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Database: PDB
Entry: 1UNQ
LinkDB: 1UNQ
Original site: 1UNQ 
HEADER    TRANSFERASE                             12-SEP-03   1UNQ              
TITLE     HIGH RESOLUTION CRYSTAL STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF
TITLE    2 PROTEIN KINASE B/AKT BOUND TO INS(1,3,4,5)-TETRAKISPHOPHATE          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAC-ALPHA SERINE/THREONINE KINASE;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PLECKSTRIN HOMOLOGY DOMAIN RESIDUES 1-123;                 
COMPND   5 SYNONYM: PROTEIN KINASE B, RAC-PK-ALPHA, PKB, C-AKT;                 
COMPND   6 EC: 2.7.1.-;                                                         
COMPND   7 ENGINEERED: 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 BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1                                  
KEYWDS    TRANSFERASE, PLECKSTRIN HOMOLOGY DOMAIN, PKB, AKT, PHOSPHOINOSITIDE,  
KEYWDS   2 SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING, PHOSPHORYLATION,       
KEYWDS   3 NUCLEAR PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.C.MILBURN,M.DEAK,S.M.KELLY,N.C.PRICE,D.R.ALESSI,D.M.F.VAN AALTEN    
REVDAT   4   13-DEC-23 1UNQ    1       LINK                                     
REVDAT   3   28-FEB-18 1UNQ    1       SOURCE AUTHOR JRNL                       
REVDAT   2   24-FEB-09 1UNQ    1       VERSN                                    
REVDAT   1   16-SEP-04 1UNQ    0                                                
JRNL        AUTH   C.C.MILBURN,M.DEAK,S.M.KELLY,N.C.PRICE,D.R.ALESSI,           
JRNL        AUTH 2 D.M.VAN AALTEN                                               
JRNL        TITL   BINDING OF PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE TO THE   
JRNL        TITL 2 PLECKSTRIN HOMOLOGY DOMAIN OF PROTEIN KINASE B INDUCES A     
JRNL        TITL 3 CONFORMATIONAL CHANGE.                                       
JRNL        REF    BIOCHEM. J.                   V. 375   531 2003              
JRNL        REFN                   ESSN 1470-8728                               
JRNL        PMID   12964941                                                     
JRNL        DOI    10.1042/BJ20031229                                           
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.C.MILBURN,M.DEAK,D.R.ALESSI,D.M.F.VAN AALTEN               
REMARK   1  TITL   HIGH RESOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN  
REMARK   1  TITL 2 OF PROTEIN KINASE B/AKT BOUND TO PHOSPHATIDYLINOSITOL        
REMARK   1  TITL 3 (3,4,5)-TRISPHOSPHATE                                        
REMARK   1  REF    CURR.BIOL.                    V.  12  1256 2002              
REMARK   1  REFN                   ISSN 0960-9822                               
REMARK   1  PMID   12176338                                                     
REMARK   1  DOI    10.1016/S0960-9822(02)00972-7                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    0.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.1                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.151                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.154                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.179                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2429                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 60005                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.142                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 46229                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 985                                           
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 28                                            
REMARK   3   SOLVENT ATOMS      : 155                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1167.5                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 961.00                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 10                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 10871                   
REMARK   3   NUMBER OF RESTRAINTS                     : 13466                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.014                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.030                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.028                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.066                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.078                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.068                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.050                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.077                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2          
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UNQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-SEP-03.                  
REMARK 100 THE DEPOSITION ID IS D_1290013513.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.920177                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60005                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.980                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1H10                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 30.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25 M AMMONIUM ACETATE, 30 % PEG        
REMARK 280  4000, 0.1 M SODIUM ACETATE (4.6), PH 4.60                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       41.45200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       17.19400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       41.45200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       17.19400            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2055  LIES ON A SPECIAL POSITION.                          
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   118                                                      
REMARK 465     ASP A   119                                                      
REMARK 465     PHE A   120                                                      
REMARK 465     ARG A   121                                                      
REMARK 465     SER A   122                                                      
REMARK 465     GLY A   123                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 117    CA   C    O    CB   CG   CD   OE1                   
REMARK 470     GLU A 117    OE2                                                 
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    ARG A  15   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG A  15   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A  67   NE  -  CZ  -  NH2 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG A  69   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A  69   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A  76   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG A  76   NE  -  CZ  -  NH1 ANGL. DEV. =   7.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TRP A  80      -93.40     62.67                                   
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 4IP A1117                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H10   RELATED DB: PDB                                   
REMARK 900 HIGH RESOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF       
REMARK 900 PROTEIN KINASE B/AKT BOUND TO INS(1,3,4,5)-TETRAKISPHOPHATE          
REMARK 900 RELATED ID: 1UNP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF PKB ALPHA     
REMARK 900 RELATED ID: 1UNR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE PH DOMAIN OF PKB ALPHA IN COMPLEX WITH A    
REMARK 900 SULFATE MOLECULE                                                     
DBREF  1UNQ A   -1     0  PDB    1UNQ     1UNQ            -1      0             
DBREF  1UNQ A    1   123  UNP    P31749   KRAC_HUMAN       1    123             
SEQRES   1 A  125  ACE SER MET SER ASP VAL ALA ILE VAL LYS GLU GLY TRP          
SEQRES   2 A  125  LEU HIS LYS ARG GLY GLU TYR ILE LYS THR TRP ARG PRO          
SEQRES   3 A  125  ARG TYR PHE LEU LEU LYS ASN ASP GLY THR PHE ILE GLY          
SEQRES   4 A  125  TYR LYS GLU ARG PRO GLN ASP VAL ASP GLN ARG GLU ALA          
SEQRES   5 A  125  PRO LEU ASN ASN PHE SER VAL ALA GLN CYS GLN LEU MET          
SEQRES   6 A  125  LYS THR GLU ARG PRO ARG PRO ASN THR PHE ILE ILE ARG          
SEQRES   7 A  125  CYS LEU GLN TRP THR THR VAL ILE GLU ARG THR PHE HIS          
SEQRES   8 A  125  VAL GLU THR PRO GLU GLU ARG GLU GLU TRP THR THR ALA          
SEQRES   9 A  125  ILE GLN THR VAL ALA ASP GLY LEU LYS LYS GLN GLU GLU          
SEQRES  10 A  125  GLU GLU MET ASP PHE ARG SER GLY                              
HET    ACE  A  -1       3                                                       
HET    4IP  A1117      28                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     4IP INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE                             
FORMUL   1  ACE    C2 H4 O                                                      
FORMUL   2  4IP    C6 H16 O18 P4                                                
FORMUL   3  HOH   *155(H2 O)                                                    
HELIX    1   1 MET A    1  VAL A    4  5                                   4    
HELIX    2   2 ASP A   44  GLU A   49  1                                   6    
HELIX    3   3 THR A   92  GLU A  116  1                                  25    
SHEET    1  AA 7 ASN A  53  SER A  56  0                                        
SHEET    2  AA 7 THR A  34  TYR A  38 -1  O  PHE A  35   N  PHE A  55           
SHEET    3  AA 7 TRP A  22  LYS A  30 -1  O  TYR A  26   N  TYR A  38           
SHEET    4  AA 7 ILE A   6  ARG A  15 -1  N  VAL A   7   O  LEU A  29           
SHEET    5  AA 7 THR A  82  HIS A  89 -1  O  THR A  87   N  ARG A  15           
SHEET    6  AA 7 THR A  72  GLN A  79 -1  O  PHE A  73   N  PHE A  88           
SHEET    7  AA 7 GLN A  61  THR A  65 -1  O  GLN A  61   N  ARG A  76           
LINK         C   ACE A  -1                 N   SER A   0     1555   1555  1.33  
CISPEP   1 ARG A   67    PRO A   68          0         7.76                     
SITE     1 AC1 28 ACE A  -1  SER A   0  MET A   1  SER A   2                    
SITE     2 AC1 28 HIS A  13  LYS A  14  GLY A  16  GLU A  17                    
SITE     3 AC1 28 TYR A  18  ILE A  19  ARG A  23  ARG A  25                    
SITE     4 AC1 28 LEU A  52  ASN A  53  PHE A  55  ARG A  86                    
SITE     5 AC1 28 HOH A2007  HOH A2105  HOH A2146  HOH A2147                    
SITE     6 AC1 28 HOH A2148  HOH A2149  HOH A2150  HOH A2151                    
SITE     7 AC1 28 HOH A2152  HOH A2153  HOH A2154  HOH A2155                    
CRYST1   82.904   34.388   44.292  90.00 115.29  90.00 C 1 2 1       4          
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      0.012062  0.000000  0.005699        0.00000                         
SCALE2      0.000000  0.029080  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.024971        0.00000                         
HETATM    1  C   ACE A  -1      25.842  13.738 -11.519  1.00 14.57           C  
ANISOU    1  C   ACE A  -1     1596   2356   1583   -446    162    141       C  
HETATM    2  O   ACE A  -1      25.616  13.709 -10.308  1.00 19.54           O  
ANISOU    2  O   ACE A  -1     2186   3548   1689  -1087    329    171       O  
HETATM    3  CH3 ACE A  -1      27.218  13.295 -12.006  1.00 17.56           C  
ANISOU    3  CH3 ACE A  -1     2058   2378   2236    311    189    237       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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