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Database: PDB
Entry: 2JJL
LinkDB: 2JJL
Original site: 2JJL 
HEADER    VIRAL PROTEIN                           14-APR-08   2JJL              
TITLE     STRUCTURE OF AVIAN REOVIRUS SIGMAC117-326, P321 CRYSTAL FORM          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIGMA-C CAPSID PROTEIN;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 117-326;                                          
COMPND   5 SYNONYM: SIGMA-3 PROTEIN;                                            
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AVIAN REOVIRUS;                                 
SOURCE   3 ORGANISM_TAXID: 38170;                                               
SOURCE   4 STRAIN: S1133;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: DE3;                                      
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28C-PLUS;                              
SOURCE  10 OTHER_DETAILS: THE AVIAN REOVIRUS STRAIN S1133 WAS ORIGINALLY        
SOURCE  11 PROVIDED BY DR. PHILIP I.MARCUS WHEN DR. J.BENAVENTE WAS A ROCHE     
SOURCE  12 VISITING SCIENTIST IN THE LABORATORY OF DR. A.SHATKIN                
KEYWDS    ALPHA-HELICAL COILED COIL, RECEPTOR-BINDING, TRIPLE BETA-SPIRAL,      
KEYWDS   2 VIRAL PROTEIN, VIRION, COILED COIL, BETA-BARREL                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.GUARDADO-CALVO,G.C.FOX,A.L.LLAMAS-SAIZ,J.BENAVENTE,M.J.VAN RAAIJ    
REVDAT   4   13-DEC-23 2JJL    1       REMARK LINK                              
REVDAT   3   07-FEB-18 2JJL    1       JRNL                                     
REVDAT   2   15-SEP-09 2JJL    1       JRNL   REMARK                            
REVDAT   1   13-JAN-09 2JJL    0                                                
JRNL        AUTH   P.GUARDADO-CALVO,G.C.FOX,A.L.LLAMAS-SAIZ,M.J.VAN RAAIJ       
JRNL        TITL   CRYSTALLOGRAPHIC STRUCTURE OF THE ALPHA-HELICAL TRIPLE       
JRNL        TITL 2 COILED-COIL DOMAIN OF AVIAN REOVIRUS S1133 FIBRE.            
JRNL        REF    J. GEN. VIROL.                V.  90   672 2009              
JRNL        REFN                   ISSN 0022-1317                               
JRNL        PMID   19218213                                                     
JRNL        DOI    10.1099/VIR.0.008276-0                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.J.VAN RAAIJ,X.L.HERMO-PARRADO,P.GUARDADO-CALVO,G.C.FOX,    
REMARK   1  AUTH 2 A.L.LLAMAS-SAIZ,C.COSTAS,J.MARTINEZ-COSTAS,J.BENAVENTE       
REMARK   1  TITL   CRYSTALLIZATION OF THE C-TERMINAL GLOBULAR DOMAIN OF AVIAN   
REMARK   1  TITL 2 REOVIRUS FIBRE.                                              
REMARK   1  REF    ACTA CRYSTALLOGR., SECT.F     V.  61   651 2005              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   16511119                                                     
REMARK   1  DOI    10.1107/S1744309105016933                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.GUARDADO-CALVO,G.C.FOX,X.L.HERMO-PARRADO,A.L.LLAMAS-SAIZ,  
REMARK   1  AUTH 2 C.COSTAS,J.MARTINEZ-COSTAS,J.BENAVENTE,M.J.VAN RAAIJ         
REMARK   1  TITL   STRUCTURE OF THE CARBOXY-TERMINAL RECEPTOR-BINDING DOMAIN OF 
REMARK   1  TITL 2 AVIAN REOVIRUS FIBRE SIGMAC.                                 
REMARK   1  REF    J.MOL.BIOL.                   V. 354   137 2005              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   16236316                                                     
REMARK   1  DOI    10.1016/J.JMB.2005.09.034                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 17714                          
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 + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1514                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3116                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 268                          
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1550                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 202                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.19000                                              
REMARK   3    B22 (A**2) : 2.19000                                              
REMARK   3    B33 (A**2) : -3.29000                                             
REMARK   3    B12 (A**2) : 1.10000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.175         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.165         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.093         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.700         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1586 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2157 ; 1.509 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   206 ; 6.499 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    65 ;36.864 ;23.385       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   243 ;13.095 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;18.644 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   257 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1194 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   594 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1112 ; 0.295 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   126 ; 0.163 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    80 ; 0.183 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.214 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1056 ; 3.225 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1666 ; 4.852 ; 7.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   594 ; 7.171 ;10.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   491 ; 8.862 ;15.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2JJL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290035918.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM16                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9840                             
REMARK 200  MONOCHROMATOR                  : SI111 DOUBLE-CRYSTAL               
REMARK 200  OPTICS                         : RD COATED FLAT AND TOROIDAL        
REMARK 200                                   MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19318                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 20.00                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 52.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 20.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.43000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.40                              
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: CHAIN C OF PDB ENTRY 2VRS                            
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6-0.75 M AMMONIUM SULPHATE, 0.1 M      
REMARK 280  TRIS-HCL PH 8.4, 25% GLYCEROL, 50 MM ZINC SULPHATE                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-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 -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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
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        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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 12620 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.8 KCAL/MOL                       
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   BIOMT1   2 -0.500000 -0.866025  0.000000       77.65700            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       38.82850            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       67.25293            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CL    CL A1327  LIES ON A SPECIAL POSITION.                          
REMARK 375 CL    CL A1328  LIES ON A SPECIAL POSITION.                          
REMARK 375 ZN    ZN A1331  LIES ON A SPECIAL POSITION.                          
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     ILE A   116                                                      
REMARK 465     LEU A   117                                                      
REMARK 465     GLN A   118                                                      
REMARK 465     THR A   119                                                      
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    VAL A 186      -65.26     68.91                                   
REMARK 500    ASN A 208      139.20   -170.39                                   
REMARK 500    HIS A 255       75.77     58.00                                   
REMARK 500    ALA A 291     -163.78   -122.19                                   
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 A2073        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A2120        DISTANCE =  5.89 ANGSTROMS                       
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                              ZN A1332  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 122   OD1                                                    
REMARK 620 2 HIS A 287   ND1 112.4                                              
REMARK 620 3 TYR A 289   OH  114.6 101.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1330  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 158   NE2                                                    
REMARK 620 2 HIS A 158   NE2 116.6                                              
REMARK 620 3 HIS A 158   NE2 108.5 127.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1331  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 212   OD1                                                    
REMARK 620 2 ASP A 212   OD1 102.3                                              
REMARK 620 N                    1                                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1327                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1328                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1329                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1330                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1331                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1332                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2BSF   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE C-TERMINAL RECEPTOR-BINDING DOMAIN OF AVIAN         
REMARK 900 REOVIRUS FIBRE SIGMAC, ZN CRYSTAL FORM.                              
REMARK 900 RELATED ID: 2VRS   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AVIAN REOVIRUS SIGMAC117-326, C2 CRYSTAL FORM           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE FIRST RESIDUE, ILE-116, IS A REMNANT OF THE EXPRESSION           
REMARK 999 TAG.                                                                 
DBREF  2JJL A  116   116  PDB    2JJL     2JJL           116    116             
DBREF  2JJL A  117   326  UNP    Q992I2   SIGC_ARVS1     117    326             
SEQRES   1 A  211  ILE LEU GLN THR THR VAL ASP GLY ASN SER THR ALA ILE          
SEQRES   2 A  211  SER ASN LEU LYS SER ASP ILE SER SER ASN GLY LEU ALA          
SEQRES   3 A  211  ILE THR ASP LEU GLN ASP ARG VAL LYS SER LEU GLU SER          
SEQRES   4 A  211  THR ALA SER HIS GLY LEU SER PHE SER PRO PRO LEU SER          
SEQRES   5 A  211  VAL ALA ASP GLY VAL VAL SER LEU ASP MET ASP PRO TYR          
SEQRES   6 A  211  PHE CYS SER GLN ARG VAL SER LEU THR SER TYR SER ALA          
SEQRES   7 A  211  GLU ALA GLN LEU MET GLN PHE ARG TRP MET ALA ARG GLY          
SEQRES   8 A  211  THR ASN GLY SER SER ASP THR ILE ASP MET THR VAL ASN          
SEQRES   9 A  211  ALA HIS CYS HIS GLY ARG ARG THR ASP TYR MET MET SER          
SEQRES  10 A  211  SER THR GLY ASN LEU THR VAL THR SER ASN VAL VAL LEU          
SEQRES  11 A  211  LEU THR PHE ASP LEU SER ASP ILE THR HIS ILE PRO SER          
SEQRES  12 A  211  ASP LEU ALA ARG LEU VAL PRO SER ALA GLY PHE GLN ALA          
SEQRES  13 A  211  ALA SER PHE PRO VAL ASP VAL SER PHE THR ARG ASP SER          
SEQRES  14 A  211  ALA THR HIS ALA TYR GLN ALA TYR GLY VAL TYR SER SER          
SEQRES  15 A  211  SER ARG VAL PHE THR ILE THR PHE PRO THR GLY GLY ASP          
SEQRES  16 A  211  GLY THR ALA ASN ILE ARG SER LEU THR VAL ARG THR GLY          
SEQRES  17 A  211  ILE ASP THR                                                  
HET     CL  A1327       1                                                       
HET     CL  A1328       1                                                       
HET    SO4  A1329       5                                                       
HET     ZN  A1330       1                                                       
HET     ZN  A1331       1                                                       
HET     ZN  A1332       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   2   CL    2(CL 1-)                                                     
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5   ZN    3(ZN 2+)                                                     
FORMUL   8  HOH   *202(H2 O)                                                    
HELIX    1   1 THR A  120  THR A  155  1                                  36    
HELIX    2   2 ASP A  259  VAL A  264  5                                   6    
HELIX    3   3 SER A  266  ALA A  271  1                                   6    
SHEET    1  AA 2 LEU A 166  ALA A 169  0                                        
SHEET    2  AA 2 VAL A 172  LEU A 175 -1  O  VAL A 172   N  ALA A 169           
SHEET    1  AB 2 CYS A 182  GLN A 184  0                                        
SHEET    2  AB 2 LEU A 188  SER A 190 -1  O  THR A 189   N  SER A 183           
SHEET    1  AC 5 ASN A 236  VAL A 239  0                                        
SHEET    2  AC 5 ALA A 313  ASP A 325 -1  O  ALA A 313   N  VAL A 239           
SHEET    3  AC 5 ARG A 226  THR A 234 -1  O  THR A 227   N  ILE A 324           
SHEET    4  AC 5 THR A 213  HIS A 223 -1  O  ASP A 215   N  THR A 234           
SHEET    5  AC 5 GLN A 196  ASN A 208 -1  O  GLN A 196   N  CYS A 222           
SHEET    1  AD 7 ASN A 236  VAL A 239  0                                        
SHEET    2  AD 7 ALA A 313  ASP A 325 -1  O  ALA A 313   N  VAL A 239           
SHEET    3  AD 7 PHE A 274  ARG A 282 -1  O  ASP A 277   N  ARG A 321           
SHEET    4  AD 7 ALA A 285  SER A 297 -1  O  ALA A 285   N  ARG A 282           
SHEET    5  AD 7 VAL A 300  PRO A 306 -1  O  VAL A 300   N  SER A 296           
SHEET    6  AD 7 VAL A 243  ASP A 249 -1  O  VAL A 244   N  PHE A 305           
SHEET    7  AD 7 GLN A 196  ASN A 208 -1  O  ARG A 205   N  THR A 247           
LINK         OD1 ASP A 122                ZN    ZN A1332     1555   1555  1.98  
LINK         NE2 HIS A 158                ZN    ZN A1330     1555   1555  2.12  
LINK         NE2 HIS A 158                ZN    ZN A1330     2655   1555  1.74  
LINK         NE2 HIS A 158                ZN    ZN A1330     3665   1555  1.93  
LINK         OD1 ASP A 212                ZN    ZN A1331     5555   1555  2.11  
LINK         OD1 ASP A 212                ZN    ZN A1331     1555   1555  2.01  
LINK         ND1 HIS A 287                ZN    ZN A1332     3666   1555  2.21  
LINK         OH  TYR A 289                ZN    ZN A1332     3666   1555  2.29  
CISPEP   1 PRO A  164    PRO A  165          0         6.96                     
SITE     1 AC1  1 ASN A 124                                                     
SITE     1 AC2  1 ASN A 138                                                     
SITE     1 AC3  3 ARG A 201  THR A 281  SER A 284                               
SITE     1 AC4  2 HIS A 158  HOH A2202                                          
SITE     1 AC5  2 ASP A 212  THR A 213                                          
SITE     1 AC6  3 ASP A 122  HIS A 287  TYR A 289                               
CRYST1   77.657   77.657  121.449  90.00  90.00 120.00 P 3 2 1       6          
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      0.012877  0.007435  0.000000        0.00000                         
SCALE2      0.000000  0.014869  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008234        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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