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Database: PDB
Entry: 2XZE
LinkDB: 2XZE
Original site: 2XZE 
HEADER    HYDROLASE/PROTEIN TRANSPORT             25-NOV-10   2XZE              
TITLE     STRUCTURAL BASIS FOR AMSH-ESCRT-III CHMP3 INTERACTION                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STAM-BINDING PROTEIN;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: MIT DOMAIN, RESIDUES 1-146;                                
COMPND   5 SYNONYM: ASSOCIATED MOLECULE WITH THE SH3 DOMAIN OF STAM,            
COMPND   6  ENDOSOME-ASSOCIATED UBIQUITIN ISOPEPTIDASE;                         
COMPND   7 EC: 3.4.19.-;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: CHARGED MULTIVESICULAR BODY PROTEIN 3;                     
COMPND  11 CHAIN: Q, R;                                                         
COMPND  12 FRAGMENT: C-TERM FRAGMENT, RESIDUES 183-222;                         
COMPND  13 SYNONYM: CHROMATIN-MODIFYING PROTEIN 3, NEUROENDOCRINE               
COMPND  14  DIFFERENTIATION FACTOR, VACUOLAR PROTEIN SORTING-ASSOCIATED         
COMPND  15  PROTEIN 24, HVPS24, CHMP3;                                          
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PPROEXHTA INVITROGEN;                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_VECTOR: PBADM-41 HIS-MBP FUSION PROTEIN WITH TEV   
SOURCE  15  PROTEASE CLEAVAGE SITE                                              
KEYWDS    HYDROLASE-PROTEIN TRANSPORT COMPLEX                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SOLOMONS,C.SABIN,W.WEISSENHORN                                      
REVDAT   1   24-AUG-11 2XZE    0                                                
JRNL        AUTH   J.SOLOMONS,C.SABIN,E.POUDEVIGNE,Y.USAMI,D.L.HULSIK,          
JRNL        AUTH 2 P.MACHEBOEUF,B.HARTLIEB,H.GOTTLINGER,W.WEISSENHORN           
JRNL        TITL   STRUCTURAL BASIS FOR ESCRT-III CHMP3 RECRUITMENT OF AMSH.    
JRNL        REF    STRUCTURE                     V.  19  1149 2011              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   21827950                                                     
JRNL        DOI    10.1016/J.STR.2011.05.011                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.LATA,M.ROESSLE,J.SOLOMONS,M.JAMIN,H.G.GOTTLINGER,          
REMARK   1  AUTH 2 D.I.SVERGUN,W.WEISSENHORN                                    
REMARK   1  TITL   STRUCTURAL BASIS FOR AUTOINHIBITION OF ESCRT-III CHMP3.      
REMARK   1  REF    J.MOL.BIOL.                   V. 378   818 2008              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   18395747                                                     
REMARK   1  DOI    10.1016/J.JMB.2008.03.030                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 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) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.73                          
REMARK   3   NUMBER OF REFLECTIONS             : 40725                          
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) : 0.19333                         
REMARK   3   R VALUE            (WORKING SET) : 0.19163                         
REMARK   3   FREE R VALUE                     : 0.22694                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2164                            
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) : 1.750                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.795                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3014                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.305                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 171                          
REMARK   3   BIN FREE R VALUE                    : 0.374                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2705                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 386                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.212                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.51                                                 
REMARK   3    B22 (A**2) : 0.51                                                 
REMARK   3    B33 (A**2) : -1.02                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.113         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.111         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.080         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.520         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2743 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3686 ; 1.298 ; 1.995       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   329 ; 4.699 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   142 ;31.884 ;24.366       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   556 ;13.394 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;14.998 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   396 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2069 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1376 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1901 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   320 ; 0.190 ; 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):    84 ; 0.221 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.159 ; 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):  1712 ; 1.136 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2660 ; 1.817 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1164 ; 3.064 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1024 ; 4.961 ; 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 2XZE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-NOV-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-43466.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9760, 0.9795                     
REMARK 200  MONOCHROMATOR                  : U35 UNDULATOR                      
REMARK 200  OPTICS                         : TORODIAL FOCUSING MIRROR           
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (Q315R)                        
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 SCALA                         
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 141404                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.75                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.85                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.3                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.10                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.64                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.20                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTO-RICKSHAW                                         
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.3 MG/ML OF AMSH PROTEIN IN 10          
REMARK 280  MM HEPES PH 8.0, 100 MM NACL WAS MIXED WITH AN EQUAL                
REMARK 280  VOLUME WELL CONDITION: 2.2 M SODIUM MALONATE,WITH 30 %              
REMARK 280  GLYCEROL AS CRYO-PROTECTANT                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      103.45500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       51.72750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      155.18250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9710 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.2 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, R                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.7 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, Q                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A   143                                                      
REMARK 465     LYS A   144                                                      
REMARK 465     GLU A   145                                                      
REMARK 465     LYS A   146                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLN B   140                                                      
REMARK 465     GLU B   141                                                      
REMARK 465     LEU B   142                                                      
REMARK 465     GLU B   143                                                      
REMARK 465     LYS B   144                                                      
REMARK 465     GLU B   145                                                      
REMARK 465     LYS B   146                                                      
REMARK 465     LYS Q   183                                                      
REMARK 465     VAL Q   184                                                      
REMARK 465     THR Q   185                                                      
REMARK 465     ASP Q   186                                                      
REMARK 465     ALA Q   187                                                      
REMARK 465     LEU Q   188                                                      
REMARK 465     PRO Q   189                                                      
REMARK 465     GLU Q   190                                                      
REMARK 465     PRO Q   191                                                      
REMARK 465     GLU Q   192                                                      
REMARK 465     PRO Q   193                                                      
REMARK 465     PRO Q   194                                                      
REMARK 465     GLY Q   195                                                      
REMARK 465     ALA Q   196                                                      
REMARK 465     MET Q   197                                                      
REMARK 465     ALA Q   198                                                      
REMARK 465     ALA Q   199                                                      
REMARK 465     LYS R   183                                                      
REMARK 465     VAL R   184                                                      
REMARK 465     THR R   185                                                      
REMARK 465     ASP R   186                                                      
REMARK 465     ALA R   187                                                      
REMARK 465     LEU R   188                                                      
REMARK 465     PRO R   189                                                      
REMARK 465     GLU R   190                                                      
REMARK 465     PRO R   191                                                      
REMARK 465     GLU R   192                                                      
REMARK 465     PRO R   193                                                      
REMARK 465     PRO R   194                                                      
REMARK 465     GLY R   195                                                      
REMARK 465     ALA R   196                                                      
REMARK 465     MET R   197                                                      
REMARK 465     ALA R   198                                                      
REMARK 465     ALA R   199                                                      
REMARK 465     SER R   200                                                      
REMARK 465     GLU R   201                                                      
REMARK 465     ASP R   202                                                      
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    ILE A  98      -69.63   -120.80                                   
REMARK 500    ILE B  98      -70.84   -124.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2GD5   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR BUDDING BY THE ESCRTIII FACTOR CHMP3           
DBREF  2XZE A    1   146  UNP    O95630   STABP_HUMAN      1    146             
DBREF  2XZE B    1   146  UNP    O95630   STABP_HUMAN      1    146             
DBREF  2XZE Q  183   222  UNP    Q9Y3E7   CHMP3_HUMAN    183    222             
DBREF  2XZE R  183   222  UNP    Q9Y3E7   CHMP3_HUMAN    183    222             
SEQRES   1 A  146  MET SER ASP HIS GLY ASP VAL SER LEU PRO PRO GLU ASP          
SEQRES   2 A  146  ARG VAL ARG ALA LEU SER GLN LEU GLY SER ALA VAL GLU          
SEQRES   3 A  146  VAL ASN GLU ASP ILE PRO PRO ARG ARG TYR PHE ARG SER          
SEQRES   4 A  146  GLY VAL GLU ILE ILE ARG MET ALA SER ILE TYR SER GLU          
SEQRES   5 A  146  GLU GLY ASN ILE GLU HIS ALA PHE ILE LEU TYR ASN LYS          
SEQRES   6 A  146  TYR ILE THR LEU PHE ILE GLU LYS LEU PRO LYS HIS ARG          
SEQRES   7 A  146  ASP TYR LYS SER ALA VAL ILE PRO GLU LYS LYS ASP THR          
SEQRES   8 A  146  VAL LYS LYS LEU LYS GLU ILE ALA PHE PRO LYS ALA GLU          
SEQRES   9 A  146  GLU LEU LYS ALA GLU LEU LEU LYS ARG TYR THR LYS GLU          
SEQRES  10 A  146  TYR THR GLU TYR ASN GLU GLU LYS LYS LYS GLU ALA GLU          
SEQRES  11 A  146  GLU LEU ALA ARG ASN MET ALA ILE GLN GLN GLU LEU GLU          
SEQRES  12 A  146  LYS GLU LYS                                                  
SEQRES   1 B  146  MET SER ASP HIS GLY ASP VAL SER LEU PRO PRO GLU ASP          
SEQRES   2 B  146  ARG VAL ARG ALA LEU SER GLN LEU GLY SER ALA VAL GLU          
SEQRES   3 B  146  VAL ASN GLU ASP ILE PRO PRO ARG ARG TYR PHE ARG SER          
SEQRES   4 B  146  GLY VAL GLU ILE ILE ARG MET ALA SER ILE TYR SER GLU          
SEQRES   5 B  146  GLU GLY ASN ILE GLU HIS ALA PHE ILE LEU TYR ASN LYS          
SEQRES   6 B  146  TYR ILE THR LEU PHE ILE GLU LYS LEU PRO LYS HIS ARG          
SEQRES   7 B  146  ASP TYR LYS SER ALA VAL ILE PRO GLU LYS LYS ASP THR          
SEQRES   8 B  146  VAL LYS LYS LEU LYS GLU ILE ALA PHE PRO LYS ALA GLU          
SEQRES   9 B  146  GLU LEU LYS ALA GLU LEU LEU LYS ARG TYR THR LYS GLU          
SEQRES  10 B  146  TYR THR GLU TYR ASN GLU GLU LYS LYS LYS GLU ALA GLU          
SEQRES  11 B  146  GLU LEU ALA ARG ASN MET ALA ILE GLN GLN GLU LEU GLU          
SEQRES  12 B  146  LYS GLU LYS                                                  
SEQRES   1 Q   40  LYS VAL THR ASP ALA LEU PRO GLU PRO GLU PRO PRO GLY          
SEQRES   2 Q   40  ALA MET ALA ALA SER GLU ASP GLU GLU GLU GLU GLU GLU          
SEQRES   3 Q   40  ALA LEU GLU ALA MET GLN SER ARG LEU ALA THR LEU ARG          
SEQRES   4 Q   40  SER                                                          
SEQRES   1 R   40  LYS VAL THR ASP ALA LEU PRO GLU PRO GLU PRO PRO GLY          
SEQRES   2 R   40  ALA MET ALA ALA SER GLU ASP GLU GLU GLU GLU GLU GLU          
SEQRES   3 R   40  ALA LEU GLU ALA MET GLN SER ARG LEU ALA THR LEU ARG          
SEQRES   4 R   40  SER                                                          
FORMUL   5  HOH   *386(H2 O)                                                    
HELIX    1   1 PRO A   10  SER A   23  1                                  14    
HELIX    2   2 PRO A   32  GLY A   54  1                                  23    
HELIX    3   3 ASN A   55  GLU A   72  1                                  18    
HELIX    4   4 LYS A   73  HIS A   77  5                                   5    
HELIX    5   5 GLU A   87  ILE A   98  1                                  12    
HELIX    6   6 ILE A   98  ILE A  138  1                                  41    
HELIX    7   7 PRO B   10  ALA B   24  1                                  15    
HELIX    8   8 PRO B   32  GLU B   53  1                                  22    
HELIX    9   9 ASN B   55  GLU B   72  1                                  18    
HELIX   10  10 LYS B   73  HIS B   77  5                                   5    
HELIX   11  11 GLU B   87  ILE B   98  1                                  12    
HELIX   12  12 ILE B   98  GLN B  139  1                                  42    
HELIX   13  13 SER Q  200  ARG Q  221  1                                  22    
HELIX   14  14 GLU R  203  MET R  213  1                                  11    
HELIX   15  15 MET R  213  ARG R  221  1                                   9    
CRYST1   45.970   45.970  206.910  90.00  90.00  90.00 P 41          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      0.021753  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.021753  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004833        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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