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Database: PDB
Entry: 1FPZ
LinkDB: 1FPZ
Original site: 1FPZ 
HEADER    HYDROLASE                               01-SEP-00   1FPZ              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP) WITH
TITLE    2 A SUBSTITUTION OF THE CATALYTIC SITE CYSTEINE (CYS140) TO A SERINE   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE INHIBITOR 3;                       
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 EC: 3.1.3.48;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PGEX-6P;                                   
SOURCE   8 OTHER_DETAILS: HOMO SAPIENS                                          
KEYWDS    ALPHA-BETA SANDWICH, HYDROLASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.SONG,N.HANLON,N.R.BROWN,M.E.M.NOBLE,L.N.JOHNSON,D.BARFORD           
REVDAT   5   14-MAR-18 1FPZ    1       SEQADV                                   
REVDAT   4   14-APR-09 1FPZ    1       REMARK                                   
REVDAT   3   24-FEB-09 1FPZ    1       VERSN                                    
REVDAT   2   01-APR-03 1FPZ    1       JRNL                                     
REVDAT   1   09-MAY-01 1FPZ    0                                                
JRNL        AUTH   H.SONG,N.HANLON,N.R.BROWN,M.E.NOBLE,L.N.JOHNSON,D.BARFORD    
JRNL        TITL   PHOSPHOPROTEIN-PROTEIN INTERACTIONS REVEALED BY THE CRYSTAL  
JRNL        TITL 2 STRUCTURE OF KINASE-ASSOCIATED PHOSPHATASE IN COMPLEX WITH   
JRNL        TITL 3 PHOSPHOCDK2.                                                 
JRNL        REF    MOL.CELL                      V.   7   615 2001              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   11463386                                                     
JRNL        DOI    10.1016/S1097-2765(01)00208-8                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.GYRURIS,E.GOLEMIS,H.CHERTKOV,R.BRENT                       
REMARK   1  TITL   CDI1, A HUMAN G1 AND S PHASE PROTEIN PHOSPHATASE THAT        
REMARK   1  TITL 2 ASSOCIATES WITH CDK2                                         
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  75   791 1993              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1  DOI    10.1016/0092-8674(93)90498-F                                 
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.W.HARPER,G.R.ADAMI,N.WEI,K.KEYOMARSI,S.J.ELLEDGE           
REMARK   1  TITL   THE P21CDK-INTERACTING PROTEIN CIP1 IS A POTENT INHIBITOR OF 
REMARK   1  TITL 2 G1 CYCLIN-DEPENDENT KINASES                                  
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  75   805 1993              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1  DOI    10.1016/0092-8674(93)90499-G                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 88032                          
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 SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4241                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8340                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 690                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.580                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FPZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000011802.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90055                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
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) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, AMMONIUM SULPHATE, SODIUM      
REMARK 280  ACETATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.49333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       46.74667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       70.12000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       23.37333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      116.86667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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     MET A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ILE A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     PHE A    12                                                      
REMARK 465     ASP A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     ASP A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 465     GLU A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     ILE A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     ASP A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     GLN A    24                                                      
REMARK 465     SER A   201                                                      
REMARK 465     SER A   202                                                      
REMARK 465     ARG A   203                                                      
REMARK 465     ASP A   204                                                      
REMARK 465     SER A   205                                                      
REMARK 465     GLN A   206                                                      
REMARK 465     SER A   207                                                      
REMARK 465     ARG A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     VAL A   210                                                      
REMARK 465     SER A   211                                                      
REMARK 465     ARG A   212                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ILE B     7                                                      
REMARK 465     GLN B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     PHE B    12                                                      
REMARK 465     ASP B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     ASP B    16                                                      
REMARK 465     GLU B    17                                                      
REMARK 465     GLU B    18                                                      
REMARK 465     PRO B    19                                                      
REMARK 465     ILE B    20                                                      
REMARK 465     GLU B    21                                                      
REMARK 465     ASP B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     GLN B    24                                                      
REMARK 465     SER B   201                                                      
REMARK 465     SER B   202                                                      
REMARK 465     ARG B   203                                                      
REMARK 465     ASP B   204                                                      
REMARK 465     SER B   205                                                      
REMARK 465     GLN B   206                                                      
REMARK 465     SER B   207                                                      
REMARK 465     ARG B   208                                                      
REMARK 465     SER B   209                                                      
REMARK 465     VAL B   210                                                      
REMARK 465     SER B   211                                                      
REMARK 465     ARG B   212                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     ILE C     7                                                      
REMARK 465     GLN C     8                                                      
REMARK 465     THR C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     GLU C    11                                                      
REMARK 465     PHE C    12                                                      
REMARK 465     ASP C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     SER C    15                                                      
REMARK 465     ASP C    16                                                      
REMARK 465     GLU C    17                                                      
REMARK 465     GLU C    18                                                      
REMARK 465     PRO C    19                                                      
REMARK 465     ILE C    20                                                      
REMARK 465     GLU C    21                                                      
REMARK 465     ASP C    22                                                      
REMARK 465     SER C   201                                                      
REMARK 465     SER C   202                                                      
REMARK 465     ARG C   203                                                      
REMARK 465     ASP C   204                                                      
REMARK 465     SER C   205                                                      
REMARK 465     GLN C   206                                                      
REMARK 465     SER C   207                                                      
REMARK 465     ARG C   208                                                      
REMARK 465     SER C   209                                                      
REMARK 465     VAL C   210                                                      
REMARK 465     SER C   211                                                      
REMARK 465     ARG C   212                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     PRO D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     ILE D     7                                                      
REMARK 465     GLN D     8                                                      
REMARK 465     THR D     9                                                      
REMARK 465     SER D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     PHE D    12                                                      
REMARK 465     ASP D    13                                                      
REMARK 465     SER D    14                                                      
REMARK 465     SER D    15                                                      
REMARK 465     ASP D    16                                                      
REMARK 465     GLU D    17                                                      
REMARK 465     GLU D    18                                                      
REMARK 465     PRO D    19                                                      
REMARK 465     ILE D    20                                                      
REMARK 465     GLU D    21                                                      
REMARK 465     ASP D    22                                                      
REMARK 465     SER D   201                                                      
REMARK 465     SER D   202                                                      
REMARK 465     ARG D   203                                                      
REMARK 465     ASP D   204                                                      
REMARK 465     SER D   205                                                      
REMARK 465     GLN D   206                                                      
REMARK 465     SER D   207                                                      
REMARK 465     ARG D   208                                                      
REMARK 465     SER D   209                                                      
REMARK 465     VAL D   210                                                      
REMARK 465     SER D   211                                                      
REMARK 465     ARG D   212                                                      
REMARK 465     MET E     1                                                      
REMARK 465     LYS E     2                                                      
REMARK 465     PRO E     3                                                      
REMARK 465     PRO E     4                                                      
REMARK 465     SER E     5                                                      
REMARK 465     SER E     6                                                      
REMARK 465     ILE E     7                                                      
REMARK 465     GLN E     8                                                      
REMARK 465     THR E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     GLU E    11                                                      
REMARK 465     PHE E    12                                                      
REMARK 465     ASP E    13                                                      
REMARK 465     SER E    14                                                      
REMARK 465     SER E    15                                                      
REMARK 465     ASP E    16                                                      
REMARK 465     GLU E    17                                                      
REMARK 465     GLU E    18                                                      
REMARK 465     PRO E    19                                                      
REMARK 465     ILE E    20                                                      
REMARK 465     GLU E    21                                                      
REMARK 465     ASP E    22                                                      
REMARK 465     GLU E    23                                                      
REMARK 465     GLN E    24                                                      
REMARK 465     SER E   201                                                      
REMARK 465     SER E   202                                                      
REMARK 465     ARG E   203                                                      
REMARK 465     ASP E   204                                                      
REMARK 465     SER E   205                                                      
REMARK 465     GLN E   206                                                      
REMARK 465     SER E   207                                                      
REMARK 465     ARG E   208                                                      
REMARK 465     SER E   209                                                      
REMARK 465     VAL E   210                                                      
REMARK 465     SER E   211                                                      
REMARK 465     ARG E   212                                                      
REMARK 465     MET F     1                                                      
REMARK 465     LYS F     2                                                      
REMARK 465     PRO F     3                                                      
REMARK 465     PRO F     4                                                      
REMARK 465     SER F     5                                                      
REMARK 465     SER F     6                                                      
REMARK 465     ILE F     7                                                      
REMARK 465     GLN F     8                                                      
REMARK 465     THR F     9                                                      
REMARK 465     SER F    10                                                      
REMARK 465     GLU F    11                                                      
REMARK 465     PHE F    12                                                      
REMARK 465     ASP F    13                                                      
REMARK 465     SER F    14                                                      
REMARK 465     SER F    15                                                      
REMARK 465     ASP F    16                                                      
REMARK 465     GLU F    17                                                      
REMARK 465     GLU F    18                                                      
REMARK 465     PRO F    19                                                      
REMARK 465     ILE F    20                                                      
REMARK 465     GLU F    21                                                      
REMARK 465     ASP F    22                                                      
REMARK 465     SER F   201                                                      
REMARK 465     SER F   202                                                      
REMARK 465     ARG F   203                                                      
REMARK 465     ASP F   204                                                      
REMARK 465     SER F   205                                                      
REMARK 465     GLN F   206                                                      
REMARK 465     SER F   207                                                      
REMARK 465     ARG F   208                                                      
REMARK 465     SER F   209                                                      
REMARK 465     VAL F   210                                                      
REMARK 465     SER F   211                                                      
REMARK 465     ARG F   212                                                      
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    PRO C    26     O    HOH C   957              2.09            
REMARK 500   O    HOH F   917     O    HOH F   987              2.12            
REMARK 500   O    HOH B   906     O    HOH B   914              2.12            
REMARK 500   O    ASN D   187     O    HIS D   190              2.12            
REMARK 500   O    CYS D    46     O    HOH D  1003              2.16            
REMARK 500   O    ASP D    63     O    HOH D   922              2.18            
REMARK 500   O    HOH A   919     O    HOH A   987              2.19            
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  GLN D    24     O    HOH E   931     5565     2.06            
REMARK 500   OE1  GLN A    61     O    GLN A   181     6554     2.14            
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    PRO A  26     -110.16    -65.66                                   
REMARK 500    ILE A  27      125.29   -175.68                                   
REMARK 500    ASP A  55      -17.26     73.38                                   
REMARK 500    VAL A  89       49.22   -142.96                                   
REMARK 500    SER A 140     -135.71   -119.02                                   
REMARK 500    LEU A 144       86.82   -157.99                                   
REMARK 500    GLU A 191       -4.01    101.30                                   
REMARK 500    ALA A 198       81.23    -57.70                                   
REMARK 500    PRO B  26     -104.95    -27.50                                   
REMARK 500    ASP B  55      -20.79     72.01                                   
REMARK 500    VAL B  89       57.43   -145.09                                   
REMARK 500    SER B 140     -136.36   -130.42                                   
REMARK 500    GLU B 191       -1.41    104.92                                   
REMARK 500    ALA B 198       81.73    -50.55                                   
REMARK 500    PRO C  26      -79.42    -32.03                                   
REMARK 500    ILE C  27      -31.98    164.29                                   
REMARK 500    HIS C  28      119.64     58.22                                   
REMARK 500    LYS C  54      100.00     24.99                                   
REMARK 500    ASP C  55      -23.21     75.89                                   
REMARK 500    VAL C  89       51.84   -141.44                                   
REMARK 500    SER C 140     -130.69   -120.42                                   
REMARK 500    TYR C 141      -63.95    -95.58                                   
REMARK 500    LEU C 144      -10.56   -162.98                                   
REMARK 500    ALA C 179     -122.13    -50.76                                   
REMARK 500    ILE C 180       80.71    -63.76                                   
REMARK 500    GLU C 191       -6.38     79.17                                   
REMARK 500    GLN D  24       37.42    -95.96                                   
REMARK 500    PRO D  26      -74.74    -24.09                                   
REMARK 500    ILE D  27      -45.29    162.20                                   
REMARK 500    HIS D  28      120.30     67.63                                   
REMARK 500    LEU D  48      107.91    -50.63                                   
REMARK 500    LYS D  54       94.20     32.54                                   
REMARK 500    ASP D  55      -16.30     72.37                                   
REMARK 500    VAL D  89       48.20   -143.99                                   
REMARK 500    SER D 140     -132.42   -117.42                                   
REMARK 500    TYR D 141      -65.19    -92.07                                   
REMARK 500    LEU D 144      -16.24   -163.74                                   
REMARK 500    ALA D 179     -121.77    -48.41                                   
REMARK 500    ILE D 180       81.86    -66.88                                   
REMARK 500    GLU D 191      -15.55     83.47                                   
REMARK 500    PRO E  26     -108.55    -73.65                                   
REMARK 500    ILE E  27      129.45    179.70                                   
REMARK 500    ASP E  55      -14.01     66.61                                   
REMARK 500    VAL E  89       55.08   -142.78                                   
REMARK 500    SER E 140     -134.40   -131.47                                   
REMARK 500    LEU E 144       80.59   -150.97                                   
REMARK 500    GLU E 191       -0.63     99.25                                   
REMARK 500    ALA E 198       81.87    -60.14                                   
REMARK 500    GLN F  24       64.37   -102.30                                   
REMARK 500    THR F  25      151.46     67.18                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR C 133         0.07    SIDE CHAIN                              
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 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 905                 
DBREF  1FPZ A    1   212  UNP    Q16667   CDKN3_HUMAN      1    212             
DBREF  1FPZ B    1   212  UNP    Q16667   CDKN3_HUMAN      1    212             
DBREF  1FPZ C    1   212  UNP    Q16667   CDKN3_HUMAN      1    212             
DBREF  1FPZ D    1   212  UNP    Q16667   CDKN3_HUMAN      1    212             
DBREF  1FPZ E    1   212  UNP    Q16667   CDKN3_HUMAN      1    212             
DBREF  1FPZ F    1   212  UNP    Q16667   CDKN3_HUMAN      1    212             
SEQADV 1FPZ SER A  140  UNP  Q16667    CYS   140 ENGINEERED MUTATION            
SEQADV 1FPZ SER B  140  UNP  Q16667    CYS   140 ENGINEERED MUTATION            
SEQADV 1FPZ SER C  140  UNP  Q16667    CYS   140 ENGINEERED MUTATION            
SEQADV 1FPZ SER D  140  UNP  Q16667    CYS   140 ENGINEERED MUTATION            
SEQADV 1FPZ SER E  140  UNP  Q16667    CYS   140 ENGINEERED MUTATION            
SEQADV 1FPZ SER F  140  UNP  Q16667    CYS   140 ENGINEERED MUTATION            
SEQRES   1 A  212  MET LYS PRO PRO SER SER ILE GLN THR SER GLU PHE ASP          
SEQRES   2 A  212  SER SER ASP GLU GLU PRO ILE GLU ASP GLU GLN THR PRO          
SEQRES   3 A  212  ILE HIS ILE SER TRP LEU SER LEU SER ARG VAL ASN CYS          
SEQRES   4 A  212  SER GLN PHE LEU GLY LEU CYS ALA LEU PRO GLY CYS LYS          
SEQRES   5 A  212  PHE LYS ASP VAL ARG ARG ASN VAL GLN LYS ASP THR GLU          
SEQRES   6 A  212  GLU LEU LYS SER CYS GLY ILE GLN ASP ILE PHE VAL PHE          
SEQRES   7 A  212  CYS THR ARG GLY GLU LEU SER LYS TYR ARG VAL PRO ASN          
SEQRES   8 A  212  LEU LEU ASP LEU TYR GLN GLN CYS GLY ILE ILE THR HIS          
SEQRES   9 A  212  HIS HIS PRO ILE ALA ASP GLY GLY THR PRO ASP ILE ALA          
SEQRES  10 A  212  SER CYS CYS GLU ILE MET GLU GLU LEU THR THR CYS LEU          
SEQRES  11 A  212  LYS ASN TYR ARG LYS THR LEU ILE HIS SER TYR GLY GLY          
SEQRES  12 A  212  LEU GLY ARG SER CYS LEU VAL ALA ALA CYS LEU LEU LEU          
SEQRES  13 A  212  TYR LEU SER ASP THR ILE SER PRO GLU GLN ALA ILE ASP          
SEQRES  14 A  212  SER LEU ARG ASP LEU ARG GLY SER GLY ALA ILE GLN THR          
SEQRES  15 A  212  ILE LYS GLN TYR ASN TYR LEU HIS GLU PHE ARG ASP LYS          
SEQRES  16 A  212  LEU ALA ALA HIS LEU SER SER ARG ASP SER GLN SER ARG          
SEQRES  17 A  212  SER VAL SER ARG                                              
SEQRES   1 B  212  MET LYS PRO PRO SER SER ILE GLN THR SER GLU PHE ASP          
SEQRES   2 B  212  SER SER ASP GLU GLU PRO ILE GLU ASP GLU GLN THR PRO          
SEQRES   3 B  212  ILE HIS ILE SER TRP LEU SER LEU SER ARG VAL ASN CYS          
SEQRES   4 B  212  SER GLN PHE LEU GLY LEU CYS ALA LEU PRO GLY CYS LYS          
SEQRES   5 B  212  PHE LYS ASP VAL ARG ARG ASN VAL GLN LYS ASP THR GLU          
SEQRES   6 B  212  GLU LEU LYS SER CYS GLY ILE GLN ASP ILE PHE VAL PHE          
SEQRES   7 B  212  CYS THR ARG GLY GLU LEU SER LYS TYR ARG VAL PRO ASN          
SEQRES   8 B  212  LEU LEU ASP LEU TYR GLN GLN CYS GLY ILE ILE THR HIS          
SEQRES   9 B  212  HIS HIS PRO ILE ALA ASP GLY GLY THR PRO ASP ILE ALA          
SEQRES  10 B  212  SER CYS CYS GLU ILE MET GLU GLU LEU THR THR CYS LEU          
SEQRES  11 B  212  LYS ASN TYR ARG LYS THR LEU ILE HIS SER TYR GLY GLY          
SEQRES  12 B  212  LEU GLY ARG SER CYS LEU VAL ALA ALA CYS LEU LEU LEU          
SEQRES  13 B  212  TYR LEU SER ASP THR ILE SER PRO GLU GLN ALA ILE ASP          
SEQRES  14 B  212  SER LEU ARG ASP LEU ARG GLY SER GLY ALA ILE GLN THR          
SEQRES  15 B  212  ILE LYS GLN TYR ASN TYR LEU HIS GLU PHE ARG ASP LYS          
SEQRES  16 B  212  LEU ALA ALA HIS LEU SER SER ARG ASP SER GLN SER ARG          
SEQRES  17 B  212  SER VAL SER ARG                                              
SEQRES   1 C  212  MET LYS PRO PRO SER SER ILE GLN THR SER GLU PHE ASP          
SEQRES   2 C  212  SER SER ASP GLU GLU PRO ILE GLU ASP GLU GLN THR PRO          
SEQRES   3 C  212  ILE HIS ILE SER TRP LEU SER LEU SER ARG VAL ASN CYS          
SEQRES   4 C  212  SER GLN PHE LEU GLY LEU CYS ALA LEU PRO GLY CYS LYS          
SEQRES   5 C  212  PHE LYS ASP VAL ARG ARG ASN VAL GLN LYS ASP THR GLU          
SEQRES   6 C  212  GLU LEU LYS SER CYS GLY ILE GLN ASP ILE PHE VAL PHE          
SEQRES   7 C  212  CYS THR ARG GLY GLU LEU SER LYS TYR ARG VAL PRO ASN          
SEQRES   8 C  212  LEU LEU ASP LEU TYR GLN GLN CYS GLY ILE ILE THR HIS          
SEQRES   9 C  212  HIS HIS PRO ILE ALA ASP GLY GLY THR PRO ASP ILE ALA          
SEQRES  10 C  212  SER CYS CYS GLU ILE MET GLU GLU LEU THR THR CYS LEU          
SEQRES  11 C  212  LYS ASN TYR ARG LYS THR LEU ILE HIS SER TYR GLY GLY          
SEQRES  12 C  212  LEU GLY ARG SER CYS LEU VAL ALA ALA CYS LEU LEU LEU          
SEQRES  13 C  212  TYR LEU SER ASP THR ILE SER PRO GLU GLN ALA ILE ASP          
SEQRES  14 C  212  SER LEU ARG ASP LEU ARG GLY SER GLY ALA ILE GLN THR          
SEQRES  15 C  212  ILE LYS GLN TYR ASN TYR LEU HIS GLU PHE ARG ASP LYS          
SEQRES  16 C  212  LEU ALA ALA HIS LEU SER SER ARG ASP SER GLN SER ARG          
SEQRES  17 C  212  SER VAL SER ARG                                              
SEQRES   1 D  212  MET LYS PRO PRO SER SER ILE GLN THR SER GLU PHE ASP          
SEQRES   2 D  212  SER SER ASP GLU GLU PRO ILE GLU ASP GLU GLN THR PRO          
SEQRES   3 D  212  ILE HIS ILE SER TRP LEU SER LEU SER ARG VAL ASN CYS          
SEQRES   4 D  212  SER GLN PHE LEU GLY LEU CYS ALA LEU PRO GLY CYS LYS          
SEQRES   5 D  212  PHE LYS ASP VAL ARG ARG ASN VAL GLN LYS ASP THR GLU          
SEQRES   6 D  212  GLU LEU LYS SER CYS GLY ILE GLN ASP ILE PHE VAL PHE          
SEQRES   7 D  212  CYS THR ARG GLY GLU LEU SER LYS TYR ARG VAL PRO ASN          
SEQRES   8 D  212  LEU LEU ASP LEU TYR GLN GLN CYS GLY ILE ILE THR HIS          
SEQRES   9 D  212  HIS HIS PRO ILE ALA ASP GLY GLY THR PRO ASP ILE ALA          
SEQRES  10 D  212  SER CYS CYS GLU ILE MET GLU GLU LEU THR THR CYS LEU          
SEQRES  11 D  212  LYS ASN TYR ARG LYS THR LEU ILE HIS SER TYR GLY GLY          
SEQRES  12 D  212  LEU GLY ARG SER CYS LEU VAL ALA ALA CYS LEU LEU LEU          
SEQRES  13 D  212  TYR LEU SER ASP THR ILE SER PRO GLU GLN ALA ILE ASP          
SEQRES  14 D  212  SER LEU ARG ASP LEU ARG GLY SER GLY ALA ILE GLN THR          
SEQRES  15 D  212  ILE LYS GLN TYR ASN TYR LEU HIS GLU PHE ARG ASP LYS          
SEQRES  16 D  212  LEU ALA ALA HIS LEU SER SER ARG ASP SER GLN SER ARG          
SEQRES  17 D  212  SER VAL SER ARG                                              
SEQRES   1 E  212  MET LYS PRO PRO SER SER ILE GLN THR SER GLU PHE ASP          
SEQRES   2 E  212  SER SER ASP GLU GLU PRO ILE GLU ASP GLU GLN THR PRO          
SEQRES   3 E  212  ILE HIS ILE SER TRP LEU SER LEU SER ARG VAL ASN CYS          
SEQRES   4 E  212  SER GLN PHE LEU GLY LEU CYS ALA LEU PRO GLY CYS LYS          
SEQRES   5 E  212  PHE LYS ASP VAL ARG ARG ASN VAL GLN LYS ASP THR GLU          
SEQRES   6 E  212  GLU LEU LYS SER CYS GLY ILE GLN ASP ILE PHE VAL PHE          
SEQRES   7 E  212  CYS THR ARG GLY GLU LEU SER LYS TYR ARG VAL PRO ASN          
SEQRES   8 E  212  LEU LEU ASP LEU TYR GLN GLN CYS GLY ILE ILE THR HIS          
SEQRES   9 E  212  HIS HIS PRO ILE ALA ASP GLY GLY THR PRO ASP ILE ALA          
SEQRES  10 E  212  SER CYS CYS GLU ILE MET GLU GLU LEU THR THR CYS LEU          
SEQRES  11 E  212  LYS ASN TYR ARG LYS THR LEU ILE HIS SER TYR GLY GLY          
SEQRES  12 E  212  LEU GLY ARG SER CYS LEU VAL ALA ALA CYS LEU LEU LEU          
SEQRES  13 E  212  TYR LEU SER ASP THR ILE SER PRO GLU GLN ALA ILE ASP          
SEQRES  14 E  212  SER LEU ARG ASP LEU ARG GLY SER GLY ALA ILE GLN THR          
SEQRES  15 E  212  ILE LYS GLN TYR ASN TYR LEU HIS GLU PHE ARG ASP LYS          
SEQRES  16 E  212  LEU ALA ALA HIS LEU SER SER ARG ASP SER GLN SER ARG          
SEQRES  17 E  212  SER VAL SER ARG                                              
SEQRES   1 F  212  MET LYS PRO PRO SER SER ILE GLN THR SER GLU PHE ASP          
SEQRES   2 F  212  SER SER ASP GLU GLU PRO ILE GLU ASP GLU GLN THR PRO          
SEQRES   3 F  212  ILE HIS ILE SER TRP LEU SER LEU SER ARG VAL ASN CYS          
SEQRES   4 F  212  SER GLN PHE LEU GLY LEU CYS ALA LEU PRO GLY CYS LYS          
SEQRES   5 F  212  PHE LYS ASP VAL ARG ARG ASN VAL GLN LYS ASP THR GLU          
SEQRES   6 F  212  GLU LEU LYS SER CYS GLY ILE GLN ASP ILE PHE VAL PHE          
SEQRES   7 F  212  CYS THR ARG GLY GLU LEU SER LYS TYR ARG VAL PRO ASN          
SEQRES   8 F  212  LEU LEU ASP LEU TYR GLN GLN CYS GLY ILE ILE THR HIS          
SEQRES   9 F  212  HIS HIS PRO ILE ALA ASP GLY GLY THR PRO ASP ILE ALA          
SEQRES  10 F  212  SER CYS CYS GLU ILE MET GLU GLU LEU THR THR CYS LEU          
SEQRES  11 F  212  LYS ASN TYR ARG LYS THR LEU ILE HIS SER TYR GLY GLY          
SEQRES  12 F  212  LEU GLY ARG SER CYS LEU VAL ALA ALA CYS LEU LEU LEU          
SEQRES  13 F  212  TYR LEU SER ASP THR ILE SER PRO GLU GLN ALA ILE ASP          
SEQRES  14 F  212  SER LEU ARG ASP LEU ARG GLY SER GLY ALA ILE GLN THR          
SEQRES  15 F  212  ILE LYS GLN TYR ASN TYR LEU HIS GLU PHE ARG ASP LYS          
SEQRES  16 F  212  LEU ALA ALA HIS LEU SER SER ARG ASP SER GLN SER ARG          
SEQRES  17 F  212  SER VAL SER ARG                                              
HET    SO4  A 900       5                                                       
HET    SO4  B 901       5                                                       
HET    SO4  C 902       5                                                       
HET    SO4  D 903       5                                                       
HET    SO4  E 904       5                                                       
HET    SO4  F 905       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   7  SO4    6(O4 S 2-)                                                   
FORMUL  13  HOH   *690(H2 O)                                                    
HELIX    1   1 SER A   35  ASN A   38  5                                   4    
HELIX    2   2 ASN A   59  GLY A   71  1                                  13    
HELIX    3   3 THR A   80  TYR A   87  1                                   8    
HELIX    4   4 ASN A   91  CYS A   99  1                                   9    
HELIX    5   5 ASP A  115  ASN A  132  1                                  18    
HELIX    6   6 GLY A  145  SER A  159  1                                  15    
HELIX    7   7 SER A  163  GLY A  176  1                                  14    
HELIX    8   8 THR A  182  HIS A  190  1                                   9    
HELIX    9   9 GLU A  191  ALA A  198  1                                   8    
HELIX   10  10 SER B   35  ASN B   38  5                                   4    
HELIX   11  11 ASN B   59  CYS B   70  1                                  12    
HELIX   12  12 THR B   80  TYR B   87  1                                   8    
HELIX   13  13 ASN B   91  CYS B   99  1                                   9    
HELIX   14  14 ASP B  115  ASN B  132  1                                  18    
HELIX   15  15 GLY B  145  SER B  159  1                                  15    
HELIX   16  16 SER B  163  GLY B  176  1                                  14    
HELIX   17  17 THR B  182  HIS B  190  1                                   9    
HELIX   18  18 GLU B  191  ALA B  198  1                                   8    
HELIX   19  19 SER C   35  ASN C   38  5                                   4    
HELIX   20  20 ASN C   59  CYS C   70  1                                  12    
HELIX   21  21 THR C   80  TYR C   87  1                                   8    
HELIX   22  22 ASN C   91  CYS C   99  1                                   9    
HELIX   23  23 ASP C  115  ASN C  132  1                                  18    
HELIX   24  24 GLY C  145  SER C  159  1                                  15    
HELIX   25  25 SER C  163  GLY C  176  1                                  14    
HELIX   26  26 THR C  182  HIS C  190  1                                   9    
HELIX   27  27 GLU C  191  ALA C  198  1                                   8    
HELIX   28  28 SER D   35  ASN D   38  5                                   4    
HELIX   29  29 ASN D   59  CYS D   70  1                                  12    
HELIX   30  30 THR D   80  TYR D   87  1                                   8    
HELIX   31  31 ASN D   91  CYS D   99  1                                   9    
HELIX   32  32 ASP D  115  ASN D  132  1                                  18    
HELIX   33  33 GLY D  145  SER D  159  1                                  15    
HELIX   34  34 SER D  163  GLY D  176  1                                  14    
HELIX   35  35 THR D  182  HIS D  190  1                                   9    
HELIX   36  36 GLU D  191  ALA D  198  1                                   8    
HELIX   37  37 SER E   35  ASN E   38  5                                   4    
HELIX   38  38 ASN E   59  CYS E   70  1                                  12    
HELIX   39  39 THR E   80  TYR E   87  1                                   8    
HELIX   40  40 ASN E   91  CYS E   99  1                                   9    
HELIX   41  41 ASP E  115  ASN E  132  1                                  18    
HELIX   42  42 GLY E  145  SER E  159  1                                  15    
HELIX   43  43 SER E  163  GLY E  176  1                                  14    
HELIX   44  44 THR E  182  HIS E  190  1                                   9    
HELIX   45  45 GLU E  191  ALA E  198  1                                   8    
HELIX   46  46 SER F   35  ASN F   38  5                                   4    
HELIX   47  47 ASN F   59  CYS F   70  1                                  12    
HELIX   48  48 THR F   80  TYR F   87  1                                   8    
HELIX   49  49 ASN F   91  CYS F   99  1                                   9    
HELIX   50  50 ASP F  115  ASN F  132  1                                  18    
HELIX   51  51 GLY F  145  SER F  159  1                                  15    
HELIX   52  52 SER F  163  GLY F  176  1                                  14    
HELIX   53  53 THR F  182  HIS F  190  1                                   9    
HELIX   54  54 GLU F  191  ALA F  198  1                                   8    
SHEET    1   A 5 SER A  30  SER A  33  0                                        
SHEET    2   A 5 PHE A  42  CYS A  46 -1  O  LEU A  43   N  LEU A  32           
SHEET    3   A 5 THR A 136  HIS A 139  1  O  THR A 136   N  GLY A  44           
SHEET    4   A 5 ASP A  74  VAL A  77  1  O  ASP A  74   N  LEU A 137           
SHEET    5   A 5 ILE A 102  HIS A 105  1  O  ILE A 102   N  ILE A  75           
SHEET    1   B 2 LYS A  52  PHE A  53  0                                        
SHEET    2   B 2 VAL A  56  ARG A  57 -1  O  VAL A  56   N  PHE A  53           
SHEET    1   C 5 SER B  30  SER B  33  0                                        
SHEET    2   C 5 PHE B  42  CYS B  46 -1  O  LEU B  43   N  LEU B  32           
SHEET    3   C 5 THR B 136  HIS B 139  1  O  THR B 136   N  GLY B  44           
SHEET    4   C 5 ASP B  74  VAL B  77  1  O  ASP B  74   N  LEU B 137           
SHEET    5   C 5 ILE B 102  HIS B 105  1  O  ILE B 102   N  ILE B  75           
SHEET    1   D 2 LYS B  52  PHE B  53  0                                        
SHEET    2   D 2 VAL B  56  ARG B  57 -1  O  VAL B  56   N  PHE B  53           
SHEET    1   E 5 SER C  30  SER C  33  0                                        
SHEET    2   E 5 PHE C  42  CYS C  46 -1  O  LEU C  43   N  LEU C  32           
SHEET    3   E 5 THR C 136  HIS C 139  1  O  THR C 136   N  GLY C  44           
SHEET    4   E 5 ASP C  74  VAL C  77  1  O  ASP C  74   N  LEU C 137           
SHEET    5   E 5 ILE C 102  HIS C 105  1  O  ILE C 102   N  ILE C  75           
SHEET    1   F 2 LYS C  52  PHE C  53  0                                        
SHEET    2   F 2 VAL C  56  ARG C  57 -1  O  VAL C  56   N  PHE C  53           
SHEET    1   G 5 SER D  30  SER D  33  0                                        
SHEET    2   G 5 PHE D  42  LEU D  45 -1  O  LEU D  43   N  LEU D  32           
SHEET    3   G 5 THR D 136  HIS D 139  1  O  THR D 136   N  GLY D  44           
SHEET    4   G 5 ASP D  74  VAL D  77  1  O  ASP D  74   N  LEU D 137           
SHEET    5   G 5 ILE D 102  HIS D 105  1  O  ILE D 102   N  ILE D  75           
SHEET    1   H 2 LYS D  52  PHE D  53  0                                        
SHEET    2   H 2 VAL D  56  ARG D  57 -1  O  VAL D  56   N  PHE D  53           
SHEET    1   I 5 SER E  30  SER E  33  0                                        
SHEET    2   I 5 PHE E  42  CYS E  46 -1  O  LEU E  43   N  LEU E  32           
SHEET    3   I 5 THR E 136  HIS E 139  1  O  THR E 136   N  GLY E  44           
SHEET    4   I 5 ASP E  74  VAL E  77  1  O  ASP E  74   N  LEU E 137           
SHEET    5   I 5 ILE E 102  HIS E 105  1  O  ILE E 102   N  ILE E  75           
SHEET    1   J 2 LYS E  52  PHE E  53  0                                        
SHEET    2   J 2 VAL E  56  ARG E  57 -1  O  VAL E  56   N  PHE E  53           
SHEET    1   K 5 SER F  30  SER F  33  0                                        
SHEET    2   K 5 PHE F  42  CYS F  46 -1  O  LEU F  43   N  LEU F  32           
SHEET    3   K 5 THR F 136  HIS F 139  1  O  THR F 136   N  GLY F  44           
SHEET    4   K 5 ASP F  74  VAL F  77  1  O  ASP F  74   N  LEU F 137           
SHEET    5   K 5 ILE F 102  HIS F 105  1  O  ILE F 102   N  ILE F  75           
SHEET    1   L 2 LYS F  52  PHE F  53  0                                        
SHEET    2   L 2 VAL F  56  ARG F  57 -1  O  VAL F  56   N  PHE F  53           
SITE     1 AC1  5 GLY A 142  LEU A 144  GLY A 145  ARG A 146                    
SITE     2 AC1  5 GLN A 181                                                     
SITE     1 AC2  9 SER B 140  TYR B 141  GLY B 142  GLY B 143                    
SITE     2 AC2  9 LEU B 144  GLY B 145  ARG B 146  GLN B 181                    
SITE     3 AC2  9 HOH B 947                                                     
SITE     1 AC3 10 SER C 140  TYR C 141  GLY C 142  GLY C 143                    
SITE     2 AC3 10 LEU C 144  GLY C 145  ARG C 146  HOH C 912                    
SITE     3 AC3 10 HOH C 923  HOH C 968                                          
SITE     1 AC4  7 SER D 140  TYR D 141  GLY D 142  GLY D 143                    
SITE     2 AC4  7 LEU D 144  GLY D 145  ARG D 146                               
SITE     1 AC5 10 ASP E 110  SER E 140  TYR E 141  GLY E 142                    
SITE     2 AC5 10 GLY E 143  LEU E 144  GLY E 145  ARG E 146                    
SITE     3 AC5 10 HOH E 906  HOH E1026                                          
SITE     1 AC6  7 SER F 140  TYR F 141  GLY F 142  GLY F 143                    
SITE     2 AC6  7 LEU F 144  GLY F 145  ARG F 146                               
CRYST1  131.930  131.930  140.240  90.00  90.00 120.00 P 65         36          
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      0.007580  0.004376  0.000000        0.00000                         
SCALE2      0.000000  0.008752  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007131        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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