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Database: PDB
Entry: 3C5H
LinkDB: 3C5H
Original site: 3C5H 
HEADER    SIGNALING PROTEIN                       31-JAN-08   3C5H              
TITLE     CRYSTAL STRUCTURE OF THE RAS HOMOLOG DOMAIN OF HUMAN GRLF1            
TITLE    2 (P190RHOGAP)                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOCORTICOID RECEPTOR DNA-BINDING FACTOR 1;              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RAS HOMOLOG DOMAIN: RESIDUES 13-249;                       
COMPND   5 SYNONYM: GLUCOCORTICOID RECEPTOR REPRESSION FACTOR 1, GRF-           
COMPND   6 1, RHO GAP P190A, P190-A;                                            
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GRLF1, GRF1, KIAA1722;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    RAS, GTPASE, GLUCORTICOID RECEPTOR, STRUCTURAL GENOMICS               
KEYWDS   2 CONSORTIUM, SGC, ALTERNATIVE SPLICING, ANTI-ONCOGENE, CELL           
KEYWDS   3 CYCLE, CYTOPLASM, DNA-BINDING, GTPASE ACTIVATION, NUCLEUS,           
KEYWDS   4 PHOSPHOPROTEIN, REPRESSOR, TRANSCRIPTION, TRANSCRIPTION              
KEYWDS   5 REGULATION, SIGNALING PROTEIN                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.SHEN,Y.TONG,W.TEMPEL,F.MACKENZIE,C.H.ARROWSMITH,                    
AUTHOR   2 A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,A.BOCHKAREV,H.PARK,                  
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   2   24-FEB-09 3C5H    1       VERSN                                    
REVDAT   1   12-FEB-08 3C5H    0                                                
JRNL        AUTH   L.SHEN,Y.TONG,W.TEMPEL,F.MACKENZIE,C.H.ARROWSMITH,           
JRNL        AUTH 2 A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,A.BOCHKAREV,H.PARK           
JRNL        TITL   CRYSTAL STRUCTURE OF THE RAS HOMOLOG DOMAIN OF               
JRNL        TITL 2 HUMAN GRLF1 (P190RHOGAP).                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0037                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.26                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 26626                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1352                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1152                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 58.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 61                           
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1799                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 96                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : -0.03000                                             
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): 0.127         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.127         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.936         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1869 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1193 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2549 ; 1.465 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2938 ; 0.954 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   238 ; 6.285 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    81 ;33.331 ;25.309       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   306 ;11.656 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;25.159 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   298 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2076 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   364 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   352 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1235 ; 0.186 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   916 ; 0.173 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   915 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    94 ; 0.131 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.027 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     9 ; 0.284 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    18 ; 0.229 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.119 ; 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):  1291 ; 2.720 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   477 ; 0.702 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1876 ; 3.601 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   785 ; 2.861 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   668 ; 3.899 ; 3.000       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DUE TO CONSIDERABLE NON-ISOMORPHISM       
REMARK   3  BETWEEN THE PHASING AND REFINEMENT DATA SETS, A PRELIMINARY         
REMARK   3  MODEL OBTAINED BY THE PROGRAM 'RESOLVE' BASED ON THE PHASING        
REMARK   3  DATA WAS USED IN MOLECULAR REPLACEMENT WITH THE HIGHER              
REMARK   3  RESOLUTION REFINEMENT DATA AND THE PROGRAM 'PHASER'. FOLLOWING      
REMARK   3  DENSITY MODIFICATION WITH 'DM', 'ARP/WARP' WAS USED FOR             
REMARK   3  AUTOTRACING OF THE HIGHER RESOLUTION MODEL. HYDROGENS HAVE          
REMARK   3  BEEN ADDED IN THE RIDING POSITIONS DURING FINAL REFINEMENT.         
REMARK   3  PROGRAMS, ARP/WARP, COOT, MOLPROBITY HAVE ALSO BEEN USED IN         
REMARK   3  REFINEMENT                                                          
REMARK   4                                                                      
REMARK   4 3C5H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046365.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-NOV-07; 06-DEC-07               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; APS                           
REMARK 200  BEAMLINE                       : 23-ID-B; 19-ID                     
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97926; 0.97931, 0.97945,         
REMARK 200                                   0.98166, 0.97243                   
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD; ADSC         
REMARK 200                                   QUANTUM 315                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26661                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NATIVE CRYSTAL, USED FOR MODEL           
REMARK 280  REFINEMENT: 26% PEG 4000, 0.1M TRIS-HCL, 0.2M MAGNESIUM             
REMARK 280  CHLORIDE, 0.1MM DTT, PH 8.0, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 291K. SELENO-METHIONINE DERIVATIVE CRYSTAL, USED        
REMARK 280  FOR MAD PHASING: 33% PEG 4000, 0.1M TRIS-HCL, 0.2M MAGNESIUM        
REMARK 280  CHLORIDE, 0.1MM DTT, PH 9.0, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 291K. A TEN-FOLD EXCESS OF GPPNHP WAS ADDED TO THE      
REMARK 280  PROTEIN SAMPLES PRIOR TO CRYSTALLIZATION.                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
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   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2                                      
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  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  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       54.47950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.47950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       25.65950            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       54.47950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.47950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       25.65950            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       54.47950            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       54.47950            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       25.65950            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       54.47950            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       54.47950            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       25.65950            
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: AUTHORS STATE THAT THE BIOLOGICAL UNIT OF THIS PROTEIN       
REMARK 300 IS UNKNOWN.                                                          
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     ARG A    81                                                      
REMARK 465     SER A    82                                                      
REMARK 465     LEU A    83                                                      
REMARK 465     GLU A    84                                                      
REMARK 465     ASP A    85                                                      
REMARK 465     CYS A    86                                                      
REMARK 465     VAL A    87                                                      
REMARK 465     GLU A    88                                                      
REMARK 465     CYS A    89                                                      
REMARK 465     GLY A   169                                                      
REMARK 465     MET A   170                                                      
REMARK 465     ASN A   171                                                      
REMARK 465     ARG A   172                                                      
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     ARG A   5    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A   6    CD   OE1  OE2                                       
REMARK 470     GLU A  25    CD   OE1  OE2                                       
REMARK 470     LYS A  26    CG   CD   CE   NZ                                   
REMARK 470     GLN A  30    CG   CD   OE1  NE2                                  
REMARK 470     ASP A  48    CG   OD1  OD2                                       
REMARK 470     LYS A  90    CG   CD   CE   NZ                                   
REMARK 470     ARG A 109    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 124    CD   CE   NZ                                        
REMARK 470     GLN A 143    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 144    CG   OD1  OD2                                       
REMARK 470     LYS A 154    CE   NZ                                             
REMARK 470     LYS A 179    CG   CD   CE   NZ                                   
REMARK 470     GLU A 207    CD   OE1  OE2                                       
REMARK 470     ARG A 208    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 211    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 221    CG   CD   CE   NZ                                   
REMARK 470     ASN A 222    CG   OD1  ND2                                       
REMARK 470     ARG A 231    CZ   NH1  NH2                                       
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    THR A  97     -153.89   -139.63                                   
REMARK 500    LEU A 141       39.85   -149.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  36   OG                                                     
REMARK 620 2 GLU A  95   OE2  83.6                                              
REMARK 620 3 GNP A 301   O2G 175.4  91.8                                        
REMARK 620 4 HOH A 390   O    93.7  94.3  86.6                                  
REMARK 620 5 GNP A 301   O2B  95.8  95.4  84.7 167.2                            
REMARK 620 6 HOH A 389   O    92.1 174.9  92.5  88.6  82.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 328   O                                                      
REMARK 620 2 HOH A 337   O    86.7                                              
REMARK 620 3 HOH A 318   O    97.3  87.6                                        
REMARK 620 4 HOH A 314   O    82.6  89.2 176.8                                  
REMARK 620 5 HOH A 312   O    92.7 179.3  92.6  90.6                            
REMARK 620 6 HOH A 323   O   170.3  88.5  91.0  88.9  92.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 302                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 303                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 301                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 304                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 305                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 307                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 308                 
DBREF  3C5H A   13   249  UNP    Q9NRY4   GRLF1_HUMAN     13    249             
SEQADV 3C5H MET A   -5  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H HIS A   -4  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H HIS A   -3  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H HIS A   -2  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H HIS A   -1  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H HIS A    0  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H HIS A    1  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H SER A    2  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H SER A    3  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H GLY A    4  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H ARG A    5  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H GLU A    6  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H ASN A    7  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H LEU A    8  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H TYR A    9  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H PHE A   10  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H GLN A   11  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3C5H GLY A   12  UNP  Q9NRY4              EXPRESSION TAG                 
SEQRES   1 A  255  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 A  255  LEU TYR PHE GLN GLY THR TYR ASN ILE SER VAL VAL GLY          
SEQRES   3 A  255  LEU SER GLY THR GLU LYS GLU LYS GLY GLN CYS GLY ILE          
SEQRES   4 A  255  GLY LYS SER CYS LEU CYS ASN ARG PHE VAL ARG PRO SER          
SEQRES   5 A  255  ALA ASP GLU PHE HIS LEU ASP HIS THR SER VAL LEU SER          
SEQRES   6 A  255  THR SER ASP PHE GLY GLY ARG VAL VAL ASN ASN ASP HIS          
SEQRES   7 A  255  PHE LEU TYR TRP GLY GLU VAL SER ARG SER LEU GLU ASP          
SEQRES   8 A  255  CYS VAL GLU CYS LYS MET HIS ILE VAL GLU GLN THR GLU          
SEQRES   9 A  255  PHE ILE ASP ASP GLN THR PHE GLN PRO HIS ARG SER THR          
SEQRES  10 A  255  ALA LEU GLN PRO TYR ILE LYS ARG ALA ALA ALA THR LYS          
SEQRES  11 A  255  LEU ALA SER ALA GLU LYS LEU MET TYR PHE CYS THR ASP          
SEQRES  12 A  255  GLN LEU GLY LEU GLU GLN ASP PHE GLU GLN LYS GLN MET          
SEQRES  13 A  255  PRO ASP GLY LYS LEU LEU VAL ASP GLY PHE LEU LEU GLY          
SEQRES  14 A  255  ILE ASP VAL SER ARG GLY MET ASN ARG ASN PHE ASP ASP          
SEQRES  15 A  255  GLN LEU LYS PHE VAL SER ASN LEU TYR ASN GLN LEU ALA          
SEQRES  16 A  255  LYS THR LYS LYS PRO ILE VAL VAL VAL LEU THR LYS CYS          
SEQRES  17 A  255  ASP GLU GLY VAL GLU ARG TYR ILE ARG ASP ALA HIS THR          
SEQRES  18 A  255  PHE ALA LEU SER LYS LYS ASN LEU GLN VAL VAL GLU THR          
SEQRES  19 A  255  SER ALA ARG SER ASN VAL ASN VAL ASP LEU ALA PHE SER          
SEQRES  20 A  255  THR LEU VAL GLN LEU ILE ASP LYS                              
HET     MG  A 302       1                                                       
HET     MG  A 303       1                                                       
HET    GNP  A 301      32                                                       
HET    UNX  A 304       1                                                       
HET    UNX  A 305       1                                                       
HET    UNX  A 306       1                                                       
HET    UNX  A 307       1                                                       
HET    UNX  A 308       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   2   MG    2(MG 2+)                                                     
FORMUL   4  GNP    C10 H17 N6 O13 P3                                            
FORMUL   5  UNX    5(X)                                                         
FORMUL  10  HOH   *96(H2 O)                                                     
HELIX    1   1 GLY A   34  ARG A   44  1                                  11    
HELIX    2   2 SER A   59  GLY A   64  1                                   6    
HELIX    3   3 ARG A  109  LEU A  113  5                                   5    
HELIX    4   4 PRO A  115  ALA A  121  1                                   7    
HELIX    5   5 CYS A  135  LEU A  139  5                                   5    
HELIX    6   6 LEU A  141  PHE A  145  5                                   5    
HELIX    7   7 MET A  150  ASP A  152  5                                   3    
HELIX    8   8 ASN A  173  THR A  191  1                                  19    
HELIX    9   9 LYS A  201  GLY A  205  5                                   5    
HELIX   10  10 VAL A  206  SER A  219  1                                  14    
HELIX   11  11 ASN A  235  LYS A  249  1                                  15    
SHEET    1   A 6 PHE A  73  VAL A  79  0                                        
SHEET    2   A 6 MET A  91  GLN A  96 -1  O  ILE A  93   N  TRP A  76           
SHEET    3   A 6 TYR A  14  GLY A  20  1  N  VAL A  18   O  VAL A  94           
SHEET    4   A 6 GLY A 159  ASP A 165  1  O  GLY A 163   N  VAL A  19           
SHEET    5   A 6 ILE A 195  THR A 200  1  O  VAL A 196   N  LEU A 162           
SHEET    6   A 6 VAL A 225  GLU A 227  1  O  VAL A 226   N  VAL A 197           
SHEET    1   B 2 VAL A  57  LEU A  58  0                                        
SHEET    2   B 2 ILE A 100  ASP A 101  1  O  ILE A 100   N  LEU A  58           
SHEET    1   C 2 LYS A 124  ALA A 126  0                                        
SHEET    2   C 2 LYS A 154  LEU A 156 -1  O  LEU A 155   N  LEU A 125           
LINK         OG  SER A  36                MG    MG A 302     1555   1555  2.11  
LINK         OE2 GLU A  95                MG    MG A 302     1555   1555  2.16  
LINK        MG    MG A 302                 O2G GNP A 301     1555   1555  1.99  
LINK        MG    MG A 302                 O   HOH A 390     1555   1555  2.10  
LINK        MG    MG A 302                 O2B GNP A 301     1555   1555  2.09  
LINK        MG    MG A 302                 O   HOH A 389     1555   1555  2.16  
LINK        MG    MG A 303                 O   HOH A 328     1555   1555  2.11  
LINK        MG    MG A 303                 O   HOH A 337     1555   1555  2.19  
LINK        MG    MG A 303                 O   HOH A 318     1555   1555  1.97  
LINK        MG    MG A 303                 O   HOH A 314     1555   1555  1.96  
LINK        MG    MG A 303                 O   HOH A 312     1555   1555  2.12  
LINK        MG    MG A 303                 O   HOH A 323     1555   1555  2.16  
SITE     1 AC1  5 SER A  36  GLU A  95  GNP A 301  HOH A 389                    
SITE     2 AC1  5 HOH A 390                                                     
SITE     1 AC2  6 HOH A 312  HOH A 314  HOH A 318  HOH A 323                    
SITE     2 AC2  6 HOH A 328  HOH A 337                                          
SITE     1 AC3 26 LYS A  28  GLY A  32  ILE A  33  GLY A  34                    
SITE     2 AC3 26 LYS A  35  SER A  36  CYS A  37  LEU A  52                    
SITE     3 AC3 26 ASP A  53  SER A  56  GLU A  95  THR A  97                    
SITE     4 AC3 26 LYS A 201  ASP A 203  SER A 229  ALA A 230                    
SITE     5 AC3 26 ARG A 231   MG A 302  HOH A 311  HOH A 316                    
SITE     6 AC3 26 HOH A 319  HOH A 389  HOH A 390  HOH A 394                    
SITE     7 AC3 26 HOH A 395  HOH A 396                                          
SITE     1 AC4  2 TYR A 116  ILE A 117                                          
SITE     1 AC5  3 VAL A  43  ARG A  44  MET A 132                               
SITE     1 AC6  3 ASN A 235  ASP A 237  LEU A 238                               
SITE     1 AC7  2 PHE A  42  ASP A 237                                          
CRYST1  108.959  108.959   51.319  90.00  90.00  90.00 I 4           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      0.009178  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009178  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019486        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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