GenomeNet

Database: PDB
Entry: 5A0F
LinkDB: 5A0F
Original site: 5A0F 
HEADER    SIGNALING PROTEIN                       20-APR-15   5A0F              
TITLE     CRYSTAL STRUCTURE OF YERSINIA AFP18-MODIFIED RHOA                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSFORMING PROTEIN RHOA;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-181;                                            
COMPND   5 SYNONYM: RAS-LIKE GTP-BINDING PROTEIN RHO, RHO CDNA CLONE 12, H12;   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: GLYCOSYLATION AT Y 34                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PGEX4T                                    
KEYWDS    SIGNALING PROTEIN, N-ACETYLGLUCOSAMINE-PROTEIN, TYROSINE              
KEYWDS   2 GLYCOSYLATION, GTPASE, BACTERIAL TOXIN EFFECTOR, TYPE 6 SECRETION    
KEYWDS   3 SYSTEM, ANTIFEEDING PROPHAGE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.JANK,M.SCHIMPL,D.M.VAN AALTEN                                       
REVDAT   5   13-MAR-19 5A0F    1       JRNL   REMARK LINK                       
REVDAT   4   13-DEC-17 5A0F    1       SOURCE AUTHOR JRNL                       
REVDAT   3   28-JUN-17 5A0F    1       REMARK                                   
REVDAT   2   29-JUL-15 5A0F    1       JRNL                                     
REVDAT   1   22-JUL-15 5A0F    0                                                
JRNL        AUTH   T.JANK,S.ECKERLE,M.STEINEMANN,C.TRILLHAASE,M.SCHIMPL,        
JRNL        AUTH 2 S.WIESE,D.M.VAN AALTEN,W.DRIEVER,K.AKTORIES                  
JRNL        TITL   TYROSINE GLYCOSYLATION OF RHO BY YERSINIA TOXIN IMPAIRS      
JRNL        TITL 2 BLASTOMERE CELL BEHAVIOUR IN ZEBRAFISH EMBRYOS.              
JRNL        REF    NAT COMMUN                    V.   6  7807 2015              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   26190758                                                     
JRNL        DOI    10.1038/NCOMMS8807                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 91.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 15937                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 866                             
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1133                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.52                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 62                           
REMARK   3   BIN FREE R VALUE                    : 0.2550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1399                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
REMARK   3   SOLVENT ATOMS            : 80                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.51000                                             
REMARK   3    B22 (A**2) : -0.51000                                             
REMARK   3    B33 (A**2) : 1.02000                                              
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): 0.164         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.134         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.912         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1476 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1391 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2007 ; 1.671 ; 2.015       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3214 ; 2.366 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   177 ; 5.258 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    65 ;38.105 ;24.769       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   254 ;12.846 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;21.436 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   225 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1617 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   306 ; 0.007 ; 0.020       
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):   711 ; 1.237 ; 1.788       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   710 ; 1.236 ; 1.788       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   887 ; 1.901 ; 2.673       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   764 ; 2.109 ; 2.117       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER 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   : 1.20                                          
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. U VALUES REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 5A0F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290063632.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU CCD                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31941                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
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 1DPF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 5 AND 1.5 M     
REMARK 280  AMMONIUM SULFATE; SITTING-DROP VAPOR-DIFFUSION AT 293.15 K,         
REMARK 280  VAPOR DIFFUSION, SITTING DROP                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
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   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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       28.31400            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       45.69600            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       45.69600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       42.47100            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       45.69600            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       45.69600            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       14.15700            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       45.69600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.69600            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       42.47100            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       45.69600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.69600            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       14.15700            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       28.31400            
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A   181                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  32    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 128    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 142    CG   CD   OE1  OE2                                  
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    TYR A  42   C     VAL A  43   N      -0.168                       
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    LYS A  98      -58.86   -124.91                                   
REMARK 500    LYS A 164       -8.91     81.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 N-ACETYL-D-GLUCOSAMINE (NAG): N-ACETYL-D-GLUCOSAMINE IS              
REMARK 600  COVALENTLY ATTACHED TO THE HYDROXYL GROUP OF TYROSINE 34            
REMARK 600  IN THE ALPHA CONFIGURATION.                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1181                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 2501                
DBREF  5A0F A    1   181  UNP    P61586   RHOA_HUMAN       1    181             
SEQRES   1 A  181  MET ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY ASP          
SEQRES   2 A  181  GLY ALA CYS GLY LYS THR CYS LEU LEU ILE VAL PHE SER          
SEQRES   3 A  181  LYS ASP GLN PHE PRO GLU VAL TYR VAL PRO THR VAL PHE          
SEQRES   4 A  181  GLU ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS GLN          
SEQRES   5 A  181  VAL GLU LEU ALA LEU TRP ASP THR ALA GLY GLN GLU ASP          
SEQRES   6 A  181  TYR ASP ARG LEU ARG PRO LEU SER TYR PRO ASP THR ASP          
SEQRES   7 A  181  VAL ILE LEU MET CYS PHE SER ILE ASP SER PRO ASP SER          
SEQRES   8 A  181  LEU GLU ASN ILE PRO GLU LYS TRP THR PRO GLU VAL LYS          
SEQRES   9 A  181  HIS PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY ASN          
SEQRES  10 A  181  LYS LYS ASP LEU ARG ASN ASP GLU HIS THR ARG ARG GLU          
SEQRES  11 A  181  LEU ALA LYS MET LYS GLN GLU PRO VAL LYS PRO GLU GLU          
SEQRES  12 A  181  GLY ARG ASP MET ALA ASN ARG ILE GLY ALA PHE GLY TYR          
SEQRES  13 A  181  MET GLU CYS SER ALA LYS THR LYS ASP GLY VAL ARG GLU          
SEQRES  14 A  181  VAL PHE GLU MET ALA THR ARG ALA ALA LEU GLN ALA              
HET    GDP  A 200      28                                                       
HET    SO4  A1181       5                                                       
HET    NDG  A2501      14                                                       
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
FORMUL   2  GDP    C10 H15 N5 O11 P2                                            
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  NDG    C8 H15 N O6                                                  
FORMUL   5  HOH   *80(H2 O)                                                     
HELIX    1   1 GLY A   17  ASP A   28  1                                  12    
HELIX    2   2 LEU A   69  TYR A   74  5                                   6    
HELIX    3   3 SER A   88  CYS A  107  1                                  20    
HELIX    4   4 LYS A  118  ARG A  122  5                                   5    
HELIX    5   5 ASP A  124  LYS A  133  1                                  10    
HELIX    6   6 LYS A  140  GLY A  152  1                                  13    
HELIX    7   7 GLY A  166  GLN A  180  1                                  15    
SHEET    1  AA 6 TYR A  42  VAL A  48  0                                        
SHEET    2  AA 6 LYS A  51  ASP A  59 -1  O  LYS A  51   N  VAL A  48           
SHEET    3  AA 6 ILE A   4  GLY A  12  1  O  ILE A   4   N  GLU A  54           
SHEET    4  AA 6 VAL A  79  SER A  85  1  O  VAL A  79   N  VAL A   9           
SHEET    5  AA 6 ILE A 112  ASN A 117  1  O  ILE A 113   N  MET A  82           
SHEET    6  AA 6 GLY A 155  GLU A 158  1  O  GLY A 155   N  LEU A 114           
LINK         OH  TYR A  34                 C1  NDG A2501     1555   1555  1.41  
CISPEP   1 PHE A   30    PRO A   31          0         0.43                     
SITE     1 AC1  6 LYS A  51  TYR A  66  ASP A  67  ARG A  68                    
SITE     2 AC1  6 LEU A  69  HOH A2041                                          
SITE     1 AC2 16 ALA A  15  CYS A  16  GLY A  17  LYS A  18                    
SITE     2 AC2 16 THR A  19  CYS A  20  ALA A  61  LYS A 118                    
SITE     3 AC2 16 ASP A 120  LEU A 121  SER A 160  ALA A 161                    
SITE     4 AC2 16 LYS A 162  HOH A2011  HOH A2036  HOH A2080                    
SITE     1 AC3 10 TYR A  34  VAL A  35  PRO A  36  THR A  37                    
SITE     2 AC3 10 GLU A  40  LEU A  69  SER A  73  HOH A2024                    
SITE     3 AC3 10 HOH A2025  HOH A2039                                          
CRYST1   91.392   91.392   56.628  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010942  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010942  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017659        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system