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Database: PDB
Entry: 1IHB
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Original site: 1IHB 
HEADER    CELL CYCLE INHIBITOR                    25-OCT-97   1IHB              
TITLE     CRYSTAL STRUCTURE OF P18-INK4C(INK6)                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 6 INHIBITOR;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: P18-INK4C(INK6);                                            
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: BL21;                                                     
SOURCE   6 GENE: P18-INK4C(INK6);                                               
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PRSETA;                                    
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: BL21;                                     
SOURCE  12 EXPRESSION_SYSTEM_GENE: P18-INK4C(INK6)                              
KEYWDS    CELL CYCLE INHIBITOR, P18-INK4C(INK6), ANKYRIN REPEAT, CDK            
KEYWDS   2 4/6 INHIBITOR                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.RAVICHANDRAN,K.SWAMINATHAN,R.MARMORSTEIN                            
REVDAT   3   24-FEB-09 1IHB    1       VERSN                                    
REVDAT   2   13-JAN-99 1IHB    1       COMPND REMARK SOURCE JRNL                
REVDAT   2 2                   1       KEYWDS                                   
REVDAT   1   02-DEC-98 1IHB    0                                                
JRNL        AUTH   R.VENKATARAMANI,K.SWAMINATHAN,R.MARMORSTEIN                  
JRNL        TITL   CRYSTAL STRUCTURE OF THE CDK4/6 INHIBITORY PROTEIN           
JRNL        TITL 2 P18INK4C PROVIDES INSIGHTS INTO ANKYRIN-LIKE                 
JRNL        TITL 3 REPEAT STRUCTURE/FUNCTION AND TUMOR-DERIVED                  
JRNL        TITL 4 P16INK4 MUTATIONS.                                           
JRNL        REF    NAT.STRUCT.BIOL.              V.   5    74 1998              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   9437433                                                      
JRNL        DOI    10.1038/NSB0198-74                                           
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 22215                          
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) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2208                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 54.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2048                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE                    : 0.3280                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 200                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.023                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2383                                    
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : NULL                                    
REMARK   3   SOLVENT ATOMS            : 207                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.10                          
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) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.48                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.890 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.720 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.690 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.580 ; 2.500                
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: BULK SOLVENT CORRECTION APPLIED           
REMARK   4                                                                      
REMARK   4 1IHB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MSC/YALE MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24019                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, 4 DEG. C, 2             
REMARK 280  MICROLITER HANGING DROP CONTAINING 5 MG/ML PROTEIN, 20 MM TRIS      
REMARK 280  (PH 8.5), 25 MM (NH4)2 HPO4, 0.5 MM DDT, 7% PEG 6K, 1 MM NACL       
REMARK 280  EQUILIBRATED OVER A RESERVOIR CONTAINING 14% PEG 6K AND 2 M         
REMARK 280  NACL. WITHIN 8 DAYS, 0.2 X 0.2 X 0.4 MM CRYSTALS., VAPOR            
REMARK 280  DIFFUSION - HANGING DROP                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       27.75500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.75500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.85000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     ALA A   161                                                      
REMARK 465     GLY A   162                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     TRP B     5                                                      
REMARK 465     GLY B     6                                                      
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   N    TRP A     5     O    HOH A   187              2.18            
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   O    ARG A   145     NH2  ARG B    54     3546     2.17            
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    THR A  69   CB  -  CA  -  C   ANGL. DEV. = -23.6 DEGREES          
REMARK 500    ARG B  54   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG B  54   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 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    ASN A  35     -165.88    -74.45                                   
REMARK 500    ASN A 159       59.48   -150.39                                   
REMARK 500    ARG B 149       72.47   -101.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1IHB A    1   162  UNP    P42773   CDN2C_HUMAN      1    162             
DBREF  1IHB B    1   162  UNP    P42773   CDN2C_HUMAN      1    162             
SEQRES   1 A  162  MET ALA GLU PRO TRP GLY ASN GLU LEU ALA SER ALA ALA          
SEQRES   2 A  162  ALA ARG GLY ASP LEU GLU GLN LEU THR SER LEU LEU GLN          
SEQRES   3 A  162  ASN ASN VAL ASN VAL ASN ALA GLN ASN GLY PHE GLY ARG          
SEQRES   4 A  162  THR ALA LEU GLN VAL MET LYS LEU GLY ASN PRO GLU ILE          
SEQRES   5 A  162  ALA ARG ARG LEU LEU LEU ARG GLY ALA ASN PRO ASP LEU          
SEQRES   6 A  162  LYS ASP ARG THR GLY PHE ALA VAL ILE HIS ASP ALA ALA          
SEQRES   7 A  162  ARG ALA GLY PHE LEU ASP THR LEU GLN THR LEU LEU GLU          
SEQRES   8 A  162  PHE GLN ALA ASP VAL ASN ILE GLU ASP ASN GLU GLY ASN          
SEQRES   9 A  162  LEU PRO LEU HIS LEU ALA ALA LYS GLU GLY HIS LEU ARG          
SEQRES  10 A  162  VAL VAL GLU PHE LEU VAL LYS HIS THR ALA SER ASN VAL          
SEQRES  11 A  162  GLY HIS ARG ASN HIS LYS GLY ASP THR ALA CYS ASP LEU          
SEQRES  12 A  162  ALA ARG LEU TYR GLY ARG ASN GLU VAL VAL SER LEU MET          
SEQRES  13 A  162  GLN ALA ASN GLY ALA GLY                                      
SEQRES   1 B  162  MET ALA GLU PRO TRP GLY ASN GLU LEU ALA SER ALA ALA          
SEQRES   2 B  162  ALA ARG GLY ASP LEU GLU GLN LEU THR SER LEU LEU GLN          
SEQRES   3 B  162  ASN ASN VAL ASN VAL ASN ALA GLN ASN GLY PHE GLY ARG          
SEQRES   4 B  162  THR ALA LEU GLN VAL MET LYS LEU GLY ASN PRO GLU ILE          
SEQRES   5 B  162  ALA ARG ARG LEU LEU LEU ARG GLY ALA ASN PRO ASP LEU          
SEQRES   6 B  162  LYS ASP ARG THR GLY PHE ALA VAL ILE HIS ASP ALA ALA          
SEQRES   7 B  162  ARG ALA GLY PHE LEU ASP THR LEU GLN THR LEU LEU GLU          
SEQRES   8 B  162  PHE GLN ALA ASP VAL ASN ILE GLU ASP ASN GLU GLY ASN          
SEQRES   9 B  162  LEU PRO LEU HIS LEU ALA ALA LYS GLU GLY HIS LEU ARG          
SEQRES  10 B  162  VAL VAL GLU PHE LEU VAL LYS HIS THR ALA SER ASN VAL          
SEQRES  11 B  162  GLY HIS ARG ASN HIS LYS GLY ASP THR ALA CYS ASP LEU          
SEQRES  12 B  162  ALA ARG LEU TYR GLY ARG ASN GLU VAL VAL SER LEU MET          
SEQRES  13 B  162  GLN ALA ASN GLY ALA GLY                                      
FORMUL   3  HOH   *207(H2 O)                                                    
HELIX    1   1 GLY A    6  ARG A   15  1                                  10    
HELIX    2   2 LEU A   18  GLN A   26  1                                   9    
HELIX    3   3 ALA A   41  VAL A   44  1                                   4    
HELIX    4   4 PRO A   50  LEU A   58  1                                   9    
HELIX    5   5 VAL A   73  ALA A   80  1                                   8    
HELIX    6   6 LEU A   83  GLU A   91  1                                   9    
HELIX    7   7 PRO A  106  LYS A  112  1                                   7    
HELIX    8   8 LEU A  116  HIS A  125  1                                  10    
HELIX    9   9 ALA A  140  LEU A  146  1                                   7    
HELIX   10  10 ASN A  150  ALA A  158  1                                   9    
HELIX   11  11 GLU B    8  ALA B   14  1                                   7    
HELIX   12  12 LEU B   18  ASN B   27  1                                  10    
HELIX   13  13 ALA B   41  VAL B   44  1                                   4    
HELIX   14  14 PRO B   50  LEU B   58  1                                   9    
HELIX   15  15 VAL B   73  ALA B   80  1                                   8    
HELIX   16  16 LEU B   83  PHE B   92  1                                  10    
HELIX   17  17 PRO B  106  LYS B  112  1                                   7    
HELIX   18  18 LEU B  116  HIS B  125  1                                  10    
HELIX   19  19 ALA B  140  LEU B  146  1                                   7    
HELIX   20  20 ASN B  150  ASN B  159  1                                  10    
CRYST1   55.510  151.700   40.460  90.00  90.00  90.00 P 21 21 2     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      0.018015  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006592  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.024716        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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