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Entry: 1N1A
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HEADER    ISOMERASE                               16-OCT-02   1N1A              
TITLE     CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF HUMAN FKBP52            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FKBP52;                                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: THE N-TERMINAL FRAGMENT (1-140);                           
COMPND   5 SYNONYM: FK506-BINDING PROTEIN 4;                                    
COMPND   6 EC: 5.2.1.8;                                                         
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: FKBP4;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A(+)                                 
KEYWDS    FKBP52, THE N-TERMINAL DOMAIN, CRYSTAL STRUCTURE, ISOMERASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.LI,Y.DING,B.WU,C.SHU,B.SHEN,Z.RAO                                   
REVDAT   2   24-FEB-09 1N1A    1       VERSN                                    
REVDAT   1   30-DEC-02 1N1A    0                                                
JRNL        AUTH   P.LI,Y.DING,B.WU,C.SHU,B.SHEN,Z.RAO                          
JRNL        TITL   STRUCTURE OF THE N-TERMINAL DOMAIN OF HUMAN FKBP52.          
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  59    16 2003              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   12499534                                                     
JRNL        DOI    10.1107/S0907444902017523                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 7790                           
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) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 822                             
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            : 1866                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 55                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.86400                                             
REMARK   3    B22 (A**2) : 13.27000                                             
REMARK   3    B33 (A**2) : -6.40600                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -14.00900                                            
REMARK   3    B23 (A**2) : 0.00000                                              
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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) : 1.257 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.056 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.889 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.633 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1N1A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-OCT-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017393.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CUKA                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26259                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.800                             
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1FKJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, AMMONIUM SULFATE, PH 8.5,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.18100            
REMARK 290   SMTRY3   2  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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER IN THE ASYMMETRIC UNIT    
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     MET A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     ASP A    72                                                      
REMARK 465     ARG A    73                                                      
REMARK 465     LYS A    74                                                      
REMARK 465     ASP A    75                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     MET B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     GLU B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     ASP B    72                                                      
REMARK 465     ARG B    73                                                      
REMARK 465     LYS B    74                                                      
REMARK 465     ASP B    75                                                      
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   O    LEU A    18     OH   TYR A   113     1455     2.07            
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    LEU A  18      -28.88    -31.10                                   
REMARK 500    SER A  69      122.10   -179.90                                   
REMARK 500    ALA A 112     -118.54   -139.04                                   
REMARK 500    ARG B  39      115.59   -164.70                                   
REMARK 500    SER B  70       22.37    -78.89                                   
REMARK 500    ALA B 112     -106.83   -127.45                                   
REMARK 500    PRO B 123      175.59    -50.95                                   
REMARK 500    GLU B 136      174.82    174.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1N1A A    2   140  UNP    Q02790   FKBP4_HUMAN      1    139             
DBREF  1N1A B    2   140  UNP    Q02790   FKBP4_HUMAN      1    139             
SEQADV 1N1A MET A    1  UNP  Q02790              INITIATING MET                 
SEQADV 1N1A MET B    1  UNP  Q02790              INITIATING MET                 
SEQRES   1 A  140  MET THR ALA GLU GLU MET LYS ALA THR GLU SER GLY ALA          
SEQRES   2 A  140  GLN SER ALA PRO LEU PRO MET GLU GLY VAL ASP ILE SER          
SEQRES   3 A  140  PRO LYS GLN ASP GLU GLY VAL LEU LYS VAL ILE LYS ARG          
SEQRES   4 A  140  GLU GLY THR GLY THR GLU MET PRO MET ILE GLY ASP ARG          
SEQRES   5 A  140  VAL PHE VAL HIS TYR THR GLY TRP LEU LEU ASP GLY THR          
SEQRES   6 A  140  LYS PHE ASP SER SER LEU ASP ARG LYS ASP LYS PHE SER          
SEQRES   7 A  140  PHE ASP LEU GLY LYS GLY GLU VAL ILE LYS ALA TRP ASP          
SEQRES   8 A  140  ILE ALA ILE ALA THR MET LYS VAL GLY GLU VAL CYS HIS          
SEQRES   9 A  140  ILE THR CYS LYS PRO GLU TYR ALA TYR GLY SER ALA GLY          
SEQRES  10 A  140  SER PRO PRO LYS ILE PRO PRO ASN ALA THR LEU VAL PHE          
SEQRES  11 A  140  GLU VAL GLU LEU PHE GLU PHE LYS GLY GLU                      
SEQRES   1 B  140  MET THR ALA GLU GLU MET LYS ALA THR GLU SER GLY ALA          
SEQRES   2 B  140  GLN SER ALA PRO LEU PRO MET GLU GLY VAL ASP ILE SER          
SEQRES   3 B  140  PRO LYS GLN ASP GLU GLY VAL LEU LYS VAL ILE LYS ARG          
SEQRES   4 B  140  GLU GLY THR GLY THR GLU MET PRO MET ILE GLY ASP ARG          
SEQRES   5 B  140  VAL PHE VAL HIS TYR THR GLY TRP LEU LEU ASP GLY THR          
SEQRES   6 B  140  LYS PHE ASP SER SER LEU ASP ARG LYS ASP LYS PHE SER          
SEQRES   7 B  140  PHE ASP LEU GLY LYS GLY GLU VAL ILE LYS ALA TRP ASP          
SEQRES   8 B  140  ILE ALA ILE ALA THR MET LYS VAL GLY GLU VAL CYS HIS          
SEQRES   9 B  140  ILE THR CYS LYS PRO GLU TYR ALA TYR GLY SER ALA GLY          
SEQRES  10 B  140  SER PRO PRO LYS ILE PRO PRO ASN ALA THR LEU VAL PHE          
SEQRES  11 B  140  GLU VAL GLU LEU PHE GLU PHE LYS GLY GLU                      
FORMUL   3  HOH   *55(H2 O)                                                     
HELIX    1   1 ILE A   87  ALA A   95  1                                   9    
HELIX    2   2 PRO A  109  ALA A  112  5                                   4    
HELIX    3   3 LEU B   18  GLY B   22  5                                   5    
HELIX    4   4 ILE B   87  ALA B   95  1                                   9    
HELIX    5   5 PRO B  109  ALA B  112  5                                   4    
SHEET    1   A 6 VAL A  23  ASP A  24  0                                        
SHEET    2   A 6 VAL A  33  ARG A  39 -1  O  LYS A  35   N  VAL A  23           
SHEET    3   A 6 VAL A 102  CYS A 107 -1  O  HIS A 104   N  VAL A  36           
SHEET    4   A 6 LEU A 128  LYS A 138 -1  O  LEU A 128   N  CYS A 107           
SHEET    5   A 6 ARG A  52  LEU A  61 -1  N  PHE A  54   O  GLU A 136           
SHEET    6   A 6 LYS A  66  SER A  69 -1  O  ASP A  68   N  GLY A  59           
SHEET    1   B 6 VAL A  23  ASP A  24  0                                        
SHEET    2   B 6 VAL A  33  ARG A  39 -1  O  LYS A  35   N  VAL A  23           
SHEET    3   B 6 VAL A 102  CYS A 107 -1  O  HIS A 104   N  VAL A  36           
SHEET    4   B 6 LEU A 128  LYS A 138 -1  O  LEU A 128   N  CYS A 107           
SHEET    5   B 6 ARG A  52  LEU A  61 -1  N  PHE A  54   O  GLU A 136           
SHEET    6   B 6 PHE A  77  ASP A  80 -1  O  PHE A  77   N  VAL A  55           
SHEET    1   C 6 VAL B  23  ASP B  24  0                                        
SHEET    2   C 6 VAL B  33  ARG B  39 -1  O  LYS B  35   N  VAL B  23           
SHEET    3   C 6 VAL B 102  CYS B 107 -1  O  HIS B 104   N  VAL B  36           
SHEET    4   C 6 LEU B 128  LYS B 138 -1  O  VAL B 132   N  CYS B 103           
SHEET    5   C 6 ARG B  52  LEU B  61 -1  N  TRP B  60   O  VAL B 129           
SHEET    6   C 6 LYS B  66  SER B  69 -1  O  ASP B  68   N  GLY B  59           
SHEET    1   D 6 VAL B  23  ASP B  24  0                                        
SHEET    2   D 6 VAL B  33  ARG B  39 -1  O  LYS B  35   N  VAL B  23           
SHEET    3   D 6 VAL B 102  CYS B 107 -1  O  HIS B 104   N  VAL B  36           
SHEET    4   D 6 LEU B 128  LYS B 138 -1  O  VAL B 132   N  CYS B 103           
SHEET    5   D 6 ARG B  52  LEU B  61 -1  N  TRP B  60   O  VAL B 129           
SHEET    6   D 6 PHE B  77  ASP B  80 -1  O  PHE B  77   N  VAL B  55           
CISPEP   1 ALA A   16    PRO A   17          0        -0.98                     
CISPEP   2 PRO A  119    PRO A  120          0        -0.42                     
CISPEP   3 PRO B  119    PRO B  120          0        -0.17                     
CRYST1   27.805   58.362   70.904  90.00  98.31  90.00 P 1 21 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      0.035965  0.000000  0.005253        0.00000                         
SCALE2      0.000000  0.017134  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014253        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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