GenomeNet

Database: PDB
Entry: 1AVV
LinkDB: 1AVV
Original site: 1AVV 
HEADER    MYRISTYLATION                           21-SEP-97   1AVV              
TITLE     HIV-1 NEF PROTEIN, UNLIGANDED CORE DOMAIN                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEGATIVE FACTOR;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CORE DOMAIN;                                               
COMPND   5 SYNONYM: NEF, F-PROTEIN;                                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 VARIANT: ISOLATE LAI;                                                
SOURCE   5 CELL_LINE: BL21;                                                     
SOURCE   6 GENE: HIV-1 NEF;                                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;                                  
SOURCE  11 EXPRESSION_SYSTEM_GENE: HIV-1 NEF                                    
KEYWDS    MYRISTYLATION, GTP-BINDING, PHOSPHORYLATION, HIV-1, NEF, VIRUS, PXXP  
KEYWDS   2 MOTIF                                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.AROLD,P.FRANKEN,C.DUMAS                                             
REVDAT   4   11-APR-18 1AVV    1       REMARK                                   
REVDAT   3   04-APR-18 1AVV    1       REMARK                                   
REVDAT   2   24-FEB-09 1AVV    1       VERSN                                    
REVDAT   1   25-MAR-98 1AVV    0                                                
JRNL        AUTH   S.AROLD,P.FRANKEN,M.P.STRUB,F.HOH,S.BENICHOU,R.BENAROUS,     
JRNL        AUTH 2 C.DUMAS                                                      
JRNL        TITL   THE CRYSTAL STRUCTURE OF HIV-1 NEF PROTEIN BOUND TO THE FYN  
JRNL        TITL 2 KINASE SH3 DOMAIN SUGGESTS A ROLE FOR THIS COMPLEX IN        
JRNL        TITL 3 ALTERED T CELL RECEPTOR SIGNALING.                           
JRNL        REF    STRUCTURE                     V.   5  1361 1997              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   9351809                                                      
JRNL        DOI    10.1016/S0969-2126(97)00286-4                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.H.LEE,K.SAKSELA,U.A.MIRZA,B.T.CHAIT,J.KURIYAN              
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE CONSERVED CORE OF HIV-1 NEF         
REMARK   1  TITL 2 COMPLEXED WITH A SRC FAMILY SH3 DOMAIN                       
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  85   931 1996              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   S.GRZESIEK,A.BAX,G.M.CLORE,A.M.GRONENBORN,J.S.HU,J.KAUFMAN,  
REMARK   1  AUTH 2 I.PALMER,S.J.STAHL,P.T.WINGFIELD                             
REMARK   1  TITL   THE SOLUTION STRUCTURE OF HIV-1 NEF REVEALS AN UNEXPECTED    
REMARK   1  TITL 2 FOLD AND PERMITS DELINEATION OF THE BINDING SURFACE FOR THE  
REMARK   1  TITL 3 SH3 DOMAIN OF HCK TYROSINE PROTEIN KINASE                    
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   3   340 1996              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 78.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 3139                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 843                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.900                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.100                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AVV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171320.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM02                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0373                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : TWO BENT MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : PRINCETON 2K                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 3812                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT AND    
REMARK 200  MIRAS                                                               
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1EFN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 3                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       85.16000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      170.32000            
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    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     LEU A    58                                                      
REMARK 465     GLU A    59                                                      
REMARK 465     ALA A    60                                                      
REMARK 465     GLN A    61                                                      
REMARK 465     GLU A    62                                                      
REMARK 465     GLU A    63                                                      
REMARK 465     GLU A    64                                                      
REMARK 465     GLU A    65                                                      
REMARK 465     VAL A    66                                                      
REMARK 465     GLY A    67                                                      
REMARK 465     PHE A    68                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     VAL A    70                                                      
REMARK 465     THR A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     GLN A    73                                                      
REMARK 465     VAL A   148                                                      
REMARK 465     GLU A   149                                                      
REMARK 465     PRO A   150                                                      
REMARK 465     ASP A   151                                                      
REMARK 465     LYS A   152                                                      
REMARK 465     VAL A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     GLU A   155                                                      
REMARK 465     ALA A   156                                                      
REMARK 465     ASN A   157                                                      
REMARK 465     LYS A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     GLU A   160                                                      
REMARK 465     ASN A   161                                                      
REMARK 465     THR A   162                                                      
REMARK 465     SER A   163                                                      
REMARK 465     LEU A   164                                                      
REMARK 465     LEU A   165                                                      
REMARK 465     HIS A   166                                                      
REMARK 465     PRO A   167                                                      
REMARK 465     VAL A   168                                                      
REMARK 465     SER A   169                                                      
REMARK 465     LEU A   170                                                      
REMARK 465     HIS A   171                                                      
REMARK 465     GLY A   172                                                      
REMARK 465     MET A   173                                                      
REMARK 465     ASP A   174                                                      
REMARK 465     ASP A   175                                                      
REMARK 465     PRO A   176                                                      
REMARK 465     GLU A   177                                                      
REMARK 465     ARG A   178                                                      
REMARK 465     LYS A   204                                                      
REMARK 465     ASN A   205                                                      
REMARK 465     CYS A   206                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 122   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  75      123.09    -36.85                                   
REMARK 500    LEU A  76      101.83    -54.34                                   
REMARK 500    LYS A  94       52.54   -155.44                                   
REMARK 500    LEU A 100      120.33    -30.95                                   
REMARK 500    THR A 117      -76.91    -55.58                                   
REMARK 500    PRO A 122       65.43    -61.49                                   
REMARK 500    ASP A 123       17.22   -150.53                                   
REMARK 500    CYS A 142       70.64   -106.25                                   
REMARK 500    ASP A 186      111.30    179.62                                   
REMARK 500    HIS A 199       78.51   -107.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1AVV A   58   206  UNP    P03406   NEF_HV1BR       58    206             
SEQRES   1 A  151  GLY SER LEU GLU ALA GLN GLU GLU GLU GLU VAL GLY PHE          
SEQRES   2 A  151  PRO VAL THR PRO GLN VAL PRO LEU ARG PRO MET THR TYR          
SEQRES   3 A  151  LYS ALA ALA VAL ASP LEU SER HIS PHE LEU LYS GLU LYS          
SEQRES   4 A  151  GLY GLY LEU GLU GLY LEU ILE HIS SER GLN ARG ARG GLN          
SEQRES   5 A  151  ASP ILE LEU ASP LEU TRP ILE TYR HIS THR GLN GLY TYR          
SEQRES   6 A  151  PHE PRO ASP TRP GLN ASN TYR THR PRO GLY PRO GLY VAL          
SEQRES   7 A  151  ARG TYR PRO LEU THR PHE GLY TRP CYS TYR LYS LEU VAL          
SEQRES   8 A  151  PRO VAL GLU PRO ASP LYS VAL GLU GLU ALA ASN LYS GLY          
SEQRES   9 A  151  GLU ASN THR SER LEU LEU HIS PRO VAL SER LEU HIS GLY          
SEQRES  10 A  151  MET ASP ASP PRO GLU ARG GLU VAL LEU GLU TRP ARG PHE          
SEQRES  11 A  151  ASP SER ARG LEU ALA PHE HIS HIS VAL ALA ARG GLU LEU          
SEQRES  12 A  151  HIS PRO GLU TYR PHE LYS ASN CYS                              
HELIX    1   1 TYR A   81  GLU A   93  1                                  13    
HELIX    2   2 GLN A  104  GLN A  118  1                                  15    
HELIX    3   3 SER A  187  ALA A  190  5                                   4    
HELIX    4   4 VAL A  194  LEU A  198  1                                   5    
SHEET    1   A 2 TYR A 143  VAL A 146  0                                        
SHEET    2   A 2 GLU A 182  PHE A 185 -1  N  ARG A 184   O  LYS A 144           
CISPEP   1 GLY A  130    PRO A  131          0         0.29                     
CRYST1   85.160   85.160   85.160  90.00  90.00  90.00 P 2 3        12          
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      0.011743  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011743  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011743        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system