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Database: PDB
Entry: 5T1H
LinkDB: 5T1H
Original site: 5T1H 
HEADER    TRANSFERASE/INHIBITOR                   19-AUG-16   5T1H              
TITLE     CRYSTAL STRUCTURE OF CK2                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CK II ALPHA;                                                
COMPND   5 EC: 2.7.11.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CSNK2A1, CK2A1;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KINASE, CK2, INHIBITOR, TRANSFERASE-INHIBITOR COMPLEX                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.D.FEGUSON                                                           
REVDAT   1   22-NOV-17 5T1H    0                                                
JRNL        AUTH   A.D.FEGUSON                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF CK2                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.11 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 89.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 59038                          
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)  : 0.179                          
REMARK   3   R VALUE            (WORKING SET)  : 0.178                          
REMARK   3   FREE R VALUE                      : 0.203                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.960                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2928                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.010                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.11                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.17                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.24                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4144                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2100                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3939                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2090                   
REMARK   3   BIN FREE R VALUE                        : 0.2260                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.95                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 205                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5586                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 223                                     
REMARK   3   SOLVENT ATOMS            : 388                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.15                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.15020                                             
REMARK   3    B22 (A**2) : -4.15020                                             
REMARK   3    B33 (A**2) : 8.30040                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.250               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.166               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.141               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.160               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.139               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5955   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8017   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2101   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 148    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 839    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5955   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 697    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7040   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.97                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.15                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.89                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   22.2346  -53.9690   -7.8511           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0782 T22:   -0.0726                                    
REMARK   3     T33:   -0.1474 T12:   -0.0205                                    
REMARK   3     T13:   -0.0276 T23:    0.0119                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6765 L22:    1.4118                                    
REMARK   3     L33:    0.8108 L12:    0.5452                                    
REMARK   3     L13:   -0.2186 L23:    0.2385                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0364 S12:   -0.0246 S13:    0.0118                     
REMARK   3     S21:    0.0840 S22:   -0.0125 S23:   -0.0626                     
REMARK   3     S31:   -0.0669 S32:    0.0383 S33:   -0.0239                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -8.2172  -42.1086   21.7450           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0449 T22:   -0.0838                                    
REMARK   3     T33:   -0.1690 T12:    0.0295                                    
REMARK   3     T13:   -0.0305 T23:   -0.0161                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5639 L22:    0.7662                                    
REMARK   3     L33:    0.7019 L12:   -0.5268                                    
REMARK   3     L13:   -0.3820 L23:   -0.0797                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0135 S12:   -0.0935 S13:    0.0354                     
REMARK   3     S21:    0.0582 S22:    0.0241 S23:    0.0308                     
REMARK   3     S31:   -0.0617 S32:   -0.0337 S33:   -0.0106                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5T1H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223469.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-FEB-15                          
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               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59135                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.110                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 127.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.70                              
REMARK 200  R MERGE                    (I) : 0.18700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.70                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
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: 5H8B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22-26% PEG 6K, 200 MM AMMONIUM           
REMARK 280  SULFATE, 100 MM MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.37000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       63.54500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       63.54500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       93.55500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       63.54500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       63.54500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.18500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       63.54500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.54500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       93.55500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       63.54500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       63.54500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       31.18500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       62.37000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -140.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000       63.54500            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      -63.54500            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000       31.18500            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -63.54500            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      -63.54500            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       31.18500            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A   333                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B   333                                                      
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    ASP A 156       38.26   -145.37                                   
REMARK 500    ASP A 175       82.85     52.44                                   
REMARK 500    ALA A 193      160.47     70.52                                   
REMARK 500    MET A 208       55.51    -90.44                                   
REMARK 500    ASP A 210     -159.91   -151.13                                   
REMARK 500    HIS A 234       72.71   -101.95                                   
REMARK 500    ASP B 156       39.59   -151.10                                   
REMARK 500    ASP B 175       82.60     50.75                                   
REMARK 500    ALA B 193      162.77     64.22                                   
REMARK 500    ASP B 210     -159.20   -152.44                                   
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 SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 418                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 419                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 75E A 420                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 418                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 419                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 420                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 75E B 421                 
DBREF  5T1H A    1   333  UNP    P68400   CSK21_HUMAN      1    333             
DBREF  5T1H B    1   333  UNP    P68400   CSK21_HUMAN      1    333             
SEQRES   1 A  333  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 A  333  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 A  333  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 A  333  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 A  333  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 A  333  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 A  333  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 A  333  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 A  333  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 A  333  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 A  333  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 A  333  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 A  333  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 A  333  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 A  333  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 A  333  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 A  333  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 A  333  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 A  333  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 A  333  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 A  333  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 A  333  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 A  333  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 A  333  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 A  333  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 A  333  THR VAL VAL LYS ASP GLN ALA ARG                              
SEQRES   1 B  333  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 B  333  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 B  333  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 B  333  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 B  333  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 B  333  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 B  333  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 B  333  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 B  333  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 B  333  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 B  333  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 B  333  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 B  333  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 B  333  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 B  333  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 B  333  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 B  333  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 B  333  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 B  333  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 B  333  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 B  333  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 B  333  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 B  333  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 B  333  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 B  333  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 B  333  THR VAL VAL LYS ASP GLN ALA ARG                              
HET    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  A 406       5                                                       
HET    SO4  A 407       5                                                       
HET    EDO  A 408       4                                                       
HET    EDO  A 409       4                                                       
HET    EDO  A 410       4                                                       
HET    EDO  A 411       4                                                       
HET    EDO  A 412       4                                                       
HET    EDO  A 413       4                                                       
HET    EDO  A 414       4                                                       
HET    EDO  A 415       4                                                       
HET    EDO  A 416       4                                                       
HET    EDO  A 417       4                                                       
HET    EDO  A 418       4                                                       
HET    EDO  A 419       4                                                       
HET    75E  A 420      27                                                       
HET    SO4  B 401       5                                                       
HET    SO4  B 402       5                                                       
HET    SO4  B 403       5                                                       
HET    SO4  B 404       5                                                       
HET    SO4  B 405       5                                                       
HET    SO4  B 406       5                                                       
HET    EDO  B 407       4                                                       
HET    EDO  B 408       4                                                       
HET    EDO  B 409       4                                                       
HET    EDO  B 410       4                                                       
HET    EDO  B 411       4                                                       
HET    EDO  B 412       4                                                       
HET    EDO  B 413       4                                                       
HET    EDO  B 414       4                                                       
HET    EDO  B 415       4                                                       
HET    EDO  B 416       4                                                       
HET    EDO  B 417       4                                                       
HET    EDO  B 418       4                                                       
HET    EDO  B 419       4                                                       
HET    EDO  B 420       4                                                       
HET    75E  B 421      27                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     75E 7-(CYCLOPROPYLAMINO)-5-[3-(6-OXO-1,6-DIHYDROPYRIDIN-3-           
HETNAM   2 75E  YL)THIOPHEN-2-YL]PYRAZOLO[1,5-A]PYRIMIDINE-3-                   
HETNAM   3 75E  CARBONITRILE                                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  SO4    13(O4 S 2-)                                                  
FORMUL  10  EDO    26(C2 H6 O2)                                                 
FORMUL  22  75E    2(C19 H14 N6 O S)                                            
FORMUL  44  HOH   *388(H2 O)                                                    
HELIX    1 AA1 PRO A   20  TRP A   24  5                                   5    
HELIX    2 AA2 ASP A   25  HIS A   29  5                                   5    
HELIX    3 AA3 ASN A   35  ASP A   37  5                                   3    
HELIX    4 AA4 LYS A   74  ARG A   89  1                                  16    
HELIX    5 AA5 ASP A  120  TYR A  125  1                                   6    
HELIX    6 AA6 GLN A  126  LEU A  128  5                                   3    
HELIX    7 AA7 THR A  129  MET A  150  1                                  22    
HELIX    8 AA8 LYS A  158  HIS A  160  5                                   3    
HELIX    9 AA9 SER A  194  LYS A  198  5                                   5    
HELIX   10 AB1 GLY A  199  VAL A  204  1                                   6    
HELIX   11 AB2 TYR A  211  ARG A  228  1                                  18    
HELIX   12 AB3 ASP A  237  GLY A  250  1                                  14    
HELIX   13 AB4 GLY A  250  TYR A  261  1                                  12    
HELIX   14 AB5 ASP A  266  ARG A  268  5                                   3    
HELIX   15 AB6 PHE A  269  GLY A  274  1                                   6    
HELIX   16 AB7 ARG A  280  VAL A  285  5                                   6    
HELIX   17 AB8 SER A  294  LEU A  305  1                                  12    
HELIX   18 AB9 ASP A  308  ARG A  312  5                                   5    
HELIX   19 AC1 THR A  314  GLU A  320  1                                   7    
HELIX   20 AC2 HIS A  321  TYR A  323  5                                   3    
HELIX   21 AC3 PHE A  324  GLN A  331  1                                   8    
HELIX   22 AC4 PRO B   20  TRP B   24  5                                   5    
HELIX   23 AC5 ASP B   25  HIS B   29  5                                   5    
HELIX   24 AC6 ASN B   35  ASP B   37  5                                   3    
HELIX   25 AC7 LYS B   74  ARG B   89  1                                  16    
HELIX   26 AC8 ASP B  120  TYR B  125  1                                   6    
HELIX   27 AC9 GLN B  126  LEU B  128  5                                   3    
HELIX   28 AD1 THR B  129  MET B  150  1                                  22    
HELIX   29 AD2 LYS B  158  HIS B  160  5                                   3    
HELIX   30 AD3 HIS B  166  ARG B  169  5                                   4    
HELIX   31 AD4 SER B  194  LYS B  198  5                                   5    
HELIX   32 AD5 GLY B  199  VAL B  204  1                                   6    
HELIX   33 AD6 TYR B  211  ARG B  228  1                                  18    
HELIX   34 AD7 ASP B  237  GLY B  250  1                                  14    
HELIX   35 AD8 GLY B  250  TYR B  261  1                                  12    
HELIX   36 AD9 ASP B  266  ILE B  272  5                                   7    
HELIX   37 AE1 ARG B  280  VAL B  285  5                                   6    
HELIX   38 AE2 ASN B  289  VAL B  293  5                                   5    
HELIX   39 AE3 SER B  294  LEU B  305  1                                  12    
HELIX   40 AE4 ASP B  308  ARG B  312  5                                   5    
HELIX   41 AE5 THR B  314  GLU B  320  1                                   7    
HELIX   42 AE6 HIS B  321  TYR B  323  5                                   3    
HELIX   43 AE7 PHE B  324  ALA B  332  1                                   9    
SHEET    1 AA1 5 TYR A  39  ARG A  47  0                                        
SHEET    2 AA1 5 SER A  51  ASN A  58 -1  O  VAL A  53   N  LEU A  45           
SHEET    3 AA1 5 LYS A  64  LEU A  70 -1  O  VAL A  67   N  PHE A  54           
SHEET    4 AA1 5 PRO A 109  GLU A 114 -1  O  PHE A 113   N  VAL A  66           
SHEET    5 AA1 5 LEU A  97  LYS A 102 -1  N  ASP A  99   O  VAL A 112           
SHEET    1 AA2 2 ILE A 152  MET A 153  0                                        
SHEET    2 AA2 2 GLU A 180  PHE A 181 -1  O  GLU A 180   N  MET A 153           
SHEET    1 AA3 2 VAL A 162  ASP A 165  0                                        
SHEET    2 AA3 2 LYS A 170  LEU A 173 -1  O  LYS A 170   N  ASP A 165           
SHEET    1 AA4 5 TYR B  39  ARG B  47  0                                        
SHEET    2 AA4 5 SER B  51  ASN B  58 -1  O  VAL B  53   N  LEU B  45           
SHEET    3 AA4 5 LYS B  64  LEU B  70 -1  O  VAL B  67   N  PHE B  54           
SHEET    4 AA4 5 PRO B 109  GLU B 114 -1  O  PHE B 113   N  VAL B  66           
SHEET    5 AA4 5 LEU B  97  LYS B 102 -1  N  VAL B 101   O  ALA B 110           
SHEET    1 AA5 2 ILE B 152  MET B 153  0                                        
SHEET    2 AA5 2 GLU B 180  PHE B 181 -1  O  GLU B 180   N  MET B 153           
SHEET    1 AA6 2 VAL B 162  ASP B 165  0                                        
SHEET    2 AA6 2 LYS B 170  LEU B 173 -1  O  LYS B 170   N  ASP B 165           
CISPEP   1 GLU A  230    PRO A  231          0        -3.13                     
CISPEP   2 GLU B  230    PRO B  231          0        -6.18                     
SITE     1 AC1  6 LYS A  77  ARG A  80  ARG A 155  ASN A 189                    
SITE     2 AC1  6 HOH A 501  HOH A 519                                          
SITE     1 AC2  4 ARG A 191  LYS A 198  ASN A 238  HOH A 551                    
SITE     1 AC3  6 TRP A  33  LYS A  75  LYS A 102  HOH A 547                    
SITE     2 AC3  6 HOH A 567  HOH A 629                                          
SITE     1 AC4  5 ARG A 280  ARG A 283  HOH A 509  HOH A 588                    
SITE     2 AC4  5 HOH A 599                                                     
SITE     1 AC5  4 LYS A  75  LYS A 102  ARG A 107  LYS B  74                    
SITE     1 AC6  5 LYS A  74  LYS A  76  LYS A  77  HOH A 519                    
SITE     2 AC6  5 ARG B 107                                                     
SITE     1 AC7  4 ARG A 275  HIS A 276  SER A 277  LYS A 279                    
SITE     1 AC8  3 LYS A 247  HIS A 276  HOH A 598                               
SITE     1 AC9  4 GLN A  36  TYR A  39  EDO A 418  HOH A 582                    
SITE     1 AD1  5 ASP A  25  TYR A  26  GLU A  27  HOH A 523                    
SITE     2 AD1  5 HOH A 619                                                     
SITE     1 AD2  3 ASP A 299  LYS A 303  LEU B 298                               
SITE     1 AD3  7 VAL A 248  LEU A 249  ARG A 278  LYS A 279                    
SITE     2 AD3  7 TRP A 281  ASP A 302  HOH A 562                               
SITE     1 AD4  4 GLU A  32  TRP A  33  TYR B 196  HIS B 234                    
SITE     1 AD5  4 VAL A 190  LYS A 198  LEU A 202  EDO A 415                    
SITE     1 AD6  5 LEU A 203  ASN A 238  TYR A 239  PHE A 269                    
SITE     2 AD6  5 EDO A 414                                                     
SITE     1 AD7  9 ARG A   8  ALA A   9  ARG A  10  ASP A 210                    
SITE     2 AD7  9 SER A 212  HIS A 309  GLN A 310  HOH A 505                    
SITE     3 AD7  9 HOH A 506                                                     
SITE     1 AD8  3 ASP A 237  ASN A 238  HOH A 579                               
SITE     1 AD9  5 PRO A  20  ARG A  21  EDO A 409  HOH A 525                    
SITE     2 AD9  5 HOH A 600                                                     
SITE     1 AE1  8 VAL A  11  HIS A 148  TYR A 211  SER A 212                    
SITE     2 AE1  8 ALA A 315  HOH A 505  HOH A 511  HOH A 518                    
SITE     1 AE2 12 VAL A  53  VAL A  66  LYS A  68  ILE A  95                    
SITE     2 AE2 12 PHE A 113  GLU A 114  VAL A 116  ASN A 118                    
SITE     3 AE2 12 MET A 163  ILE A 174  ASP A 175  HOH A 597                    
SITE     1 AE3  5 LYS B  77  ARG B  80  ARG B 155  ASN B 189                    
SITE     2 AE3  5 HOH B 553                                                     
SITE     1 AE4  4 LYS B 229  HIS B 234  ARG B 244  HOH B 513                    
SITE     1 AE5  4 TRP B  33  LYS B  75  LYS B 102  HOH B 609                    
SITE     1 AE6  5 ARG A  47  LYS A  74  LYS A  76  LYS B  75                    
SITE     2 AE6  5 HOH B 623                                                     
SITE     1 AE7  5 ARG B 278  LYS B 279  ARG B 280  HOH B 550                    
SITE     2 AE7  5 HOH B 569                                                     
SITE     1 AE8 10 SER A 277  ARG A 278  GLU B 252  ARG B 275                    
SITE     2 AE8 10 SER B 277  ARG B 278  HOH B 510  HOH B 512                    
SITE     3 AE8 10 HOH B 551  HOH B 586                                          
SITE     1 AE9  3 ASP B  25  TYR B  26  GLU B  27                               
SITE     1 AF1  7 ASP A 299  ASP A 302  LYS A 303  ARG A 306                    
SITE     2 AF1  7 TRP B 281  GLU B 282  HOH B 627                               
SITE     1 AF2  4 HIS B 276  SER B 277  LYS B 279  HOH B 508                    
SITE     1 AF3  4 ARG B 191  LYS B 198  ASN B 238  HOH B 563                    
SITE     1 AF4  7 ALA B   9  ARG B  10  VAL B  11  ASP B 210                    
SITE     2 AF4  7 TYR B 211  EDO B 418  HOH B 515                               
SITE     1 AF5  5 PHE B 232  PHE B 233  ARG B 244  VAL B 248                    
SITE     2 AF5  5 HOH B 513                                                     
SITE     1 AF6  5 ASP B 156  LYS B 158  ALA B 193  SER B 194                    
SITE     2 AF6  5 HOH B 528                                                     
SITE     1 AF7  3 ASP B 132  PHE B 135  ARG B 169                               
SITE     1 AF8  3 LEU A 298  ASP B 299  LYS B 303                               
SITE     1 AF9  3 GLN B  36  TYR B  39  ASP B 103                               
SITE     1 AG1  8 ARG A 195  HIS B  29  VAL B  30  VAL B  31                    
SITE     2 AG1  8 GLU B  32  ILE B  82  GLU B  86  HOH B 527                    
SITE     1 AG2  9 VAL B  11  HIS B 148  TYR B 211  SER B 212                    
SITE     2 AG2  9 THR B 314  ALA B 315  EDO B 411  HOH B 504                    
SITE     3 AG2  9 HOH B 542                                                     
SITE     1 AG3  8 ASN B 118  ASP B 120  PHE B 121  PRO B 159                    
SITE     2 AG3  8 HIS B 160  VAL B 162  HOH B 577  HOH B 579                    
SITE     1 AG4  3 LYS B 102  PRO B 104  HOH B 559                               
SITE     1 AG5 12 VAL B  53  VAL B  66  LYS B  68  ILE B  95                    
SITE     2 AG5 12 PHE B 113  GLU B 114  HIS B 115  VAL B 116                    
SITE     3 AG5 12 MET B 163  ILE B 174  ASP B 175  HOH B 546                    
CRYST1  127.090  127.090  124.740  90.00  90.00  90.00 P 43 21 2    16          
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      0.007868  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007868  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008017        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system