11 B  223  TRP ALA ALA ALA VAL ASN ASN VAL ASP ALA ALA VAL VAL          
SEQRES  12 B  223  LEU LEU LYS ASN GLY ALA ASN LYS ASP MET GLN ASN ASN          
SEQRES  13 B  223  ARG GLU GLU THR PRO LEU PHE LEU ALA ALA ARG GLU GLY          
SEQRES  14 B  223  SER TYR GLU THR ALA LYS VAL LEU LEU ASP HIS PHE ALA          
SEQRES  15 B  223  ASN ARG ASP ILE THR ASP HIS MET ASP ARG LEU PRO ARG          
SEQRES  16 B  223  ASP ILE ALA GLN GLU ARG MET HIS HIS ASP ILE VAL ARG          
SEQRES  17 B  223  LEU LEU ASP GLU TYR ASN LEU VAL ARG SER PRO GLN LEU          
SEQRES  18 B  223  HIS GLY                                                      
HET    SO4  B 502       5                                                       
HET    SO4  B 503       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *404(H2 O)                                                    
HELIX    1   1 THR A 1931  TYR A 1939  1                                   9    
HELIX    2   2 ARG A 1941  ALA A 1951  1                                  11    
HELIX    3   3 THR A 1964  ALA A 1972  1                                   9    
HELIX    4   4 ALA A 1974  ASN A 1984  1                                  11    
HELIX    5   5 THR A 1998  ALA A 2007  1                                  10    
HELIX    6   6 VAL A 2008  SER A 2018  1                                  11    
HELIX    7   7 SER A 2031  VAL A 2039  1                                   9    
HELIX    8   8 ASN A 2041  ASN A 2051  1                                  11    
HELIX    9   9 THR A 2064  GLY A 2073  1                                  10    
HELIX   10  10 SER A 2074  HIS A 2084  1                                  11    
HELIX   11  11 LEU A 2097  ARG A 2105  1                                   9    
HELIX   12  12 HIS A 2107  TYR A 2117  1                                  11    
HELIX   13  13 SER B 1912  GLN B 1917  1                                   6    
HELIX   14  14 THR B 1931  TYR B 1939  1                                   9    
HELIX   15  15 ARG B 1941  ALA B 1951  1                                  11    
HELIX   16  16 THR B 1964  ASP B 1973  1                                  10    
HELIX   17  17 ALA B 1974  ARG B 1983  1                                  10    
HELIX   18  18 THR B 1998  ALA B 2007  1                                  10    
HELIX   19  19 VAL B 2008  SER B 2018  1                                  11    
HELIX   20  20 SER B 2031  VAL B 2039  1                                   9    
HELIX   21  21 ASN B 2041  ASN B 2051  1                                  11    
HELIX   22  22 THR B 2064  GLY B 2073  1                                  10    
HELIX   23  23 SER B 2074  HIS B 2084  1                                  11    
HELIX   24  24 LEU B 2097  ARG B 2105  1                                   9    
HELIX   25  25 HIS B 2107  TYR B 2117  1                                  11    
SHEET    1   A 2 ILE A1911  SER A1912  0                                        
SHEET    2   A 2 ILE A1915  TYR A1916 -1  O  ILE A1915   N  SER A1912           
SITE     1 AC1  4 HOH B  57  ASP B1973  GLN B1975  GLY B1976                    
SITE     1 AC2  4 HOH B 284  HOH B 311  ARG B2071  ARG B2096                    
CRYST1   97.933   97.933  109.068  90.00  90.00 120.00 P 65         12          
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      0.010211  0.005895  0.000000        0.00000                         
SCALE2      0.000000  0.011791  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009169        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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