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Database: PDB
Entry: 4EQA
LinkDB: 4EQA
Original site: 4EQA 
HEADER    UNKNOWN FUNCTION                        18-APR-12   4EQA              
TITLE     CRYSTAL STRUCTURE OF PA1844 IN COMPLEX WITH PA1845 FROM PSEUDOMONAS   
TITLE    2 AERUGINOSA PAO1                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: THE TRUNCTION, UNP RESIDUES 6-148;                         
COMPND   5 SYNONYM: PA1844 PROTEIN;                                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;                          
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: THE TRUNCTION, UNP RESIDUES 20-172;                        
COMPND  11 SYNONYM: PA1845 PROTEIN;                                             
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 STRAIN: PAO1;                                                        
SOURCE   5 GENE: PA1844;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE  13 ORGANISM_TAXID: 208964;                                              
SOURCE  14 STRAIN: PAO1;                                                        
SOURCE  15 GENE: PA1845;                                                        
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ORIGAMI    2(DE3);                         
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET21B                                    
KEYWDS    TYPE VI SECRETION, T6S, ANTITOXIN-TOXIN COMPLEX, UNKNOWN FUNCTION     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.SHANG,N.LI,J.ZHANG,D.LU,Q.YU,Y.ZHAO,X.LIU,S.XU,L.GU                 
REVDAT   2   24-JUL-13 4EQA    1       JRNL                                     
REVDAT   1   12-SEP-12 4EQA    0                                                
JRNL        AUTH   G.SHANG,X.LIU,D.LU,J.ZHANG,N.LI,C.ZHU,S.LIU,Q.YU,Y.ZHAO,     
JRNL        AUTH 2 H.ZHANG,J.HU,H.CANG,S.XU,L.GU                                
JRNL        TITL   STRUCTURAL INSIGHT INTO HOW PSEUDOMONAS AERUGINOSA           
JRNL        TITL 2 PEPTIDOGLYCANHYDROLASE TSE1 AND ITS IMMUNITY PROTEIN TSI1    
JRNL        TITL 3 FUNCTION.                                                    
JRNL        REF    BIOCHEM.J.                    V. 448   201 2012              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   22931054                                                     
JRNL        DOI    10.1042/BJ20120668                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 67828                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1967                            
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 27.2245 -  3.8515    0.95     4647   139  0.1519 0.1696        
REMARK   3     2  3.8515 -  3.0584    1.00     4820   144  0.1577 0.1494        
REMARK   3     3  3.0584 -  2.6722    1.00     4801   144  0.1791 0.2403        
REMARK   3     4  2.6722 -  2.4280    1.00     4803   144  0.1820 0.2465        
REMARK   3     5  2.4280 -  2.2541    1.00     4806   143  0.1817 0.2061        
REMARK   3     6  2.2541 -  2.1213    0.99     4774   143  0.1813 0.2303        
REMARK   3     7  2.1213 -  2.0151    1.00     4769   142  0.1901 0.2226        
REMARK   3     8  2.0151 -  1.9274    0.99     4764   144  0.1851 0.2365        
REMARK   3     9  1.9274 -  1.8532    0.98     4720   143  0.1875 0.2412        
REMARK   3    10  1.8532 -  1.7893    0.98     4728   140  0.1883 0.2556        
REMARK   3    11  1.7893 -  1.7333    0.97     4616   139  0.1832 0.2399        
REMARK   3    12  1.7333 -  1.6838    0.97     4674   137  0.1884 0.2102        
REMARK   3    13  1.6838 -  1.6395    0.96     4604   139  0.2031 0.2734        
REMARK   3    14  1.6395 -  1.5995    0.91     4335   126  0.2126 0.2614        
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              : 0.35                                          
REMARK   3   B_SOL              : 45.56                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.130           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.83550                                              
REMARK   3    B22 (A**2) : -3.09470                                             
REMARK   3    B33 (A**2) : 0.25920                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -4.82050                                             
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      :  0.006           4665                                  
REMARK   3   ANGLE     :  0.979           6314                                  
REMARK   3   CHIRALITY :  0.068            664                                  
REMARK   3   PLANARITY :  0.005            842                                  
REMARK   3   DIHEDRAL  : 11.820           1714                                  
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): -11.2997  24.3289 -15.2746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0877 T22:   0.0847                                     
REMARK   3      T33:   0.0958 T12:  -0.0030                                     
REMARK   3      T13:  -0.0070 T23:   0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6273 L22:   0.6258                                     
REMARK   3      L33:   0.4633 L12:  -0.0186                                     
REMARK   3      L13:   0.1819 L23:  -0.0645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0008 S12:   0.0408 S13:  -0.0098                       
REMARK   3      S21:  -0.0976 S22:  -0.0251 S23:   0.1036                       
REMARK   3      S31:   0.0176 S32:   0.0313 S33:   0.0191                       
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 4EQA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071938.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68954                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.10800                            
REMARK 200  R SYM                      (I) : 0.10800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.36400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.900                              
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: 4EQ8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M BIS-TRIS PH 6.5,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
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       49.60200            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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     ALA C   170                                                      
REMARK 465     LYS C   171                                                      
REMARK 465     LYS C   172                                                      
REMARK 465     ALA D   170                                                      
REMARK 465     LYS D   171                                                      
REMARK 465     LYS D   172                                                      
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    SER A  60      -38.39   -134.80                                   
REMARK 500    LYS A 104      -49.58   -140.87                                   
REMARK 500    GLN A 121       46.74   -101.59                                   
REMARK 500    THR B  88      -39.96   -131.68                                   
REMARK 500    LYS B 104      -47.52   -139.40                                   
REMARK 500    GLN B 121       48.87   -105.25                                   
REMARK 500    ASP C  43     -165.32   -124.41                                   
REMARK 500    GLN C 168       61.19     34.23                                   
REMARK 500    ASP D  21      -60.53   -141.89                                   
REMARK 500    ASP D  43     -166.02   -116.58                                   
REMARK 500    ASN D  56       20.89   -151.50                                   
REMARK 500    GLN D 168       56.93     31.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EQ8   RELATED DB: PDB                                   
REMARK 900 THE APO FORM OF PA1844                                               
DBREF  4EQA A    6   148  UNP    Q9I2Q1   Q9I2Q1_PSEAE     6    148             
DBREF  4EQA B    6   148  UNP    Q9I2Q1   Q9I2Q1_PSEAE     6    148             
DBREF  4EQA C   20   172  UNP    Q9I2Q0   Q9I2Q0_PSEAE    20    172             
DBREF  4EQA D   20   172  UNP    Q9I2Q0   Q9I2Q0_PSEAE    20    172             
SEQADV 4EQA SER A    3  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EQA HIS A    4  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EQA MET A    5  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EQA SER B    3  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EQA HIS B    4  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EQA MET B    5  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQRES   1 A  146  SER HIS MET GLN CYS ILE VAL ASN ALA CYS LYS ASN SER          
SEQRES   2 A  146  TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN LYS ASP          
SEQRES   3 A  146  ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA GLU LEU          
SEQRES   4 A  146  GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA MET VAL          
SEQRES   5 A  146  ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA SER GLY          
SEQRES   6 A  146  ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE LEU VAL          
SEQRES   7 A  146  ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS VAL ALA          
SEQRES   8 A  146  VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS TYR PRO          
SEQRES   9 A  146  MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL GLY GLN          
SEQRES  10 A  146  SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP ASN ARG          
SEQRES  11 A  146  THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR SER LEU          
SEQRES  12 A  146  ALA SER CYS                                                  
SEQRES   1 B  146  SER HIS MET GLN CYS ILE VAL ASN ALA CYS LYS ASN SER          
SEQRES   2 B  146  TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN LYS ASP          
SEQRES   3 B  146  ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA GLU LEU          
SEQRES   4 B  146  GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA MET VAL          
SEQRES   5 B  146  ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA SER GLY          
SEQRES   6 B  146  ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE LEU VAL          
SEQRES   7 B  146  ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS VAL ALA          
SEQRES   8 B  146  VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS TYR PRO          
SEQRES   9 B  146  MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL GLY GLN          
SEQRES  10 B  146  SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP ASN ARG          
SEQRES  11 B  146  THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR SER LEU          
SEQRES  12 B  146  ALA SER CYS                                                  
SEQRES   1 C  153  ALA ASP CYS THR PHE THR GLN LEU GLU ILE VAL PRO GLN          
SEQRES   2 C  153  PHE GLY SER PRO ASN MET PHE GLY GLY GLU ASP GLU HIS          
SEQRES   3 C  153  VAL ARG VAL MET PHE SER ASN GLU ASP PRO ASN ASP ASP          
SEQRES   4 C  153  ASN PRO ASP ALA PHE PRO GLU PRO PRO VAL TYR LEU ALA          
SEQRES   5 C  153  ASP ARG ASP SER GLY ASN ASP CYS ARG ILE GLU ASP GLY          
SEQRES   6 C  153  GLY ILE TRP SER ARG GLY GLY VAL PHE LEU SER GLN ASP          
SEQRES   7 C  153  GLY ARG ARG VAL LEU MET HIS GLU PHE SER GLY SER SER          
SEQRES   8 C  153  ALA GLU LEU VAL SER TYR ASP SER ALA THR CYS LYS VAL          
SEQRES   9 C  153  VAL HIS ARG GLU ASP ILE SER GLY GLN ARG TRP ALA VAL          
SEQRES  10 C  153  ASP LYS ASP GLY LEU ARG LEU GLY GLN LYS CYS SER GLY          
SEQRES  11 C  153  GLU SER VAL ASP SER CYS ALA LYS ILE VAL LYS ARG SER          
SEQRES  12 C  153  LEU ALA PRO PHE CYS GLN THR ALA LYS LYS                      
SEQRES   1 D  153  ALA ASP CYS THR PHE THR GLN LEU GLU ILE VAL PRO GLN          
SEQRES   2 D  153  PHE GLY SER PRO ASN MET PHE GLY GLY GLU ASP GLU HIS          
SEQRES   3 D  153  VAL ARG VAL MET PHE SER ASN GLU ASP PRO ASN ASP ASP          
SEQRES   4 D  153  ASN PRO ASP ALA PHE PRO GLU PRO PRO VAL TYR LEU ALA          
SEQRES   5 D  153  ASP ARG ASP SER GLY ASN ASP CYS ARG ILE GLU ASP GLY          
SEQRES   6 D  153  GLY ILE TRP SER ARG GLY GLY VAL PHE LEU SER GLN ASP          
SEQRES   7 D  153  GLY ARG ARG VAL LEU MET HIS GLU PHE SER GLY SER SER          
SEQRES   8 D  153  ALA GLU LEU VAL SER TYR ASP SER ALA THR CYS LYS VAL          
SEQRES   9 D  153  VAL HIS ARG GLU ASP ILE SER GLY GLN ARG TRP ALA VAL          
SEQRES  10 D  153  ASP LYS ASP GLY LEU ARG LEU GLY GLN LYS CYS SER GLY          
SEQRES  11 D  153  GLU SER VAL ASP SER CYS ALA LYS ILE VAL LYS ARG SER          
SEQRES  12 D  153  LEU ALA PRO PHE CYS GLN THR ALA LYS LYS                      
FORMUL   5  HOH   *779(H2 O)                                                    
HELIX    1   1 GLN A    6  TRP A   16  1                                  11    
HELIX    2   2 PRO A   25  ASP A   28  5                                   4    
HELIX    3   3 ASN A   29  GLY A   42  1                                  14    
HELIX    4   4 ASN A   49  TRP A   61  1                                  13    
HELIX    5   5 SER A   66  GLN A   76  1                                  11    
HELIX    6   6 LEU A  100  LYS A  104  5                                   5    
HELIX    7   7 GLY A  115  GLN A  119  5                                   5    
HELIX    8   8 GLY A  127  VAL A  129  5                                   3    
HELIX    9   9 THR A  133  ARG A  137  5                                   5    
HELIX   10  10 GLN B    6  TRP B   16  1                                  11    
HELIX   11  11 SER B   19  GLY B   23  5                                   5    
HELIX   12  12 PRO B   25  ASP B   28  5                                   4    
HELIX   13  13 ASN B   29  GLY B   42  1                                  14    
HELIX   14  14 ASN B   49  TRP B   61  1                                  13    
HELIX   15  15 SER B   66  GLN B   76  1                                  11    
HELIX   16  16 LEU B  100  LYS B  104  5                                   5    
HELIX   17  17 GLY B  115  GLN B  119  5                                   5    
HELIX   18  18 GLY B  127  VAL B  129  5                                   3    
HELIX   19  19 THR B  133  ARG B  137  5                                   5    
HELIX   20  20 SER C  151  ASP C  153  5                                   3    
HELIX   21  21 LEU C  163  GLN C  168  1                                   6    
HELIX   22  22 SER D  151  ASP D  153  5                                   3    
HELIX   23  23 LEU D  163  GLN D  168  1                                   6    
SHEET    1   A 6 THR A  62  LYS A  63  0                                        
SHEET    2   A 6 ASN A 139  VAL A 142 -1  O  VAL A 142   N  THR A  62           
SHEET    3   A 6 VAL A  80  LEU A  84 -1  N  ILE A  81   O  TYR A 141           
SHEET    4   A 6 HIS A  91  VAL A  95 -1  O  VAL A  95   N  VAL A  80           
SHEET    5   A 6 MET A 107  CYS A 110 -1  O  TRP A 109   N  VAL A  94           
SHEET    6   A 6 SER A 120  SER A 125 -1  O  SER A 120   N  CYS A 110           
SHEET    1   B 6 THR B  62  LYS B  63  0                                        
SHEET    2   B 6 ASN B 139  VAL B 142 -1  O  VAL B 142   N  THR B  62           
SHEET    3   B 6 VAL B  80  LEU B  84 -1  N  ILE B  81   O  TYR B 141           
SHEET    4   B 6 HIS B  91  VAL B  95 -1  O  VAL B  95   N  VAL B  80           
SHEET    5   B 6 MET B 107  CYS B 110 -1  O  TRP B 109   N  VAL B  94           
SHEET    6   B 6 SER B 120  SER B 125 -1  O  SER B 120   N  CYS B 110           
SHEET    1   C 3 PHE C  24  GLN C  26  0                                        
SHEET    2   C 3 TRP C  87  SER C  95 -1  O  LEU C  94   N  THR C  25           
SHEET    3   C 3 ALA C  62  PHE C  63 -1  N  PHE C  63   O  TRP C  87           
SHEET    1   D 5 PHE C  24  GLN C  26  0                                        
SHEET    2   D 5 TRP C  87  SER C  95 -1  O  LEU C  94   N  THR C  25           
SHEET    3   D 5 ARG C 100  SER C 107 -1  O  LEU C 102   N  PHE C  93           
SHEET    4   D 5 SER C 110  ASP C 117 -1  O  VAL C 114   N  MET C 103           
SHEET    5   D 5 VAL C 123  ASP C 128 -1  O  VAL C 124   N  SER C 115           
SHEET    1   E 5 VAL C  30  PRO C  31  0                                        
SHEET    2   E 5 MET C  38  GLU C  42 -1  O  GLY C  40   N  VAL C  30           
SHEET    3   E 5 VAL C  46  SER C  51 -1  O  PHE C  50   N  PHE C  39           
SHEET    4   E 5 VAL C  68  ASP C  72 -1  O  TYR C  69   N  MET C  49           
SHEET    5   E 5 ASP C  78  ILE C  81 -1  O  ILE C  81   N  VAL C  68           
SHEET    1   F 3 ARG C 133  ASP C 137  0                                        
SHEET    2   F 3 GLY C 140  CYS C 147 -1  O  GLY C 144   N  ARG C 133           
SHEET    3   F 3 CYS C 155  ARG C 161 -1  O  VAL C 159   N  LEU C 143           
SHEET    1   G 3 PHE D  24  GLN D  26  0                                        
SHEET    2   G 3 TRP D  87  SER D  95 -1  O  LEU D  94   N  THR D  25           
SHEET    3   G 3 ALA D  62  PHE D  63 -1  N  PHE D  63   O  TRP D  87           
SHEET    1   H 5 PHE D  24  GLN D  26  0                                        
SHEET    2   H 5 TRP D  87  SER D  95 -1  O  LEU D  94   N  THR D  25           
SHEET    3   H 5 ARG D 100  SER D 107 -1  O  LEU D 102   N  PHE D  93           
SHEET    4   H 5 SER D 110  ASP D 117 -1  O  VAL D 114   N  MET D 103           
SHEET    5   H 5 VAL D 123  ASP D 128 -1  O  VAL D 124   N  SER D 115           
SHEET    1   I 5 VAL D  30  GLN D  32  0                                        
SHEET    2   I 5 SER D  35  GLU D  42 -1  O  GLY D  40   N  VAL D  30           
SHEET    3   I 5 VAL D  46  SER D  51 -1  O  PHE D  50   N  PHE D  39           
SHEET    4   I 5 VAL D  68  ASP D  72 -1  O  TYR D  69   N  MET D  49           
SHEET    5   I 5 ASP D  78  ILE D  81 -1  O  ILE D  81   N  VAL D  68           
SHEET    1   J 3 ARG D 133  ASP D 137  0                                        
SHEET    2   J 3 GLY D 140  CYS D 147 -1  O  GLY D 144   N  ARG D 133           
SHEET    3   J 3 CYS D 155  ARG D 161 -1  O  ARG D 161   N  LEU D 141           
SSBOND   1 CYS A    7    CYS A  148                          1555   1555  2.04  
SSBOND   2 CYS B    7    CYS B  148                          1555   1555  2.03  
SSBOND   3 CYS C   22    CYS C  167                          1555   1555  2.04  
SSBOND   4 CYS C   79    CYS C  121                          1555   1555  2.04  
SSBOND   5 CYS C  147    CYS C  155                          1555   1555  2.02  
SSBOND   6 CYS D   22    CYS D  167                          1555   1555  2.04  
SSBOND   7 CYS D   79    CYS D  121                          1555   1555  2.05  
SSBOND   8 CYS D  147    CYS D  155                          1555   1555  2.03  
CISPEP   1 PRO C   66    PRO C   67          0         3.43                     
CISPEP   2 GLY C   85    ILE C   86          0        -3.13                     
CISPEP   3 PRO D   66    PRO D   67          0         3.06                     
CISPEP   4 GLY D   85    ILE D   86          0        -3.07                     
CRYST1   48.514   99.204   56.333  90.00  98.82  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      0.020613  0.000000  0.003198        0.00000                         
SCALE2      0.000000  0.010080  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017964        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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