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Database: PDB
Entry: 3SPV
LinkDB: 3SPV
Original site: 3SPV 
HEADER    IMMUNE SYSTEM                           04-JUL-11   3SPV              
TITLE     CRYSTAL STRUCTURE OF A PEPTIDE-HLA COMPLEX                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, B-8 ALPHA CHAIN;   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 25-300;                                       
COMPND   5 SYNONYM: HLA B8 HEAVY CHAIN, MHC CLASS I ANTIGEN B*8;                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3;                           
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: PEPTIDE FROM TRANS-ACTIVATOR PROTEIN BZLF1;                
COMPND  14 CHAIN: C;                                                            
COMPND  15 SYNONYM: EB1, ZEBRA;                                                 
COMPND  16 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: HLA-B;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: B2M;                                                           
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET30;                                    
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 SYNTHETIC: YES;                                                      
SOURCE  23 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 4;                            
SOURCE  24 ORGANISM_COMMON: EPSTEIN-BARR VIRUS;                                 
SOURCE  25 ORGANISM_TAXID: 10377;                                               
SOURCE  26 OTHER_DETAILS: SYNTHETIC PEPTIDE                                     
KEYWDS    IMMUNOLOGY, RECEPTOR, HLA, HLA-B*0801, EBV, MHC, TCR, T CELL, IMMUNE  
KEYWDS   2 SYSTEM                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.GRAS,J.ROSSJOHN                                                     
REVDAT   1   04-JUL-12 3SPV    0                                                
JRNL        AUTH   S.GRAS,J.ROSSJOHN                                            
JRNL        TITL   CRYSTAL STRUCTURE OF A PEPTIDE-HLA COMPLEX                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_357)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.58                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 103679                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5202                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.5865 -  2.7981    1.00    11066   567  0.1774 0.1937        
REMARK   3     2  2.7981 -  2.2219    0.99    10743   545  0.1912 0.2296        
REMARK   3     3  2.2219 -  1.9413    0.99    10508   564  0.1840 0.1917        
REMARK   3     4  1.9413 -  1.7640    0.97    10351   549  0.1896 0.2028        
REMARK   3     5  1.7640 -  1.6376    0.95    10027   536  0.1860 0.2167        
REMARK   3     6  1.6376 -  1.5411    0.93     9877   501  0.1966 0.2262        
REMARK   3     7  1.5411 -  1.4639    0.90     9538   523  0.2114 0.2517        
REMARK   3     8  1.4639 -  1.4002    0.87     9164   475  0.2408 0.2669        
REMARK   3     9  1.4002 -  1.3463    0.83     8722   480  0.2639 0.2917        
REMARK   3    10  1.3463 -  1.2999    0.81     8481   462  0.2880 0.3264        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 27.52                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.95                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.39020                                              
REMARK   3    B22 (A**2) : -1.73080                                             
REMARK   3    B33 (A**2) : 1.34060                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           3648                                  
REMARK   3   ANGLE     :  1.036           5009                                  
REMARK   3   CHIRALITY :  0.073            504                                  
REMARK   3   PLANARITY :  0.005            687                                  
REMARK   3   DIHEDRAL  : 12.360           1384                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3SPV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JUL-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066504.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.984                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 111282                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 8.000                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.360                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1M05                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-20% PEG 4000, 0.2M AMMONIUM           
REMARK 280  ACETATE, 0.1M NA-CITRATE, PH 5.6, VAPOR DIFFUSION, TEMPERATURE      
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       25.28000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.01000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.73000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.01000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.28000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.73000            
REMARK 290   SMTRY3   4  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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET B  99   C     MET B  99   OXT    -0.128                       
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    ARG A  14       71.75   -155.54                                   
REMARK 500    ASP A  29     -121.96     49.35                                   
REMARK 500    ARG A 239      -20.62     89.10                                   
REMARK 500    TRP B  60       -3.10     80.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 279  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  74   OD2                                                    
REMARK 620 2 LEU A  95   O   126.4                                              
REMARK 620 3 SER A  97   OG  106.1 120.4                                        
REMARK 620 4 HOH A 346   O    67.5 123.9  50.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 277                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 278                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 279                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1M05   RELATED DB: PDB                                   
DBREF  3SPV A    1   276  UNP    P30460   1B08_HUMAN      25    300             
DBREF  3SPV B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  3SPV C    1     8  UNP    P03206   BZLF1_EBVB9    190    197             
SEQRES   1 A  276  GLY SER HIS SER MET ARG TYR PHE ASP THR ALA MET SER          
SEQRES   2 A  276  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE SER VAL GLY          
SEQRES   3 A  276  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 A  276  ALA ALA SER PRO ARG GLU GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 A  276  GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG ASN THR GLN          
SEQRES   6 A  276  ILE PHE LYS THR ASN THR GLN THR ASP ARG GLU SER LEU          
SEQRES   7 A  276  ARG ASN LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY          
SEQRES   8 A  276  SER HIS THR LEU GLN SER MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  276  PRO ASP GLY ARG LEU LEU ARG GLY HIS ASN GLN TYR ALA          
SEQRES  10 A  276  TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 A  276  ARG SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE THR          
SEQRES  12 A  276  GLN ARG LYS TRP GLU ALA ALA ARG VAL ALA GLU GLN ASP          
SEQRES  13 A  276  ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG          
SEQRES  14 A  276  ARG TYR LEU GLU ASN GLY LYS ASP THR LEU GLU ARG ALA          
SEQRES  15 A  276  ASP PRO PRO LYS THR HIS VAL THR HIS HIS PRO ILE SER          
SEQRES  16 A  276  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 A  276  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 A  276  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 A  276  PRO ALA GLY ASP ARG THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 A  276  VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 A  276  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 A  276  TRP GLU PRO                                                  
SEQRES   1 B   99  ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 B   99  PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR          
SEQRES   3 B   99  VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU          
SEQRES   4 B   99  LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER          
SEQRES   5 B   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU          
SEQRES   6 B   99  TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR          
SEQRES   7 B   99  ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS          
SEQRES   8 B   99  ILE VAL LYS TRP ASP ARG ASP MET                              
SEQRES   1 C    8  ARG ALA LYS PHE LYS GLN LEU LEU                              
HET    ACT  A 277       4                                                       
HET    ACT  A 278       4                                                       
HET     NA  A 279       1                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM      NA SODIUM ION                                                       
FORMUL   4  ACT    2(C2 H3 O2 1-)                                               
FORMUL   6   NA    NA 1+                                                        
FORMUL   7  HOH   *536(H2 O)                                                    
HELIX    1   1 ALA A   49  GLN A   54  1                                   6    
HELIX    2   2 GLY A   56  TYR A   85  1                                  30    
HELIX    3   3 ASP A  137  ALA A  150  1                                  14    
HELIX    4   4 ARG A  151  GLY A  162  1                                  12    
HELIX    5   5 GLY A  162  GLY A  175  1                                  14    
HELIX    6   6 GLY A  175  GLU A  180  1                                   6    
HELIX    7   7 THR A  225  THR A  228  5                                   4    
HELIX    8   8 GLU A  253  GLN A  255  5                                   3    
SHEET    1   A 7 THR A  31  ASP A  37  0                                        
SHEET    2   A 7 ARG A  21  VAL A  28 -1  N  GLY A  26   O  PHE A  33           
SHEET    3   A 7 HIS A   3  MET A  12 -1  N  PHE A   8   O  VAL A  25           
SHEET    4   A 7 THR A  94  VAL A 103 -1  O  LEU A  95   N  ALA A  11           
SHEET    5   A 7 LEU A 109  TYR A 118 -1  O  LEU A 110   N  ASP A 102           
SHEET    6   A 7 LYS A 121  LEU A 126 -1  O  TYR A 123   N  TYR A 116           
SHEET    7   A 7 TRP A 133  ALA A 135 -1  O  THR A 134   N  ALA A 125           
SHEET    1   B 4 LYS A 186  PRO A 193  0                                        
SHEET    2   B 4 GLU A 198  PHE A 208 -1  O  TRP A 204   N  HIS A 188           
SHEET    3   B 4 PHE A 241  PRO A 250 -1  O  VAL A 249   N  ALA A 199           
SHEET    4   B 4 GLU A 229  LEU A 230 -1  N  GLU A 229   O  ALA A 246           
SHEET    1   C 4 LYS A 186  PRO A 193  0                                        
SHEET    2   C 4 GLU A 198  PHE A 208 -1  O  TRP A 204   N  HIS A 188           
SHEET    3   C 4 PHE A 241  PRO A 250 -1  O  VAL A 249   N  ALA A 199           
SHEET    4   C 4 ARG A 234  PRO A 235 -1  N  ARG A 234   O  GLN A 242           
SHEET    1   D 4 GLU A 222  ASP A 223  0                                        
SHEET    2   D 4 THR A 214  ARG A 219 -1  N  ARG A 219   O  GLU A 222           
SHEET    3   D 4 TYR A 257  GLN A 262 -1  O  HIS A 260   N  THR A 216           
SHEET    4   D 4 LEU A 270  LEU A 272 -1  O  LEU A 272   N  CYS A 259           
SHEET    1   E 4 LYS B   6  SER B  11  0                                        
SHEET    2   E 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3   E 4 PHE B  62  PHE B  70 -1  O  THR B  68   N  LEU B  23           
SHEET    4   E 4 GLU B  50  HIS B  51 -1  N  GLU B  50   O  TYR B  67           
SHEET    1   F 4 LYS B   6  SER B  11  0                                        
SHEET    2   F 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3   F 4 PHE B  62  PHE B  70 -1  O  THR B  68   N  LEU B  23           
SHEET    4   F 4 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    1   G 4 GLU B  44  ARG B  45  0                                        
SHEET    2   G 4 ILE B  35  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3   G 4 TYR B  78  HIS B  84 -1  O  ALA B  79   N  LEU B  40           
SHEET    4   G 4 LYS B  91  LYS B  94 -1  O  LYS B  91   N  VAL B  82           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.06  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.03  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
LINK         OD2 ASP A  74                NA    NA A 279     1555   1555  2.91  
LINK         O   LEU A  95                NA    NA A 279     1555   1555  2.91  
LINK         OG BSER A  97                NA    NA A 279     1555   1555  3.03  
LINK        NA    NA A 279                 O   HOH A 346     1555   1555  2.93  
CISPEP   1 PRO A   43    ARG A   44          0        -1.05                     
CISPEP   2 ARG A   44    GLU A   45          0         9.23                     
CISPEP   3 TYR A  209    PRO A  210          0         3.03                     
CISPEP   4 HIS B   31    PRO B   32          0         0.63                     
SITE     1 AC1  6 MET A  12  ARG A  14  ARG A  17  ARG A 131                    
SITE     2 AC1  6 HOH A 291  ASP B  34                                          
SITE     1 AC2  5 SER A  92  HIS A  93  ASP A 119  HOH A 404                    
SITE     2 AC2  5 ILE B   1                                                     
SITE     1 AC3  6 ASP A   9  ASP A  74  LEU A  95  SER A  97                    
SITE     2 AC3  6 HOH A 346  LYS C   5                                          
CRYST1   50.560   81.460  110.020  90.00  90.00  90.00 P 21 21 21    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      0.019778  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012276  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009089        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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