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Database: PDB
Entry: 4DDP
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Original site: 4DDP 
HEADER    MEMBRANE PROTEIN                        19-JAN-12   4DDP              
TITLE     CRYSTAL STRUCTURE OF BECLIN 1 EVOLUTIONARILY CONSERVED DOMAIN(ECD)    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BECLIN-1;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 241-450;                                      
COMPND   5 SYNONYM: COILED-COIL MYOSIN-LIKE BCL2-INTERACTING PROTEIN, PROTEIN   
COMPND   6 GT197;                                                               
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BECN1, GT197;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    BECLIN 1, ECD, AUTOPHAGY, MEMBRANE BINDING, MEMBRANE PROTEIN          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.J.HUANG,W.Y.CHOI,J.W.WANG,Y.G.SHI                                   
REVDAT   2   20-MAR-24 4DDP    1       REMARK                                   
REVDAT   1   22-FEB-12 4DDP    0                                                
JRNL        AUTH   W.HUANG,W.CHOI,W.HU,N.MI,Q.GUO,M.MA,M.LIU,Y.TIAN,P.LU,       
JRNL        AUTH 2 F.L.WANG,H.DENG,L.LIU,N.GAO,L.YU,Y.SHI                       
JRNL        TITL   CRYSTAL STRUCTURE AND BIOCHEMICAL ANALYSES REVEAL BECLIN 1   
JRNL        TITL 2 AS A NOVEL MEMBRANE BINDING PROTEIN                          
JRNL        REF    CELL RES.                                  2012              
JRNL        REFN                   ISSN 1001-0602                               
JRNL        PMID   22310240                                                     
JRNL        DOI    10.1038/CR.2012.24                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_596)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.41                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 24700                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1243                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 32.4151 -  3.2161    0.92     2725   147  0.1700 0.1767        
REMARK   3     2  3.2161 -  2.5530    0.98     2840   152  0.1655 0.2140        
REMARK   3     3  2.5530 -  2.2304    0.98     2825   147  0.1514 0.2016        
REMARK   3     4  2.2304 -  2.0265    0.97     2797   148  0.1614 0.1816        
REMARK   3     5  2.0265 -  1.8813    0.96     2723   143  0.1788 0.2078        
REMARK   3     6  1.8813 -  1.7704    0.92     2629   120  0.1894 0.2579        
REMARK   3     7  1.7704 -  1.6817    0.88     2505   112  0.2132 0.2324        
REMARK   3     8  1.6817 -  1.6085    0.84     2358   150  0.2520 0.2897        
REMARK   3     9  1.6085 -  1.5466    0.72     2055   124  0.2951 0.3269        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 1.01                                          
REMARK   3   K_SOL              : 0.44                                          
REMARK   3   B_SOL              : 43.95                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.890           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 19.20430                                             
REMARK   3    B22 (A**2) : -9.67440                                             
REMARK   3    B33 (A**2) : -9.52990                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -6.58550                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           1625                                  
REMARK   3   ANGLE     :  1.274           2190                                  
REMARK   3   CHIRALITY :  0.083            225                                  
REMARK   3   PLANARITY :  0.007            277                                  
REMARK   3   DIHEDRAL  : 16.034            582                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  28.8198  -3.9292  17.3240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2124 T22:   0.2068                                     
REMARK   3      T33:   0.1896 T12:   0.0417                                     
REMARK   3      T13:   0.0034 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8275 L22:   1.8621                                     
REMARK   3      L33:   1.5292 L12:   0.2464                                     
REMARK   3      L13:   0.0823 L23:   0.0560                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0182 S12:   0.0220 S13:  -0.0268                       
REMARK   3      S21:  -0.0437 S22:  -0.0418 S23:  -0.0853                       
REMARK   3      S31:   0.0665 S32:   0.1095 S33:   0.0077                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4DDP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-FEB-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000070199.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26572                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.547                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 0.3M NACL, 0.1M TRIS PH    
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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       40.37300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       16.78150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       40.37300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       16.78150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     LEU A   241                                                      
REMARK 465     GLU A   242                                                      
REMARK 465     LEU A   243                                                      
REMARK 465     ASP A   244                                                      
REMARK 465     ASP A   245                                                      
REMARK 465     GLU A   246                                                      
REMARK 465     LEU A   247                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     LYS A   266                                                      
REMARK 465     THR A   267                                                      
REMARK 465     ASN A   268                                                      
REMARK 465     GLU A   387                                                      
REMARK 465     TYR A   448                                                      
REMARK 465     ASN A   449                                                      
REMARK 465     LYS A   450                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 389    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   546     O    HOH A   596              2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500  HD22  ASN A   271    HD22  ASN A   271     2655     0.63            
REMARK 500   ND2  ASN A   271    HD22  ASN A   271     2655     1.57            
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    TRP A 277     -158.21   -152.20                                   
REMARK 500    ARG A 327      -31.70     76.49                                   
REMARK 500    TYR A 333       49.56   -154.14                                   
REMARK 500    LEU A 351       56.31   -104.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4DDP A  241   450  UNP    Q14457   BECN1_HUMAN    241    450             
SEQRES   1 A  210  LEU GLU LEU ASP ASP GLU LEU LYS SER VAL GLU ASN GLN          
SEQRES   2 A  210  MET ARG TYR ALA GLN THR GLN LEU ASP LYS LEU LYS LYS          
SEQRES   3 A  210  THR ASN VAL PHE ASN ALA THR PHE HIS ILE TRP HIS SER          
SEQRES   4 A  210  GLY GLN PHE GLY THR ILE ASN ASN PHE ARG LEU GLY ARG          
SEQRES   5 A  210  LEU PRO SER VAL PRO VAL GLU TRP ASN GLU ILE ASN ALA          
SEQRES   6 A  210  ALA TRP GLY GLN THR VAL LEU LEU LEU HIS ALA LEU ALA          
SEQRES   7 A  210  ASN LYS MET GLY LEU LYS PHE GLN ARG TYR ARG LEU VAL          
SEQRES   8 A  210  PRO TYR GLY ASN HIS SER TYR LEU GLU SER LEU THR ASP          
SEQRES   9 A  210  LYS SER LYS GLU LEU PRO LEU TYR CYS SER GLY GLY LEU          
SEQRES  10 A  210  ARG PHE PHE TRP ASP ASN LYS PHE ASP HIS ALA MET VAL          
SEQRES  11 A  210  ALA PHE LEU ASP CYS VAL GLN GLN PHE LYS GLU GLU VAL          
SEQRES  12 A  210  GLU LYS GLY GLU THR ARG PHE CYS LEU PRO TYR ARG MET          
SEQRES  13 A  210  ASP VAL GLU LYS GLY LYS ILE GLU ASP THR GLY GLY SER          
SEQRES  14 A  210  GLY GLY SER TYR SER ILE LYS THR GLN PHE ASN SER GLU          
SEQRES  15 A  210  GLU GLN TRP THR LYS ALA LEU LYS PHE MET LEU THR ASN          
SEQRES  16 A  210  LEU LYS TRP GLY LEU ALA TRP VAL SER SER GLN PHE TYR          
SEQRES  17 A  210  ASN LYS                                                      
FORMUL   2  HOH   *115(H2 O)                                                    
HELIX    1   1 SER A  249  LYS A  263  1                                  15    
HELIX    2   2 GLU A  299  GLY A  322  1                                  24    
HELIX    3   3 TYR A  333  HIS A  336  5                                   4    
HELIX    4   4 LEU A  357  TRP A  361  5                                   5    
HELIX    5   5 ASN A  363  LYS A  385  1                                  23    
HELIX    6   6 SER A  421  PHE A  447  1                                  27    
SHEET    1   A 3 ILE A 276  SER A 279  0                                        
SHEET    2   A 3 PHE A 282  ILE A 285 -1  O  THR A 284   N  TRP A 277           
SHEET    3   A 3 PHE A 288  ARG A 289 -1  O  PHE A 288   N  ILE A 285           
SHEET    1   B 3 TYR A 328  VAL A 331  0                                        
SHEET    2   B 3 TYR A 338  SER A 341 -1  O  TYR A 338   N  VAL A 331           
SHEET    3   B 3 LEU A 349  PRO A 350 -1  O  LEU A 349   N  LEU A 339           
SHEET    1   C 3 MET A 396  ASP A 397  0                                        
SHEET    2   C 3 LYS A 402  GLU A 404 -1  O  LYS A 402   N  ASP A 397           
SHEET    3   C 3 SER A 412  SER A 414 -1  O  TYR A 413   N  ILE A 403           
CRYST1   80.746   33.563   74.765  90.00 113.49  90.00 C 1 2 1       4          
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      0.012385  0.000000  0.005383        0.00000                         
SCALE2      0.000000  0.029795  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014584        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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