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Database: PDB
Entry: 3SZ6
LinkDB: 3SZ6
Original site: 3SZ6 
HEADER    HEME-BINDING PROTEIN                    18-JUL-11   3SZ6              
TITLE     ISDX1, AN ANTHRAX HEMOPHORE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CONSERVED DOMAIN PROTEIN;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 26-146;                                       
COMPND   5 SYNONYM: IRON TRANSPORT-ASSOCIATED DOMAIN PROTEIN;                   
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;                          
SOURCE   4 ORGANISM_TAXID: 1392;                                                
SOURCE   5 GENE: BAS4443, BA_4788, GBAA_4788;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IG FOLD, HEMOPHORE, HEME-BINDING PROTEIN                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.B.POOR,A.W.MARESSO,F.MURPHY,C.HE                                    
REVDAT   2   28-FEB-24 3SZ6    1       REMARK                                   
REVDAT   1   28-MAR-12 3SZ6    0                                                
JRNL        AUTH   M.T.EKWOROMADU,C.B.POOR,C.P.OWENS,M.A.BALDERAS,M.FABIAN,     
JRNL        AUTH 2 J.S.OLSON,F.MURPHY,E.BALKABASI,E.S.HONSA,C.HE,C.W.GOULDING,  
JRNL        AUTH 3 A.W.MARESSO                                                  
JRNL        TITL   DIFFERENTIAL FUNCTION OF LIP RESIDUES IN THE MECHANISM AND   
JRNL        TITL 2 BIOLOGY OF AN ANTHRAX HEMOPHORE.                             
JRNL        REF    PLOS PATHOG.                  V.   8 02559 2012              
JRNL        REFN                   ISSN 1553-7366                               
JRNL        PMID   22412371                                                     
JRNL        DOI    10.1371/JOURNAL.PPAT.1002559                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.060                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22863                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.120                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2314                            
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 25.5768 -  4.6209    0.98     1309   146  0.2179 0.2249        
REMARK   3     2  4.6209 -  3.6712    0.99     1315   149  0.1683 0.1821        
REMARK   3     3  3.6712 -  3.2081    0.99     1340   154  0.1995 0.2131        
REMARK   3     4  3.2081 -  2.9153    0.98     1291   143  0.2147 0.2244        
REMARK   3     5  2.9153 -  2.7066    0.97     1302   142  0.2375 0.2624        
REMARK   3     6  2.7066 -  2.5471    0.96     1294   139  0.2349 0.2638        
REMARK   3     7  2.5471 -  2.4197    0.95     1252   152  0.2188 0.2554        
REMARK   3     8  2.4197 -  2.3144    0.95     1272   137  0.2223 0.2529        
REMARK   3     9  2.3144 -  2.2254    0.94     1259   146  0.1979 0.2573        
REMARK   3    10  2.2254 -  2.1486    0.96     1259   145  0.2052 0.2327        
REMARK   3    11  2.1486 -  2.0815    0.94     1270   132  0.2035 0.2687        
REMARK   3    12  2.0815 -  2.0220    0.94     1256   135  0.2031 0.2462        
REMARK   3    13  2.0220 -  1.9688    0.90     1169   144  0.2112 0.2584        
REMARK   3    14  1.9688 -  1.9208    0.85     1113   144  0.2092 0.2895        
REMARK   3    15  1.9208 -  1.8771    0.76     1033   114  0.2415 0.3176        
REMARK   3    16  1.8771 -  1.8372    0.70      921    96  0.2857 0.3767        
REMARK   3    17  1.8372 -  1.8004    0.65      894    96  0.2845 0.3512        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.46                                          
REMARK   3   B_SOL              : 61.86                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.400           
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) : 6.34990                                              
REMARK   3    B22 (A**2) : 1.22530                                              
REMARK   3    B33 (A**2) : -7.57520                                             
REMARK   3    B12 (A**2) : 1.86660                                              
REMARK   3    B13 (A**2) : -3.01070                                             
REMARK   3    B23 (A**2) : -6.47710                                             
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      :  0.002           1951                                  
REMARK   3   ANGLE     :  0.566           2632                                  
REMARK   3   CHIRALITY :  0.038            295                                  
REMARK   3   PLANARITY :  0.002            333                                  
REMARK   3   DIHEDRAL  :  8.939            747                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4001   6.4654   2.0083              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1476 T22:   0.1991                                     
REMARK   3      T33:   0.1264 T12:   0.0195                                     
REMARK   3      T13:   0.0035 T23:  -0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9096 L22:   1.0411                                     
REMARK   3      L33:   1.8453 L12:  -0.4783                                     
REMARK   3      L13:  -1.0033 L23:  -0.0750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0374 S12:   0.2103 S13:  -0.0491                       
REMARK   3      S21:  -0.1561 S22:  -0.0901 S23:   0.0094                       
REMARK   3      S31:  -0.0119 S32:  -0.2255 S33:   0.0553                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4469  18.3866 -17.0553              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2246 T22:   0.2031                                     
REMARK   3      T33:   0.1640 T12:   0.0152                                     
REMARK   3      T13:   0.0084 T23:  -0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7070 L22:   0.9070                                     
REMARK   3      L33:   2.4926 L12:   0.4413                                     
REMARK   3      L13:   1.6329 L23:   0.2199                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0489 S12:  -0.2573 S13:   0.0683                       
REMARK   3      S21:   0.2351 S22:  -0.0740 S23:   0.0803                       
REMARK   3      S31:   0.1949 S32:  -0.3673 S33:   0.1073                       
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 3SZ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000066834.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 3.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97929                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24541                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M NACL, 0.1 M CITRIC ACID (PH 3.5) ,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     LYS A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     ALA A    30                                                      
REMARK 465     ASP B    26                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     LYS B    28                                                      
REMARK 465     ALA B    29                                                      
REMARK 465     ALA B    30                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ASP B    48     O    HOH B   169              2.17            
REMARK 500   O    HOH B   206     O    HOH B   210              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET B  55   N     MET B  55   CA     -0.138                       
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    ILE A 133       -1.92    -51.27                                   
REMARK 500    ASN A 135      105.05    -56.60                                   
REMARK 500    ASN B 135       49.35    -88.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 147                 
DBREF  3SZ6 A   26   146  UNP    Q81L44   Q81L44_BACAN    26    146             
DBREF  3SZ6 B   26   146  UNP    Q81L44   Q81L44_BACAN    26    146             
SEQRES   1 A  121  ASP ALA LYS ALA ALA THR LYS LEU ALA ASP GLY LYS TYR          
SEQRES   2 A  121  ASN ILE ALA PHE THR VAL TRP LYS GLY ASP LYS ASP GLU          
SEQRES   3 A  121  SER SER ARG MET ASN ARG TYR PHE GLU SER PRO ALA THR          
SEQRES   4 A  121  LEU THR VAL LYS ASN GLY LYS GLN TYR VAL SER PHE LYS          
SEQRES   5 A  121  VAL LYS ASP SER THR SER ILE LYS SER PHE GLN VAL GLU          
SEQRES   6 A  121  LYS ASP GLY GLN PHE VAL GLU THR THR VAL LEU SER GLU          
SEQRES   7 A  121  ASN LYS LYS ASP ASN THR ARG VAL VAL GLU PHE GLU VAL          
SEQRES   8 A  121  ALA ASP LEU SER LYS LYS LEU ASN GLY LYS VAL LYS ILE          
SEQRES   9 A  121  ASN ILE PRO ILE ILE ASN TYR ASN ALA SER TYR ASP ILE          
SEQRES  10 A  121  ARG PHE VAL PHE                                              
SEQRES   1 B  121  ASP ALA LYS ALA ALA THR LYS LEU ALA ASP GLY LYS TYR          
SEQRES   2 B  121  ASN ILE ALA PHE THR VAL TRP LYS GLY ASP LYS ASP GLU          
SEQRES   3 B  121  SER SER ARG MET ASN ARG TYR PHE GLU SER PRO ALA THR          
SEQRES   4 B  121  LEU THR VAL LYS ASN GLY LYS GLN TYR VAL SER PHE LYS          
SEQRES   5 B  121  VAL LYS ASP SER THR SER ILE LYS SER PHE GLN VAL GLU          
SEQRES   6 B  121  LYS ASP GLY GLN PHE VAL GLU THR THR VAL LEU SER GLU          
SEQRES   7 B  121  ASN LYS LYS ASP ASN THR ARG VAL VAL GLU PHE GLU VAL          
SEQRES   8 B  121  ALA ASP LEU SER LYS LYS LEU ASN GLY LYS VAL LYS ILE          
SEQRES   9 B  121  ASN ILE PRO ILE ILE ASN TYR ASN ALA SER TYR ASP ILE          
SEQRES  10 B  121  ARG PHE VAL PHE                                              
HET     CL  A   1       1                                                       
HET     CL  B   1       1                                                       
HET    GOL  B 147       6                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *161(H2 O)                                                    
HELIX    1   1 SER A   53  PHE A   59  5                                   7    
HELIX    2   2 ASP A   80  THR A   82  5                                   3    
HELIX    3   3 SER B   53  TYR B   58  5                                   6    
HELIX    4   4 ASP B   80  THR B   82  5                                   3    
SHEET    1   A 5 GLY A  36  ILE A  40  0                                        
SHEET    2   A 5 ALA A  63  LYS A  68 -1  O  LEU A  65   N  TYR A  38           
SHEET    3   A 5 LYS A  71  VAL A  78 -1  O  SER A  75   N  THR A  64           
SHEET    4   A 5 THR A 109  GLU A 115 -1  O  ARG A 110   N  VAL A  78           
SHEET    5   A 5 THR A  99  ASN A 104 -1  N  ASN A 104   O  THR A 109           
SHEET    1   B 5 THR A  43  LYS A  46  0                                        
SHEET    2   B 5 ASN A 137  VAL A 145 -1  O  ARG A 143   N  TRP A  45           
SHEET    3   B 5 LEU A 123  ASN A 130 -1  N  VAL A 127   O  TYR A 140           
SHEET    4   B 5 ILE A  84  GLU A  90 -1  N  GLN A  88   O  LYS A 126           
SHEET    5   B 5 PHE A  95  GLU A  97 -1  O  VAL A  96   N  VAL A  89           
SHEET    1   C 5 GLY B  36  ILE B  40  0                                        
SHEET    2   C 5 ALA B  63  LYS B  68 -1  O  LEU B  65   N  TYR B  38           
SHEET    3   C 5 LYS B  71  VAL B  78 -1  O  SER B  75   N  THR B  64           
SHEET    4   C 5 THR B 109  GLU B 115 -1  O  ARG B 110   N  VAL B  78           
SHEET    5   C 5 THR B  99  ASN B 104 -1  N  ASN B 104   O  THR B 109           
SHEET    1   D 5 THR B  43  LYS B  46  0                                        
SHEET    2   D 5 TYR B 136  VAL B 145 -1  O  ARG B 143   N  TRP B  45           
SHEET    3   D 5 LEU B 123  ILE B 131 -1  N  ILE B 129   O  ALA B 138           
SHEET    4   D 5 ILE B  84  LYS B  91 -1  N  LYS B  85   O  LYS B 128           
SHEET    5   D 5 GLN B  94  GLU B  97 -1  O  GLN B  94   N  LYS B  91           
CISPEP   1 SER A   61    PRO A   62          0         2.31                     
CISPEP   2 SER B   61    PRO B   62          0         4.21                     
SITE     1 AC1  3 LYS A 122  ARG A 143  ALA B  41                               
SITE     1 AC2  2 ALA A  41  ARG B 143                                          
SITE     1 AC3  9 LYS B  85  SER B  86  PHE B  87  GLU B  97                    
SITE     2 AC3  9 THR B  98  VAL B 100  ARG B 110  VAL B 112                    
SITE     3 AC3  9 HOH B 191                                                     
CRYST1   36.637   43.659   47.408  99.24  96.53 107.35 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.027295  0.008529  0.004977        0.00000                         
SCALE2      0.000000  0.023997  0.005027        0.00000                         
SCALE3      0.000000  0.000000  0.021692        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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