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Database: PDB
Entry: 1GVJ
LinkDB: 1GVJ
Original site: 1GVJ 
HEADER    TRANSCRIPTION                           14-FEB-02   1GVJ              
TITLE     ETS-1 DNA BINDING AND AUTOINHIBITORY DOMAINS                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-ETS-1 PROTEIN;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 297-441;                                          
COMPND   5 SYNONYM: P54;                                                        
COMPND   6 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: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PAR2156                                   
KEYWDS    TRANSCRIPTION, ETS-1, AUTOINHIBITION, ETS DOMAIN                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.TAHIROV,K.OGATA                                                   
REVDAT   3   08-MAY-19 1GVJ    1       REMARK                                   
REVDAT   2   24-FEB-09 1GVJ    1       VERSN                                    
REVDAT   1   06-FEB-04 1GVJ    0                                                
JRNL        AUTH   T.H.TAHIROV,T.INOUE-BUNGO,K.OGATA                            
JRNL        TITL   CRYSTAL STRUCTURE OF C-ETS-1 DNA-BINDING AND AUTOINHIBITORY  
JRNL        TITL 2 DOMAINS                                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.53 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1125447.620                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 40277                          
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 SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2010                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.53                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.63                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5884                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280                       
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 318                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2361                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 293                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.17000                                              
REMARK   3    B22 (A**2) : -0.94000                                             
REMARK   3    B33 (A**2) : -0.24000                                             
REMARK   3    B12 (A**2) : -2.39000                                             
REMARK   3    B13 (A**2) : 1.35000                                              
REMARK   3    B23 (A**2) : -0.70000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.26                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.0                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.22                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.720                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.790 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.750 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.750 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.010 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 46.09                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-FEB-02.                  
REMARK 100 THE DEPOSITION ID IS D_1290009446.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL45XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.02                               
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU IMAGE PLATE RAXIS V         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40937                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.520                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 3.103                              
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6480                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.021                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1AWC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 30% W/V PEG      
REMARK 280  4000, 0.1 M SODIUM CITRATE PH 5.6, PROTEIN CONCENTRATION 15 MG/     
REMARK 280  ML PLUS 10 MM DTT, TEMPERATURE 297 K, FOR CRYOPROTECTION 10% OF     
REMARK 280  PEG 400 WAS ADDED., PH 5.60                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A   438                                                      
REMARK 465     ALA A   439                                                      
REMARK 465     ASP A   440                                                      
REMARK 465     GLU A   441                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO A 437    CA   C    O    CB   CG   CD                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA B 439      -72.28    -63.47                                   
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 B2152        DISTANCE =  5.92 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2STT   RELATED DB: PDB                                   
REMARK 900 SOLUTION NMR STRUCTURE OF THE HUMAN ETS1/ DEOXYRIBONUCLEIC ACID      
REMARK 900 COMPLEX, 25 STRUCTURES                                               
REMARK 900 RELATED ID: 2STW   RELATED DB: PDB                                   
REMARK 900 SOLUTION NMR STRUCTURE OF THE HUMAN ETS1/ DEOXYRIBONUCLEIC ACID      
REMARK 900 COMPLEX, RESTRAINED REGULARIZED MEAN STRUCTURE                       
DBREF  1GVJ A  296   296  PDB    1GVJ     1GVJ           296    296             
DBREF  1GVJ A  297   441  UNP    P14921   ETS1_HUMAN     297    441             
DBREF  1GVJ B  296   296  PDB    1GVJ     1GVJ           296    296             
DBREF  1GVJ B  297   441  UNP    P14921   ETS1_HUMAN     297    441             
SEQRES   1 A  146  MET ASN HIS LYS PRO LYS GLY THR PHE LYS ASP TYR VAL          
SEQRES   2 A  146  ARG ASP ARG ALA ASP LEU ASN LYS ASP LYS PRO VAL ILE          
SEQRES   3 A  146  PRO ALA ALA ALA LEU ALA GLY TYR THR GLY SER GLY PRO          
SEQRES   4 A  146  ILE GLN LEU TRP GLN PHE LEU LEU GLU LEU LEU THR ASP          
SEQRES   5 A  146  LYS SER CYS GLN SER PHE ILE SER TRP THR GLY ASP GLY          
SEQRES   6 A  146  TRP GLU PHE LYS LEU SER ASP PRO ASP GLU VAL ALA ARG          
SEQRES   7 A  146  ARG TRP GLY LYS ARG LYS ASN LYS PRO LYS MET ASN TYR          
SEQRES   8 A  146  GLU LYS LEU SER ARG GLY LEU ARG TYR TYR TYR ASP LYS          
SEQRES   9 A  146  ASN ILE ILE HIS LYS THR ALA GLY LYS ARG TYR VAL TYR          
SEQRES  10 A  146  ARG PHE VAL CYS ASP LEU GLN SER LEU LEU GLY TYR THR          
SEQRES  11 A  146  PRO GLU GLU LEU HIS ALA MET LEU ASP VAL LYS PRO ASP          
SEQRES  12 A  146  ALA ASP GLU                                                  
SEQRES   1 B  146  MET ASN HIS LYS PRO LYS GLY THR PHE LYS ASP TYR VAL          
SEQRES   2 B  146  ARG ASP ARG ALA ASP LEU ASN LYS ASP LYS PRO VAL ILE          
SEQRES   3 B  146  PRO ALA ALA ALA LEU ALA GLY TYR THR GLY SER GLY PRO          
SEQRES   4 B  146  ILE GLN LEU TRP GLN PHE LEU LEU GLU LEU LEU THR ASP          
SEQRES   5 B  146  LYS SER CYS GLN SER PHE ILE SER TRP THR GLY ASP GLY          
SEQRES   6 B  146  TRP GLU PHE LYS LEU SER ASP PRO ASP GLU VAL ALA ARG          
SEQRES   7 B  146  ARG TRP GLY LYS ARG LYS ASN LYS PRO LYS MET ASN TYR          
SEQRES   8 B  146  GLU LYS LEU SER ARG GLY LEU ARG TYR TYR TYR ASP LYS          
SEQRES   9 B  146  ASN ILE ILE HIS LYS THR ALA GLY LYS ARG TYR VAL TYR          
SEQRES  10 B  146  ARG PHE VAL CYS ASP LEU GLN SER LEU LEU GLY TYR THR          
SEQRES  11 B  146  PRO GLU GLU LEU HIS ALA MET LEU ASP VAL LYS PRO ASP          
SEQRES  12 B  146  ALA ASP GLU                                                  
FORMUL   3  HOH   *293(H2 O)                                                    
HELIX    1   1 THR A  303  LEU A  314  1                                  12    
HELIX    2   2 PRO A  322  GLY A  331  1                                  10    
HELIX    3   3 GLN A  336  THR A  346  1                                  11    
HELIX    4   4 ASP A  347  GLN A  351  5                                   5    
HELIX    5   5 ASP A  367  ASN A  380  1                                  14    
HELIX    6   6 ASN A  385  TYR A  396  1                                  12    
HELIX    7   7 ASP A  417  GLY A  423  1                                   7    
HELIX    8   8 THR A  425  LEU A  433  1                                   9    
HELIX    9   9 THR B  303  ASP B  313  1                                  11    
HELIX   10  10 PRO B  322  GLY B  331  1                                  10    
HELIX   11  11 GLN B  336  THR B  346  1                                  11    
HELIX   12  12 ASP B  347  GLN B  351  5                                   5    
HELIX   13  13 ASP B  367  ASN B  380  1                                  14    
HELIX   14  14 ASN B  385  LYS B  399  1                                  15    
HELIX   15  15 ASP B  417  GLY B  423  1                                   7    
HELIX   16  16 THR B  425  LEU B  433  1                                   9    
SHEET    1  AA 4 SER A 355  TRP A 356  0                                        
SHEET    2  AA 4 GLU A 362  LYS A 364 -1  O  LYS A 364   N  SER A 355           
SHEET    3  AA 4 VAL A 411  PHE A 414 -1  O  TYR A 412   N  PHE A 363           
SHEET    4  AA 4 ILE A 402  LYS A 404 -1  O  HIS A 403   N  ARG A 413           
SHEET    1  BA 4 ILE B 354  TRP B 356  0                                        
SHEET    2  BA 4 GLU B 362  LEU B 365 -1  O  LYS B 364   N  SER B 355           
SHEET    3  BA 4 VAL B 411  PHE B 414 -1  O  TYR B 412   N  PHE B 363           
SHEET    4  BA 4 ILE B 402  LYS B 404 -1  O  HIS B 403   N  ARG B 413           
CRYST1   40.475   42.842   49.771 115.25  97.30 102.40 P 1           2          
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      0.024707  0.005432  0.006463        0.00000                         
SCALE2      0.000000  0.023899  0.012673        0.00000                         
SCALE3      0.000000  0.000000  0.022928        0.00000                         
MTRIX1   1  0.286870 -0.957350 -0.034340       22.02220    1                    
MTRIX2   1 -0.957160 -0.287920  0.030660       27.59034    1                    
MTRIX3   1 -0.039240  0.024080 -0.998940       49.12850    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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