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Database: PDB
Entry: 4JKS
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HEADER    TRANSFERASE                             11-MAR-13   4JKS              
TITLE     CRYSTAL STRUCTURE OF PROBABLE SUGAR KINASE PROTEIN FROM RHIZOBIUM ETLI
TITLE    2 CFN 42 COMPLEXED WITH DMSO, NYSGRC TARGET 14306                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE SUGAR KINASE PROTEIN;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHIZOBIUM ETLI;                                 
SOURCE   3 ORGANISM_TAXID: 347834;                                              
SOURCE   4 STRAIN: CFN 42;                                                      
SOURCE   5 GENE: RHE_CH00135;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON+RIL;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)                              
KEYWDS    STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, NYSGRC, PSI-       
KEYWDS   2 BIOLOGY, NEW YORK STRUCTURAL GENOMICS RESEARCH CONSORTIUM,           
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.N.MALASHKEVICH,R.BHOSLE,R.TORO,B.HILLERICH,A.GIZZI,S.GARFORTH,      
AUTHOR   2 A.KAR,M.K.CHAN,J.LAFLUER,H.PATEL,B.MATIKAINEN,S.CHAMALA,S.LIM,       
AUTHOR   3 A.CELIKGIL,G.VILLEGAS,B.EVANS,J.LOVE,A.FISER,K.KHAFIZOV,R.SEIDEL,    
AUTHOR   4 J.B.BONANNO,S.C.ALMO,NEW YORK STRUCTURAL GENOMICS RESEARCH           
AUTHOR   5 CONSORTIUM (NYSGRC)                                                  
REVDAT   3   06-DEC-23 4JKS    1       REMARK                                   
REVDAT   2   20-SEP-23 4JKS    1       REMARK SEQADV LINK                       
REVDAT   1   27-MAR-13 4JKS    0                                                
JRNL        AUTH   V.N.MALASHKEVICH,R.BHOSLE,R.TORO,B.HILLERICH,A.GIZZI,        
JRNL        AUTH 2 S.GARFORTH,A.KAR,M.K.CHAN,J.LAFLUER,H.PATEL,B.MATIKAINEN,    
JRNL        AUTH 3 S.CHAMALA,S.LIM,A.CELIKGIL,G.VILLEGAS,B.EVANS,J.LOVE,        
JRNL        AUTH 4 A.FISER,K.KHAFIZOV,R.SEIDEL,J.B.BONANNO,S.C.ALMO             
JRNL        TITL   CRYSTAL STRUCTURE OF PROBABLE SUGAR KINASE PROTEIN FROM      
JRNL        TITL 2 RHIZOBIUM ETLI CFN 42 COMPLEXED WITH DMSO, NYSGRC TARGET     
JRNL        TITL 3 14306                                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 1.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 107348                         
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) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5359                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.51                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.55                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7430                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 381                          
REMARK   3   BIN FREE R VALUE                    : 0.1890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5008                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 616                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.33000                                             
REMARK   3    B22 (A**2) : -0.26000                                             
REMARK   3    B33 (A**2) : 0.59000                                              
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.019         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.016         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.022         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.197         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5325 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7242 ; 1.175 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   714 ; 5.292 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   256 ;37.112 ;24.023       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   831 ;12.746 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;12.677 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   812 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4121 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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):  5325 ; 2.592 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   195 ;22.238 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  5642 ;11.741 ; 5.000       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -1        A   328                          
REMARK   3    RESIDUE RANGE :   A   401        A   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7346  -7.5369 -20.4648              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0112 T22:   0.0156                                     
REMARK   3      T33:   0.0012 T12:  -0.0025                                     
REMARK   3      T13:  -0.0024 T23:   0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1781 L22:   0.1872                                     
REMARK   3      L33:   0.1280 L12:   0.0177                                     
REMARK   3      L13:  -0.0313 L23:  -0.0398                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0057 S12:  -0.0049 S13:  -0.0070                       
REMARK   3      S21:   0.0032 S22:   0.0016 S23:   0.0053                       
REMARK   3      S31:   0.0129 S32:   0.0102 S33:  -0.0073                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    -1        B   328                          
REMARK   3    RESIDUE RANGE :   B   401        B   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.7203  29.3683 -20.3165              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0116 T22:   0.0166                                     
REMARK   3      T33:   0.0013 T12:  -0.0014                                     
REMARK   3      T13:   0.0032 T23:  -0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1564 L22:   0.2837                                     
REMARK   3      L33:   0.1531 L12:   0.0428                                     
REMARK   3      L13:   0.0540 L23:   0.0675                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0030 S12:  -0.0199 S13:   0.0083                       
REMARK   3      S21:   0.0063 S22:   0.0005 S23:   0.0030                       
REMARK   3      S31:  -0.0133 S32:  -0.0148 S33:  -0.0035                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 4JKS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000078170.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 107497                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.510                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4E3A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 0.1M              
REMARK 280  BIS:TRIS:HCL, PH 6.5,25% PEG3350, SOAKED IN 13% DMSO, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 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       40.41500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.21450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.58250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.21450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.41500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.58250            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 9.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MSE A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     GLY A   -14                                                      
REMARK 465     VAL A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     LEU A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     THR A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     ASN A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     TYR A    -5                                                      
REMARK 465     PHE A    -4                                                      
REMARK 465     GLN A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     MSE B   -23                                                      
REMARK 465     HIS B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     GLY B   -14                                                      
REMARK 465     VAL B   -13                                                      
REMARK 465     ASP B   -12                                                      
REMARK 465     LEU B   -11                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     THR B    -9                                                      
REMARK 465     GLU B    -8                                                      
REMARK 465     ASN B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     TYR B    -5                                                      
REMARK 465     PHE B    -4                                                      
REMARK 465     GLN B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 104       64.90   -107.47                                   
REMARK 500    SER A 186      -54.13     72.68                                   
REMARK 500    SER A 245     -124.08     50.97                                   
REMARK 500    ASP A 270      112.90   -164.47                                   
REMARK 500    SER B 186      -54.73     74.59                                   
REMARK 500    SER B 245     -123.11     51.16                                   
REMARK 500    ASP B 270      110.95   -164.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4E3A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: NYSGRC-014306   RELATED DB: TARGETTRACK                  
REMARK 900 RELATED ID: 4JKU   RELATED DB: PDB                                   
DBREF  4JKS A   -1   328  UNP    Q2KDX6   Q2KDX6_RHIEC     1    330             
DBREF  4JKS B   -1   328  UNP    Q2KDX6   Q2KDX6_RHIEC     1    330             
SEQADV 4JKS MSE A  -23  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS A  -22  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS A  -21  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS A  -20  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS A  -19  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS A  -18  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS A  -17  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS SER A  -16  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS SER A  -15  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS GLY A  -14  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS VAL A  -13  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS ASP A  -12  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS LEU A  -11  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS GLY A  -10  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS THR A   -9  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS GLU A   -8  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS ASN A   -7  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS LEU A   -6  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS TYR A   -5  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS PHE A   -4  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS GLN A   -3  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS SER A   -2  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS MSE B  -23  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS B  -22  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS B  -21  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS B  -20  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS B  -19  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS B  -18  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS HIS B  -17  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS SER B  -16  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS SER B  -15  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS GLY B  -14  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS VAL B  -13  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS ASP B  -12  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS LEU B  -11  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS GLY B  -10  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS THR B   -9  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS GLU B   -8  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS ASN B   -7  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS LEU B   -6  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS TYR B   -5  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS PHE B   -4  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS GLN B   -3  UNP  Q2KDX6              EXPRESSION TAG                 
SEQADV 4JKS SER B   -2  UNP  Q2KDX6              EXPRESSION TAG                 
SEQRES   1 A  352  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  352  GLY THR GLU ASN LEU TYR PHE GLN SER MSE THR ARG PHE          
SEQRES   3 A  352  ASP VAL LEU THR VAL GLY ASN ALA ILE VAL ASP ILE ILE          
SEQRES   4 A  352  SER ARG CYS ASN ASP GLN PHE LEU ILE ASP ASN GLN ILE          
SEQRES   5 A  352  THR LYS ALA ALA MSE ASN LEU ILE ASP ALA GLU ARG ALA          
SEQRES   6 A  352  GLU LEU LEU TYR SER ARG MSE GLY PRO ALA LEU GLU ALA          
SEQRES   7 A  352  SER GLY GLY SER ALA GLY ASN THR ALA ALA GLY VAL ALA          
SEQRES   8 A  352  ASN LEU GLY GLY LYS ALA ALA TYR PHE GLY ASN VAL ALA          
SEQRES   9 A  352  ALA ASP GLN LEU GLY ASP ILE PHE THR HIS ASP ILE ARG          
SEQRES  10 A  352  ALA GLN GLY VAL HIS TYR GLN THR LYS PRO LYS GLY ALA          
SEQRES  11 A  352  PHE PRO PRO THR ALA ARG SER MSE ILE PHE VAL THR GLU          
SEQRES  12 A  352  ASP GLY GLU ARG SER MSE ASN THR TYR LEU GLY ALA CYS          
SEQRES  13 A  352  VAL GLU LEU GLY PRO GLU ASP VAL GLU ALA ASP VAL VAL          
SEQRES  14 A  352  ALA ASP ALA LYS VAL THR TYR PHE GLU GLY TYR LEU TRP          
SEQRES  15 A  352  ASP PRO PRO ARG ALA LYS GLU ALA ILE LEU ASP CYS ALA          
SEQRES  16 A  352  ARG ILE ALA HIS GLN HIS GLY ARG GLU MSE SER MSE THR          
SEQRES  17 A  352  LEU SER ASP SER PHE CYS VAL ASP ARG TYR ARG GLY GLU          
SEQRES  18 A  352  PHE LEU ASP LEU MSE ARG SER GLY LYS VAL ASP ILE VAL          
SEQRES  19 A  352  PHE ALA ASN ARG GLN GLU ALA LEU SER LEU TYR GLN THR          
SEQRES  20 A  352  ASP ASP PHE GLU GLU ALA LEU ASN ARG ILE ALA ALA ASP          
SEQRES  21 A  352  CYS LYS ILE ALA ALA VAL THR MSE SER GLU ASN GLY ALA          
SEQRES  22 A  352  VAL ILE LEU LYS GLY ARG GLU ARG TYR TYR VAL ASN ALA          
SEQRES  23 A  352  ILE ARG ILE ARG GLU VAL VAL ASP THR THR GLY ALA GLY          
SEQRES  24 A  352  ASP LEU PHE ALA SER GLY PHE LEU TYR GLY TYR THR GLN          
SEQRES  25 A  352  GLY ARG SER LEU GLU ASP CYS GLY LYS LEU GLY CYS LEU          
SEQRES  26 A  352  ALA ALA GLY ILE VAL ILE GLN GLN ILE GLY PRO ARG PRO          
SEQRES  27 A  352  MSE THR SER LEU SER GLU ALA ALA LYS GLN ALA GLY LEU          
SEQRES  28 A  352  ILE                                                          
SEQRES   1 B  352  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  352  GLY THR GLU ASN LEU TYR PHE GLN SER MSE THR ARG PHE          
SEQRES   3 B  352  ASP VAL LEU THR VAL GLY ASN ALA ILE VAL ASP ILE ILE          
SEQRES   4 B  352  SER ARG CYS ASN ASP GLN PHE LEU ILE ASP ASN GLN ILE          
SEQRES   5 B  352  THR LYS ALA ALA MSE ASN LEU ILE ASP ALA GLU ARG ALA          
SEQRES   6 B  352  GLU LEU LEU TYR SER ARG MSE GLY PRO ALA LEU GLU ALA          
SEQRES   7 B  352  SER GLY GLY SER ALA GLY ASN THR ALA ALA GLY VAL ALA          
SEQRES   8 B  352  ASN LEU GLY GLY LYS ALA ALA TYR PHE GLY ASN VAL ALA          
SEQRES   9 B  352  ALA ASP GLN LEU GLY ASP ILE PHE THR HIS ASP ILE ARG          
SEQRES  10 B  352  ALA GLN GLY VAL HIS TYR GLN THR LYS PRO LYS GLY ALA          
SEQRES  11 B  352  PHE PRO PRO THR ALA ARG SER MSE ILE PHE VAL THR GLU          
SEQRES  12 B  352  ASP GLY GLU ARG SER MSE ASN THR TYR LEU GLY ALA CYS          
SEQRES  13 B  352  VAL GLU LEU GLY PRO GLU ASP VAL GLU ALA ASP VAL VAL          
SEQRES  14 B  352  ALA ASP ALA LYS VAL THR TYR PHE GLU GLY TYR LEU TRP          
SEQRES  15 B  352  ASP PRO PRO ARG ALA LYS GLU ALA ILE LEU ASP CYS ALA          
SEQRES  16 B  352  ARG ILE ALA HIS GLN HIS GLY ARG GLU MSE SER MSE THR          
SEQRES  17 B  352  LEU SER ASP SER PHE CYS VAL ASP ARG TYR ARG GLY GLU          
SEQRES  18 B  352  PHE LEU ASP LEU MSE ARG SER GLY LYS VAL ASP ILE VAL          
SEQRES  19 B  352  PHE ALA ASN ARG GLN GLU ALA LEU SER LEU TYR GLN THR          
SEQRES  20 B  352  ASP ASP PHE GLU GLU ALA LEU ASN ARG ILE ALA ALA ASP          
SEQRES  21 B  352  CYS LYS ILE ALA ALA VAL THR MSE SER GLU ASN GLY ALA          
SEQRES  22 B  352  VAL ILE LEU LYS GLY ARG GLU ARG TYR TYR VAL ASN ALA          
SEQRES  23 B  352  ILE ARG ILE ARG GLU VAL VAL ASP THR THR GLY ALA GLY          
SEQRES  24 B  352  ASP LEU PHE ALA SER GLY PHE LEU TYR GLY TYR THR GLN          
SEQRES  25 B  352  GLY ARG SER LEU GLU ASP CYS GLY LYS LEU GLY CYS LEU          
SEQRES  26 B  352  ALA ALA GLY ILE VAL ILE GLN GLN ILE GLY PRO ARG PRO          
SEQRES  27 B  352  MSE THR SER LEU SER GLU ALA ALA LYS GLN ALA GLY LEU          
SEQRES  28 B  352  ILE                                                          
MODRES 4JKS MSE A   -1  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE A   33  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE A   48  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE A  114  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE A  125  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE A  181  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE A  183  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE A  202  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE A  244  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE A  315  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE B   -1  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE B   33  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE B   48  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE B  114  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE B  125  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE B  181  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE B  183  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE B  202  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE B  244  MET  SELENOMETHIONINE                                   
MODRES 4JKS MSE B  315  MET  SELENOMETHIONINE                                   
HET    MSE  A  -1       8                                                       
HET    MSE  A  33       8                                                       
HET    MSE  A  48       8                                                       
HET    MSE  A 114       8                                                       
HET    MSE  A 125       8                                                       
HET    MSE  A 181       8                                                       
HET    MSE  A 183       8                                                       
HET    MSE  A 202       8                                                       
HET    MSE  A 244       8                                                       
HET    MSE  A 315       8                                                       
HET    MSE  B  -1       8                                                       
HET    MSE  B  33       8                                                       
HET    MSE  B  48       8                                                       
HET    MSE  B 114       8                                                       
HET    MSE  B 125       8                                                       
HET    MSE  B 181       8                                                       
HET    MSE  B 183       8                                                       
HET    MSE  B 202       8                                                       
HET    MSE  B 244       8                                                       
HET    MSE  B 315       8                                                       
HET    ADN  A 401      19                                                       
HET    DMS  A 402       4                                                       
HET    DMS  A 403       4                                                       
HET    ADN  B 401      19                                                       
HET    DMS  B 402       4                                                       
HET    DMS  B 403       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     ADN ADENOSINE                                                        
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   1  MSE    20(C5 H11 N O2 SE)                                           
FORMUL   3  ADN    2(C10 H13 N5 O4)                                             
FORMUL   4  DMS    4(C2 H6 O S)                                                 
FORMUL   9  HOH   *616(H2 O)                                                    
HELIX    1   1 ASN A   19  ASN A   26  1                                   8    
HELIX    2   2 ASP A   37  MSE A   48  1                                  12    
HELIX    3   3 GLY A   57  GLY A   70  1                                  14    
HELIX    4   4 ASP A   82  GLN A   95  1                                  14    
HELIX    5   5 LEU A  129  LEU A  135  5                                   7    
HELIX    6   6 GLY A  136  VAL A  140  5                                   5    
HELIX    7   7 GLU A  141  ASP A  147  1                                   7    
HELIX    8   8 TYR A  156  ASP A  159  5                                   4    
HELIX    9   9 ARG A  162  HIS A  177  1                                  16    
HELIX   10  10 ASP A  187  SER A  204  1                                  18    
HELIX   11  11 ARG A  214  TYR A  221  1                                   8    
HELIX   12  12 ASP A  225  CYS A  237  1                                  13    
HELIX   13  13 SER A  245  ASN A  247  5                                   3    
HELIX   14  14 GLY A  273  GLN A  288  1                                  16    
HELIX   15  15 SER A  291  ILE A  307  1                                  17    
HELIX   16  16 SER A  317  ALA A  325  1                                   9    
HELIX   17  17 ASN B   19  ASN B   26  1                                   8    
HELIX   18  18 ASP B   37  MSE B   48  1                                  12    
HELIX   19  19 GLY B   57  GLY B   70  1                                  14    
HELIX   20  20 ASP B   82  GLN B   95  1                                  14    
HELIX   21  21 LEU B  129  LEU B  135  5                                   7    
HELIX   22  22 GLY B  136  VAL B  140  5                                   5    
HELIX   23  23 GLU B  141  ASP B  147  1                                   7    
HELIX   24  24 TYR B  156  ASP B  159  5                                   4    
HELIX   25  25 ARG B  162  HIS B  177  1                                  16    
HELIX   26  26 ASP B  187  SER B  204  1                                  18    
HELIX   27  27 ARG B  214  GLN B  222  1                                   9    
HELIX   28  28 ASP B  225  CYS B  237  1                                  13    
HELIX   29  29 SER B  245  ASN B  247  5                                   3    
HELIX   30  30 GLY B  273  GLN B  288  1                                  16    
HELIX   31  31 SER B  291  ILE B  307  1                                  17    
HELIX   32  32 SER B  317  ALA B  325  1                                   9    
SHEET    1   A 9 HIS A  98  TYR A  99  0                                        
SHEET    2   A 9 ALA A  73  PHE A  76  1  N  ALA A  73   O  HIS A  98           
SHEET    3   A 9 PHE A   2  VAL A   7  1  N  THR A   6   O  ALA A  74           
SHEET    4   A 9 ALA A 148  GLU A 154  1  O  TYR A 152   N  LEU A   5           
SHEET    5   A 9 GLU A 180  THR A 184  1  O  SER A 182   N  THR A 151           
SHEET    6   A 9 ILE A 209  ASN A 213  1  O  PHE A 211   N  MSE A 183           
SHEET    7   A 9 ILE A 239  THR A 243  1  O  ALA A 241   N  VAL A 210           
SHEET    8   A 9 ALA A 249  LYS A 253 -1  O  LEU A 252   N  ALA A 240           
SHEET    9   A 9 GLU A 256  VAL A 260 -1  O  VAL A 260   N  ALA A 249           
SHEET    1   B 5 MSE A  33  LEU A  35  0                                        
SHEET    2   B 5 ARG A 123  TYR A 128  1  O  MSE A 125   N  ASN A  34           
SHEET    3   B 5 ALA A 111  VAL A 117 -1  N  MSE A 114   O  ASN A 126           
SHEET    4   B 5 ILE A  11  ARG A  17  1  N  ILE A  14   O  ILE A 115           
SHEET    5   B 5 LEU A  52  SER A  55 -1  O  LEU A  52   N  ILE A  15           
SHEET    1   C 9 HIS B  98  TYR B  99  0                                        
SHEET    2   C 9 ALA B  73  PHE B  76  1  N  TYR B  75   O  HIS B  98           
SHEET    3   C 9 PHE B   2  VAL B   7  1  N  THR B   6   O  ALA B  74           
SHEET    4   C 9 ALA B 148  GLU B 154  1  O  TYR B 152   N  LEU B   5           
SHEET    5   C 9 GLU B 180  THR B 184  1  O  SER B 182   N  THR B 151           
SHEET    6   C 9 ILE B 209  ASN B 213  1  O  PHE B 211   N  MSE B 183           
SHEET    7   C 9 ILE B 239  THR B 243  1  O  ALA B 241   N  VAL B 210           
SHEET    8   C 9 ALA B 249  LYS B 253 -1  O  LEU B 252   N  ALA B 240           
SHEET    9   C 9 GLU B 256  VAL B 260 -1  O  VAL B 260   N  ALA B 249           
SHEET    1   D 5 MSE B  33  LEU B  35  0                                        
SHEET    2   D 5 ARG B 123  TYR B 128  1  O  MSE B 125   N  ASN B  34           
SHEET    3   D 5 ALA B 111  VAL B 117 -1  N  MSE B 114   O  ASN B 126           
SHEET    4   D 5 ILE B  11  ARG B  17  1  N  ILE B  14   O  ILE B 115           
SHEET    5   D 5 LEU B  52  SER B  55 -1  O  LEU B  52   N  ILE B  15           
LINK         C   MSE A  -1                 N   THR A   0     1555   1555  1.33  
LINK         C   ALA A  32                 N   MSE A  33     1555   1555  1.33  
LINK         C   MSE A  33                 N   ASN A  34     1555   1555  1.33  
LINK         C   ARG A  47                 N   MSE A  48     1555   1555  1.33  
LINK         C   MSE A  48                 N   GLY A  49     1555   1555  1.33  
LINK         C   SER A 113                 N   MSE A 114     1555   1555  1.34  
LINK         C   MSE A 114                 N   ILE A 115     1555   1555  1.33  
LINK         C   SER A 124                 N   MSE A 125     1555   1555  1.33  
LINK         C   MSE A 125                 N   ASN A 126     1555   1555  1.33  
LINK         C   GLU A 180                 N   MSE A 181     1555   1555  1.33  
LINK         C   MSE A 181                 N   SER A 182     1555   1555  1.33  
LINK         C   SER A 182                 N   MSE A 183     1555   1555  1.33  
LINK         C   MSE A 183                 N   THR A 184     1555   1555  1.33  
LINK         C   LEU A 201                 N   MSE A 202     1555   1555  1.33  
LINK         C   MSE A 202                 N   ARG A 203     1555   1555  1.33  
LINK         C   THR A 243                 N   MSE A 244     1555   1555  1.33  
LINK         C   MSE A 244                 N   SER A 245     1555   1555  1.33  
LINK         C   PRO A 314                 N   MSE A 315     1555   1555  1.33  
LINK         C   MSE A 315                 N   THR A 316     1555   1555  1.34  
LINK         C   MSE B  -1                 N   THR B   0     1555   1555  1.33  
LINK         C   ALA B  32                 N   MSE B  33     1555   1555  1.33  
LINK         C   MSE B  33                 N   ASN B  34     1555   1555  1.34  
LINK         C   ARG B  47                 N   MSE B  48     1555   1555  1.33  
LINK         C   MSE B  48                 N   GLY B  49     1555   1555  1.33  
LINK         C   SER B 113                 N   MSE B 114     1555   1555  1.34  
LINK         C   MSE B 114                 N   ILE B 115     1555   1555  1.33  
LINK         C   SER B 124                 N   MSE B 125     1555   1555  1.33  
LINK         C   MSE B 125                 N   ASN B 126     1555   1555  1.33  
LINK         C   GLU B 180                 N   MSE B 181     1555   1555  1.33  
LINK         C   MSE B 181                 N   SER B 182     1555   1555  1.33  
LINK         C   SER B 182                 N   MSE B 183     1555   1555  1.33  
LINK         C   MSE B 183                 N   THR B 184     1555   1555  1.32  
LINK         C   LEU B 201                 N   MSE B 202     1555   1555  1.33  
LINK         C   MSE B 202                 N   ARG B 203     1555   1555  1.33  
LINK         C   THR B 243                 N   MSE B 244     1555   1555  1.33  
LINK         C   MSE B 244                 N   SER B 245     1555   1555  1.33  
LINK         C   PRO B 314                 N   MSE B 315     1555   1555  1.33  
LINK         C   MSE B 315                 N   THR B 316     1555   1555  1.33  
CISPEP   1 PHE A  107    PRO A  108          0        -2.13                     
CISPEP   2 PHE B  107    PRO B  108          0        -1.44                     
CISPEP   3 PHE B  107    PRO B  108          0        -0.47                     
SITE     1 AC1 19 ASN A   9  ILE A  11  ASP A  13  MSE A  33                    
SITE     2 AC1 19 GLY A  56  GLY A  57  SER A  58  ASN A  61                    
SITE     3 AC1 19 MSE A 125  THR A 127  GLU A 154  TYR A 156                    
SITE     4 AC1 19 THR A 272  ASP A 276  PRO A 312  HOH A 504                    
SITE     5 AC1 19 HOH A 515  HOH A 543  HOH A 699                               
SITE     1 AC2  6 ILE A  14  ALA A  41  TYR A  45  ARG A 112                    
SITE     2 AC2  6 DMS A 403  HOH A 628                                          
SITE     1 AC3  5 ALA A  38  GLU A  42  ARG A 112  DMS A 402                    
SITE     2 AC3  5 HOH A 704                                                     
SITE     1 AC4 19 ASN B   9  ILE B  11  ASP B  13  MSE B  33                    
SITE     2 AC4 19 GLY B  56  GLY B  57  SER B  58  ASN B  61                    
SITE     3 AC4 19 MSE B 125  THR B 127  GLU B 154  TYR B 156                    
SITE     4 AC4 19 GLY B 273  ASP B 276  PRO B 312  HOH B 510                    
SITE     5 AC4 19 HOH B 525  HOH B 544  HOH B 691                               
SITE     1 AC5  4 GLU B  42  ARG B 112  DMS B 403  HOH B 703                    
SITE     1 AC6  6 ILE B  14  ALA B  41  GLU B  42  TYR B  45                    
SITE     2 AC6  6 ARG B 112  DMS B 402                                          
CRYST1   80.830   91.165   92.429  90.00  90.00  90.00 P 21 21 21    8          
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      0.012372  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010969  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010819        0.00000                         
HETATM    1  N   MSE A  -1      35.115 -24.415 -21.180  1.00 41.48           N  
ANISOU    1  N   MSE A  -1     5015   4732   6014   1171    557   -720       N  
HETATM    2  CA  MSE A  -1      34.905 -22.933 -21.233  1.00 41.18           C  
ANISOU    2  CA  MSE A  -1     4246   4914   6485   1213    225    365       C  
HETATM    3  C   MSE A  -1      34.221 -22.559 -22.519  1.00 39.07           C  
ANISOU    3  C   MSE A  -1     3931   4990   5921    966    571    182       C  
HETATM    4  O   MSE A  -1      34.509 -23.124 -23.579  1.00 38.19           O  
ANISOU    4  O   MSE A  -1     4991   3565   5954    453   -312      9       O  
HETATM    5  CB  MSE A  -1      36.226 -22.167 -21.074  1.00 49.45           C  
ANISOU    5  CB  MSE A  -1     5260   6276   7253    144    358   -118       C  
HETATM    6  CG  MSE A  -1      37.351 -22.697 -21.961  1.00 51.30           C  
ANISOU    6  CG  MSE A  -1     5563   7608   6320    250    620    275       C  
HETATM    7 SE   MSE A  -1      38.890 -21.462 -21.986  1.00 52.29          SE  
ANISOU    7 SE   MSE A  -1     5257   9393   5216    122    419   1362      SE  
HETATM    8  CE  MSE A  -1      39.651 -22.159 -23.657  1.00 30.29           C  
ANISOU    8  CE  MSE A  -1     3012   5278   3217   -547  -1167   2488       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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