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Database: PDB
Entry: 3HTU
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Original site: 3HTU 
HEADER    PROTEIN TRANSPORT                       12-JUN-09   3HTU              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN VPS25-VPS20 SUBCOMPLEX                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VACUOLAR PROTEIN-SORTING-ASSOCIATED PROTEIN 25;            
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 FRAGMENT: THE C-TERMINAL WH2 DOMAIN OF VPS25: UNP RESIDUES           
COMPND   5 102-176;                                                             
COMPND   6 SYNONYM: HVPS25, ESCRT-II COMPLEX SUBUNIT VPS25, ELL-                
COMPND   7 ASSOCIATED PROTEIN OF 20 KDA, DERMAL PAPILLA-DERIVED                 
COMPND   8 PROTEIN 9;                                                           
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: VACUOLAR PROTEIN-SORTING-ASSOCIATED PROTEIN 20;            
COMPND  12 CHAIN: B, D, F, H;                                                   
COMPND  13 FRAGMENT: THE FIRST HELIX OF VPS20: UNP RESIDUES 11-48;              
COMPND  14 SYNONYM: CHROMATIN-MODIFYING PROTEIN 6, CHARGED                      
COMPND  15 MULTIVESICULAR BODY PROTEIN 6, VPS20, HVPS20;                        
COMPND  16 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: DERP9, EAP20, VPS25;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PST39;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CHMP6, VPS20;                                                  
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;                             
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PST39                                     
KEYWDS    ESCRT-II, ESCRT-III, VPS20, VPS25, MVB, CYTOPLASM, NUCLEUS,           
KEYWDS   2 POLYMORPHISM, PROTEIN TRANSPORT, TRANSCRIPTION,                      
KEYWDS   3 TRANSCRIPTION REGULATION, TRANSPORT, COILED COIL, ENDOSOME,          
KEYWDS   4 LIPOPROTEIN, MEMBRANE, MYRISTATE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.J.IM,J.H.HURLEY                                                     
REVDAT   1   25-AUG-09 3HTU    0                                                
JRNL        AUTH   Y.J.IM,T.WOLLERT,E.BOURA,J.H.HURLEY                          
JRNL        TITL   STRUCTURE AND FUNCTION OF THE ESCRT-II-III                   
JRNL        TITL 2 INTERFACE IN MULTIVESICULAR BODY BIOGENESIS.                 
JRNL        REF    DEV.CELL                      V.  17   234 2009              
JRNL        REFN                   ISSN 1534-5807                               
JRNL        PMID   19686684                                                     
JRNL        DOI    10.1016/J.DEVCEL.2009.07.008                                 
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 28995                          
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) : 0.240                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1544                            
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) : 1843                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 94                           
REMARK   3   BIN FREE R VALUE                    : 0.2920                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3657                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 213                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.66000                                             
REMARK   3    B22 (A**2) : 1.31000                                              
REMARK   3    B33 (A**2) : -0.65000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.05000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.204         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.970        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3709 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4974 ; 1.288 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   431 ; 5.747 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   223 ;40.134 ;24.350       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   719 ;19.808 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;12.225 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   523 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2865 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1715 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2474 ; 0.294 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   215 ; 0.152 ; 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):   121 ; 0.219 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    22 ; 0.179 ; 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):  2240 ; 1.193 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3472 ; 1.957 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1658 ; 2.538 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1502 ; 3.647 ; 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   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3HTU COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053574.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111) CHANNEL                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30553                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.1000                            
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     (%) : 87.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.28100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.030                              
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 3CUO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8.0, 35% PEG 4000,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       25.52150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7380 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.8 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7240 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.7 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6770 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.5 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7260 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -0.9 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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    98                                                      
REMARK 465     ALA A    99                                                      
REMARK 465     MET A   100                                                      
REMARK 465     GLY A   101                                                      
REMARK 465     ARG B    45                                                      
REMARK 465     ALA B    46                                                      
REMARK 465     LEU B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     GLY C    98                                                      
REMARK 465     ALA C    99                                                      
REMARK 465     MET C   100                                                      
REMARK 465     GLY C   101                                                      
REMARK 465     ALA D    46                                                      
REMARK 465     LEU D    47                                                      
REMARK 465     ALA D    48                                                      
REMARK 465     GLY E    98                                                      
REMARK 465     ALA E    99                                                      
REMARK 465     MET E   100                                                      
REMARK 465     GLY E   101                                                      
REMARK 465     GLU F    42                                                      
REMARK 465     ARG F    43                                                      
REMARK 465     GLU F    44                                                      
REMARK 465     ARG F    45                                                      
REMARK 465     ALA F    46                                                      
REMARK 465     LEU F    47                                                      
REMARK 465     ALA F    48                                                      
REMARK 465     GLY G    98                                                      
REMARK 465     ALA G    99                                                      
REMARK 465     MET G   100                                                      
REMARK 465     GLY G   101                                                      
REMARK 465     ALA H    46                                                      
REMARK 465     LEU H    47                                                      
REMARK 465     ALA H    48                                                      
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    SER A 118      -82.58     92.31                                   
REMARK 500    ASN C 122      -20.71     78.11                                   
REMARK 500    ARG E 117       62.47   -107.77                                   
REMARK 500    ASN G 132       -5.45   -143.86                                   
REMARK 500    SER G 168     -102.26     21.60                                   
REMARK 500    SER H  11      -46.29    -27.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     ASP E 169        24.5      L          L   OUTSIDE RANGE          
REMARK 500     SER H  11        19.8      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH H 203        DISTANCE =  5.26 ANGSTROMS                       
DBREF  3HTU A  102   176  UNP    Q9BRG1   VPS25_HUMAN    102    176             
DBREF  3HTU B   11    48  UNP    Q96FZ7   CHMP6_HUMAN     11     48             
DBREF  3HTU C  102   176  UNP    Q9BRG1   VPS25_HUMAN    102    176             
DBREF  3HTU D   11    48  UNP    Q96FZ7   CHMP6_HUMAN     11     48             
DBREF  3HTU E  102   176  UNP    Q9BRG1   VPS25_HUMAN    102    176             
DBREF  3HTU F   11    48  UNP    Q96FZ7   CHMP6_HUMAN     11     48             
DBREF  3HTU G  102   176  UNP    Q9BRG1   VPS25_HUMAN    102    176             
DBREF  3HTU H   11    48  UNP    Q96FZ7   CHMP6_HUMAN     11     48             
SEQADV 3HTU GLY A   98  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU ALA A   99  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU MET A  100  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU GLY A  101  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU GLY B   10  UNP  Q96FZ7              EXPRESSION TAG                 
SEQADV 3HTU GLY C   98  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU ALA C   99  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU MET C  100  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU GLY C  101  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU GLY D   10  UNP  Q96FZ7              EXPRESSION TAG                 
SEQADV 3HTU GLY E   98  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU ALA E   99  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU MET E  100  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU GLY E  101  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU GLY F   10  UNP  Q96FZ7              EXPRESSION TAG                 
SEQADV 3HTU GLY G   98  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU ALA G   99  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU MET G  100  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU GLY G  101  UNP  Q9BRG1              EXPRESSION TAG                 
SEQADV 3HTU GLY H   10  UNP  Q96FZ7              EXPRESSION TAG                 
SEQRES   1 A   79  GLY ALA MET GLY ARG ARG PRO GLU GLU TRP GLY LYS LEU          
SEQRES   2 A   79  ILE TYR GLN TRP VAL SER ARG SER GLY GLN ASN ASN SER          
SEQRES   3 A   79  VAL PHE THR LEU TYR GLU LEU THR ASN GLY GLU ASP THR          
SEQRES   4 A   79  GLU ASP GLU GLU PHE HIS GLY LEU ASP GLU ALA THR LEU          
SEQRES   5 A   79  LEU ARG ALA LEU GLN ALA LEU GLN GLN GLU HIS LYS ALA          
SEQRES   6 A   79  GLU ILE ILE THR VAL SER ASP GLY ARG GLY VAL LYS PHE          
SEQRES   7 A   79  PHE                                                          
SEQRES   1 B   39  GLY SER ARG VAL THR GLU GLN ASP LYS ALA ILE LEU GLN          
SEQRES   2 B   39  LEU LYS GLN GLN ARG ASP LYS LEU ARG GLN TYR GLN LYS          
SEQRES   3 B   39  ARG ILE ALA GLN GLN LEU GLU ARG GLU ARG ALA LEU ALA          
SEQRES   1 C   79  GLY ALA MET GLY ARG ARG PRO GLU GLU TRP GLY LYS LEU          
SEQRES   2 C   79  ILE TYR GLN TRP VAL SER ARG SER GLY GLN ASN ASN SER          
SEQRES   3 C   79  VAL PHE THR LEU TYR GLU LEU THR ASN GLY GLU ASP THR          
SEQRES   4 C   79  GLU ASP GLU GLU PHE HIS GLY LEU ASP GLU ALA THR LEU          
SEQRES   5 C   79  LEU ARG ALA LEU GLN ALA LEU GLN GLN GLU HIS LYS ALA          
SEQRES   6 C   79  GLU ILE ILE THR VAL SER ASP GLY ARG GLY VAL LYS PHE          
SEQRES   7 C   79  PHE                                                          
SEQRES   1 D   39  GLY SER ARG VAL THR GLU GLN ASP LYS ALA ILE LEU GLN          
SEQRES   2 D   39  LEU LYS GLN GLN ARG ASP LYS LEU ARG GLN TYR GLN LYS          
SEQRES   3 D   39  ARG ILE ALA GLN GLN LEU GLU ARG GLU ARG ALA LEU ALA          
SEQRES   1 E   79  GLY ALA MET GLY ARG ARG PRO GLU GLU TRP GLY LYS LEU          
SEQRES   2 E   79  ILE TYR GLN TRP VAL SER ARG SER GLY GLN ASN ASN SER          
SEQRES   3 E   79  VAL PHE THR LEU TYR GLU LEU THR ASN GLY GLU ASP THR          
SEQRES   4 E   79  GLU ASP GLU GLU PHE HIS GLY LEU ASP GLU ALA THR LEU          
SEQRES   5 E   79  LEU ARG ALA LEU GLN ALA LEU GLN GLN GLU HIS LYS ALA          
SEQRES   6 E   79  GLU ILE ILE THR VAL SER ASP GLY ARG GLY VAL LYS PHE          
SEQRES   7 E   79  PHE                                                          
SEQRES   1 F   39  GLY SER ARG VAL THR GLU GLN ASP LYS ALA ILE LEU GLN          
SEQRES   2 F   39  LEU LYS GLN GLN ARG ASP LYS LEU ARG GLN TYR GLN LYS          
SEQRES   3 F   39  ARG ILE ALA GLN GLN LEU GLU ARG GLU ARG ALA LEU ALA          
SEQRES   1 G   79  GLY ALA MET GLY ARG ARG PRO GLU GLU TRP GLY LYS LEU          
SEQRES   2 G   79  ILE TYR GLN TRP VAL SER ARG SER GLY GLN ASN ASN SER          
SEQRES   3 G   79  VAL PHE THR LEU TYR GLU LEU THR ASN GLY GLU ASP THR          
SEQRES   4 G   79  GLU ASP GLU GLU PHE HIS GLY LEU ASP GLU ALA THR LEU          
SEQRES   5 G   79  LEU ARG ALA LEU GLN ALA LEU GLN GLN GLU HIS LYS ALA          
SEQRES   6 G   79  GLU ILE ILE THR VAL SER ASP GLY ARG GLY VAL LYS PHE          
SEQRES   7 G   79  PHE                                                          
SEQRES   1 H   39  GLY SER ARG VAL THR GLU GLN ASP LYS ALA ILE LEU GLN          
SEQRES   2 H   39  LEU LYS GLN GLN ARG ASP LYS LEU ARG GLN TYR GLN LYS          
SEQRES   3 H   39  ARG ILE ALA GLN GLN LEU GLU ARG GLU ARG ALA LEU ALA          
FORMUL   9  HOH   *213(H2 O)                                                    
HELIX    1   1 ARG A  103  ARG A  117  1                                  15    
HELIX    2   2 THR A  126  GLY A  133  1                                   8    
HELIX    3   3 ASP A  145  GLU A  159  1                                  15    
HELIX    4   4 THR B   14  GLU B   44  1                                  31    
HELIX    5   5 ARG C  103  GLY C  119  1                                  17    
HELIX    6   6 LEU C  127  GLY C  133  1                                   7    
HELIX    7   7 ASP C  145  GLN C  157  1                                  13    
HELIX    8   8 THR D   14  ARG D   43  1                                  30    
HELIX    9   9 ARG E  103  ARG E  117  1                                  15    
HELIX   10  10 LEU E  127  GLY E  133  1                                   7    
HELIX   11  11 GLU E  134  GLU E  137  5                                   4    
HELIX   12  12 ASP E  145  GLU E  159  1                                  15    
HELIX   13  13 THR F   14  LEU F   41  1                                  28    
HELIX   14  14 ARG G  103  GLY G  119  1                                  17    
HELIX   15  15 LEU G  127  GLY G  133  1                                   7    
HELIX   16  16 ASP G  145  GLU G  159  1                                  15    
HELIX   17  17 THR H   14  ARG H   45  1                                  32    
SHEET    1   A 3 VAL A 124  PHE A 125  0                                        
SHEET    2   A 3 GLY A 172  PHE A 175 -1  O  VAL A 173   N  PHE A 125           
SHEET    3   A 3 ALA A 162  ILE A 165 -1  N  ILE A 165   O  GLY A 172           
SHEET    1   B 3 VAL C 124  THR C 126  0                                        
SHEET    2   B 3 GLY C 170  PHE C 175 -1  O  VAL C 173   N  PHE C 125           
SHEET    3   B 3 ALA C 162  VAL C 167 -1  N  VAL C 167   O  GLY C 170           
SHEET    1   C 3 VAL E 124  THR E 126  0                                        
SHEET    2   C 3 GLY E 170  PHE E 175 -1  O  VAL E 173   N  PHE E 125           
SHEET    3   C 3 ALA E 162  VAL E 167 -1  N  ILE E 165   O  GLY E 172           
SHEET    1   D 3 VAL G 124  THR G 126  0                                        
SHEET    2   D 3 ARG G 171  PHE G 175 -1  O  VAL G 173   N  PHE G 125           
SHEET    3   D 3 ALA G 162  THR G 166 -1  N  GLU G 163   O  LYS G 174           
CRYST1   58.562   51.043   76.987  90.00  90.39  90.00 P 1 21 1      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      0.017076  0.000000  0.000115        0.00000                         
SCALE2      0.000000  0.019591  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012989        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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