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Database: PDB
Entry: 4FQB
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Original site: 4FQB 
HEADER    TOXIN/IMMUNE SYSTEM                     25-JUN-12   4FQB              
TITLE     CRYSTAL STRUCTURE OF TOXIC EFFECTOR TSE1 IN COMPLEX WITH IMMUNE       
TITLE    2 PROTEIN TSI1                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TOXIC EFFECTOR TSE1;                                       
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: IMMUNE PROTEIN TSI1;                                       
COMPND   7 CHAIN: B, D, F, H;                                                   
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PAO1;                    
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 GENE: PA1844;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET29B(+);                                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PAO1;                    
SOURCE  12 ORGANISM_TAXID: 208964;                                              
SOURCE  13 GENE: PA1845;                                                        
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;                                  
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET29B(+)                                 
KEYWDS    BETA SHEET, TOXIC EFFECTOR WITH IMMUNE PROTEIN, TOXIN-IMMUNE SYSTEM   
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.WANG,L.LI,W.ZHANG                                                   
REVDAT   1   26-JUN-13 4FQB    0                                                
JRNL        AUTH   L.LI,W.ZHANG,T.WANG                                          
JRNL        TITL   STRUCTURAL BASIS OF TSE1 IN COMPLEX WITH TSI1                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 40994                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2201                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.69                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2899                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 134                          
REMARK   3   BIN FREE R VALUE                    : 0.4570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8932                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 72                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 83.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.56000                                              
REMARK   3    B22 (A**2) : 1.56000                                              
REMARK   3    B33 (A**2) : -2.34000                                             
REMARK   3    B12 (A**2) : 0.78000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.774         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.323         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.250         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.308        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9169 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12415 ; 1.810 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1174 ; 6.525 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   430 ;32.733 ;24.326       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1467 ;18.174 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    64 ;20.620 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1306 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7128 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   149                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2370 -17.0670 -33.5480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4024 T22:   0.4209                                     
REMARK   3      T33:   0.3990 T12:  -0.3558                                     
REMARK   3      T13:   0.0838 T23:   0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8868 L22:   7.4654                                     
REMARK   3      L33:   6.5970 L12:  -0.9865                                     
REMARK   3      L13:  -1.8476 L23:   2.6604                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0870 S12:   0.6019 S13:   0.0979                       
REMARK   3      S21:  -0.6482 S22:   0.2541 S23:  -1.5374                       
REMARK   3      S31:  -0.1368 S32:   0.4470 S33:  -0.1671                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    21        B   169                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.6740  -7.2440 -12.9780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3931 T22:   0.2662                                     
REMARK   3      T33:   0.0442 T12:  -0.2794                                     
REMARK   3      T13:  -0.1004 T23:   0.0589                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5528 L22:   6.2650                                     
REMARK   3      L33:   6.4061 L12:   0.8755                                     
REMARK   3      L13:  -1.4692 L23:  -0.6632                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0121 S12:  -0.2098 S13:   0.2873                       
REMARK   3      S21:   0.3645 S22:   0.0326 S23:  -0.0334                       
REMARK   3      S31:  -0.1959 S32:  -0.2898 S33:  -0.0447                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     4        C   149                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.8380  44.3090 -19.0860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3970 T22:   0.4386                                     
REMARK   3      T33:   0.7551 T12:  -0.2547                                     
REMARK   3      T13:   0.1711 T23:   0.0506                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8639 L22:   7.2683                                     
REMARK   3      L33:   3.8023 L12:  -1.2121                                     
REMARK   3      L13:   0.6510 L23:  -1.0588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0163 S12:   0.3098 S13:   0.2031                       
REMARK   3      S21:   0.2381 S22:   0.1204 S23:   1.6712                       
REMARK   3      S31:   0.0269 S32:  -0.8780 S33:  -0.1368                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    23        D   169                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.8690  30.2040 -14.7460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4071 T22:   0.1630                                     
REMARK   3      T33:   0.1023 T12:  -0.2332                                     
REMARK   3      T13:   0.0917 T23:  -0.0503                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2301 L22:   3.8213                                     
REMARK   3      L33:   4.7209 L12:   1.5017                                     
REMARK   3      L13:   1.1079 L23:  -0.1686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1256 S12:   0.1577 S13:  -0.3354                       
REMARK   3      S21:   0.0866 S22:   0.0103 S23:  -0.0133                       
REMARK   3      S31:   0.0794 S32:   0.2416 S33:  -0.1359                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     4        E   149                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3670 -48.6180 -35.8070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4120 T22:   0.4213                                     
REMARK   3      T33:   0.5262 T12:  -0.2728                                     
REMARK   3      T13:  -0.0122 T23:   0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.5922 L22:   8.5332                                     
REMARK   3      L33:   5.5325 L12:   3.8473                                     
REMARK   3      L13:   2.0863 L23:   2.1384                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1070 S12:   0.0699 S13:  -0.4654                       
REMARK   3      S21:   0.2936 S22:  -0.0855 S23:  -1.3376                       
REMARK   3      S31:   0.2439 S32:   0.7459 S33:   0.1925                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    23        F   169                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.3420 -53.1350 -41.8160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3674 T22:   0.2400                                     
REMARK   3      T33:   0.0724 T12:  -0.2519                                     
REMARK   3      T13:   0.0872 T23:  -0.1128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1623 L22:   4.8620                                     
REMARK   3      L33:   5.4121 L12:  -1.4248                                     
REMARK   3      L13:  -0.0990 L23:  -0.4032                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0060 S12:   0.3113 S13:  -0.0255                       
REMARK   3      S21:  -0.0222 S22:  -0.1797 S23:   0.0056                       
REMARK   3      S31:   0.0851 S32:  -0.1632 S33:   0.1857                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     4        G   149                          
REMARK   3    ORIGIN FOR THE GROUP (A): -51.9830  -9.3740 -13.4720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6507 T22:   0.4743                                     
REMARK   3      T33:   0.6637 T12:  -0.0518                                     
REMARK   3      T13:   0.2812 T23:   0.0755                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1217 L22:   7.4567                                     
REMARK   3      L33:   7.0123 L12:   2.4275                                     
REMARK   3      L13:  -4.0326 L23:  -0.8690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0600 S12:  -0.3394 S13:   0.6226                       
REMARK   3      S21:   0.8681 S22:   0.0184 S23:   1.4206                       
REMARK   3      S31:  -0.3111 S32:  -0.6462 S33:  -0.0784                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    23        H   169                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.1840  -0.3910 -30.6150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2913 T22:   0.2468                                     
REMARK   3      T33:   0.1643 T12:  -0.1104                                     
REMARK   3      T13:  -0.0579 T23:   0.1405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2616 L22:   4.3057                                     
REMARK   3      L33:   6.8302 L12:   0.6660                                     
REMARK   3      L13:  -0.9405 L23:  -0.4300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0121 S12:   0.1207 S13:   0.6781                       
REMARK   3      S21:   0.4520 S22:  -0.0054 S23:   0.2560                       
REMARK   3      S31:  -0.6271 S32:   0.0144 S33:  -0.0068                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4FQB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073221.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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) : 1.0090                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43188                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.10000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4FQA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CITRATE, 20% V/V 2-         
REMARK 280  PROPANOL, 20% W/V PEG4000,1MM DTT, 3% V/V ETHYLENE GLYCOL, PH       
REMARK 280  5.6, VAPOR DIFFUSION, TEMPERATURE 293K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      195.53400            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       97.76700            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       97.76700            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      195.53400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: 1:1 IN COMPLEX WITH TSI1                                     
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: 2090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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: 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: 2030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 1950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: 4                                                       
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: 2090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     LEU A   150                                                      
REMARK 465     PRO A   151                                                      
REMARK 465     ARG A   152                                                      
REMARK 465     ALA A   153                                                      
REMARK 465     SER A   154                                                      
REMARK 465     LEU A   155                                                      
REMARK 465     GLU A   156                                                      
REMARK 465     HIS A   157                                                      
REMARK 465     HIS A   158                                                      
REMARK 465     HIS A   159                                                      
REMARK 465     HIS A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     HIS A   162                                                      
REMARK 465     MET B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     ASP B    21                                                      
REMARK 465     ALA B   170                                                      
REMARK 465     LYS B   171                                                      
REMARK 465     LYS B   172                                                      
REMARK 465     LEU B   173                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     HIS B   175                                                      
REMARK 465     HIS B   176                                                      
REMARK 465     HIS B   177                                                      
REMARK 465     HIS B   178                                                      
REMARK 465     HIS B   179                                                      
REMARK 465     HIS B   180                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     LEU C   150                                                      
REMARK 465     PRO C   151                                                      
REMARK 465     ARG C   152                                                      
REMARK 465     ALA C   153                                                      
REMARK 465     SER C   154                                                      
REMARK 465     LEU C   155                                                      
REMARK 465     GLU C   156                                                      
REMARK 465     HIS C   157                                                      
REMARK 465     HIS C   158                                                      
REMARK 465     HIS C   159                                                      
REMARK 465     HIS C   160                                                      
REMARK 465     HIS C   161                                                      
REMARK 465     HIS C   162                                                      
REMARK 465     MET D    19                                                      
REMARK 465     ALA D    20                                                      
REMARK 465     ASP D    21                                                      
REMARK 465     ALA D   170                                                      
REMARK 465     LYS D   171                                                      
REMARK 465     LYS D   172                                                      
REMARK 465     LEU D   173                                                      
REMARK 465     GLU D   174                                                      
REMARK 465     HIS D   175                                                      
REMARK 465     HIS D   176                                                      
REMARK 465     HIS D   177                                                      
REMARK 465     HIS D   178                                                      
REMARK 465     HIS D   179                                                      
REMARK 465     HIS D   180                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ASP E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     LEU E   150                                                      
REMARK 465     PRO E   151                                                      
REMARK 465     ARG E   152                                                      
REMARK 465     ALA E   153                                                      
REMARK 465     SER E   154                                                      
REMARK 465     LEU E   155                                                      
REMARK 465     GLU E   156                                                      
REMARK 465     HIS E   157                                                      
REMARK 465     HIS E   158                                                      
REMARK 465     HIS E   159                                                      
REMARK 465     HIS E   160                                                      
REMARK 465     HIS E   161                                                      
REMARK 465     HIS E   162                                                      
REMARK 465     MET F    19                                                      
REMARK 465     ALA F    20                                                      
REMARK 465     ASP F    21                                                      
REMARK 465     ALA F   170                                                      
REMARK 465     LYS F   171                                                      
REMARK 465     LYS F   172                                                      
REMARK 465     LEU F   173                                                      
REMARK 465     GLU F   174                                                      
REMARK 465     HIS F   175                                                      
REMARK 465     HIS F   176                                                      
REMARK 465     HIS F   177                                                      
REMARK 465     HIS F   178                                                      
REMARK 465     HIS F   179                                                      
REMARK 465     HIS F   180                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ASP G     2                                                      
REMARK 465     SER G     3                                                      
REMARK 465     LEU G   150                                                      
REMARK 465     PRO G   151                                                      
REMARK 465     ARG G   152                                                      
REMARK 465     ALA G   153                                                      
REMARK 465     SER G   154                                                      
REMARK 465     LEU G   155                                                      
REMARK 465     GLU G   156                                                      
REMARK 465     HIS G   157                                                      
REMARK 465     HIS G   158                                                      
REMARK 465     HIS G   159                                                      
REMARK 465     HIS G   160                                                      
REMARK 465     HIS G   161                                                      
REMARK 465     HIS G   162                                                      
REMARK 465     MET H    19                                                      
REMARK 465     ALA H    20                                                      
REMARK 465     ASP H    21                                                      
REMARK 465     ALA H   170                                                      
REMARK 465     LYS H   171                                                      
REMARK 465     LYS H   172                                                      
REMARK 465     LEU H   173                                                      
REMARK 465     GLU H   174                                                      
REMARK 465     HIS H   175                                                      
REMARK 465     HIS H   176                                                      
REMARK 465     HIS H   177                                                      
REMARK 465     HIS H   178                                                      
REMARK 465     HIS H   179                                                      
REMARK 465     HIS H   180                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     SER A   15   OG                                                  
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   NH1  ARG F    99     O    GLN F   168              2.04            
REMARK 500   O    SER F   151     OG   SER F   154              2.05            
REMARK 500   O    ALA G   146     O    CYS G   148              2.11            
REMARK 500   ND2  ASN C    14     OE2  GLU C    40              2.13            
REMARK 500   O    CYS E     7     N    ASN E    10              2.14            
REMARK 500   OE1  GLU F    42     NH2  ARG F    47              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    PHE D    33     OG   SER D    35     4555     2.12            
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    GLU B  28   CD    GLU B  28   OE1     0.075                       
REMARK 500    TRP D 134   CE2   TRP D 134   CD2     0.084                       
REMARK 500    HIS F 125   CG    HIS F 125   CD2     0.055                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    PRO A  44   C   -  N   -  CD  ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ARG A 137   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B  47   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    GLY B  85   N   -  CA  -  C   ANGL. DEV. = -22.2 DEGREES          
REMARK 500    ARG B 133   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    CYS C   7   CB  -  CA  -  C   ANGL. DEV. = -14.1 DEGREES          
REMARK 500    CYS C 148   N   -  CA  -  CB  ANGL. DEV. = -18.4 DEGREES          
REMARK 500    GLY D  85   N   -  CA  -  C   ANGL. DEV. = -19.5 DEGREES          
REMARK 500    LEU E 145   CA  -  CB  -  CG  ANGL. DEV. = -17.0 DEGREES          
REMARK 500    GLY F  85   N   -  CA  -  C   ANGL. DEV. = -17.9 DEGREES          
REMARK 500    GLY F  90   C   -  N   -  CA  ANGL. DEV. = -13.6 DEGREES          
REMARK 500    PRO G  44   C   -  N   -  CD  ANGL. DEV. = -16.9 DEGREES          
REMARK 500    PRO H  36   C   -  N   -  CD  ANGL. DEV. = -16.6 DEGREES          
REMARK 500    GLN H 145   CB  -  CA  -  C   ANGL. DEV. = -39.0 DEGREES          
REMARK 500    GLN H 145   N   -  CA  -  C   ANGL. DEV. =  24.7 DEGREES          
REMARK 500    LYS H 146   N   -  CA  -  C   ANGL. DEV. = -30.8 DEGREES          
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    GLN A   6      -71.80    -38.73                                   
REMARK 500    CYS A   7      -36.92    -36.24                                   
REMARK 500    ALA A  22     -131.01     51.39                                   
REMARK 500    THR A  88      -73.84   -103.21                                   
REMARK 500    LYS A 104      -30.01   -143.41                                   
REMARK 500    GLN A 121       47.79   -103.06                                   
REMARK 500    ALA A 146       96.21    -68.91                                   
REMARK 500    SER B 107      114.83   -165.14                                   
REMARK 500    HIS B 125      143.90   -171.07                                   
REMARK 500    ALA B 156      -72.18    -63.56                                   
REMARK 500    ALA C  22     -119.61     46.46                                   
REMARK 500    ASN C  49     -167.62    -78.49                                   
REMARK 500    THR C  88      -67.34   -109.37                                   
REMARK 500    GLN C 103       -0.30     75.23                                   
REMARK 500    GLN C 121       46.48   -105.65                                   
REMARK 500    ARG C 135      -38.35    -36.92                                   
REMARK 500    SER D 107      115.23   -160.03                                   
REMARK 500    CYS D 121        7.04     56.00                                   
REMARK 500    ASP D 137     -154.00   -129.04                                   
REMARK 500    CYS E   7      -87.94    -49.36                                   
REMARK 500    ILE E   8      -71.68    -15.82                                   
REMARK 500    TYR E  20      -38.60    -39.06                                   
REMARK 500    ALA E  22     -134.42     52.65                                   
REMARK 500    THR E  88      -62.55   -102.26                                   
REMARK 500    LYS E 104      -32.53   -131.90                                   
REMARK 500    GLN E 121       50.15    -98.83                                   
REMARK 500    ASP F 137     -152.14   -127.59                                   
REMARK 500    LYS F 146       63.01     60.13                                   
REMARK 500    CYS F 167      132.71   -171.47                                   
REMARK 500    TYR G  20      -38.09    -35.78                                   
REMARK 500    ALA G  22     -134.48     49.77                                   
REMARK 500    ASN G  49     -169.55    -73.92                                   
REMARK 500    THR G  88      -75.18   -103.28                                   
REMARK 500    LYS G 104      -25.74   -146.69                                   
REMARK 500    GLN G 121       50.81   -106.18                                   
REMARK 500    ASN H  37        1.58     83.54                                   
REMARK 500    ASP H  43     -163.27   -129.53                                   
REMARK 500    ASP H 137     -152.52   -127.53                                   
REMARK 500    GLN H 145       78.24   -152.12                                   
REMARK 500    LYS H 146       99.84    169.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY B   90     GLY B   91                  137.34                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER C 147        18.8      L          L   OUTSIDE RANGE           
REMARK 500    GLN H 145        25.0      L          L   OUTSIDE RANGE           
REMARK 500    LYS H 146        50.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 202        DISTANCE =  5.29 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FQA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TOXIC EFFECTOR TSE1                             
DBREF  4FQB A    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4FQB B   20   172  UNP    Q9I2Q0   Q9I2Q0_PSEAE    20    172             
DBREF  4FQB C    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4FQB D   20   172  UNP    Q9I2Q0   Q9I2Q0_PSEAE    20    172             
DBREF  4FQB E    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4FQB F   20   172  UNP    Q9I2Q0   Q9I2Q0_PSEAE    20    172             
DBREF  4FQB G    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4FQB H   20   172  UNP    Q9I2Q0   Q9I2Q0_PSEAE    20    172             
SEQADV 4FQB LEU A  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB GLU A  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS A  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS A  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS A  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS A  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS A  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS A  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB MET B   19  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB LEU B  173  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB GLU B  174  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS B  175  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS B  176  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS B  177  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS B  178  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS B  179  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS B  180  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB LEU C  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB GLU C  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS C  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS C  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS C  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS C  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS C  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS C  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB MET D   19  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB LEU D  173  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB GLU D  174  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS D  175  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS D  176  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS D  177  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS D  178  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS D  179  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS D  180  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB LEU E  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB GLU E  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS E  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS E  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS E  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS E  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS E  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS E  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB MET F   19  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB LEU F  173  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB GLU F  174  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS F  175  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS F  176  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS F  177  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS F  178  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS F  179  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS F  180  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB LEU G  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB GLU G  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS G  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS G  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS G  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS G  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS G  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB HIS G  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4FQB MET H   19  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB LEU H  173  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB GLU H  174  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS H  175  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS H  176  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS H  177  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS H  178  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS H  179  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQADV 4FQB HIS H  180  UNP  Q9I2Q0              EXPRESSION TAG                 
SEQRES   1 A  162  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 A  162  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 A  162  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 A  162  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 A  162  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 A  162  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 A  162  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 A  162  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 A  162  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 A  162  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 A  162  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 A  162  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER LEU GLU          
SEQRES  13 A  162  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  162  MET ALA ASP CYS THR PHE THR GLN LEU GLU ILE VAL PRO          
SEQRES   2 B  162  GLN PHE GLY SER PRO ASN MET PHE GLY GLY GLU ASP GLU          
SEQRES   3 B  162  HIS VAL ARG VAL MET PHE SER ASN GLU ASP PRO ASN ASP          
SEQRES   4 B  162  ASP ASN PRO ASP ALA PHE PRO GLU PRO PRO VAL TYR LEU          
SEQRES   5 B  162  ALA ASP ARG ASP SER GLY ASN ASP CYS ARG ILE GLU ASP          
SEQRES   6 B  162  GLY GLY ILE TRP SER ARG GLY GLY VAL PHE LEU SER GLN          
SEQRES   7 B  162  ASP GLY ARG ARG VAL LEU MET HIS GLU PHE SER GLY SER          
SEQRES   8 B  162  SER ALA GLU LEU VAL SER TYR ASP SER ALA THR CYS LYS          
SEQRES   9 B  162  VAL VAL HIS ARG GLU ASP ILE SER GLY GLN ARG TRP ALA          
SEQRES  10 B  162  VAL ASP LYS ASP GLY LEU ARG LEU GLY GLN LYS CYS SER          
SEQRES  11 B  162  GLY GLU SER VAL ASP SER CYS ALA LYS ILE VAL LYS ARG          
SEQRES  12 B  162  SER LEU ALA PRO PHE CYS GLN THR ALA LYS LYS LEU GLU          
SEQRES  13 B  162  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 C  162  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 C  162  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 C  162  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 C  162  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 C  162  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 C  162  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 C  162  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 C  162  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 C  162  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 C  162  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 C  162  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 C  162  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER LEU GLU          
SEQRES  13 C  162  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 D  162  MET ALA ASP CYS THR PHE THR GLN LEU GLU ILE VAL PRO          
SEQRES   2 D  162  GLN PHE GLY SER PRO ASN MET PHE GLY GLY GLU ASP GLU          
SEQRES   3 D  162  HIS VAL ARG VAL MET PHE SER ASN GLU ASP PRO ASN ASP          
SEQRES   4 D  162  ASP ASN PRO ASP ALA PHE PRO GLU PRO PRO VAL TYR LEU          
SEQRES   5 D  162  ALA ASP ARG ASP SER GLY ASN ASP CYS ARG ILE GLU ASP          
SEQRES   6 D  162  GLY GLY ILE TRP SER ARG GLY GLY VAL PHE LEU SER GLN          
SEQRES   7 D  162  ASP GLY ARG ARG VAL LEU MET HIS GLU PHE SER GLY SER          
SEQRES   8 D  162  SER ALA GLU LEU VAL SER TYR ASP SER ALA THR CYS LYS          
SEQRES   9 D  162  VAL VAL HIS ARG GLU ASP ILE SER GLY GLN ARG TRP ALA          
SEQRES  10 D  162  VAL ASP LYS ASP GLY LEU ARG LEU GLY GLN LYS CYS SER          
SEQRES  11 D  162  GLY GLU SER VAL ASP SER CYS ALA LYS ILE VAL LYS ARG          
SEQRES  12 D  162  SER LEU ALA PRO PHE CYS GLN THR ALA LYS LYS LEU GLU          
SEQRES  13 D  162  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 E  162  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 E  162  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 E  162  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 E  162  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 E  162  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 E  162  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 E  162  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 E  162  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 E  162  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 E  162  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 E  162  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 E  162  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER LEU GLU          
SEQRES  13 E  162  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 F  162  MET ALA ASP CYS THR PHE THR GLN LEU GLU ILE VAL PRO          
SEQRES   2 F  162  GLN PHE GLY SER PRO ASN MET PHE GLY GLY GLU ASP GLU          
SEQRES   3 F  162  HIS VAL ARG VAL MET PHE SER ASN GLU ASP PRO ASN ASP          
SEQRES   4 F  162  ASP ASN PRO ASP ALA PHE PRO GLU PRO PRO VAL TYR LEU          
SEQRES   5 F  162  ALA ASP ARG ASP SER GLY ASN ASP CYS ARG ILE GLU ASP          
SEQRES   6 F  162  GLY GLY ILE TRP SER ARG GLY GLY VAL PHE LEU SER GLN          
SEQRES   7 F  162  ASP GLY ARG ARG VAL LEU MET HIS GLU PHE SER GLY SER          
SEQRES   8 F  162  SER ALA GLU LEU VAL SER TYR ASP SER ALA THR CYS LYS          
SEQRES   9 F  162  VAL VAL HIS ARG GLU ASP ILE SER GLY GLN ARG TRP ALA          
SEQRES  10 F  162  VAL ASP LYS ASP GLY LEU ARG LEU GLY GLN LYS CYS SER          
SEQRES  11 F  162  GLY GLU SER VAL ASP SER CYS ALA LYS ILE VAL LYS ARG          
SEQRES  12 F  162  SER LEU ALA PRO PHE CYS GLN THR ALA LYS LYS LEU GLU          
SEQRES  13 F  162  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 G  162  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 G  162  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 G  162  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 G  162  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 G  162  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 G  162  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 G  162  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 G  162  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 G  162  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 G  162  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 G  162  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 G  162  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER LEU GLU          
SEQRES  13 G  162  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 H  162  MET ALA ASP CYS THR PHE THR GLN LEU GLU ILE VAL PRO          
SEQRES   2 H  162  GLN PHE GLY SER PRO ASN MET PHE GLY GLY GLU ASP GLU          
SEQRES   3 H  162  HIS VAL ARG VAL MET PHE SER ASN GLU ASP PRO ASN ASP          
SEQRES   4 H  162  ASP ASN PRO ASP ALA PHE PRO GLU PRO PRO VAL TYR LEU          
SEQRES   5 H  162  ALA ASP ARG ASP SER GLY ASN ASP CYS ARG ILE GLU ASP          
SEQRES   6 H  162  GLY GLY ILE TRP SER ARG GLY GLY VAL PHE LEU SER GLN          
SEQRES   7 H  162  ASP GLY ARG ARG VAL LEU MET HIS GLU PHE SER GLY SER          
SEQRES   8 H  162  SER ALA GLU LEU VAL SER TYR ASP SER ALA THR CYS LYS          
SEQRES   9 H  162  VAL VAL HIS ARG GLU ASP ILE SER GLY GLN ARG TRP ALA          
SEQRES  10 H  162  VAL ASP LYS ASP GLY LEU ARG LEU GLY GLN LYS CYS SER          
SEQRES  11 H  162  GLY GLU SER VAL ASP SER CYS ALA LYS ILE VAL LYS ARG          
SEQRES  12 H  162  SER LEU ALA PRO PHE CYS GLN THR ALA LYS LYS LEU GLU          
SEQRES  13 H  162  HIS HIS HIS HIS HIS HIS                                      
FORMUL   9  HOH   *72(H2 O)                                                     
HELIX    1   1 ASP A    5  ASP A   17  1                                  13    
HELIX    2   2 PRO A   25  ASP A   28  5                                   4    
HELIX    3   3 ASN A   29  LEU A   41  1                                  13    
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 ASN A  131  ASP A  136  1                                   6    
HELIX   10  10 SER B  151  ASP B  153  5                                   3    
HELIX   11  11 LEU B  163  CYS B  167  5                                   5    
HELIX   12  12 ASP C    5  TRP C   16  1                                  12    
HELIX   13  13 PRO C   25  ASP C   28  5                                   4    
HELIX   14  14 ASN C   29  LEU C   41  1                                  13    
HELIX   15  15 ASN C   49  TRP C   61  1                                  13    
HELIX   16  16 SER C   66  GLN C   76  1                                  11    
HELIX   17  17 LEU C  100  LYS C  104  5                                   5    
HELIX   18  18 GLY C  115  GLN C  119  5                                   5    
HELIX   19  19 GLY C  127  VAL C  129  5                                   3    
HELIX   20  20 ASN C  131  ASP C  136  1                                   6    
HELIX   21  21 SER D  151  CYS D  155  5                                   5    
HELIX   22  22 ASP E    5  LYS E   18  1                                  14    
HELIX   23  23 PRO E   25  ASP E   28  5                                   4    
HELIX   24  24 ASN E   29  LEU E   41  1                                  13    
HELIX   25  25 ASN E   49  TRP E   61  1                                  13    
HELIX   26  26 SER E   66  GLN E   76  1                                  11    
HELIX   27  27 LEU E  100  LYS E  104  5                                   5    
HELIX   28  28 GLY E  115  GLN E  119  5                                   5    
HELIX   29  29 ASN E  131  ASP E  136  1                                   6    
HELIX   30  30 SER F  151  CYS F  155  5                                   5    
HELIX   31  31 LEU F  163  CYS F  167  5                                   5    
HELIX   32  32 ASP G    5  LYS G   18  1                                  14    
HELIX   33  33 PRO G   25  ASP G   28  5                                   4    
HELIX   34  34 ASN G   29  LEU G   41  1                                  13    
HELIX   35  35 ASN G   49  TRP G   61  1                                  13    
HELIX   36  36 SER G   66  GLN G   76  1                                  11    
HELIX   37  37 LEU G  100  LYS G  104  5                                   5    
HELIX   38  38 GLY G  115  GLN G  119  5                                   5    
HELIX   39  39 GLY G  127  VAL G  129  5                                   3    
HELIX   40  40 ASN G  131  ASP G  136  1                                   6    
HELIX   41  41 SER H  151  CYS H  155  5                                   5    
SHEET    1   A 6 THR A  62  LEU A  64  0                                        
SHEET    2   A 6 ASN A 139  VAL A 142 -1  O  TYR A 140   N  LEU A  64           
SHEET    3   A 6 VAL A  80  LEU A  84 -1  N  GLY A  83   O  ASN A 139           
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 3 PHE B  24  GLN B  26  0                                        
SHEET    2   B 3 ILE B  86  SER B  95 -1  O  LEU B  94   N  THR B  25           
SHEET    3   B 3 ALA B  62  PHE B  63 -1  N  PHE B  63   O  TRP B  87           
SHEET    1   C 5 PHE B  24  GLN B  26  0                                        
SHEET    2   C 5 ILE B  86  SER B  95 -1  O  LEU B  94   N  THR B  25           
SHEET    3   C 5 ARG B 100  SER B 107 -1  O  LEU B 102   N  PHE B  93           
SHEET    4   C 5 SER B 110  ASP B 117 -1  O  TYR B 116   N  VAL B 101           
SHEET    5   C 5 VAL B 123  ASP B 128 -1  O  VAL B 124   N  SER B 115           
SHEET    1   D 5 VAL B  30  PRO B  31  0                                        
SHEET    2   D 5 MET B  38  GLU B  42 -1  O  GLY B  40   N  VAL B  30           
SHEET    3   D 5 VAL B  46  SER B  51 -1  O  PHE B  50   N  PHE B  39           
SHEET    4   D 5 VAL B  68  ASP B  72 -1  O  ALA B  71   N  ARG B  47           
SHEET    5   D 5 ASP B  78  ILE B  81 -1  O  ILE B  81   N  VAL B  68           
SHEET    1   E 6 ARG B 133  ASP B 137  0                                        
SHEET    2   E 6 GLY B 140  CYS B 147 -1  O  GLY B 144   N  ARG B 133           
SHEET    3   E 6 CYS B 155  ARG B 161 -1  O  ARG B 161   N  LEU B 141           
SHEET    4   E 6 LYS D 157  ARG D 161 -1  O  ILE D 158   N  ILE B 158           
SHEET    5   E 6 GLY D 140  GLN D 145 -1  N  LEU D 143   O  VAL D 159           
SHEET    6   E 6 ARG D 133  ASP D 137 -1  N  ARG D 133   O  GLY D 144           
SHEET    1   F 6 THR C  62  LEU C  64  0                                        
SHEET    2   F 6 ASN C 139  VAL C 142 -1  O  VAL C 142   N  THR C  62           
SHEET    3   F 6 VAL C  80  LEU C  84 -1  N  GLY C  83   O  ASN C 139           
SHEET    4   F 6 HIS C  91  VAL C  95 -1  O  VAL C  95   N  VAL C  80           
SHEET    5   F 6 MET C 107  CYS C 110 -1  O  TRP C 109   N  VAL C  94           
SHEET    6   F 6 SER C 120  SER C 125 -1  O  LYS C 124   N  CYS C 108           
SHEET    1   G 3 PHE D  24  GLN D  26  0                                        
SHEET    2   G 3 ILE D  86  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 ILE D  86  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  GLU D 112   N  GLU D 105           
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  PRO D  31  0                                        
SHEET    2   I 5 MET D  38  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 ASN D  77  ILE D  81 -1  O  CYS D  79   N  LEU D  70           
SHEET    1   J 6 THR E  62  LEU E  64  0                                        
SHEET    2   J 6 ASN E 139  VAL E 142 -1  O  VAL E 142   N  THR E  62           
SHEET    3   J 6 VAL E  80  LEU E  84 -1  N  GLY E  83   O  ASN E 139           
SHEET    4   J 6 HIS E  91  VAL E  95 -1  O  VAL E  95   N  VAL E  80           
SHEET    5   J 6 MET E 107  CYS E 110 -1  O  TRP E 109   N  VAL E  94           
SHEET    6   J 6 SER E 120  SER E 125 -1  O  LYS E 124   N  CYS E 108           
SHEET    1   K 3 PHE F  24  GLN F  26  0                                        
SHEET    2   K 3 ILE F  86  SER F  95 -1  O  LEU F  94   N  THR F  25           
SHEET    3   K 3 ALA F  62  PHE F  63 -1  N  PHE F  63   O  TRP F  87           
SHEET    1   L 5 PHE F  24  GLN F  26  0                                        
SHEET    2   L 5 ILE F  86  SER F  95 -1  O  LEU F  94   N  THR F  25           
SHEET    3   L 5 ARG F 100  SER F 107 -1  O  LEU F 102   N  PHE F  93           
SHEET    4   L 5 SER F 110  ASP F 117 -1  O  TYR F 116   N  VAL F 101           
SHEET    5   L 5 VAL F 123  ASP F 128 -1  O  VAL F 124   N  SER F 115           
SHEET    1   M 5 VAL F  30  PRO F  31  0                                        
SHEET    2   M 5 MET F  38  GLU F  42 -1  O  GLY F  40   N  VAL F  30           
SHEET    3   M 5 VAL F  46  SER F  51 -1  O  VAL F  48   N  GLY F  41           
SHEET    4   M 5 VAL F  68  ASP F  72 -1  O  ALA F  71   N  ARG F  47           
SHEET    5   M 5 ASP F  78  ILE F  81 -1  O  ILE F  81   N  VAL F  68           
SHEET    1   N 3 ARG F 133  VAL F 136  0                                        
SHEET    2   N 3 LEU F 141  GLN F 145 -1  O  GLY F 144   N  ARG F 133           
SHEET    3   N 3 LYS F 157  ARG F 161 -1  O  VAL F 159   N  LEU F 143           
SHEET    1   O 6 THR G  62  LEU G  64  0                                        
SHEET    2   O 6 ASN G 139  VAL G 142 -1  O  VAL G 142   N  THR G  62           
SHEET    3   O 6 VAL G  80  LEU G  84 -1  N  ILE G  81   O  TYR G 141           
SHEET    4   O 6 HIS G  91  VAL G  95 -1  O  VAL G  95   N  VAL G  80           
SHEET    5   O 6 MET G 107  CYS G 110 -1  O  TRP G 109   N  VAL G  94           
SHEET    6   O 6 SER G 120  SER G 125 -1  O  LYS G 124   N  CYS G 108           
SHEET    1   P 3 PHE H  24  GLN H  26  0                                        
SHEET    2   P 3 ILE H  86  SER H  95 -1  O  LEU H  94   N  THR H  25           
SHEET    3   P 3 ALA H  62  PHE H  63 -1  N  PHE H  63   O  TRP H  87           
SHEET    1   Q 5 PHE H  24  GLN H  26  0                                        
SHEET    2   Q 5 ILE H  86  SER H  95 -1  O  LEU H  94   N  THR H  25           
SHEET    3   Q 5 ARG H 100  SER H 107 -1  O  ARG H 100   N  SER H  95           
SHEET    4   Q 5 SER H 110  ASP H 117 -1  O  TYR H 116   N  VAL H 101           
SHEET    5   Q 5 VAL H 123  ASP H 128 -1  O  VAL H 124   N  SER H 115           
SHEET    1   R 5 VAL H  30  PRO H  31  0                                        
SHEET    2   R 5 MET H  38  GLU H  42 -1  O  GLY H  40   N  VAL H  30           
SHEET    3   R 5 VAL H  46  SER H  51 -1  O  PHE H  50   N  PHE H  39           
SHEET    4   R 5 VAL H  68  ASP H  72 -1  O  TYR H  69   N  MET H  49           
SHEET    5   R 5 ASP H  78  ILE H  81 -1  O  ILE H  81   N  VAL H  68           
SHEET    1   S 3 ARG H 133  ASP H 137  0                                        
SHEET    2   S 3 GLY H 140  GLY H 144 -1  O  ARG H 142   N  ALA H 135           
SHEET    3   S 3 ILE H 158  ARG H 161 -1  O  VAL H 159   N  LEU H 143           
SSBOND   1 CYS A    7    CYS A  148                          1555   1555  1.98  
SSBOND   2 CYS B   22    CYS B  167                          1555   1555  1.99  
SSBOND   3 CYS B   79    CYS B  121                          1555   1555  2.05  
SSBOND   4 CYS B  147    CYS B  155                          1555   1555  1.98  
SSBOND   5 CYS C    7    CYS C  148                          1555   1555  2.01  
SSBOND   6 CYS D   22    CYS D  167                          1555   1555  1.97  
SSBOND   7 CYS D   79    CYS D  121                          1555   1555  2.03  
SSBOND   8 CYS D  147    CYS D  155                          1555   1555  1.95  
SSBOND   9 CYS E    7    CYS E  148                          1555   1555  1.97  
SSBOND  10 CYS F   22    CYS F  167                          1555   1555  1.97  
SSBOND  11 CYS F   79    CYS F  121                          1555   1555  2.06  
SSBOND  12 CYS F  147    CYS F  155                          1555   1555  1.95  
SSBOND  13 CYS G    7    CYS G  148                          1555   1555  2.00  
SSBOND  14 CYS H   22    CYS H  167                          1555   1555  1.98  
SSBOND  15 CYS H   79    CYS H  121                          1555   1555  2.05  
SSBOND  16 CYS H  147    CYS H  155                          1555   1555  1.99  
CISPEP   1 PRO B   66    PRO B   67          0         2.88                     
CISPEP   2 PRO D   66    PRO D   67          0        -2.40                     
CISPEP   3 PRO F   66    PRO F   67          0        -5.24                     
CISPEP   4 PRO H   66    PRO H   67          0         2.60                     
CRYST1   97.710   97.710  293.301  90.00  90.00 120.00 P 32 2 1     24          
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      0.010234  0.005909  0.000000        0.00000                         
SCALE2      0.000000  0.011818  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003409        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2 -0.823381 -0.104279  0.557825       10.11087    1                    
MTRIX2   2 -0.110474 -0.934712 -0.337800       17.12139    1                    
MTRIX3   2  0.556631 -0.339764  0.758104        0.86033    1                    
MTRIX1   3  0.767203 -0.306086 -0.563658      -31.10011    1                    
MTRIX2   3 -0.238761 -0.951919  0.191945      -56.83527    1                    
MTRIX3   3 -0.595309 -0.012682 -0.803397      -64.38976    1                    
MTRIX1   4 -0.937735  0.346850  0.018658      -43.09138    1                    
MTRIX2   4  0.336986  0.895413  0.290991       12.96126    1                    
MTRIX3   4  0.084223  0.279160 -0.956544      -39.46775    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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