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Database: PDB
Entry: 5BRZ
LinkDB: 5BRZ
Original site: 5BRZ 
HEADER    IMMUNE SYSTEM                           01-JUN-15   5BRZ              
TITLE     MAGE-A3 REACTIVE TCR IN COMPLEX WITH MAGE-A3 IN HLA-A1                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-1 ALPHA CHAIN;   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MHC CLASS I ANTIGEN A*1;                                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   8 CHAIN: B;                                                            
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: GLU-VAL-ASP-PRO-ILE-GLY-HIS-LEU-TYR;                       
COMPND  12 CHAIN: C;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: PROTEIN TRAV21,T-CELL RECEPTOR ALPHA CHAIN C REGION;       
COMPND  16 CHAIN: D;                                                            
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 5;                                                           
COMPND  19 MOLECULE: PROTEIN TRBV5-1,HUMAN NKT TCR BETA CHAIN;                  
COMPND  20 CHAIN: E;                                                            
COMPND  21 SYNONYM: V_SEGMENT TRANSLATION PRODUCT;                              
COMPND  22 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HLA-A, HLAA;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: B2M, CDABP0092, HDCMA22P;                                      
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 MOL_ID: 4;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: TRAV21, TRAC, TCRA;                                            
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  26 MOL_ID: 5;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  28 ORGANISM_COMMON: HUMAN;                                              
SOURCE  29 ORGANISM_TAXID: 9606;                                                
SOURCE  30 GENE: TCRBV5S1A1T, TRBV5-1, B2M, HDCMA22P;                           
SOURCE  31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IMMUNO PMHC TCR MAGE, IMMUNE SYSTEM                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.C.RAMAN,P.J.RIZKALLAH,R.SIMMONS,Z.DONNELLAN,J.DUKES,G.BOSSI,      
AUTHOR   2 G.LEPROVOST,T.MAHON,E.HICKMAN,M.LOMAX,J.OATES,N.HASSAN,A.VUIDEPOT,   
AUTHOR   3 M.SAMI,D.K.COLE,B.K.JAKOBSEN                                         
REVDAT   1   02-MAR-16 5BRZ    0                                                
JRNL        AUTH   M.C.RAMAN,P.J.RIZKALLAH,R.SIMMONS,Z.DONNELLAN,J.DUKES,       
JRNL        AUTH 2 G.BOSSI,G.S.LE PROVOST,P.TODOROV,E.BASTON,E.HICKMAN,T.MAHON, 
JRNL        AUTH 3 N.HASSAN,A.VUIDEPOT,M.SAMI,D.K.COLE,B.K.JAKOBSEN             
JRNL        TITL   DIRECT MOLECULAR MIMICRY ENABLES OFF-TARGET CARDIOVASCULAR   
JRNL        TITL 2 TOXICITY BY AN ENHANCED AFFINITY TCR DESIGNED FOR CANCER     
JRNL        TITL 3 IMMUNOTHERAPY.                                               
JRNL        REF    SCI REP                       V.   6 18851 2016              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   26758806                                                     
JRNL        DOI    10.1038/SREP18851                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
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) : 2.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 82.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 26433                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1399                            
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) : 2.62                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1915                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.4420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6566                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 17                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.48000                                             
REMARK   3    B22 (A**2) : 2.19000                                              
REMARK   3    B33 (A**2) : -0.23000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.06000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.359         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.290         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.693        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6771 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6099 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9198 ; 1.597 ; 1.939       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14040 ; 0.841 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   817 ; 7.924 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   346 ;36.060 ;23.757       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1081 ;20.193 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    53 ;18.791 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   964 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7759 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1658 ; 0.001 ; 0.020       
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):  3283 ; 1.403 ; 2.788       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3282 ; 1.403 ; 2.787       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4095 ; 2.336 ; 4.176       
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  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   180                          
REMARK   3    RESIDUE RANGE :   C     1        C     9                          
REMARK   3    ORIGIN FOR THE GROUP (A): 139.5752  35.6415 165.2618              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0428 T22:   0.0941                                     
REMARK   3      T33:   0.1427 T12:  -0.0228                                     
REMARK   3      T13:   0.0758 T23:  -0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0602 L22:   1.7629                                     
REMARK   3      L33:   4.0922 L12:   0.4476                                     
REMARK   3      L13:   0.1752 L23:  -0.3287                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0287 S12:  -0.2311 S13:  -0.1300                       
REMARK   3      S21:   0.0294 S22:  -0.0214 S23:  -0.0117                       
REMARK   3      S31:   0.0907 S32:  -0.1950 S33:   0.0501                       
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 :   A   181        A   276                          
REMARK   3    ORIGIN FOR THE GROUP (A): 138.5647  50.1081 198.4523              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4001 T22:   0.4440                                     
REMARK   3      T33:   0.4687 T12:   0.1201                                     
REMARK   3      T13:   0.0782 T23:  -0.1014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3539 L22:   6.3834                                     
REMARK   3      L33:   5.3505 L12:   0.4083                                     
REMARK   3      L13:   1.8461 L23:   2.8907                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3315 S12:  -0.3624 S13:   0.7784                       
REMARK   3      S21:   0.4505 S22:  -0.1500 S23:   0.3405                       
REMARK   3      S31:  -0.8980 S32:  -0.5286 S33:   0.4815                       
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 :   B     0        B    99                          
REMARK   3    ORIGIN FOR THE GROUP (A): 153.6654  35.4344 189.0251              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1272 T22:   0.1729                                     
REMARK   3      T33:   0.2335 T12:   0.0044                                     
REMARK   3      T13:   0.0173 T23:  -0.0492                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7000 L22:   3.5744                                     
REMARK   3      L33:   8.0576 L12:   0.0125                                     
REMARK   3      L13:  -0.2886 L23:  -1.8139                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0065 S12:  -0.3052 S13:  -0.2089                       
REMARK   3      S21:   0.5020 S22:   0.0270 S23:  -0.3286                       
REMARK   3      S31:   0.1688 S32:   0.3443 S33:  -0.0204                       
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     1        D   115                          
REMARK   3    ORIGIN FOR THE GROUP (A): 116.8131  31.2537 142.1310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1048 T22:   0.2764                                     
REMARK   3      T33:   0.3620 T12:  -0.0057                                     
REMARK   3      T13:   0.0616 T23:   0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7641 L22:   3.2634                                     
REMARK   3      L33:   7.4066 L12:   0.6273                                     
REMARK   3      L13:   3.7489 L23:   2.4392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1024 S12:  -0.1296 S13:   0.0684                       
REMARK   3      S21:  -0.2642 S22:  -0.1681 S23:   0.5668                       
REMARK   3      S31:   0.0687 S32:  -0.6976 S33:   0.0658                       
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 :   D   116        D   210                          
REMARK   3    ORIGIN FOR THE GROUP (A): 106.1847  14.6519 113.1312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5412 T22:   0.7322                                     
REMARK   3      T33:   0.5837 T12:  -0.0364                                     
REMARK   3      T13:  -0.2053 T23:  -0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2202 L22:   7.8764                                     
REMARK   3      L33:   4.1280 L12:  -3.2382                                     
REMARK   3      L13:  -0.3158 L23:   0.2496                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1507 S12:  -0.0756 S13:  -0.2863                       
REMARK   3      S21:   0.2091 S22:   0.0687 S23:   0.5886                       
REMARK   3      S31:   0.1345 S32:  -0.4733 S33:   0.0820                       
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 :   E     0        E   115                          
REMARK   3    ORIGIN FOR THE GROUP (A): 134.0754  15.9466 141.7681              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1570 T22:   0.1531                                     
REMARK   3      T33:   0.1382 T12:   0.0181                                     
REMARK   3      T13:   0.0804 T23:   0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0559 L22:   6.1057                                     
REMARK   3      L33:   3.9977 L12:   0.9375                                     
REMARK   3      L13:   1.0147 L23:   1.7025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0528 S12:   0.0560 S13:  -0.1137                       
REMARK   3      S21:  -0.0092 S22:   0.1189 S23:  -0.0406                       
REMARK   3      S31:   0.4981 S32:  -0.0266 S33:  -0.1717                       
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 :   E   116        E   246                          
REMARK   3    ORIGIN FOR THE GROUP (A): 122.6918  12.0844 113.4509              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4744 T22:   0.3278                                     
REMARK   3      T33:   0.2611 T12:   0.0086                                     
REMARK   3      T13:   0.0097 T23:  -0.0833                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2164 L22:   4.3005                                     
REMARK   3      L33:   6.4296 L12:  -2.5046                                     
REMARK   3      L13:   3.4148 L23:  -4.3116                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2481 S12:   0.5484 S13:   0.0431                       
REMARK   3      S21:  -0.4169 S22:  -0.1366 S23:   0.3158                       
REMARK   3      S31:   0.3898 S32:   0.1596 S33:  -0.1116                       
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 ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 5BRZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210283.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JAN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.1.27, AIMLESS            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27833                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.620                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 82.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.91500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.1                                          
REMARK 200 STARTING MODEL: 1W72 AND 3O4L                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM CHLORIDE, 0.1M HEPES       
REMARK 280  PH7, 15% PEG 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       86.79500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.75000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       86.79500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.75000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11840 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -154.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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 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    LEU E  47   CA  -  CB  -  CG  ANGL. DEV. =  15.8 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    ARG A  17       33.61    -30.35                                   
REMARK 500    ASP A  29     -120.15     46.05                                   
REMARK 500    ASN A  86       78.44     31.43                                   
REMARK 500    ILE A 194      -53.78   -125.54                                   
REMARK 500    SER A 195     -169.60   -114.42                                   
REMARK 500    GLU A 212      104.38    -59.35                                   
REMARK 500    LEU A 230       88.60   -160.61                                   
REMARK 500    PRO B  32     -165.31    -79.00                                   
REMARK 500    ASN B  42       40.27     35.88                                   
REMARK 500    SER B  57     -166.21   -102.35                                   
REMARK 500    TRP B  60        0.14     82.98                                   
REMARK 500    LYS B  75      -41.76     79.99                                   
REMARK 500    ASP B  98       46.12    -97.23                                   
REMARK 500    LEU D  12      122.12   -179.88                                   
REMARK 500    PRO D  41      111.64    -34.30                                   
REMARK 500    SER D  60      108.22   -169.04                                   
REMARK 500    SER D  81      135.35    -35.59                                   
REMARK 500    ASP D  85       39.31    -98.94                                   
REMARK 500    ALA D  87     -179.96   -172.67                                   
REMARK 500    ASN D 119       67.69   -116.43                                   
REMARK 500    ASP D 129      103.63    -37.26                                   
REMARK 500    LYS D 131      139.28    -32.34                                   
REMARK 500    SER D 132       48.99    -73.27                                   
REMARK 500    SER D 133     -155.35   -136.29                                   
REMARK 500    ASP D 142       62.30      4.90                                   
REMARK 500    ASP D 154      -60.69     37.49                                   
REMARK 500    ASP D 171       30.68    -88.54                                   
REMARK 500    PHE D 186       88.19    -56.78                                   
REMARK 500    PHE D 192       41.85   -104.21                                   
REMARK 500    GLN E  42       -5.53     77.97                                   
REMARK 500    LEU E  47      -66.23    -99.31                                   
REMARK 500    SER E  52       71.09     44.59                                   
REMARK 500    GLN E 138       13.54     56.71                                   
REMARK 500    ASP E 152       56.15    -67.95                                   
REMARK 500    HIS E 153       73.15   -119.29                                   
REMARK 500    ASN E 161     -137.34     50.35                                   
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 ASP D  134     LYS D  135                  146.90                    
REMARK 500 PHE D  192     ASN D  193                  147.98                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5BS0   RELATED DB: PDB                                   
DBREF  5BRZ A    1   274  UNP    P30443   1A01_HUMAN      25    298             
DBREF  5BRZ B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  5BRZ C    1     9  PDB    5BRZ     5BRZ             1      9             
DBREF1 5BRZ D    3    94  UNP                  A0A0B4J279_HUMAN                 
DBREF2 5BRZ D     A0A0B4J279                         21         112             
DBREF  5BRZ D  118   198  UNP    P01848   TCA_HUMAN        4     84             
DBREF  5BRZ E    3    95  UNP    A0A578   A0A578_HUMAN    21    113             
DBREF  5BRZ E  102   242  UNP    K7N5M4   K7N5M4_HUMAN   108    248             
SEQADV 5BRZ PRO A  275  UNP  P30443              EXPRESSION TAG                 
SEQADV 5BRZ MET B    0  UNP  P61769              INITIATING METHIONINE          
SEQADV 5BRZ ALA D    2  UNP  A0A0B4J27           EXPRESSION TAG                 
SEQADV 5BRZ TYR D   50  UNP  A0A0B4J27 LEU    68 CONFLICT                       
SEQADV 5BRZ VAL D   51  UNP  A0A0B4J27 ILE    69 CONFLICT                       
SEQADV 5BRZ ARG D   52  UNP  A0A0B4J27 GLN    70 CONFLICT                       
SEQADV 5BRZ PRO D   53  UNP  A0A0B4J27 SER    71 CONFLICT                       
SEQADV 5BRZ TYR D   54  UNP  A0A0B4J27 SER    72 CONFLICT                       
SEQADV 5BRZ PRO D   95  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ GLY D   96  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ GLY D   97  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ ALA D   98  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ GLY D   99  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ PRO D  100  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ PHE D  101  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ PHE D  102  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ VAL D  103  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ VAL D  104  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ PHE D  105  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ GLY D  106  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ LYS D  107  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ GLY D  108  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ THR D  109  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ LYS D  110  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ LEU D  111  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ SER D  112  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ VAL D  113  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ ILE D  114  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ PRO D  115  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ ASN D  116  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ ILE D  117  UNP  A0A0B4J27           LINKER                         
SEQADV 5BRZ CYS D  163  UNP  P01848    THR    49 CONFLICT                       
SEQADV 5BRZ PHE E   96  UNP  A0A578              LINKER                         
SEQADV 5BRZ ASN E   97  UNP  A0A578              LINKER                         
SEQADV 5BRZ MET E   98  UNP  A0A578              LINKER                         
SEQADV 5BRZ ALA E   99  UNP  A0A578              LINKER                         
SEQADV 5BRZ THR E  100  UNP  A0A578              LINKER                         
SEQADV 5BRZ GLY E  101  UNP  A0A578              LINKER                         
SEQADV 5BRZ ASP E  202  UNP  K7N5M4    ASN   208 CONFLICT                       
SEQADV 5BRZ ASP E  243  UNP  K7N5M4              EXPRESSION TAG                 
SEQRES   1 A  275  GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER          
SEQRES   2 A  275  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 A  275  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 A  275  ALA ALA SER GLN LYS MET GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 A  275  GLU GLN GLU GLY PRO GLU TYR TRP ASP GLN GLU THR ARG          
SEQRES   6 A  275  ASN MET LYS ALA HIS SER GLN THR ASP ARG ALA ASN LEU          
SEQRES   7 A  275  GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ASP GLY          
SEQRES   8 A  275  SER HIS THR ILE GLN ILE MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  275  PRO ASP GLY ARG PHE LEU ARG GLY TYR ARG GLN ASP ALA          
SEQRES  10 A  275  TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 A  275  ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN ILE THR          
SEQRES  12 A  275  LYS ARG LYS TRP GLU ALA VAL HIS ALA ALA GLU GLN ARG          
SEQRES  13 A  275  ARG VAL TYR LEU GLU GLY ARG CYS VAL ASP GLY LEU ARG          
SEQRES  14 A  275  ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR          
SEQRES  15 A  275  ASP PRO PRO LYS THR HIS MET THR HIS HIS PRO ILE SER          
SEQRES  16 A  275  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 A  275  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 A  275  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 A  275  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 A  275  VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 A  275  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 A  275  TRP PRO                                                      
SEQRES   1 B  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 B  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 B  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 B  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 B  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 B  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 B  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 B  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 C    9  GLU VAL ASP PRO ILE GLY HIS LEU TYR                          
SEQRES   1 D  197  ALA GLN GLU VAL THR GLN ILE PRO ALA ALA LEU SER VAL          
SEQRES   2 D  197  PRO GLU GLY GLU ASN LEU VAL LEU ASN CYS SER PHE THR          
SEQRES   3 D  197  ASP SER ALA ILE TYR ASN LEU GLN TRP PHE ARG GLN ASP          
SEQRES   4 D  197  PRO GLY LYS GLY LEU THR SER LEU LEU TYR VAL ARG PRO          
SEQRES   5 D  197  TYR GLN ARG GLU GLN THR SER GLY ARG LEU ASN ALA SER          
SEQRES   6 D  197  LEU ASP LYS SER SER GLY ARG SER THR LEU TYR ILE ALA          
SEQRES   7 D  197  ALA SER GLN PRO GLY ASP SER ALA THR TYR LEU CYS ALA          
SEQRES   8 D  197  VAL ARG PRO GLY GLY ALA GLY PRO PHE PHE VAL VAL PHE          
SEQRES   9 D  197  GLY LYS GLY THR LYS LEU SER VAL ILE PRO ASN ILE GLN          
SEQRES  10 D  197  ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER LYS          
SEQRES  11 D  197  SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE ASP          
SEQRES  12 D  197  SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP VAL          
SEQRES  13 D  197  TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER MET          
SEQRES  14 D  197  ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN LYS          
SEQRES  15 D  197  SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER ILE          
SEQRES  16 D  197  ILE PRO                                                      
SEQRES   1 E  241  ALA GLY VAL THR GLN THR PRO ARG TYR LEU ILE LYS THR          
SEQRES   2 E  241  ARG GLY GLN GLN VAL THR LEU SER CYS SER PRO ILE SER          
SEQRES   3 E  241  GLY HIS ARG SER VAL SER TRP TYR GLN GLN THR PRO GLY          
SEQRES   4 E  241  GLN GLY LEU GLN PHE LEU PHE GLU TYR PHE SER GLU THR          
SEQRES   5 E  241  GLN ARG ASN LYS GLY ASN PHE PRO GLY ARG PHE SER GLY          
SEQRES   6 E  241  ARG GLN PHE SER ASN SER ARG SER GLU MET ASN VAL SER          
SEQRES   7 E  241  THR LEU GLU LEU GLY ASP SER ALA LEU TYR LEU CYS ALA          
SEQRES   8 E  241  SER SER PHE ASN MET ALA THR GLY GLN TYR PHE GLY PRO          
SEQRES   9 E  241  GLY THR ARG LEU THR VAL THR GLU ASP LEU LYS ASN VAL          
SEQRES  10 E  241  PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU ALA          
SEQRES  11 E  241  GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS LEU          
SEQRES  12 E  241  ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER TRP          
SEQRES  13 E  241  TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS THR          
SEQRES  14 E  241  ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN ASP          
SEQRES  15 E  241  SER ARG TYR ALA LEU SER SER ARG LEU ARG VAL SER ALA          
SEQRES  16 E  241  THR PHE TRP GLN ASP PRO ARG ASN HIS PHE ARG CYS GLN          
SEQRES  17 E  241  VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP THR          
SEQRES  18 E  241  GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER ALA          
SEQRES  19 E  241  GLU ALA TRP GLY ARG ALA ASP                                  
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HET    SO4  B 101       5                                                       
HET    SO4  D 201       5                                                       
HET    SO4  D 202       5                                                       
HET    SO4  E 301       5                                                       
HET    SO4  E 302       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   6  SO4    7(O4 S 2-)                                                   
FORMUL  13  HOH   *17(H2 O)                                                     
HELIX    1 AA1 ALA A   49  GLU A   55  5                                   7    
HELIX    2 AA2 GLY A   56  TYR A   85  1                                  30    
HELIX    3 AA3 ASP A  137  VAL A  150  1                                  14    
HELIX    4 AA4 HIS A  151  GLY A  162  1                                  12    
HELIX    5 AA5 GLY A  162  GLY A  175  1                                  14    
HELIX    6 AA6 GLY A  175  GLN A  180  1                                   6    
HELIX    7 AA7 ALA D  187  PHE D  192  1                                   6    
HELIX    8 AA8 GLU E   83  SER E   87  5                                   5    
HELIX    9 AA9 ASP E  115  VAL E  119  5                                   5    
HELIX   10 AB1 SER E  130  GLN E  138  1                                   9    
HELIX   11 AB2 ALA E  197  GLN E  201  1                                   5    
SHEET    1 AA1 8 GLU A  46  PRO A  47  0                                        
SHEET    2 AA1 8 THR A  31  ASP A  37 -1  N  ARG A  35   O  GLU A  46           
SHEET    3 AA1 8 GLY A  18  VAL A  28 -1  N  VAL A  28   O  THR A  31           
SHEET    4 AA1 8 HIS A   3  ARG A  14 -1  N  ARG A   6   O  TYR A  27           
SHEET    5 AA1 8 THR A  94  VAL A 103 -1  O  ILE A  97   N  PHE A   9           
SHEET    6 AA1 8 PHE A 109  TYR A 118 -1  O  ALA A 117   N  GLN A  96           
SHEET    7 AA1 8 LYS A 121  LEU A 126 -1  O  LYS A 121   N  TYR A 118           
SHEET    8 AA1 8 TRP A 133  ALA A 135 -1  O  THR A 134   N  ALA A 125           
SHEET    1 AA2 4 LYS A 186  PRO A 193  0                                        
SHEET    2 AA2 4 GLU A 198  PHE A 208 -1  O  LEU A 206   N  LYS A 186           
SHEET    3 AA2 4 PHE A 241  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
SHEET    4 AA2 4 THR A 228  LEU A 230 -1  N  GLU A 229   O  ALA A 246           
SHEET    1 AA3 4 LYS A 186  PRO A 193  0                                        
SHEET    2 AA3 4 GLU A 198  PHE A 208 -1  O  LEU A 206   N  LYS A 186           
SHEET    3 AA3 4 PHE A 241  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
SHEET    4 AA3 4 ARG A 234  PRO A 235 -1  N  ARG A 234   O  GLN A 242           
SHEET    1 AA4 4 GLU A 222  ASP A 223  0                                        
SHEET    2 AA4 4 ILE A 213  ARG A 219 -1  N  ARG A 219   O  GLU A 222           
SHEET    3 AA4 4 TYR A 257  HIS A 263 -1  O  GLN A 262   N  THR A 214           
SHEET    4 AA4 4 LEU A 270  LEU A 272 -1  O  LEU A 272   N  CYS A 259           
SHEET    1 AA5 4 LYS B   6  SER B  11  0                                        
SHEET    2 AA5 4 ASN B  21  PHE B  30 -1  O  SER B  28   N  LYS B   6           
SHEET    3 AA5 4 PHE B  62  PHE B  70 -1  O  TYR B  66   N  CYS B  25           
SHEET    4 AA5 4 GLU B  50  HIS B  51 -1  N  GLU B  50   O  TYR B  67           
SHEET    1 AA6 4 LYS B   6  SER B  11  0                                        
SHEET    2 AA6 4 ASN B  21  PHE B  30 -1  O  SER B  28   N  LYS B   6           
SHEET    3 AA6 4 PHE B  62  PHE B  70 -1  O  TYR B  66   N  CYS B  25           
SHEET    4 AA6 4 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    1 AA7 4 GLU B  44  ILE B  46  0                                        
SHEET    2 AA7 4 GLU B  36  LYS B  41 -1  N  LEU B  39   O  ILE B  46           
SHEET    3 AA7 4 TYR B  78  ASN B  83 -1  O  ARG B  81   N  ASP B  38           
SHEET    4 AA7 4 LYS B  91  LYS B  94 -1  O  VAL B  93   N  CYS B  80           
SHEET    1 AA8 5 VAL D   5  THR D   6  0                                        
SHEET    2 AA8 5 LEU D  20  PHE D  26 -1  O  SER D  25   N  THR D   6           
SHEET    3 AA8 5 ARG D  73  ILE D  78 -1  O  SER D  74   N  CYS D  24           
SHEET    4 AA8 5 LEU D  63  ASP D  68 -1  N  ASN D  64   O  TYR D  77           
SHEET    5 AA8 5 GLU D  57  SER D  60 -1  N  GLN D  58   O  ALA D  65           
SHEET    1 AA9 5 ALA D  11  PRO D  15  0                                        
SHEET    2 AA9 5 THR D 109  ILE D 114  1  O  SER D 112   N  LEU D  12           
SHEET    3 AA9 5 ALA D  87  PRO D  95 -1  N  ALA D  87   O  LEU D 111           
SHEET    4 AA9 5 ILE D  31  GLN D  39 -1  N  TYR D  32   O  ARG D  94           
SHEET    5 AA9 5 LEU D  45  VAL D  51 -1  O  LEU D  49   N  TRP D  36           
SHEET    1 AB1 4 ALA D  11  PRO D  15  0                                        
SHEET    2 AB1 4 THR D 109  ILE D 114  1  O  SER D 112   N  LEU D  12           
SHEET    3 AB1 4 ALA D  87  PRO D  95 -1  N  ALA D  87   O  LEU D 111           
SHEET    4 AB1 4 VAL D 104  PHE D 105 -1  O  VAL D 104   N  VAL D  93           
SHEET    1 AB2 8 TYR D 158  ILE D 159  0                                        
SHEET    2 AB2 8 SER D 176  TRP D 180 -1  O  TRP D 180   N  TYR D 158           
SHEET    3 AB2 8 SER D 136  THR D 141 -1  N  PHE D 140   O  ALA D 177           
SHEET    4 AB2 8 ALA D 123  ASP D 129 -1  N  ALA D 123   O  THR D 141           
SHEET    5 AB2 8 GLU E 123  GLU E 128 -1  O  GLU E 128   N  ARG D 128           
SHEET    6 AB2 8 LYS E 139  PHE E 149 -1  O  VAL E 143   N  PHE E 127           
SHEET    7 AB2 8 TYR E 187  SER E 196 -1  O  TYR E 187   N  PHE E 149           
SHEET    8 AB2 8 VAL E 169  THR E 171 -1  N  CYS E 170   O  ARG E 192           
SHEET    1 AB3 8 TYR D 158  ILE D 159  0                                        
SHEET    2 AB3 8 SER D 176  TRP D 180 -1  O  TRP D 180   N  TYR D 158           
SHEET    3 AB3 8 SER D 136  THR D 141 -1  N  PHE D 140   O  ALA D 177           
SHEET    4 AB3 8 ALA D 123  ASP D 129 -1  N  ALA D 123   O  THR D 141           
SHEET    5 AB3 8 GLU E 123  GLU E 128 -1  O  GLU E 128   N  ARG D 128           
SHEET    6 AB3 8 LYS E 139  PHE E 149 -1  O  VAL E 143   N  PHE E 127           
SHEET    7 AB3 8 TYR E 187  SER E 196 -1  O  TYR E 187   N  PHE E 149           
SHEET    8 AB3 8 LEU E 176  LYS E 177 -1  N  LEU E 176   O  ALA E 188           
SHEET    1 AB4 2 LEU D 165  ASP D 166  0                                        
SHEET    2 AB4 2 LYS D 173  SER D 174 -1  O  SER D 174   N  LEU D 165           
SHEET    1 AB5 4 THR E   6  THR E   8  0                                        
SHEET    2 AB5 4 VAL E  20  SER E  25 -1  O  SER E  23   N  THR E   8           
SHEET    3 AB5 4 SER E  75  VAL E  79 -1  O  MET E  77   N  LEU E  22           
SHEET    4 AB5 4 PHE E  65  GLN E  69 -1  N  SER E  66   O  ASN E  78           
SHEET    1 AB6 6 TYR E  11  THR E  15  0                                        
SHEET    2 AB6 6 THR E 108  THR E 113  1  O  THR E 111   N  LYS E  14           
SHEET    3 AB6 6 ALA E  88  SER E  95 -1  N  ALA E  88   O  LEU E 110           
SHEET    4 AB6 6 SER E  32  THR E  39 -1  N  GLN E  38   O  LEU E  89           
SHEET    5 AB6 6 GLY E  43  PHE E  51 -1  O  PHE E  48   N  TRP E  35           
SHEET    6 AB6 6 THR E  54  LYS E  58 -1  O  THR E  54   N  PHE E  51           
SHEET    1 AB7 4 TYR E  11  THR E  15  0                                        
SHEET    2 AB7 4 THR E 108  THR E 113  1  O  THR E 111   N  LYS E  14           
SHEET    3 AB7 4 ALA E  88  SER E  95 -1  N  ALA E  88   O  LEU E 110           
SHEET    4 AB7 4 GLN E 102  PHE E 104 -1  O  TYR E 103   N  SER E  94           
SHEET    1 AB8 4 LYS E 163  VAL E 165  0                                        
SHEET    2 AB8 4 VAL E 154  VAL E 160 -1  N  VAL E 160   O  LYS E 163           
SHEET    3 AB8 4 HIS E 206  PHE E 213 -1  O  ARG E 208   N  TRP E 159           
SHEET    4 AB8 4 GLN E 232  TRP E 239 -1  O  ALA E 238   N  PHE E 207           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.13  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.08  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.06  
SSBOND   4 CYS D   24    CYS D   91                          1555   1555  2.07  
SSBOND   5 CYS D  138    CYS D  188                          1555   1555  2.07  
SSBOND   6 CYS D  163    CYS E  170                          1555   1555  2.06  
SSBOND   7 CYS E   24    CYS E   92                          1555   1555  2.01  
SSBOND   8 CYS E  144    CYS E  209                          1555   1555  2.03  
CISPEP   1 TYR A  209    PRO A  210          0         1.88                     
CISPEP   2 HIS B   31    PRO B   32          0         9.33                     
CISPEP   3 ILE D    8    PRO D    9          0         1.03                     
CISPEP   4 THR E    8    PRO E    9          0       -11.59                     
CISPEP   5 TYR E  150    PRO E  151          0        -2.03                     
SITE     1 AC1  6 TYR A  85  TYR A 118  LYS A 121  ASP A 122                    
SITE     2 AC1  6 TYR A 123  ASP A 137                                          
SITE     1 AC2  6 ILE A  97  ARG A 114  ASP A 116  TRP A 147                    
SITE     2 AC2  6 ARG A 156  HIS C   7                                          
SITE     1 AC3  7 ARG A  21  ILE A  23  ASP A  37  HIS B  51                    
SITE     2 AC3  7 SER B  52  ASP B  53  LEU B  54                               
SITE     1 AC4  6 ARG D  52  GLN D  55  GLN D  58  ARG E  16                    
SITE     2 AC4  6 GLU E  83  LEU E  84                                          
SITE     1 AC5  6 PHE D 102  VAL D 103  VAL D 104  PHE D 105                    
SITE     2 AC5  6 LEU E  44  PHE E  46                                          
SITE     1 AC6  3 ARG A 131  PRO E  62  ARG E  64                               
SITE     1 AC7  3 VAL E 165  HIS E 166  SER E 167                               
CRYST1  173.590   47.500  119.250  90.00 109.12  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005761  0.000000  0.001997        0.00000                         
SCALE2      0.000000  0.021053  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008875        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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