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Database: PDB
Entry: 2OKK
LinkDB: 2OKK
Original site: 2OKK 
HEADER    LYASE                                   17-JAN-07   2OKK              
TITLE     THE X-RAY CRYSTAL STRUCTURE OF THE 65KDA ISOFORM OF GLUTAMIC ACID     
TITLE    2 DECARBOXYLASE (GAD65)                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE DECARBOXYLASE 2;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 88-584;                                           
COMPND   5 SYNONYM: GLUTAMATE DECARBOXYLASE 65 KDA ISOFORM, GAD-65, 65 KDA      
COMPND   6 GLUTAMIC ACID DECARBOXYLASE;                                         
COMPND   7 EC: 4.1.1.15;                                                        
COMPND   8 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: GAD2, GAD65;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: YRD-15;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PRJ                                       
KEYWDS    PLP-DEPENDENT DECARBOXYLASE, LYASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.BUCKLE,G.FENALTI,R.H.P.LAW,J.C.WHISSTOCK                          
REVDAT   5   13-JUL-11 2OKK    1       VERSN                                    
REVDAT   4   22-SEP-09 2OKK    1       HETATM                                   
REVDAT   3   24-FEB-09 2OKK    1       VERSN                                    
REVDAT   2   24-APR-07 2OKK    1       JRNL                                     
REVDAT   1   27-MAR-07 2OKK    0                                                
JRNL        AUTH   G.FENALTI,R.H.LAW,A.M.BUCKLE,C.LANGENDORF,K.TUCK,C.J.ROSADO, 
JRNL        AUTH 2 N.G.FAUX,K.MAHMOOD,C.S.HAMPE,J.P.BANGA,M.WILCE,              
JRNL        AUTH 3 J.SCHMIDBERGER,J.ROSSJOHN,O.EL-KABBANI,R.N.PIKE,A.I.SMITH,   
JRNL        AUTH 4 I.R.MACKAY,M.J.ROWLEY,J.C.WHISSTOCK                          
JRNL        TITL   GABA PRODUCTION BY GLUTAMIC ACID DECARBOXYLASE IS REGULATED  
JRNL        TITL 2 BY A DYNAMIC CATALYTIC LOOP.                                 
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  14   280 2007              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   17384644                                                     
JRNL        DOI    10.1038/NSMB1228                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 20648                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1077                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1389                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.85                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.3540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3770                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 92                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.32000                                             
REMARK   3    B22 (A**2) : 0.94000                                              
REMARK   3    B33 (A**2) : 0.37000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.454         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.269         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.203         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.110        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3877 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5246 ; 1.352 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   480 ; 5.799 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   156 ;37.868 ;24.038       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   658 ;17.640 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;17.402 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   578 ; 0.129 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2879 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1811 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2611 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   165 ; 0.143 ; 0.200       
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):   111 ; 0.174 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.117 ; 0.200       
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):  2463 ; 1.021 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3849 ; 1.908 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1629 ; 3.756 ; 7.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1397 ; 5.202 ;10.000       
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 : BABINET MODEL WITH 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 2OKK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041251.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20717                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.190                             
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2OKJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% ETHANOL, 100  MM MES, 10 MM 2-       
REMARK 280  MERCAPTOETHANOL, 20 MM CACL2, PH 6.2, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       60.00450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.00450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       39.12550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.52850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       39.12550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.52850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       60.00450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       39.12550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.52850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       60.00450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       39.12550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       49.52850            
REMARK 290   SMTRY3   8  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 300 REMARK: THE BIOLOGICAL UNIT (DIMER) IS GENERATED BY APPLYING         
REMARK 300 CRYSTALLOGRAPHIC SYMMETRY.                                           
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: 13330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.0 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      -60.00450            
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 596  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     ALA A   423                                                      
REMARK 465     SER A   424                                                      
REMARK 465     TYR A   425                                                      
REMARK 465     LEU A   426                                                      
REMARK 465     PHE A   427                                                      
REMARK 465     GLN A   428                                                      
REMARK 465     GLN A   429                                                      
REMARK 465     ASP A   430                                                      
REMARK 465     LYS A   431                                                      
REMARK 465     HIS A   432                                                      
REMARK 465     TYR A   433                                                      
REMARK 465     ASP A   518                                                      
REMARK 465     ASN A   519                                                      
REMARK 465     GLU A   520                                                      
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     PHE A  91    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 102    CG   OD1  OD2                                       
REMARK 470     ARG A 105    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 120    OE1  NE2                                            
REMARK 470     LYS A 124    CD   CE   NZ                                        
REMARK 470     ASN A 139    CG   OD1                                            
REMARK 470     ASP A 151    OD1  OD2                                            
REMARK 470     GLN A 152    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 303    CD   CE   NZ                                        
REMARK 470     ARG A 307    CZ   NH1  NH2                                       
REMARK 470     HIS A 422    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 435    CG   CD1  CD2                                       
REMARK 470     SER A 436    OG                                                  
REMARK 470     TYR A 437    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 460    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 473    CD   CE   NZ                                        
REMARK 470     GLU A 476    CD   OE1  OE2                                       
REMARK 470     THR A 515    OG1  CG2                                            
REMARK 470     GLU A 517    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 521    CD   OE1  OE2                                       
REMARK 470     ARG A 522    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 523    CG   SD   CE                                        
REMARK 470     ARG A 536    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP A 584    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 201       66.24     38.81                                   
REMARK 500    ALA A 336       79.64   -101.84                                   
REMARK 500    VAL A 340      -71.00    -94.98                                   
REMARK 500    LLP A 396      -94.81    -84.58                                   
REMARK 500    GLN A 403       80.21     75.74                                   
REMARK 500    THR A 439      -37.44     94.84                                   
REMARK 500    CYS A 446      -86.28   -106.93                                   
REMARK 500    HIS A 501      139.38    111.29                                   
REMARK 500    SER A 512       32.31    -90.40                                   
REMARK 500    LEU A 513      -15.01   -152.87                                   
REMARK 500    ASN A 555      110.41    -29.57                                   
REMARK 500    SER A 562       -4.31   -150.92                                   
REMARK 500    GLN A 583       81.06   -153.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A  500     HIS A  501                  -36.58                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE A 205        22.1      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 403        24.0      L          L   OUTSIDE RANGE           
REMARK 500    THR A 439        23.7      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 500        19.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 501         7.0      L          L   EXPECTING SP3           
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 ABU A 585                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ABU A 586                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 587                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OKJ   RELATED DB: PDB                                   
DBREF  2OKK A   88   584  UNP    Q05329   DCE2_HUMAN      88    584             
SEQRES   1 A  497  ASN TYR ALA PHE LEU HIS ALA THR ASP LEU LEU PRO ALA          
SEQRES   2 A  497  CYS ASP GLY GLU ARG PRO THR LEU ALA PHE LEU GLN ASP          
SEQRES   3 A  497  VAL MET ASN ILE LEU LEU GLN TYR VAL VAL LYS SER PHE          
SEQRES   4 A  497  ASP ARG SER THR LYS VAL ILE ASP PHE HIS TYR PRO ASN          
SEQRES   5 A  497  GLU LEU LEU GLN GLU TYR ASN TRP GLU LEU ALA ASP GLN          
SEQRES   6 A  497  PRO GLN ASN LEU GLU GLU ILE LEU MET HIS CYS GLN THR          
SEQRES   7 A  497  THR LEU LYS TYR ALA ILE LYS THR GLY HIS PRO ARG TYR          
SEQRES   8 A  497  PHE ASN GLN LEU SER THR GLY LEU ASP MET VAL GLY LEU          
SEQRES   9 A  497  ALA ALA ASP TRP LEU THR SER THR ALA ASN THR ASN MET          
SEQRES  10 A  497  PHE THR TYR GLU ILE ALA PRO VAL PHE VAL LEU LEU GLU          
SEQRES  11 A  497  TYR VAL THR LEU LYS LYS MET ARG GLU ILE ILE GLY TRP          
SEQRES  12 A  497  PRO GLY GLY SER GLY ASP GLY ILE PHE SER PRO GLY GLY          
SEQRES  13 A  497  ALA ILE SER ASN MET TYR ALA MET MET ILE ALA ARG PHE          
SEQRES  14 A  497  LYS MET PHE PRO GLU VAL LYS GLU LYS GLY MET ALA ALA          
SEQRES  15 A  497  LEU PRO ARG LEU ILE ALA PHE THR SER GLU HIS SER HIS          
SEQRES  16 A  497  PHE SER LEU LYS LYS GLY ALA ALA ALA LEU GLY ILE GLY          
SEQRES  17 A  497  THR ASP SER VAL ILE LEU ILE LYS CYS ASP GLU ARG GLY          
SEQRES  18 A  497  LYS MET ILE PRO SER ASP LEU GLU ARG ARG ILE LEU GLU          
SEQRES  19 A  497  ALA LYS GLN LYS GLY PHE VAL PRO PHE LEU VAL SER ALA          
SEQRES  20 A  497  THR ALA GLY THR THR VAL TYR GLY ALA PHE ASP PRO LEU          
SEQRES  21 A  497  LEU ALA VAL ALA ASP ILE CYS LYS LYS TYR LYS ILE TRP          
SEQRES  22 A  497  MET HIS VAL ASP ALA ALA TRP GLY GLY GLY LEU LEU MET          
SEQRES  23 A  497  SER ARG LYS HIS LYS TRP LYS LEU SER GLY VAL GLU ARG          
SEQRES  24 A  497  ALA ASN SER VAL THR TRP ASN PRO HIS LLP MET MET GLY          
SEQRES  25 A  497  VAL PRO LEU GLN CYS SER ALA LEU LEU VAL ARG GLU GLU          
SEQRES  26 A  497  GLY LEU MET GLN ASN CYS ASN GLN MET HIS ALA SER TYR          
SEQRES  27 A  497  LEU PHE GLN GLN ASP LYS HIS TYR ASP LEU SER TYR ASP          
SEQRES  28 A  497  THR GLY ASP LYS ALA LEU GLN CYS GLY ARG HIS VAL ASP          
SEQRES  29 A  497  VAL PHE LYS LEU TRP LEU MET TRP ARG ALA LYS GLY THR          
SEQRES  30 A  497  THR GLY PHE GLU ALA HIS VAL ASP LYS CYS LEU GLU LEU          
SEQRES  31 A  497  ALA GLU TYR LEU TYR ASN ILE ILE LYS ASN ARG GLU GLY          
SEQRES  32 A  497  TYR GLU MET VAL PHE ASP GLY LYS PRO GLN HIS THR ASN          
SEQRES  33 A  497  VAL CYS PHE TRP TYR ILE PRO PRO SER LEU ARG THR LEU          
SEQRES  34 A  497  GLU ASP ASN GLU GLU ARG MET SER ARG LEU SER LYS VAL          
SEQRES  35 A  497  ALA PRO VAL ILE LYS ALA ARG MET MET GLU TYR GLY THR          
SEQRES  36 A  497  THR MET VAL SER TYR GLN PRO LEU GLY ASP LYS VAL ASN          
SEQRES  37 A  497  PHE PHE ARG MET VAL ILE SER ASN PRO ALA ALA THR HIS          
SEQRES  38 A  497  GLN ASP ILE ASP PHE LEU ILE GLU GLU ILE GLU ARG LEU          
SEQRES  39 A  497  GLY GLN ASP                                                  
MODRES 2OKK LLP A  396  LYS                                                     
HET    LLP  A 396      24                                                       
HET    ABU  A 585       7                                                       
HET    ABU  A 586       7                                                       
HET    GOL  A 587       6                                                       
HETNAM     LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-                
HETNAM   2 LLP  PYRIDIN-4-YLMETHANE)                                            
HETNAM     ABU GAMMA-AMINO-BUTANOIC ACID                                        
HETNAM     GOL GLYCEROL                                                         
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
HETSYN     ABU GAMMA(AMINO)-BUTYRIC ACID                                        
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  LLP    C14 H24 N3 O7 P                                              
FORMUL   2  ABU    2(C4 H9 N O2)                                                
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  HOH   *92(H2 O)                                                     
HELIX    1   1 ASN A   88  LEU A   92  5                                   5    
HELIX    2   2 HIS A   93  LEU A   97  5                                   5    
HELIX    3   3 GLY A  103  ASP A  127  1                                  25    
HELIX    4   4 TYR A  137  TYR A  145  1                                   9    
HELIX    5   5 ASN A  155  ALA A  170  1                                  16    
HELIX    6   6 ASP A  187  ASN A  201  1                                  15    
HELIX    7   7 ALA A  210  GLY A  229  1                                  20    
HELIX    8   8 TRP A  230  SER A  234  5                                   5    
HELIX    9   9 GLY A  242  PHE A  259  1                                  18    
HELIX   10  10 GLU A  261  GLY A  266  1                                   6    
HELIX   11  11 MET A  267  LEU A  270  5                                   4    
HELIX   12  12 PHE A  283  LEU A  292  1                                  10    
HELIX   13  13 GLY A  295  ASP A  297  5                                   3    
HELIX   14  14 ILE A  311  LYS A  325  1                                  15    
HELIX   15  15 PRO A  346  LYS A  358  1                                  13    
HELIX   16  16 TRP A  367  SER A  374  5                                   8    
HELIX   17  17 HIS A  377  SER A  382  5                                   6    
HELIX   18  18 GLY A  383  ALA A  387  5                                   5    
HELIX   19  19 GLY A  413  GLN A  420  1                                   8    
HELIX   20  20 ASP A  434  ASP A  438  5                                   5    
HELIX   21  21 THR A  439  ALA A  443  5                                   5    
HELIX   22  22 ASP A  451  ASN A  487  1                                  37    
HELIX   23  23 ARG A  522  SER A  527  1                                   6    
HELIX   24  24 LYS A  528  GLY A  541  1                                  14    
HELIX   25  25 THR A  567  GLY A  582  1                                  16    
SHEET    1   A 5 TYR A 178  PHE A 179  0                                        
SHEET    2   A 5 MET A 544  LEU A 550  1  O  MET A 544   N  PHE A 179           
SHEET    3   A 5 LYS A 553  MET A 559 -1  O  ARG A 558   N  SER A 546           
SHEET    4   A 5 VAL A 504  TYR A 508 -1  N  VAL A 504   O  MET A 559           
SHEET    5   A 5 TYR A 491  MET A 493 -1  N  GLU A 492   O  TRP A 507           
SHEET    1   B 7 ASP A 236  SER A 240  0                                        
SHEET    2   B 7 SER A 405  VAL A 409 -1  O  VAL A 409   N  ASP A 236           
SHEET    3   B 7 SER A 389  TRP A 392 -1  N  VAL A 390   O  LEU A 408           
SHEET    4   B 7 TRP A 360  ALA A 365  1  N  VAL A 363   O  THR A 391           
SHEET    5   B 7 VAL A 328  THR A 335  1  N  ALA A 334   O  ASP A 364           
SHEET    6   B 7 LEU A 273  SER A 278  1  N  PHE A 276   O  SER A 333           
SHEET    7   B 7 VAL A 299  ILE A 302  1  O  ILE A 302   N  THR A 277           
LINK         C   HIS A 395                 N   LLP A 396     1555   1555  1.33  
LINK         C   LLP A 396                 N   MET A 397     1555   1555  1.33  
CISPEP   1 LEU A   98    PRO A   99          0        11.19                     
CISPEP   2 ASP A  438    THR A  439          0         5.41                     
CISPEP   3 GLN A  583    ASP A  584          0         1.45                     
SITE     1 AC1  6 GLN A 181  LEU A 182  SER A 183  PHE A 205                    
SITE     2 AC1  6 THR A 339  ARG A 558                                          
SITE     1 AC2  8 GLN A 181  LEU A 182  SER A 183  ASN A 203                    
SITE     2 AC2  8 HIS A 282  LLP A 396  CYS A 446  HOH A 661                    
SITE     1 AC3  5 GLU A 279  SER A 281  HIS A 282  PHE A 283                    
SITE     2 AC3  5 LYS A 286                                                     
CRYST1   78.251   99.057  120.009  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012779  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010095  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008333        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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