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Database: PDB
Entry: 5CYI
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HEADER    TRANSFERASE                             30-JUL-15   5CYI              
TITLE     CDK2/CYCLIN A COVALENT COMPLEX WITH 6-(CYCLOHEXYLMETHOXY)-N-(4-       
TITLE    2 (VINYLSULFONYL)PHENYL)-9H-PURIN-2-AMINE (NU6300)                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2,P33 PROTEIN KINASE;          
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 174-432;                                      
COMPND  11 SYNONYM: CYCLIN-A;                                                   
COMPND  12 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: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CDK2 CYCLIN A COVALENT INHIBITOR VINYLSULPHONE, TRANSFERASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.ANSCOMBE,E.MESCHINI,R.M.VIDAL,M.P.MARTIN,D.STAUNTON,M.GEITMANN,     
AUTHOR   2 U.H.DANIELSON,W.A.STANLEY,L.Z.WANG,T.REUILLON,B.T.GOLDING,C.CANO,    
AUTHOR   3 D.R.NEWELL,M.E.M.NOBLE,S.R.WEDGE,J.A.ENDICOTT,R.J.GRIFFIN            
REVDAT   3   30-AUG-17 5CYI    1       REMARK                                   
REVDAT   2   30-SEP-15 5CYI    1       JRNL                                     
REVDAT   1   16-SEP-15 5CYI    0                                                
JRNL        AUTH   E.ANSCOMBE,E.MESCHINI,R.MORA-VIDAL,M.P.MARTIN,D.STAUNTON,    
JRNL        AUTH 2 M.GEITMANN,U.H.DANIELSON,W.A.STANLEY,L.Z.WANG,T.REUILLON,    
JRNL        AUTH 3 B.T.GOLDING,C.CANO,D.R.NEWELL,M.E.NOBLE,S.R.WEDGE,           
JRNL        AUTH 4 J.A.ENDICOTT,R.J.GRIFFIN                                     
JRNL        TITL   IDENTIFICATION AND CHARACTERIZATION OF AN IRREVERSIBLE       
JRNL        TITL 2 INHIBITOR OF CDK2.                                           
JRNL        REF    CHEM.BIOL.                    V.  22  1159 2015              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   26320860                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2015.07.018                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0123                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 74.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 101635                         
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) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4914                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7041                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.25                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 343                          
REMARK   3   BIN FREE R VALUE                    : 0.3740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8947                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 492                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.32000                                             
REMARK   3    B22 (A**2) : 1.58000                                              
REMARK   3    B33 (A**2) : -0.25000                                             
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): 0.186         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.163         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.177         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.238         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9254 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12565 ; 1.742 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1110 ; 6.514 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   396 ;42.001 ;23.939       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1623 ;17.062 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;15.032 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1419 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6855 ; 0.008 ; 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):  4446 ; 3.960 ; 5.008       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5554 ; 6.122 ; 7.492       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4808 ; 4.187 ; 5.460       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A    84                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8580  59.5450  55.4470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0777 T22:   0.1069                                     
REMARK   3      T33:   0.0400 T12:  -0.0320                                     
REMARK   3      T13:   0.0069 T23:   0.0233                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1523 L22:   0.5902                                     
REMARK   3      L33:   0.9344 L12:  -0.0093                                     
REMARK   3      L13:  -0.3167 L23:  -0.3065                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1072 S12:  -0.0680 S13:   0.0178                       
REMARK   3      S21:   0.0004 S22:  -0.1448 S23:  -0.1476                       
REMARK   3      S31:  -0.1962 S32:   0.2572 S33:   0.0376                       
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: U VALUES      : WITH TLS ADDED            
REMARK   4                                                                      
REMARK   4 5CYI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212371.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : PH 7.0                             
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 101717                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.340                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.18100                            
REMARK 200  R SYM                      (I) : 0.17000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 4.32800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.500                              
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: 1H1S                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 5 MG PER ML. 0.6 TO 0.8 M     
REMARK 280  KCL, 0.9 TO 1.2 M (NH4)2SO4, AND 100 MM HEPES (PH 7.0), VAPOR       
REMARK 280  DIFFUSION, TEMPERATURE 277K                                         
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       37.14300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.33650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.64450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.33650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.14300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.64450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 3080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     MET B   173                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     PRO C    -3                                                      
REMARK 465     LEU C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     MET D   173                                                      
REMARK 465     GLU D   174                                                      
REMARK 465     VAL D   175                                                      
REMARK 465     PRO D   176                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   507     O    HOH A   606              1.93            
REMARK 500   O    HOH A   468     O    HOH A   577              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU C     8     OE1  GLN D   403     3655     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  37   CB  -  CG  -  CD2 ANGL. DEV. =  13.5 DEGREES          
REMARK 500    ASP A  38   CB  -  CG  -  OD1 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    LEU A 148   CB  -  CG  -  CD2 ANGL. DEV. =  13.5 DEGREES          
REMARK 500    VAL A 230   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    ASP B 177   CB  -  CG  -  OD1 ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ASP B 177   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    VAL C 230   CB  -  CA  -  C   ANGL. DEV. = -12.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  41       33.16    -90.84                                   
REMARK 500    ASP A 127       42.12   -162.40                                   
REMARK 500    ASP A 145       80.48     47.15                                   
REMARK 500    VAL A 164      138.66     78.36                                   
REMARK 500    SER A 181     -150.48   -153.97                                   
REMARK 500    THR A 290     -168.47   -125.66                                   
REMARK 500    ARG A 297       74.10   -113.25                                   
REMARK 500    TRP B 372      110.28    -36.02                                   
REMARK 500    THR C  41      -88.18   -121.10                                   
REMARK 500    THR C  41      -87.07   -121.10                                   
REMARK 500    ASP C 127       42.97   -164.80                                   
REMARK 500    ASP C 145       81.07     47.68                                   
REMARK 500    VAL C 164      137.97     76.95                                   
REMARK 500    SER C 181     -149.58   -153.07                                   
REMARK 500    GLN D 323       88.71   -151.24                                   
REMARK 500    TRP D 372      110.78    -38.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A   40     THR A   41                  144.72                    
REMARK 500 THR A   41     GLU A   42                  135.88                    
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 55S A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 55S C 301                 
DBREF  5CYI A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  5CYI B  174   432  UNP    P20248   CCNA2_HUMAN    174    432             
DBREF  5CYI C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  5CYI D  174   432  UNP    P20248   CCNA2_HUMAN    174    432             
SEQADV 5CYI GLY A   -4  UNP  P24941              EXPRESSION TAG                 
SEQADV 5CYI PRO A   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 5CYI LEU A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 5CYI GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 5CYI SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 5CYI MET B  173  UNP  P20248              INITIATING METHIONINE          
SEQADV 5CYI GLY C   -4  UNP  P24941              EXPRESSION TAG                 
SEQADV 5CYI PRO C   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 5CYI LEU C   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 5CYI GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 5CYI SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 5CYI MET D  173  UNP  P20248              INITIATING METHIONINE          
SEQRES   1 A  303  GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU          
SEQRES   2 A  303  LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA          
SEQRES   3 A  303  ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS          
SEQRES   4 A  303  ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR          
SEQRES   5 A  303  ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS          
SEQRES   6 A  303  PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU          
SEQRES   7 A  303  ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP          
SEQRES   8 A  303  LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE          
SEQRES   9 A  303  PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU          
SEQRES  10 A  303  GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS          
SEQRES  11 A  303  ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU          
SEQRES  12 A  303  GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA          
SEQRES  13 A  303  PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL          
SEQRES  14 A  303  THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS          
SEQRES  15 A  303  LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY          
SEQRES  16 A  303  CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE          
SEQRES  17 A  303  PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE          
SEQRES  18 A  303  ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY          
SEQRES  19 A  303  VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS          
SEQRES  20 A  303  TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU          
SEQRES  21 A  303  ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS          
SEQRES  22 A  303  TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU          
SEQRES  23 A  303  ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO          
SEQRES  24 A  303  HIS LEU ARG LEU                                              
SEQRES   1 B  260  MET GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR          
SEQRES   2 B  260  LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY          
SEQRES   3 B  260  TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG          
SEQRES   4 B  260  ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU          
SEQRES   5 B  260  TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN          
SEQRES   6 B  260  TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG          
SEQRES   7 B  260  GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU          
SEQRES   8 B  260  ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA          
SEQRES   9 B  260  GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS          
SEQRES  10 B  260  GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU          
SEQRES  11 B  260  THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU          
SEQRES  12 B  260  THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS          
SEQRES  13 B  260  VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU          
SEQRES  14 B  260  ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL          
SEQRES  15 B  260  ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL          
SEQRES  16 B  260  THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR          
SEQRES  17 B  260  GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP          
SEQRES  18 B  260  LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN          
SEQRES  19 B  260  GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS          
SEQRES  20 B  260  GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU          
SEQRES   1 C  303  GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU          
SEQRES   2 C  303  LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA          
SEQRES   3 C  303  ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS          
SEQRES   4 C  303  ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR          
SEQRES   5 C  303  ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS          
SEQRES   6 C  303  PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU          
SEQRES   7 C  303  ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP          
SEQRES   8 C  303  LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE          
SEQRES   9 C  303  PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU          
SEQRES  10 C  303  GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS          
SEQRES  11 C  303  ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU          
SEQRES  12 C  303  GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA          
SEQRES  13 C  303  PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL          
SEQRES  14 C  303  THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS          
SEQRES  15 C  303  LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY          
SEQRES  16 C  303  CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE          
SEQRES  17 C  303  PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE          
SEQRES  18 C  303  ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY          
SEQRES  19 C  303  VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS          
SEQRES  20 C  303  TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU          
SEQRES  21 C  303  ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS          
SEQRES  22 C  303  TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU          
SEQRES  23 C  303  ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO          
SEQRES  24 C  303  HIS LEU ARG LEU                                              
SEQRES   1 D  260  MET GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR          
SEQRES   2 D  260  LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY          
SEQRES   3 D  260  TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG          
SEQRES   4 D  260  ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU          
SEQRES   5 D  260  TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN          
SEQRES   6 D  260  TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG          
SEQRES   7 D  260  GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU          
SEQRES   8 D  260  ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA          
SEQRES   9 D  260  GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS          
SEQRES  10 D  260  GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU          
SEQRES  11 D  260  THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU          
SEQRES  12 D  260  THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS          
SEQRES  13 D  260  VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU          
SEQRES  14 D  260  ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL          
SEQRES  15 D  260  ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL          
SEQRES  16 D  260  THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR          
SEQRES  17 D  260  GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP          
SEQRES  18 D  260  LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN          
SEQRES  19 D  260  GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS          
SEQRES  20 D  260  GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU          
MODRES 5CYI TPO A  160  THR  MODIFIED RESIDUE                                   
MODRES 5CYI TPO C  160  THR  MODIFIED RESIDUE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    55S  A 301      29                                                       
HET    55S  C 301      29                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     55S 6-(CYCLOHEXYLMETHOXY)-N-[4-(ETHYLSULFONYL)PHENYL]-9H-            
HETNAM   2 55S  PURIN-2-AMINE                                                   
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  55S    2(C20 H25 N5 O3 S)                                           
FORMUL   7  HOH   *492(H2 O)                                                    
HELIX    1 AA1 PRO A   45  LEU A   58  1                                  14    
HELIX    2 AA2 LEU A   87  SER A   94  1                                   8    
HELIX    3 AA3 PRO A  100  HIS A  121  1                                  22    
HELIX    4 AA4 LYS A  129  GLN A  131  5                                   3    
HELIX    5 AA5 THR A  165  ARG A  169  5                                   5    
HELIX    6 AA6 ALA A  170  LEU A  175  1                                   6    
HELIX    7 AA7 THR A  182  ARG A  199  1                                  18    
HELIX    8 AA8 SER A  207  GLY A  220  1                                  14    
HELIX    9 AA9 GLY A  229  MET A  233  5                                   5    
HELIX   10 AB1 ASP A  247  VAL A  252  1                                   6    
HELIX   11 AB2 ASP A  256  LEU A  267  1                                  12    
HELIX   12 AB3 SER A  276  ALA A  282  1                                   7    
HELIX   13 AB4 HIS A  283  GLN A  287  5                                   5    
HELIX   14 AB5 VAL B  175  ASP B  177  5                                   3    
HELIX   15 AB6 TYR B  178  CYS B  193  1                                  16    
HELIX   16 AB7 GLY B  198  GLN B  203  5                                   6    
HELIX   17 AB8 THR B  207  TYR B  225  1                                  19    
HELIX   18 AB9 GLN B  228  MET B  246  1                                  19    
HELIX   19 AC1 LEU B  249  GLY B  251  5                                   3    
HELIX   20 AC2 LYS B  252  GLU B  269  1                                  18    
HELIX   21 AC3 GLU B  274  THR B  282  1                                   9    
HELIX   22 AC4 THR B  287  LEU B  302  1                                  16    
HELIX   23 AC5 THR B  310  LEU B  320  1                                  11    
HELIX   24 AC6 ASN B  326  ASP B  343  1                                  18    
HELIX   25 AC7 ASP B  343  LEU B  348  1                                   6    
HELIX   26 AC8 LEU B  351  GLY B  369  1                                  19    
HELIX   27 AC9 PRO B  373  GLY B  381  1                                   9    
HELIX   28 AD1 THR B  383  ALA B  401  1                                  19    
HELIX   29 AD2 PRO B  402  HIS B  404  5                                   3    
HELIX   30 AD3 GLN B  407  TYR B  413  1                                   7    
HELIX   31 AD4 LYS B  414  HIS B  419  5                                   6    
HELIX   32 AD5 GLY B  420  LEU B  424  5                                   5    
HELIX   33 AD6 PRO C   45  LEU C   58  1                                  14    
HELIX   34 AD7 LEU C   87  SER C   94  1                                   8    
HELIX   35 AD8 PRO C  100  HIS C  121  1                                  22    
HELIX   36 AD9 LYS C  129  GLN C  131  5                                   3    
HELIX   37 AE1 ASP C  145  ALA C  149  5                                   5    
HELIX   38 AE2 THR C  165  ARG C  169  5                                   5    
HELIX   39 AE3 ALA C  170  LEU C  175  1                                   6    
HELIX   40 AE4 THR C  182  ARG C  199  1                                  18    
HELIX   41 AE5 SER C  207  GLY C  220  1                                  14    
HELIX   42 AE6 GLY C  229  MET C  233  5                                   5    
HELIX   43 AE7 ASP C  247  VAL C  252  1                                   6    
HELIX   44 AE8 ASP C  256  LEU C  267  1                                  12    
HELIX   45 AE9 SER C  276  ALA C  282  1                                   7    
HELIX   46 AF1 HIS C  283  GLN C  287  5                                   5    
HELIX   47 AF2 TYR D  178  CYS D  193  1                                  16    
HELIX   48 AF3 GLY D  198  GLN D  203  5                                   6    
HELIX   49 AF4 THR D  207  TYR D  225  1                                  19    
HELIX   50 AF5 GLN D  228  MET D  246  1                                  19    
HELIX   51 AF6 LEU D  249  GLY D  251  5                                   3    
HELIX   52 AF7 LYS D  252  GLU D  269  1                                  18    
HELIX   53 AF8 GLU D  274  THR D  282  1                                   9    
HELIX   54 AF9 THR D  287  LEU D  302  1                                  16    
HELIX   55 AG1 THR D  310  LEU D  320  1                                  11    
HELIX   56 AG2 ASN D  326  ASP D  343  1                                  18    
HELIX   57 AG3 ASP D  343  LEU D  348  1                                   6    
HELIX   58 AG4 LEU D  351  GLY D  369  1                                  19    
HELIX   59 AG5 PRO D  373  GLY D  381  1                                   9    
HELIX   60 AG6 THR D  383  ALA D  401  1                                  19    
HELIX   61 AG7 PRO D  402  HIS D  404  5                                   3    
HELIX   62 AG8 GLN D  407  TYR D  413  1                                   7    
HELIX   63 AG9 LYS D  414  HIS D  419  5                                   6    
HELIX   64 AH1 GLY D  420  LEU D  424  5                                   5    
SHEET    1 AA1 5 PHE A   4  GLY A  11  0                                        
SHEET    2 AA1 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  GLY A  11           
SHEET    3 AA1 5 VAL A  29  ARG A  36 -1  O  LEU A  32   N  TYR A  19           
SHEET    4 AA1 5 LYS A  75  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5 AA1 5 LEU A  66  HIS A  71 -1  N  ILE A  70   O  TYR A  77           
SHEET    1 AA2 3 GLN A  85  ASP A  86  0                                        
SHEET    2 AA2 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3 AA2 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1 AA3 2 VAL A 123  LEU A 124  0                                        
SHEET    2 AA3 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1 AA4 5 PHE C   4  GLY C  11  0                                        
SHEET    2 AA4 5 VAL C  17  ASN C  23 -1  O  VAL C  18   N  GLY C  11           
SHEET    3 AA4 5 VAL C  29  ARG C  36 -1  O  LEU C  32   N  TYR C  19           
SHEET    4 AA4 5 LYS C  75  GLU C  81 -1  O  PHE C  80   N  ALA C  31           
SHEET    5 AA4 5 LEU C  66  HIS C  71 -1  N  ILE C  70   O  TYR C  77           
SHEET    1 AA5 3 GLN C  85  ASP C  86  0                                        
SHEET    2 AA5 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3 AA5 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1 AA6 2 VAL C 123  LEU C 124  0                                        
SHEET    2 AA6 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         NZ  LYS A  89                 C   55S A 301     1555   1555  1.27  
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.34  
LINK         NZ  LYS C  89                 C   55S C 301     1555   1555  1.28  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.34  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
CISPEP   1 VAL A  154    PRO A  155          0        -9.04                     
CISPEP   2 GLN B  323    PRO B  324          0       -11.04                     
CISPEP   3 ASP B  345    PRO B  346          0        14.89                     
CISPEP   4 VAL C  154    PRO C  155          0        -4.81                     
CISPEP   5 GLN D  323    PRO D  324          0       -12.05                     
CISPEP   6 ASP D  345    PRO D  346          0        13.41                     
SITE     1 AC1 14 ALA A  31  VAL A  64  PHE A  80  GLU A  81                    
SITE     2 AC1 14 LEU A  83  HIS A  84  GLN A  85  ASP A  86                    
SITE     3 AC1 14 LYS A  89  ASN A 132  LEU A 134  HOH A 537                    
SITE     4 AC1 14 HOH A 570  HOH A 574                                          
SITE     1 AC2 20 ILE C  10  GLU C  12  GLY C  13  ALA C  31                    
SITE     2 AC2 20 VAL C  64  PHE C  80  GLU C  81  LEU C  83                    
SITE     3 AC2 20 HIS C  84  GLN C  85  ASP C  86  LEU C  87                    
SITE     4 AC2 20 LYS C  88  PHE C  90  MET C  91  ASP C  92                    
SITE     5 AC2 20 ALA C  93  ASN C 132  LEU C 134  HOH C 443                    
CRYST1   74.286  135.289  148.673  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      0.013461  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007392  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006726        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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