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Database: PDB
Entry: 2HEI
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Original site: 2HEI 
HEADER    TRANSPORT PROTEIN                       21-JUN-06   2HEI              
TITLE     CRYSTAL STRUCTURE OF HUMAN RAB5B IN COMPLEX WITH GDP                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED PROTEIN RAB-5B;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 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: RAB5B;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS (DE-3)-RIL;                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P28A-LIC                                  
KEYWDS    G-PROTEIN, RAB, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM,  
KEYWDS   2 SGC, TRANSPORT PROTEIN                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.HONG,L.SHEN,J.WANG,W.TEMPEL,R.LANDRY,C.H.ARROWSMITH,A.M.EDWARDS,    
AUTHOR   2 M.SUNDSTROM,J.WEIGELT,A.BOCHKAREV,H.PARK,STRUCTURAL GENOMICS         
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   4   30-AUG-23 2HEI    1       REMARK SEQADV                            
REVDAT   3   18-OCT-17 2HEI    1       REMARK                                   
REVDAT   2   24-FEB-09 2HEI    1       VERSN                                    
REVDAT   1   04-JUL-06 2HEI    0                                                
JRNL        AUTH   B.HONG,L.SHEN,J.WANG,W.TEMPEL,R.LANDRY,C.H.ARROWSMITH,       
JRNL        AUTH 2 A.M.EDWARDS,M.SUNDSTROM,J.WEIGELT,A.BOCHKAREV,H.PARK         
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN RAB5B IN COMPLEX WITH GDP         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC REFMAC_5.2.0019                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 45443                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN SHELLS                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.262                           
REMARK   3   FREE R VALUE                     : 0.294                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.327                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2875                            
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) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3331                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.85                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : 0.3420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2559                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 124                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.37500                                             
REMARK   3    B22 (A**2) : 0.51700                                              
REMARK   3    B33 (A**2) : -0.14300                                             
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): 0.123         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.119         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.075         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.000         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2690 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1770 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3649 ; 1.488 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4336 ; 1.139 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   328 ; 6.085 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   112 ;34.633 ;24.821       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   463 ;12.151 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;14.429 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   421 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2910 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   536 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   498 ; 0.210 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1876 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1282 ; 0.180 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1307 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   128 ; 0.131 ; 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):    26 ; 0.229 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    62 ; 0.269 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.106 ; 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):  1809 ; 2.432 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   664 ; 0.687 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2615 ; 2.907 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1205 ; 2.466 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1032 ; 3.232 ; 3.000       
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 BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2HEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000038255.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAY-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50161                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1N6I                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% P3350, 0.1M NAOAC, PH 4.5, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       20.65100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.75050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.18500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.75050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.65100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.18500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). ACCORDING TO AUTHORS, THE              
REMARK 300 BIOLOGICAL UNIT OF THE PROTEIN IS NOT KNOWN                          
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 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 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     GLY A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     LYS A    17                                                      
REMARK 465     ASP A    65                                                      
REMARK 465     ASP A    66                                                      
REMARK 465     THR A    67                                                      
REMARK 465     SER A   184                                                      
REMARK 465     GLU A   185                                                      
REMARK 465     PRO A   186                                                      
REMARK 465     GLN A   187                                                      
REMARK 465     ASN A   188                                                      
REMARK 465     LEU A   189                                                      
REMARK 465     GLY A   190                                                      
REMARK 465     GLY A   191                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     ASP B    65                                                      
REMARK 465     ASP B    66                                                      
REMARK 465     SER B   184                                                      
REMARK 465     GLU B   185                                                      
REMARK 465     PRO B   186                                                      
REMARK 465     GLN B   187                                                      
REMARK 465     ASN B   188                                                      
REMARK 465     LEU B   189                                                      
REMARK 465     GLY B   190                                                      
REMARK 465     GLY B   191                                                      
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  91    CZ   NH1  NH2                                       
REMARK 470     GLN A 105    CD   OE1  NE2                                       
REMARK 470     LYS A 180    CE   NZ                                             
REMARK 470     LYS B  17    CG   CD   CE   NZ                                   
REMARK 470     GLN B 105    CD   OE1  NE2                                       
REMARK 470     ARG B 120    NE   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    ALA A  30        7.58     83.25                                   
REMARK 500    ALA A 167       -3.83     82.36                                   
REMARK 500    ALA B  30        8.90     80.00                                   
REMARK 500    LEU B 137       47.99    -98.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1D A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1D B 302                 
DBREF  2HEI A   15   191  UNP    P61020   RAB5B_HUMAN     15    191             
DBREF  2HEI B   15   191  UNP    P61020   RAB5B_HUMAN     15    191             
SEQADV 2HEI GLY A   13  UNP  P61020              CLONING ARTIFACT               
SEQADV 2HEI SER A   14  UNP  P61020              CLONING ARTIFACT               
SEQADV 2HEI GLY B   13  UNP  P61020              CLONING ARTIFACT               
SEQADV 2HEI SER B   14  UNP  P61020              CLONING ARTIFACT               
SEQRES   1 A  179  GLY SER ALA SER LYS ILE CYS GLN PHE LYS LEU VAL LEU          
SEQRES   2 A  179  LEU GLY GLU SER ALA VAL GLY LYS SER SER LEU VAL LEU          
SEQRES   3 A  179  ARG PHE VAL LYS GLY GLN PHE HIS GLU TYR GLN GLU SER          
SEQRES   4 A  179  THR ILE GLY ALA ALA PHE LEU THR GLN SER VAL CYS LEU          
SEQRES   5 A  179  ASP ASP THR THR VAL LYS PHE GLU ILE TRP ASP THR ALA          
SEQRES   6 A  179  GLY GLN GLU ARG TYR HIS SER LEU ALA PRO MET TYR TYR          
SEQRES   7 A  179  ARG GLY ALA GLN ALA ALA ILE VAL VAL TYR ASP ILE THR          
SEQRES   8 A  179  ASN GLN GLU THR PHE ALA ARG ALA LYS THR TRP VAL LYS          
SEQRES   9 A  179  GLU LEU GLN ARG GLN ALA SER PRO SER ILE VAL ILE ALA          
SEQRES  10 A  179  LEU ALA GLY ASN LYS ALA ASP LEU ALA ASN LYS ARG MET          
SEQRES  11 A  179  VAL GLU TYR GLU GLU ALA GLN ALA TYR ALA ASP ASP ASN          
SEQRES  12 A  179  SER LEU LEU PHE MET GLU THR SER ALA LYS THR ALA MET          
SEQRES  13 A  179  ASN VAL ASN ASP LEU PHE LEU ALA ILE ALA LYS LYS LEU          
SEQRES  14 A  179  PRO LYS SER GLU PRO GLN ASN LEU GLY GLY                      
SEQRES   1 B  179  GLY SER ALA SER LYS ILE CYS GLN PHE LYS LEU VAL LEU          
SEQRES   2 B  179  LEU GLY GLU SER ALA VAL GLY LYS SER SER LEU VAL LEU          
SEQRES   3 B  179  ARG PHE VAL LYS GLY GLN PHE HIS GLU TYR GLN GLU SER          
SEQRES   4 B  179  THR ILE GLY ALA ALA PHE LEU THR GLN SER VAL CYS LEU          
SEQRES   5 B  179  ASP ASP THR THR VAL LYS PHE GLU ILE TRP ASP THR ALA          
SEQRES   6 B  179  GLY GLN GLU ARG TYR HIS SER LEU ALA PRO MET TYR TYR          
SEQRES   7 B  179  ARG GLY ALA GLN ALA ALA ILE VAL VAL TYR ASP ILE THR          
SEQRES   8 B  179  ASN GLN GLU THR PHE ALA ARG ALA LYS THR TRP VAL LYS          
SEQRES   9 B  179  GLU LEU GLN ARG GLN ALA SER PRO SER ILE VAL ILE ALA          
SEQRES  10 B  179  LEU ALA GLY ASN LYS ALA ASP LEU ALA ASN LYS ARG MET          
SEQRES  11 B  179  VAL GLU TYR GLU GLU ALA GLN ALA TYR ALA ASP ASP ASN          
SEQRES  12 B  179  SER LEU LEU PHE MET GLU THR SER ALA LYS THR ALA MET          
SEQRES  13 B  179  ASN VAL ASN ASP LEU PHE LEU ALA ILE ALA LYS LYS LEU          
SEQRES  14 B  179  PRO LYS SER GLU PRO GLN ASN LEU GLY GLY                      
HET    GDP  A 201      28                                                       
HET    D1D  A 202       8                                                       
HET    GDP  B 301      28                                                       
HET    D1D  B 302       8                                                       
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     D1D (4S,5S)-1,2-DITHIANE-4,5-DIOL                                    
FORMUL   3  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   4  D1D    2(C4 H8 O2 S2)                                               
FORMUL   7  HOH   *124(H2 O)                                                    
HELIX    1   1 GLY A   32  GLY A   43  1                                  12    
HELIX    2   2 TYR A   82  SER A   84  5                                   3    
HELIX    3   3 LEU A   85  ARG A   91  1                                   7    
HELIX    4   4 ASN A  104  ALA A  122  1                                  19    
HELIX    5   5 LYS A  134  ARG A  141  5                                   8    
HELIX    6   6 GLU A  144  ASN A  155  1                                  12    
HELIX    7   7 ASN A  169  LEU A  181  1                                  13    
HELIX    8   8 GLY B   32  GLY B   43  1                                  12    
HELIX    9   9 TYR B   82  SER B   84  5                                   3    
HELIX   10  10 LEU B   85  ARG B   91  1                                   7    
HELIX   11  11 ASN B  104  ALA B  122  1                                  19    
HELIX   12  12 LYS B  134  ARG B  141  5                                   8    
HELIX   13  13 GLU B  144  ASN B  155  1                                  12    
HELIX   14  14 ASN B  169  LEU B  181  1                                  13    
SHEET    1   A 6 LEU A  58  VAL A  62  0                                        
SHEET    2   A 6 VAL A  69  TRP A  74 -1  O  ILE A  73   N  LEU A  58           
SHEET    3   A 6 CYS A  19  LEU A  26  1  N  CYS A  19   O  LYS A  70           
SHEET    4   A 6 ALA A  95  ASP A 101  1  O  ILE A  97   N  LEU A  26           
SHEET    5   A 6 VAL A 127  ASN A 133  1  O  ALA A 129   N  VAL A  98           
SHEET    6   A 6 LEU A 158  GLU A 161  1  O  LEU A 158   N  LEU A 130           
SHEET    1   B 6 LEU B  58  VAL B  62  0                                        
SHEET    2   B 6 THR B  68  ASP B  75 -1  O  VAL B  69   N  VAL B  62           
SHEET    3   B 6 ILE B  18  LEU B  26  1  N  PHE B  21   O  LYS B  70           
SHEET    4   B 6 ALA B  95  ASP B 101  1  O  VAL B  99   N  LEU B  26           
SHEET    5   B 6 VAL B 127  ASN B 133  1  O  ASN B 133   N  TYR B 100           
SHEET    6   B 6 LEU B 158  GLU B 161  1  O  LEU B 158   N  LEU B 130           
SITE     1 AC1 22 ALA A  30  VAL A  31  GLY A  32  LYS A  33                    
SITE     2 AC1 22 SER A  34  SER A  35  PHE A  45  GLU A  47                    
SITE     3 AC1 22 TYR A  48  SER A  51  ALA A  77  ASN A 133                    
SITE     4 AC1 22 LYS A 134  ASP A 136  LEU A 137  SER A 163                    
SITE     5 AC1 22 ALA A 164  LYS A 165  HOH A 221  HOH A 223                    
SITE     6 AC1 22 HOH A 244  HOH A 266                                          
SITE     1 AC2  9 THR A  76  GLN A  79  GLU A  80  HIS A  83                    
SITE     2 AC2  9 ALA A  86  TYR A  89  TYR A  90  TRP A 114                    
SITE     3 AC2  9 GLU A 117                                                     
SITE     1 AC3 23 ALA B  30  VAL B  31  GLY B  32  LYS B  33                    
SITE     2 AC3 23 SER B  34  SER B  35  PHE B  45  GLU B  47                    
SITE     3 AC3 23 TYR B  48  SER B  51  ALA B  77  ASN B 133                    
SITE     4 AC3 23 LYS B 134  ASP B 136  LEU B 137  SER B 163                    
SITE     5 AC3 23 ALA B 164  LYS B 165  HOH B 310  HOH B 315                    
SITE     6 AC3 23 HOH B 338  HOH B 360  HOH B 361                               
SITE     1 AC4  8 THR B  76  GLN B  79  GLU B  80  HIS B  83                    
SITE     2 AC4  8 ALA B  86  TYR B  89  TRP B 114  GLU B 117                    
CRYST1   41.302   78.370   95.501  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024212  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012760  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010471        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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