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Database: PDB
Entry: 1OCC
LinkDB: 1OCC
Original site: 1OCC 
ANISOU 3724  CE2 PHE A 472    12722  17253  11089   -343  -1613   1684       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    CYCLO-LIGASE                            28-MAR-95   1DTS              
TITLE     CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN       
TITLE    2 SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DETHIOBIOTIN SYNTHETASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 6.3.3.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562                                                  
KEYWDS    CYCLO-LIGASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.HUANG,Y.LINDQVIST,G.SCHNEIDER                                       
REVDAT   5   16-NOV-11 1DTS    1       HETATM                                   
REVDAT   4   13-JUL-11 1DTS    1       VERSN                                    
REVDAT   3   24-FEB-09 1DTS    1       VERSN                                    
REVDAT   2   01-APR-03 1DTS    1       JRNL                                     
REVDAT   1   20-APR-95 1DTS    0                                                
JRNL        AUTH   W.HUANG,Y.LINDQVIST,G.SCHNEIDER,K.J.GIBSON,D.FLINT,G.LORIMER 
JRNL        TITL   CRYSTAL STRUCTURE OF AN ATP-DEPENDENT CARBOXYLASE,           
JRNL        TITL 2 DETHIOBIOTIN SYNTHETASE, AT 1.65 A RESOLUTION.               
JRNL        REF    STRUCTURE                     V.   2   407 1994              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   8081756                                                      
JRNL        DOI    10.1016/S0969-2126(00)00042-3                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.50                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 21134                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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            : 1660                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 189                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.80                            
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  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 1DTS 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        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       36.60000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.60000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.60000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.60000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 2790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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 A 489  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     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A 154   NE2   HIS A 154   CD2    -0.066                       
REMARK 500    HIS A 164   CG    HIS A 164   CD2     0.069                       
REMARK 500    HIS A 164   NE2   HIS A 164   CD2    -0.074                       
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    TYR A   4   CB  -  CG  -  CD1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    TYR A  31   CB  -  CG  -  CD1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    TRP A 111   CD1 -  CG  -  CD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    TRP A 111   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    TRP A 120   CD1 -  CG  -  CD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    TRP A 120   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    TRP A 133   CD1 -  CG  -  CD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    TRP A 133   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TRP A 172   CD1 -  CG  -  CD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    TRP A 172   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG A 183   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    TRP A 205   CD1 -  CG  -  CD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    TRP A 205   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    TRP A 205   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 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    PHE A 121       38.24    -89.52                                   
REMARK 500    PRO A 179      155.34    -49.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 423        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH A 487        DISTANCE =  8.13 ANGSTROMS                       
DBREF  1DTS A    1   223  UNP    P13000   BIOD_ECOLI       1    223             
SEQADV 1DTS     A       UNP  P13000    ASN   209 DELETION                       
SEQADV 1DTS     A       UNP  P13000    PRO   210 DELETION                       
SEQADV 1DTS     A       UNP  P13000    GLU   211 DELETION                       
SEQADV 1DTS     A       UNP  P13000    ASN   212 DELETION                       
SEQRES   1 A  221  MET SER LYS ARG TYR PHE VAL THR GLY THR ASP THR GLU          
SEQRES   2 A  221  VAL GLY LYS THR VAL ALA SER CYS ALA LEU LEU GLN ALA          
SEQRES   3 A  221  ALA LYS ALA ALA GLY TYR ARG THR ALA GLY TYR LYS PRO          
SEQRES   4 A  221  VAL ALA SER GLY SER GLU LYS THR PRO GLU GLY LEU ARG          
SEQRES   5 A  221  ASN SER ASP ALA LEU ALA LEU GLN ARG ASN SER SER LEU          
SEQRES   6 A  221  GLN LEU ASP TYR ALA THR VAL ASN PRO TYR THR PHE ALA          
SEQRES   7 A  221  GLU PRO THR SER PRO HIS ILE ILE SER ALA GLN GLU GLY          
SEQRES   8 A  221  ARG PRO ILE GLU SER LEU VAL MET SER ALA GLY LEU ARG          
SEQRES   9 A  221  ALA LEU GLU GLN GLN ALA ASP TRP VAL LEU VAL GLU GLY          
SEQRES  10 A  221  ALA GLY GLY TRP PHE THR PRO LEU SER ASP THR PHE THR          
SEQRES  11 A  221  PHE ALA ASP TRP VAL THR GLN GLU GLN LEU PRO VAL ILE          
SEQRES  12 A  221  LEU VAL VAL GLY VAL LYS LEU GLY CYS ILE ASN HIS ALA          
SEQRES  13 A  221  MET LEU THR ALA GLN VAL ILE GLN HIS ALA GLY LEU THR          
SEQRES  14 A  221  LEU ALA GLY TRP VAL ALA ASN ASP VAL THR PRO PRO GLY          
SEQRES  15 A  221  LYS ARG HIS ALA GLU TYR MET THR THR LEU THR ARG MET          
SEQRES  16 A  221  ILE PRO ALA PRO LEU LEU GLY GLU ILE PRO TRP LEU ALA          
SEQRES  17 A  221  GLU ALA ALA THR GLY LYS TYR ILE ASN LEU ALA LEU LEU          
FORMUL   2  HOH   *189(H2 O)                                                    
HELIX    1  A1 GLY A   14  ALA A   28  1                                  15    
HELIX    2  A2 SER A   53  ASN A   61  1                                   9    
HELIX    3 A2A ASP A   67  VAL A   71  1                                   5    
HELIX    4 A3A THR A   80  GLY A   90  1                                  11    
HELIX    5  A3 SER A   95  GLU A  106  1                                  12    
HELIX    6  A4 PHE A  130  GLU A  137  1                                   8    
HELIX    7  A5 LEU A  149  ALA A  165  1                                  17    
HELIX    8  A6 HIS A  184  MET A  194  1                                  11    
HELIX    9  A7 THR A  215  TYR A  218  5                                   4    
HELIX   10  A8 ASN A  220  LEU A  224  5                                   5    
SHEET    1  S1 7 PRO A  73  PHE A  76  0                                        
SHEET    2  S1 7 THR A  33  GLY A  42  1  N  ALA A  40   O  TYR A  74           
SHEET    3  S1 7 TRP A 111  GLU A 115  1  N  LEU A 113   O  ALA A  34           
SHEET    4  S1 7 SER A   1  GLY A   8  1  N  TYR A   4   O  VAL A 112           
SHEET    5  S1 7 VAL A 141  GLY A 146  1  N  ILE A 142   O  PHE A   5           
SHEET    6  S1 7 LEU A 169  ASN A 175  1  N  VAL A 173   O  LEU A 143           
SHEET    7  S1 7 LEU A 199  ILE A 203  1  N  ILE A 203   O  ALA A 174           
CRYST1   73.200   49.200   61.800  90.00 107.10  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      0.013661  0.000000  0.004203        0.00000                         
SCALE2      0.000000  0.020325  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016930        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       10-JUL-12   4G11              
TITLE     X-RAY STRUCTURE OF PI3K-GAMMA BOUND TO A 4-(MORPHOLIN-4-YL)- (6-OXO-1,
TITLE    2 6-DIHYDROPYRIMIDIN-2-YL)AMIDE INHIBITOR                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3 SUBUNIT GAMMA ISOFORM;                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 144-1102;                                     
COMPND   6 SYNONYM: PI3-KINASE SUBUNIT GAMMA, PI3K-GAMMA, PI3KGAMMA, PTDINS-3-  
COMPND   7 KINASE SUBUNIT GAMMA, PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE 
COMPND   8 110 KDA CATALYTIC SUBUNIT GAMMA, PTDINS-3-KINASE SUBUNIT P110-GAMMA, 
COMPND   9 P110GAMMA, PHOSPHOINOSITIDE-3-KINASE CATALYTIC GAMMA POLYPEPTIDE,    
COMPND  10 SERINE/THREONINE PROTEIN KINASE PIK3CG, P120-PI3K;                   
COMPND  11 EC: 2.7.1.153, 2.7.11.1;                                             
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PIK3CG;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: BACULOVIRUS                               
KEYWDS    PHOSPHOINOSITIDE 3-KINASE GAMMA, SECONDARY MESSENGER GENERATION,      
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.MORALES                                                             
REVDAT   1   14-NOV-12 4G11    0                                                
JRNL        AUTH   V.CERTAL,F.HALLEY,A.VIRONE-ODDOS,F.THOMPSON,B.FILOCHE-ROMME, 
JRNL        AUTH 2 Y.EL-AHMAD,J.C.CARRY,C.DELORME,A.KARLSSON,P.Y.ABECASSIS,     
JRNL        AUTH 3 L.VINCENT,H.BONNEVAUX,J.P.NICOLAS,R.MORALES,N.MICHOT,I.VADE, 
JRNL        AUTH 4 A.LOUBOUTIN,S.PERRON,G.DOERFLINGER,B.TRIC,S.MONGET,          
JRNL        AUTH 5 C.LENGAUER,L.SCHIO                                           
JRNL        TITL   PREPARATION AND OPTIMIZATION OF NEW                          
JRNL        TITL 2 4-(MORPHOLIN-4-YL)-(6-OXO-1,6-DIHYDROPYRIMIDIN-2-YL)AMIDE    
JRNL        TITL 3 DERIVATIVES AS PI3K BETA INHIBITORS                          
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  22  6381 2012              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   22981333                                                     
JRNL        DOI    10.1016/J.BMCL.2012.08.072                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 61.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 11709                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.285                           
REMARK   3   R VALUE            (WORKING SET) : 0.282                           
REMARK   3   FREE R VALUE                     : 0.349                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 609                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 843                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 48                           
REMARK   3   BIN FREE R VALUE                    : 0.4050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6778                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.23000                                             
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : -0.07000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.36000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.955         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.841         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 54.406        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.872                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.769                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6943 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9389 ; 0.800 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   827 ; 3.272 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   327 ;28.302 ;24.281       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1259 ;14.624 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;11.265 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1053 ; 0.048 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5170 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4G11 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073602.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.972400                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROCESS                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12318                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1E8Y                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG3350, 0.2M NA MALONATE, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       70.31500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.69000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       70.31500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.69000            
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: 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 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     LYS A   254                                                      
REMARK 465     LYS A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     SER A   257                                                      
REMARK 465     LEU A   258                                                      
REMARK 465     MET A   259                                                      
REMARK 465     ASP A   260                                                      
REMARK 465     ILE A   261                                                      
REMARK 465     PRO A   262                                                      
REMARK 465     GLU A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     GLN A   265                                                      
REMARK 465     SER A   266                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     TRP A   323                                                      
REMARK 465     PRO A   324                                                      
REMARK 465     LEU A   325                                                      
REMARK 465     VAL A   326                                                      
REMARK 465     ASP A   327                                                      
REMARK 465     ASP A   328                                                      
REMARK 465     CYS A   329                                                      
REMARK 465     THR A   330                                                      
REMARK 465     GLY A   331                                                      
REMARK 465     VAL A   332                                                      
REMARK 465     THR A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     TYR A   335                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     GLN A   338                                                      
REMARK 465     LEU A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     ILE A   341                                                      
REMARK 465     HIS A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     ASP A   345                                                      
REMARK 465     HIS A   346                                                      
REMARK 465     GLU A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     VAL A   349                                                      
REMARK 465     PHE A   350                                                      
REMARK 465     THR A   351                                                      
REMARK 465     VAL A   352                                                      
REMARK 465     SER A   353                                                      
REMARK 465     LEU A   354                                                      
REMARK 465     TRP A   355                                                      
REMARK 465     ASP A   356                                                      
REMARK 465     GLY A   436                                                      
REMARK 465     LYS A   437                                                      
REMARK 465     ALA A   438                                                      
REMARK 465     PRO A   439                                                      
REMARK 465     ALA A   440                                                      
REMARK 465     LEU A   441                                                      
REMARK 465     SER A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     LYS A   444                                                      
REMARK 465     ALA A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     ALA A   447                                                      
REMARK 465     GLU A   448                                                      
REMARK 465     SER A   449                                                      
REMARK 465     PRO A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     SER A   452                                                      
REMARK 465     GLU A   453                                                      
REMARK 465     SER A   454                                                      
REMARK 465     LYS A   455                                                      
REMARK 465     GLY A   456                                                      
REMARK 465     LYS A   457                                                      
REMARK 465     VAL A   458                                                      
REMARK 465     GLN A   459                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     GLY A   491                                                      
REMARK 465     GLU A   492                                                      
REMARK 465     ASP A   493                                                      
REMARK 465     GLN A   494                                                      
REMARK 465     GLY A   495                                                      
REMARK 465     SER A   496                                                      
REMARK 465     TYR A   523                                                      
REMARK 465     CYS A   524                                                      
REMARK 465     LEU A   529                                                      
REMARK 465     PRO A   530                                                      
REMARK 465     LYS A   531                                                      
REMARK 465     HIS A   532                                                      
REMARK 465     GLN A   533                                                      
REMARK 465     PRO A   534                                                      
REMARK 465     THR A   535                                                      
REMARK 465     PRO A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     PRO A   538                                                      
REMARK 465     GLU A   539                                                      
REMARK 465     GLY A   540                                                      
REMARK 465     ASP A   541                                                      
REMARK 465     ARG A   542                                                      
REMARK 465     VAL A   543                                                      
REMARK 465     ALA A   901                                                      
REMARK 465     ILE A   968                                                      
REMARK 465     LEU A   969                                                      
REMARK 465     GLY A   970                                                      
REMARK 465     ASN A   971                                                      
REMARK 465     TYR A   972                                                      
REMARK 465     LYS A   973                                                      
REMARK 465     SER A   974                                                      
REMARK 465     PHE A   975                                                      
REMARK 465     LEU A   976                                                      
REMARK 465     GLY A   977                                                      
REMARK 465     ILE A   978                                                      
REMARK 465     ASN A   979                                                      
REMARK 465     LYS A   980                                                      
REMARK 465     HIS A  1089                                                      
REMARK 465     LEU A  1090                                                      
REMARK 465     VAL A  1091                                                      
REMARK 465     LEU A  1092                                                      
REMARK 465     GLY A  1093                                                      
REMARK 465     ILE A  1094                                                      
REMARK 465     LYS A  1095                                                      
REMARK 465     GLN A  1096                                                      
REMARK 465     GLY A  1097                                                      
REMARK 465     GLU A  1098                                                      
REMARK 465     LYS A  1099                                                      
REMARK 465     HIS A  1100                                                      
REMARK 465     SER A  1101                                                      
REMARK 465     ALA A  1102                                                      
REMARK 465     HIS A  1103                                                      
REMARK 465     HIS A  1104                                                      
REMARK 465     HIS A  1105                                                      
REMARK 465     HIS A  1106                                                      
REMARK 465     HIS A  1107                                                      
REMARK 465     HIS A  1108                                                      
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     MET A 143    CG   SD   CE                                        
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     MET A  804   CB   CG   SD   CE                                   
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    ALA A 216       32.22    -91.75                                   
REMARK 500    ASN A 217       -4.61   -147.92                                   
REMARK 500    ARG A 226       59.97   -159.65                                   
REMARK 500    SER A 227      -93.30     76.99                                   
REMARK 500    PRO A 237       26.14    -60.68                                   
REMARK 500    ASP A 238       42.18   -150.17                                   
REMARK 500    PHE A 248      -51.53   -135.41                                   
REMARK 500    MET A 252      -70.44   -101.51                                   
REMARK 500    ARG A 375     -151.11   -144.63                                   
REMARK 500    ASN A 376     -110.02    -78.99                                   
REMARK 500    GLN A 391      -27.51     68.42                                   
REMARK 500    PHE A 473       -1.73     70.26                                   
REMARK 500    ASP A 521       84.97   -160.24                                   
REMARK 500    ALA A 545       84.45     54.22                                   
REMARK 500    PHE A 578       50.04   -107.60                                   
REMARK 500    ARG A 613       54.02   -109.42                                   
REMARK 500    ASP A 758      -55.97   -158.97                                   
REMARK 500    VAL A 759      100.16     56.95                                   
REMARK 500    ASN A 776     -134.19    -74.15                                   
REMARK 500    SER A 777       30.69    -86.89                                   
REMARK 500    PRO A 810     -167.17   -102.05                                   
REMARK 500    VAL A 896     -146.88    -99.05                                   
REMARK 500    ASP A 964       81.22     49.40                                   
REMARK 500    LEU A 987       64.72   -153.18                                   
REMARK 500    LYS A1000       91.64     57.71                                   
REMARK 500    LYS A1001     -139.72   -154.28                                   
REMARK 500    PRO A1040     -135.60    -70.40                                   
REMARK 500    LYS A1045      -63.66   -128.51                                   
REMARK 500    THR A1056       55.94     35.86                                   
REMARK 500    TRP A1086       80.77    -60.74                                   
REMARK 500    PHE A1087      -33.50   -147.81                                   
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 0W7 A 1201                
DBREF  4G11 A  144  1102  UNP    P48736   PK3CG_HUMAN    144   1102             
SEQADV 4G11 MET A  143  UNP  P48736              EXPRESSION TAG                 
SEQADV 4G11 HIS A 1103  UNP  P48736              EXPRESSION TAG                 
SEQADV 4G11 HIS A 1104  UNP  P48736              EXPRESSION TAG                 
SEQADV 4G11 HIS A 1105  UNP  P48736              EXPRESSION TAG                 
SEQADV 4G11 HIS A 1106  UNP  P48736              EXPRESSION TAG                 
SEQADV 4G11 HIS A 1107  UNP  P48736              EXPRESSION TAG                 
SEQADV 4G11 HIS A 1108  UNP  P48736              EXPRESSION TAG                 
SEQRES   1 A  966  MET SER GLU GLU SER GLN ALA PHE GLN ARG GLN LEU THR          
SEQRES   2 A  966  ALA LEU ILE GLY TYR ASP VAL THR ASP VAL SER ASN VAL          
SEQRES   3 A  966  HIS ASP ASP GLU LEU GLU PHE THR ARG ARG GLY LEU VAL          
SEQRES   4 A  966  THR PRO ARG MET ALA GLU VAL ALA SER ARG ASP PRO LYS          
SEQRES   5 A  966  LEU TYR ALA MET HIS PRO TRP VAL THR SER LYS PRO LEU          
SEQRES   6 A  966  PRO GLU TYR LEU TRP LYS LYS ILE ALA ASN ASN CYS ILE          
SEQRES   7 A  966  PHE ILE VAL ILE HIS ARG SER THR THR SER GLN THR ILE          
SEQRES   8 A  966  LYS VAL SER PRO ASP ASP THR PRO GLY ALA ILE LEU GLN          
SEQRES   9 A  966  SER PHE PHE THR LYS MET ALA LYS LYS LYS SER LEU MET          
SEQRES  10 A  966  ASP ILE PRO GLU SER GLN SER GLU GLN ASP PHE VAL LEU          
SEQRES  11 A  966  ARG VAL CYS GLY ARG ASP GLU TYR LEU VAL GLY GLU THR          
SEQRES  12 A  966  PRO ILE LYS ASN PHE GLN TRP VAL ARG HIS CYS LEU LYS          
SEQRES  13 A  966  ASN GLY GLU GLU ILE HIS VAL VAL LEU ASP THR PRO PRO          
SEQRES  14 A  966  ASP PRO ALA LEU ASP GLU VAL ARG LYS GLU GLU TRP PRO          
SEQRES  15 A  966  LEU VAL ASP ASP CYS THR GLY VAL THR GLY TYR HIS GLU          
SEQRES  16 A  966  GLN LEU THR ILE HIS GLY LYS ASP HIS GLU SER VAL PHE          
SEQRES  17 A  966  THR VAL SER LEU TRP ASP CYS ASP ARG LYS PHE ARG VAL          
SEQRES  18 A  966  LYS ILE ARG GLY ILE ASP ILE PRO VAL LEU PRO ARG ASN          
SEQRES  19 A  966  THR ASP LEU THR VAL PHE VAL GLU ALA ASN ILE GLN HIS          
SEQRES  20 A  966  GLY GLN GLN VAL LEU CYS GLN ARG ARG THR SER PRO LYS          
SEQRES  21 A  966  PRO PHE THR GLU GLU VAL LEU TRP ASN VAL TRP LEU GLU          
SEQRES  22 A  966  PHE SER ILE LYS ILE LYS ASP LEU PRO LYS GLY ALA LEU          
SEQRES  23 A  966  LEU ASN LEU GLN ILE TYR CYS GLY LYS ALA PRO ALA LEU          
SEQRES  24 A  966  SER SER LYS ALA SER ALA GLU SER PRO SER SER GLU SER          
SEQRES  25 A  966  LYS GLY LYS VAL GLN LEU LEU TYR TYR VAL ASN LEU LEU          
SEQRES  26 A  966  LEU ILE ASP HIS ARG PHE LEU LEU ARG ARG GLY GLU TYR          
SEQRES  27 A  966  VAL LEU HIS MET TRP GLN ILE SER GLY LYS GLY GLU ASP          
SEQRES  28 A  966  GLN GLY SER PHE ASN ALA ASP LYS LEU THR SER ALA THR          
SEQRES  29 A  966  ASN PRO ASP LYS GLU ASN SER MET SER ILE SER ILE LEU          
SEQRES  30 A  966  LEU ASP ASN TYR CYS HIS PRO ILE ALA LEU PRO LYS HIS          
SEQRES  31 A  966  GLN PRO THR PRO ASP PRO GLU GLY ASP ARG VAL ARG ALA          
SEQRES  32 A  966  GLU MET PRO ASN GLN LEU ARG LYS GLN LEU GLU ALA ILE          
SEQRES  33 A  966  ILE ALA THR ASP PRO LEU ASN PRO LEU THR ALA GLU ASP          
SEQRES  34 A  966  LYS GLU LEU LEU TRP HIS PHE ARG TYR GLU SER LEU LYS          
SEQRES  35 A  966  HIS PRO LYS ALA TYR PRO LYS LEU PHE SER SER VAL LYS          
SEQRES  36 A  966  TRP GLY GLN GLN GLU ILE VAL ALA LYS THR TYR GLN LEU          
SEQRES  37 A  966  LEU ALA ARG ARG GLU VAL TRP ASP GLN SER ALA LEU ASP          
SEQRES  38 A  966  VAL GLY LEU THR MET GLN LEU LEU ASP CYS ASN PHE SER          
SEQRES  39 A  966  ASP GLU ASN VAL ARG ALA ILE ALA VAL GLN LYS LEU GLU          
SEQRES  40 A  966  SER LEU GLU ASP ASP ASP VAL LEU HIS TYR LEU LEU GLN          
SEQRES  41 A  966  LEU VAL GLN ALA VAL LYS PHE GLU PRO TYR HIS ASP SER          
SEQRES  42 A  966  ALA LEU ALA ARG PHE LEU LEU LYS ARG GLY LEU ARG ASN          
SEQRES  43 A  966  LYS ARG ILE GLY HIS PHE LEU PHE TRP PHE LEU ARG SER          
SEQRES  44 A  966  GLU ILE ALA GLN SER ARG HIS TYR GLN GLN ARG PHE ALA          
SEQRES  45 A  966  VAL ILE LEU GLU ALA TYR LEU ARG GLY CYS GLY THR ALA          
SEQRES  46 A  966  MET LEU HIS ASP PHE THR GLN GLN VAL GLN VAL ILE GLU          
SEQRES  47 A  966  MET LEU GLN LYS VAL THR LEU ASP ILE LYS SER LEU SER          
SEQRES  48 A  966  ALA GLU LYS TYR ASP VAL SER SER GLN VAL ILE SER GLN          
SEQRES  49 A  966  LEU LYS GLN LYS LEU GLU ASN LEU GLN ASN SER GLN LEU          
SEQRES  50 A  966  PRO GLU SER PHE ARG VAL PRO TYR ASP PRO GLY LEU LYS          
SEQRES  51 A  966  ALA GLY ALA LEU ALA ILE GLU LYS CYS LYS VAL MET ALA          
SEQRES  52 A  966  SER LYS LYS LYS PRO LEU TRP LEU GLU PHE LYS CYS ALA          
SEQRES  53 A  966  ASP PRO THR ALA LEU SER ASN GLU THR ILE GLY ILE ILE          
SEQRES  54 A  966  PHE LYS HIS GLY ASP ASP LEU ARG GLN ASP MET LEU ILE          
SEQRES  55 A  966  LEU GLN ILE LEU ARG ILE MET GLU SER ILE TRP GLU THR          
SEQRES  56 A  966  GLU SER LEU ASP LEU CYS LEU LEU PRO TYR GLY CYS ILE          
SEQRES  57 A  966  SER THR GLY ASP LYS ILE GLY MET ILE GLU ILE VAL LYS          
SEQRES  58 A  966  ASP ALA THR THR ILE ALA LYS ILE GLN GLN SER THR VAL          
SEQRES  59 A  966  GLY ASN THR GLY ALA PHE LYS ASP GLU VAL LEU ASN HIS          
SEQRES  60 A  966  TRP LEU LYS GLU LYS SER PRO THR GLU GLU LYS PHE GLN          
SEQRES  61 A  966  ALA ALA VAL GLU ARG PHE VAL TYR SER CYS ALA GLY TYR          
SEQRES  62 A  966  CYS VAL ALA THR PHE VAL LEU GLY ILE GLY ASP ARG HIS          
SEQRES  63 A  966  ASN ASP ASN ILE MET ILE THR GLU THR GLY ASN LEU PHE          
SEQRES  64 A  966  HIS ILE ASP PHE GLY HIS ILE LEU GLY ASN TYR LYS SER          
SEQRES  65 A  966  PHE LEU GLY ILE ASN LYS GLU ARG VAL PRO PHE VAL LEU          
SEQRES  66 A  966  THR PRO ASP PHE LEU PHE VAL MET GLY THR SER GLY LYS          
SEQRES  67 A  966  LYS THR SER PRO HIS PHE GLN LYS PHE GLN ASP ILE CYS          
SEQRES  68 A  966  VAL LYS ALA TYR LEU ALA LEU ARG HIS HIS THR ASN LEU          
SEQRES  69 A  966  LEU ILE ILE LEU PHE SER MET MET LEU MET THR GLY MET          
SEQRES  70 A  966  PRO GLN LEU THR SER LYS GLU ASP ILE GLU TYR ILE ARG          
SEQRES  71 A  966  ASP ALA LEU THR VAL GLY LYS ASN GLU GLU ASP ALA LYS          
SEQRES  72 A  966  LYS TYR PHE LEU ASP GLN ILE GLU VAL CYS ARG ASP LYS          
SEQRES  73 A  966  GLY TRP THR VAL GLN PHE ASN TRP PHE LEU HIS LEU VAL          
SEQRES  74 A  966  LEU GLY ILE LYS GLN GLY GLU LYS HIS SER ALA HIS HIS          
SEQRES  75 A  966  HIS HIS HIS HIS                                              
HET    0W7  A1201      23                                                       
HETNAM     0W7 2-[4-(MORPHOLIN-4-YL)-6-OXO-1,6-DIHYDROPYRIMIDIN-2-YL]-          
HETNAM   2 0W7  N-PHENYLACETAMIDE                                               
FORMUL   2  0W7    C16 H18 N4 O3                                                
HELIX    1   1 SER A  144  GLY A  159  1                                  16    
HELIX    2   2 ASP A  171  LEU A  180  1                                  10    
HELIX    3   3 LEU A  180  ALA A  189  1                                  10    
HELIX    4   4 ASP A  192  HIS A  199  1                                   8    
HELIX    5   5 PRO A  208  LYS A  213  1                                   6    
HELIX    6   6 THR A  240  THR A  250  1                                  11    
HELIX    7   7 PRO A  286  ASN A  289  5                                   4    
HELIX    8   8 PHE A  290  GLY A  300  1                                  11    
HELIX    9   9 ASP A  312  GLU A  317  5                                   6    
HELIX   10  10 ASN A  498  LEU A  502  5                                   5    
HELIX   11  11 PRO A  548  THR A  561  1                                  14    
HELIX   12  12 THR A  568  PHE A  578  1                                  11    
HELIX   13  13 PHE A  578  LYS A  584  1                                   7    
HELIX   14  14 HIS A  585  LYS A  587  5                                   3    
HELIX   15  15 ALA A  588  SER A  594  1                                   7    
HELIX   16  16 GLN A  600  ALA A  612  1                                  13    
HELIX   17  17 ARG A  614  SER A  620  1                                   7    
HELIX   18  18 ASP A  623  LEU A  630  1                                   8    
HELIX   19  19 ASP A  637  GLU A  649  1                                  13    
HELIX   20  20 GLU A  652  ALA A  666  1                                  15    
HELIX   21  21 VAL A  667  GLU A  670  5                                   4    
HELIX   22  22 SER A  675  ASN A  688  1                                  14    
HELIX   23  23 ASN A  688  SER A  706  1                                  19    
HELIX   24  24 TYR A  709  ARG A  722  1                                  14    
HELIX   25  25 GLY A  725  LEU A  752  1                                  28    
HELIX   26  26 SER A  760  GLN A  775  1                                  16    
HELIX   27  27 ILE A  798  CYS A  801  5                                   4    
HELIX   28  28 ASP A  837  GLU A  858  1                                  22    
HELIX   29  29 ILE A  888  VAL A  896  1                                   9    
HELIX   30  30 GLU A  905  SER A  915  1                                  11    
HELIX   31  31 THR A  917  LEU A  942  1                                  26    
HELIX   32  32 HIS A  948  ASP A  950  5                                   3    
HELIX   33  33 THR A  988  GLY A  996  1                                   9    
HELIX   34  34 SER A 1003  HIS A 1022  1                                  20    
HELIX   35  35 HIS A 1023  GLY A 1038  1                                  16    
HELIX   36  36 LYS A 1045  LEU A 1055  1                                  11    
HELIX   37  37 ASN A 1060  GLY A 1079  1                                  20    
HELIX   38  38 TRP A 1080  TRP A 1086  1                                   7    
SHEET    1   A 4 THR A 229  VAL A 235  0                                        
SHEET    2   A 4 ILE A 220  ARG A 226 -1  N  ILE A 220   O  VAL A 235           
SHEET    3   A 4 ILE A 303  ASP A 308  1  O  VAL A 305   N  HIS A 225           
SHEET    4   A 4 VAL A 271  VAL A 274 -1  N  VAL A 271   O  ASP A 308           
SHEET    1   B 3 VAL A 393  ARG A 398  0                                        
SHEET    2   B 3 THR A 380  GLN A 388 -1  N  ILE A 387   O  LEU A 394           
SHEET    3   B 3 LYS A 402  PRO A 403 -1  O  LYS A 402   N  VAL A 381           
SHEET    1   C 8 VAL A 393  ARG A 398  0                                        
SHEET    2   C 8 THR A 380  GLN A 388 -1  N  ILE A 387   O  LEU A 394           
SHEET    3   C 8 LEU A 428  TYR A 434 -1  O  GLN A 432   N  GLU A 384           
SHEET    4   C 8 TYR A 462  LEU A 467 -1  O  LEU A 466   N  LEU A 429           
SHEET    5   C 8 GLY A 478  GLN A 486 -1  O  TRP A 485   N  TYR A 463           
SHEET    6   C 8 MET A 514  LEU A 520 -1  O  MET A 514   N  MET A 484           
SHEET    7   C 8 LYS A 360  ASP A 369 -1  N  ASP A 369   O  SER A 515           
SHEET    8   C 8 GLU A 407  LYS A 419 -1  O  VAL A 408   N  ILE A 368           
SHEET    1   D 6 PHE A 783  VAL A 785  0                                        
SHEET    2   D 6 ASP A 788  LEU A 796 -1  O  ALA A 793   N  PHE A 783           
SHEET    3   D 6 LEU A 811  CYS A 817 -1  O  LYS A 816   N  ALA A 795           
SHEET    4   D 6 ILE A 828  HIS A 834 -1  O  ILE A 830   N  LEU A 813           
SHEET    5   D 6 ILE A 876  GLU A 880 -1  O  ILE A 879   N  ILE A 831           
SHEET    6   D 6 CYS A 869  SER A 871 -1  N  ILE A 870   O  MET A 878           
SHEET    1   E 3 ALA A 885  THR A 887  0                                        
SHEET    2   E 3 ILE A 952  THR A 955 -1  O  ILE A 954   N  THR A 886           
SHEET    3   E 3 LEU A 960  HIS A 962 -1  O  PHE A 961   N  MET A 953           
SITE     1 AC1 10 MET A 804  PRO A 810  TRP A 812  LYS A 833                    
SITE     2 AC1 10 GLU A 880  ILE A 881  VAL A 882  MET A 953                    
SITE     3 AC1 10 ILE A 963  ASP A 964                                          
CRYST1  140.630   67.380  105.890  90.00  96.14  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      0.007111  0.000000  0.000765        0.00000                         
SCALE2      0.000000  0.014841  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009498        0.00000                         
(ATOM LINES ARE NOT SHOWN.)

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