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Database: PDB
Entry: 4MJH
LinkDB: 4MJH
Original site: 4MJH 
HEADER    CHAPERONE                               03-SEP-13   4MJH              
TITLE     HUMAN HSP27 CORE DOMAIN IN COMPLEX WITH C-TERMINAL PEPTIDE            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN BETA-1;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: CORE DOMAIN (UNP RESIDUES 84-176);                         
COMPND   5 SYNONYM: HSPB1, 28 KDA HEAT SHOCK PROTEIN, ESTROGEN-REGULATED 24 KDA 
COMPND   6 PROTEIN, HEAT SHOCK 27 KDA PROTEIN, HSP 27, STRESS-RESPONSIVE PROTEIN
COMPND   7 27, SRP27;                                                           
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: HEAT SHOCK PROTEIN BETA-1;                                 
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: C-TERMINAL PEPTIDE (UNP RESIDUES 179-186);                 
COMPND  13 SYNONYM: HSPB1, 28 KDA HEAT SHOCK PROTEIN, ESTROGEN-REGULATED 24 KDA 
COMPND  14 PROTEIN, HEAT SHOCK 27 KDA PROTEIN, HSP 27, STRESS-RESPONSIVE PROTEIN
COMPND  15 27, SRP27;                                                           
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HSP27, HSP28, HSPB1;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) ROSETTA 2;                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606                                                 
KEYWDS    SMALL HEAT SHOCK PROTEIN, CANCER, AMYLOID, CHAPERONE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.LAGANOWSKY,D.CASCIO,M.R.SAWAYA,D.EISENBERG                          
REVDAT   3   11-OCT-17 4MJH    1       REMARK                                   
REVDAT   2   14-MAY-14 4MJH    1       JRNL                                     
REVDAT   1   09-APR-14 4MJH    0                                                
JRNL        AUTH   G.K.HOCHBERG,H.ECROYD,C.LIU,D.COX,D.CASCIO,M.R.SAWAYA,       
JRNL        AUTH 2 M.P.COLLIER,J.STROUD,J.A.CARVER,A.J.BALDWIN,C.V.ROBINSON,    
JRNL        AUTH 3 D.S.EISENBERG,J.L.BENESCH,A.LAGANOWSKY                       
JRNL        TITL   THE STRUCTURED CORE DOMAIN OF ALPHA B-CRYSTALLIN CAN PREVENT 
JRNL        TITL 2 AMYLOID FIBRILLATION AND ASSOCIATED TOXICITY.                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111 E1562 2014              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24711386                                                     
JRNL        DOI    10.1073/PNAS.1322673111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.1_1168                                    
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.05                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.390                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 5308                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.236                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 265                             
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 37.0533 -  3.2741    0.99     2564   135  0.2203 0.2407        
REMARK   3     2  3.2741 -  2.5990    0.98     2479   130  0.2767 0.3486        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.120           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.45                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.47                          
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  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           1426                                  
REMARK   3   ANGLE     :  0.995           1942                                  
REMARK   3   CHIRALITY :  0.074            230                                  
REMARK   3   PLANARITY :  0.005            249                                  
REMARK   3   DIHEDRAL  : 16.408            528                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9978  26.0768  52.2274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2497 T22:   0.2187                                     
REMARK   3      T33:   0.3122 T12:   0.0496                                     
REMARK   3      T13:   0.0102 T23:   0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4067 L22:   0.9515                                     
REMARK   3      L33:   2.7307 L12:   0.4901                                     
REMARK   3      L13:  -0.4452 L23:  -0.5670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0432 S12:  -0.0808 S13:  -0.2013                       
REMARK   3      S21:   0.0428 S22:  -0.0142 S23:   0.0298                       
REMARK   3      S31:   0.0243 S32:   0.0645 S33:   0.0975                       
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 4MJH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000081987.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-MAR-11                          
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 FR-E+ DW                    
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CONFOCAL VARIMAX HF                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5331                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.599                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.050                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.2100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.180                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
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   (%): 36.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.5, 0.2 M MAGNESIUM      
REMARK 280  CHLORIDE, 30% PEG4000, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 298K                                                    
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       24.48000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 830 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 5750 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 850 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 5650 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     GLY A    84                                                      
REMARK 465     LYS A   171                                                      
REMARK 465     LEU A   172                                                      
REMARK 465     ALA A   173                                                      
REMARK 465     THR A   174                                                      
REMARK 465     GLN A   175                                                      
REMARK 465     SER A   176                                                      
REMARK 465     GLU B   186                                                      
REMARK 465     GLY C    84                                                      
REMARK 465     VAL C    85                                                      
REMARK 465     HIS C    90                                                      
REMARK 465     THR C    91                                                      
REMARK 465     ALA C    92                                                      
REMARK 465     ASP C    93                                                      
REMARK 465     PRO C   170                                                      
REMARK 465     LYS C   171                                                      
REMARK 465     LEU C   172                                                      
REMARK 465     ALA C   173                                                      
REMARK 465     THR C   174                                                      
REMARK 465     GLN C   175                                                      
REMARK 465     SER C   176                                                      
REMARK 465     GLU D   186                                                      
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     GLU A  87    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 185    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     GLU C  87    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  89    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE D 185    CG   CD1  CD2  CE1  CE2  CZ                         
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   OG1  THR C   110     OG1  THR C   121              2.18            
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    ARG A  94      112.23   -166.93                                   
REMARK 500    ASP A 115       70.57     37.42                                   
REMARK 500    ASP A 129     -164.19   -129.26                                   
REMARK 500    ASP C 129     -159.37   -135.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4MJH A   84   176  UNP    P04792   HSPB1_HUMAN     84    176             
DBREF  4MJH B  179   186  UNP    P04792   HSPB1_HUMAN    179    186             
DBREF  4MJH C   84   176  UNP    P04792   HSPB1_HUMAN     84    176             
DBREF  4MJH D  179   186  UNP    P04792   HSPB1_HUMAN    179    186             
SEQRES   1 A   93  GLY VAL SER GLU ILE ARG HIS THR ALA ASP ARG TRP ARG          
SEQRES   2 A   93  VAL SER LEU ASP VAL ASN HIS PHE ALA PRO ASP GLU LEU          
SEQRES   3 A   93  THR VAL LYS THR LYS ASP GLY VAL VAL GLU ILE THR GLY          
SEQRES   4 A   93  LYS HIS GLU GLU ARG GLN ASP GLU HIS GLY TYR ILE SER          
SEQRES   5 A   93  ARG CYS PHE THR ARG LYS TYR THR LEU PRO PRO GLY VAL          
SEQRES   6 A   93  ASP PRO THR GLN VAL SER SER SER LEU SER PRO GLU GLY          
SEQRES   7 A   93  THR LEU THR VAL GLU ALA PRO MET PRO LYS LEU ALA THR          
SEQRES   8 A   93  GLN SER                                                      
SEQRES   1 B    8  ILE THR ILE PRO VAL THR PHE GLU                              
SEQRES   1 C   93  GLY VAL SER GLU ILE ARG HIS THR ALA ASP ARG TRP ARG          
SEQRES   2 C   93  VAL SER LEU ASP VAL ASN HIS PHE ALA PRO ASP GLU LEU          
SEQRES   3 C   93  THR VAL LYS THR LYS ASP GLY VAL VAL GLU ILE THR GLY          
SEQRES   4 C   93  LYS HIS GLU GLU ARG GLN ASP GLU HIS GLY TYR ILE SER          
SEQRES   5 C   93  ARG CYS PHE THR ARG LYS TYR THR LEU PRO PRO GLY VAL          
SEQRES   6 C   93  ASP PRO THR GLN VAL SER SER SER LEU SER PRO GLU GLY          
SEQRES   7 C   93  THR LEU THR VAL GLU ALA PRO MET PRO LYS LEU ALA THR          
SEQRES   8 C   93  GLN SER                                                      
SEQRES   1 D    8  ILE THR ILE PRO VAL THR PHE GLU                              
FORMUL   5  HOH   *(H2 O)                                                       
HELIX    1   1 ALA A  105  ASP A  107  5                                   3    
HELIX    2   2 ALA C  105  ASP C  107  5                                   3    
SHEET    1   A 4 SER A  86  ILE A  88  0                                        
SHEET    2   A 4 ARG A  94  ASP A 100 -1  O  SER A  98   N  GLU A  87           
SHEET    3   A 4 THR A 162  PRO A 168 -1  O  LEU A 163   N  LEU A  99           
SHEET    4   A 4 SER A 154  LEU A 157 -1  N  SER A 156   O  THR A 164           
SHEET    1   B 6 LEU A 109  LYS A 114  0                                        
SHEET    2   B 6 VAL A 117  GLN A 128 -1  O  GLU A 119   N  LYS A 112           
SHEET    3   B 6 TYR A 133  THR A 143 -1  O  ARG A 140   N  ILE A 120           
SHEET    4   B 6 TYR C 133  THR C 143 -1  O  CYS C 137   N  CYS A 137           
SHEET    5   B 6 VAL C 117  GLN C 128 -1  N  ILE C 120   O  ARG C 140           
SHEET    6   B 6 LEU C 109  LYS C 114 -1  N  LYS C 112   O  GLU C 119           
SHEET    1   C 4 ILE C  88  ARG C  89  0                                        
SHEET    2   C 4 TRP C  95  ASP C 100 -1  O  ARG C  96   N  ARG C  89           
SHEET    3   C 4 THR C 162  ALA C 167 -1  O  ALA C 167   N  TRP C  95           
SHEET    4   C 4 SER C 154  LEU C 157 -1  N  SER C 154   O  GLU C 166           
CRYST1   31.280   48.960   57.540  90.00  99.95  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      0.031969  0.000000  0.005609        0.00000                         
SCALE2      0.000000  0.020425  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017645        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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