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Database: PDB
Entry: 2GZH
LinkDB: 2GZH
Original site: 2GZH 
HEADER    PROTEIN TRANSPORT                       11-MAY-06   2GZH              
TITLE     CRYSTAL STRUCTURE OF RAB11 IN COMPLEX WITH RAB11-FAMILY               
TITLE    2 INTERACTING PROTEIN 2                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED PROTEIN RAB-11A;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: G PROTEIN DOMAIN;                                          
COMPND   5 SYNONYM: RAB-11, YL8;                                                
COMPND   6 EC: 3.6.5.2;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RAB11-FIP2 LONG ISOFORM;                                   
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: RAB11-FIP2 RAB-BINDING DOMAIN;                             
COMPND  13 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: RAB11A;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-28B;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PMAL-C2X                                  
KEYWDS    RAS-LIKE G PROTEIN FOLD, A-HELICAL COILED COIL, PROTEIN               
KEYWDS   2 TRANSPORT                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.R.KHAN                                                              
REVDAT   3   24-FEB-09 2GZH    1       VERSN                                    
REVDAT   2   29-AUG-06 2GZH    1       JRNL                                     
REVDAT   1   15-AUG-06 2GZH    0                                                
JRNL        AUTH   W.N.JAGOE,A.J.LINDSAY,R.J.READ,A.J.MCCOY,                    
JRNL        AUTH 2 M.W.MCCAFFREY,A.R.KHAN                                       
JRNL        TITL   CRYSTAL STRUCTURE OF RAB11 IN COMPLEX WITH RAB11             
JRNL        TITL 2 FAMILY INTERACTING PROTEIN 2.                                
JRNL        REF    STRUCTURE                     V.  14  1273 2006              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   16905101                                                     
JRNL        DOI    10.1016/J.STR.2006.06.010                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.47 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 9719                           
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 492                             
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) : 2.47                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 684                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2220                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 43                           
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1809                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 125                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.15000                                              
REMARK   3    B22 (A**2) : 0.15000                                              
REMARK   3    B33 (A**2) : -0.22000                                             
REMARK   3    B12 (A**2) : 0.07000                                              
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): 0.541         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.290         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.204         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.799         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1889 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2555 ; 1.977 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   224 ; 7.096 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    91 ;31.526 ;23.297       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   332 ;18.903 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;21.656 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   290 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1393 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   921 ; 0.256 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1273 ; 0.317 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   160 ; 0.181 ; 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):    92 ; 0.224 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.192 ; 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):  1152 ; 1.213 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1806 ; 2.146 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   843 ; 2.830 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   749 ; 4.631 ; 4.500       
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2GZH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB037739.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98175                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADSC                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10234                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.470                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 16.000                             
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.29700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 15.900                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM PHOSPHATE BUFFER,               
REMARK 280  APPROXIMATELY 0.3M CONCENTRATION, PH 5, VAPOR DIFFUSION,            
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.46667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       74.93333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       74.93333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       37.46667            
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 SECOND PART OF THE BIOLOGICAL UNIT IS GENERATED BY       
REMARK 300 THE CRYSTALLOGRAPHIC 2-FOLD AXIS, TRANSFORMATION (1,-1,-1).          
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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       74.93333            
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     GLY A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     GLY B   406                                                      
REMARK 465     ALA B   407                                                      
REMARK 465     MET B   408                                                      
REMARK 465     ALA B   409                                                      
REMARK 465     ALA B   410                                                      
REMARK 465     LYS B   411                                                      
REMARK 465     PHE B   412                                                      
REMARK 465     ARG B   413                                                      
REMARK 465     ALA B   414                                                      
REMARK 465     SER B   415                                                      
REMARK 465     ASN B   416                                                      
REMARK 465     ILE B   417                                                      
REMARK 465     MET B   418                                                      
REMARK 465     PRO B   419                                                      
REMARK 465     SER B   420                                                      
REMARK 465     SER B   421                                                      
REMARK 465     SER B   422                                                      
REMARK 465     PHE B   423                                                      
REMARK 465     HIS B   424                                                      
REMARK 465     MET B   425                                                      
REMARK 465     SER B   426                                                      
REMARK 465     PRO B   427                                                      
REMARK 465     THR B   428                                                      
REMARK 465     SER B   429                                                      
REMARK 465     ASN B   430                                                      
REMARK 465     GLU B   431                                                      
REMARK 465     ASP B   432                                                      
REMARK 465     LEU B   433                                                      
REMARK 465     ARG B   434                                                      
REMARK 465     LYS B   435                                                      
REMARK 465     ILE B   436                                                      
REMARK 465     PRO B   437                                                      
REMARK 465     ASP B   438                                                      
REMARK 465     SER B   439                                                      
REMARK 465     ASN B   440                                                      
REMARK 465     PRO B   441                                                      
REMARK 465     PHE B   442                                                      
REMARK 465     ASP B   443                                                      
REMARK 465     ALA B   444                                                      
REMARK 465     THR B   445                                                      
REMARK 465     ALA B   446                                                      
REMARK 465     ARG B   504                                                      
REMARK 465     LYS B   505                                                      
REMARK 465     ALA B   506                                                      
REMARK 465     GLY B   507                                                      
REMARK 465     LYS B   508                                                      
REMARK 465     PHE B   509                                                      
REMARK 465     SER B   510                                                      
REMARK 465     ASN B   511                                                      
REMARK 465     SER B   512                                                      
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     TYR A 173    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER B 450    CB   OG                                             
REMARK 470     LEU B 451    CB   CG   CD1  CD2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CA   GLU A     7     O    HOH A   659              0.00            
REMARK 500   NH1  ARG A   140     OE1  GLU A   144              1.43            
REMARK 500   N    GLU A     7     O    HOH A   659              1.49            
REMARK 500   C    GLU A     7     O    HOH A   659              1.53            
REMARK 500   CB   GLU A     7     O    HOH A   659              1.55            
REMARK 500   CE   LYS A    41     O    HOH A   548              2.17            
REMARK 500   O    HOH A   576     O    HOH A   629              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 475   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A   7      171.15     71.55                                   
REMARK 500    TYR A   8      161.57    164.39                                   
REMARK 500    ASP A  56     -135.21     56.90                                   
REMARK 500    ARG A  72      -77.87    -81.59                                   
REMARK 500    ASP A 114      143.54    -39.29                                   
REMARK 500    LYS A 125       39.91     70.70                                   
REMARK 500    LEU A 128       55.15    -90.85                                   
REMARK 500    SER A 158       -9.38     92.37                                   
REMARK 500    ASN A 160       -0.50     67.60                                   
REMARK 500    ARG B 449     -115.56    -65.86                                   
REMARK 500    SER B 450      -56.13     64.35                                   
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 950  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  25   OG                                                     
REMARK 620 2 THR A  43   OG1  68.8                                              
REMARK 620 3 GTP A 900   O2B  89.4 153.0                                        
REMARK 620 4 GTP A 900   O2G 153.7  93.9 100.1                                  
REMARK 620 5 HOH A 658   O    98.7  98.4 100.5 103.5                            
REMARK 620 6 HOH A 655   O    80.2  80.4  80.4  77.3 178.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 951  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 648   O                                                      
REMARK 620 2 HOH A 657   O   164.5                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 901                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 950                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 951                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 900                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2GZD   RELATED DB: PDB                                   
REMARK 900 SAME COMPLEX IN ORTHORHOMBIC SPACE GROUP                             
DBREF  2GZH A    2   173  UNP    P62491   RB11A_HUMAN      1    172             
DBREF  2GZH B  410   512  UNP    Q7L804   RFIP2_HUMAN    410    512             
SEQADV 2GZH MET A    1  UNP  P62491              CLONING ARTIFACT               
SEQADV 2GZH LEU A   70  UNP  P62491    GLN    69 ENGINEERED                     
SEQADV 2GZH MSE A  120  UNP  P62491    MET   119 MODIFIED RESIDUE               
SEQADV 2GZH GLY B  406  UNP  Q7L804              CLONING ARTIFACT               
SEQADV 2GZH ALA B  407  UNP  Q7L804              CLONING ARTIFACT               
SEQADV 2GZH MET B  408  UNP  Q7L804              CLONING ARTIFACT               
SEQADV 2GZH ALA B  409  UNP  Q7L804              CLONING ARTIFACT               
SEQADV 2GZH MSE B  489  UNP  Q7L804    MET   489 MODIFIED RESIDUE               
SEQRES   1 A  173  MET GLY THR ARG ASP ASP GLU TYR ASP TYR LEU PHE LYS          
SEQRES   2 A  173  VAL VAL LEU ILE GLY ASP SER GLY VAL GLY LYS SER ASN          
SEQRES   3 A  173  LEU LEU SER ARG PHE THR ARG ASN GLU PHE ASN LEU GLU          
SEQRES   4 A  173  SER LYS SER THR ILE GLY VAL GLU PHE ALA THR ARG SER          
SEQRES   5 A  173  ILE GLN VAL ASP GLY LYS THR ILE LYS ALA GLN ILE TRP          
SEQRES   6 A  173  ASP THR ALA GLY LEU GLU ARG TYR ARG ALA ILE THR SER          
SEQRES   7 A  173  ALA TYR TYR ARG GLY ALA VAL GLY ALA LEU LEU VAL TYR          
SEQRES   8 A  173  ASP ILE ALA LYS HIS LEU THR TYR GLU ASN VAL GLU ARG          
SEQRES   9 A  173  TRP LEU LYS GLU LEU ARG ASP HIS ALA ASP SER ASN ILE          
SEQRES  10 A  173  VAL ILE MSE LEU VAL GLY ASN LYS SER ASP LEU ARG HIS          
SEQRES  11 A  173  LEU ARG ALA VAL PRO THR ASP GLU ALA ARG ALA PHE ALA          
SEQRES  12 A  173  GLU LYS ASN GLY LEU SER PHE ILE GLU THR SER ALA LEU          
SEQRES  13 A  173  ASP SER THR ASN VAL GLU ALA ALA PHE GLN THR ILE LEU          
SEQRES  14 A  173  THR GLU ILE TYR                                              
SEQRES   1 B  107  GLY ALA MET ALA ALA LYS PHE ARG ALA SER ASN ILE MET          
SEQRES   2 B  107  PRO SER SER SER PHE HIS MET SER PRO THR SER ASN GLU          
SEQRES   3 B  107  ASP LEU ARG LYS ILE PRO ASP SER ASN PRO PHE ASP ALA          
SEQRES   4 B  107  THR ALA GLY TYR ARG SER LEU THR TYR GLU GLU VAL LEU          
SEQRES   5 B  107  GLN GLU LEU VAL LYS HIS LYS GLU LEU LEU ARG ARG LYS          
SEQRES   6 B  107  ASP THR HIS ILE ARG GLU LEU GLU ASP TYR ILE ASP ASN          
SEQRES   7 B  107  LEU LEU VAL ARG VAL MSE GLU GLU THR PRO SER ILE LEU          
SEQRES   8 B  107  ARG VAL PRO TYR GLU PRO SER ARG LYS ALA GLY LYS PHE          
SEQRES   9 B  107  SER ASN SER                                                  
MODRES 2GZH MSE A  120  MET  SELENOMETHIONINE                                   
MODRES 2GZH MSE B  489  MET  SELENOMETHIONINE                                   
HET    MSE  A 120       8                                                       
HET    MSE  B 489       8                                                       
HET    PO4  A 901       5                                                       
HET     MG  A 950       1                                                       
HET     MG  A 951       1                                                       
HET    GTP  A 900      32                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
FORMUL   1  MSE    2(C5 H11 N O2 SE)                                            
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  GTP    C10 H16 N5 O14 P3                                            
FORMUL   7  HOH   *125(H2 O)                                                    
HELIX    1   1 GLY A   23  ASN A   34  1                                  12    
HELIX    2   2 ILE A   76  ARG A   82  1                                   7    
HELIX    3   3 LYS A   95  ASN A  101  1                                   7    
HELIX    4   4 ASN A  101  ALA A  113  1                                  13    
HELIX    5   5 LEU A  128  ARG A  132  5                                   5    
HELIX    6   6 PRO A  135  ASN A  146  1                                  12    
HELIX    7   7 ASN A  160  GLU A  171  1                                  12    
HELIX    8   8 THR B  452  THR B  492  1                                  41    
HELIX    9   9 PRO B  493  ARG B  497  5                                   5    
SHEET    1   A 6 VAL A  46  VAL A  55  0                                        
SHEET    2   A 6 LYS A  58  THR A  67 -1  O  ALA A  62   N  ARG A  51           
SHEET    3   A 6 TYR A  10  ILE A  17  1  N  PHE A  12   O  GLN A  63           
SHEET    4   A 6 GLY A  86  ASP A  92  1  O  VAL A  90   N  ILE A  17           
SHEET    5   A 6 VAL A 118  ASN A 124  1  O  MSE A 120   N  LEU A  89           
SHEET    6   A 6 SER A 149  GLU A 152  1  O  SER A 149   N  LEU A 121           
LINK        MG    MG A 950                 OG  SER A  25     1555   1555  2.18  
LINK        MG    MG A 950                 OG1 THR A  43     1555   1555  2.18  
LINK        MG    MG A 950                 O2B GTP A 900     1555   1555  2.16  
LINK        MG    MG A 950                 O2G GTP A 900     1555   1555  2.18  
LINK         C   ILE A 119                 N   MSE A 120     1555   1555  1.32  
LINK         C   MSE A 120                 N   LEU A 121     1555   1555  1.33  
LINK        MG    MG A 950                 O   HOH A 658     1555   1555  2.10  
LINK        MG    MG A 950                 O   HOH A 655     1555   1555  2.23  
LINK        MG    MG A 951                 O   HOH A 648     1555   1555  2.90  
LINK        MG    MG A 951                 O   HOH A 657     1555   1555  2.10  
LINK         C   VAL B 488                 N   MSE B 489     1555   1555  1.32  
LINK         C   MSE B 489                 N   GLU B 490     1555   1555  1.32  
CISPEP   1 VAL B  498    PRO B  499          0        16.72                     
SITE     1 AC1  7 THR A 167  THR A 170  HOH A 604  LYS B 470                    
SITE     2 AC1  7 ASP B 471  ILE B 474  ARG B 475                               
SITE     1 AC2  5 SER A  25  THR A  43  HOH A 655  HOH A 658                    
SITE     2 AC2  5 GTP A 900                                                     
SITE     1 AC3  3 GLU A 108  HOH A 648  HOH A 657                               
SITE     1 AC4 27 SER A  20  GLY A  21  VAL A  22  GLY A  23                    
SITE     2 AC4 27 LYS A  24  SER A  25  ASN A  26  PHE A  36                    
SITE     3 AC4 27 ASN A  37  LEU A  38  SER A  40  SER A  42                    
SITE     4 AC4 27 THR A  43  GLY A  69  ASN A 124  LYS A 125                    
SITE     5 AC4 27 ASP A 127  LEU A 128  SER A 154  ALA A 155                    
SITE     6 AC4 27 LEU A 156  HOH A 565  HOH A 606  HOH A 611                    
SITE     7 AC4 27 HOH A 655  HOH A 658   MG A 950                               
CRYST1   64.740   64.740  112.400  90.00  90.00 120.00 P 31 2 1      6          
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      0.015446  0.008918  0.000000        0.00000                         
SCALE2      0.000000  0.017836  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008897        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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