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Database: PDB
Entry: 5JSB
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HEADER    VIRAL PROTEIN/INHIBITOR                 07-MAY-16   5JSB              
TITLE     CRYSTAL STRUCTURE OF MCL1-INHIBITOR COMPLEX                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- 
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A, C, E, G, I, K;                                             
COMPND   5 SYNONYM: BCL-2-LIKE PROTEIN 3,BCL2-L-3,BCL-2-RELATED PROTEIN         
COMPND   6 EAT/MCL1,MCL1/EAT;                                                   
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MCL-1 INHIBITOR;                                           
COMPND  10 CHAIN: B, D, F, H, J, L;                                             
COMPND  11 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: MCL1, BCL2L3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET29B;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  12 ORGANISM_TAXID: 32630;                                               
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET29B;                                   
SOURCE  17 OTHER_DETAILS: ROSETTA DESIGNED AND GENE SYNTHESIZED (HENESCRIPT)    
KEYWDS    MCL-1, ANTIMCL1, COMPLEX, VIRAL PROTEIN-INHIBITOR COMPLEX             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.W.SHEN,B.L.STODDARD                                                 
REVDAT   4   25-DEC-19 5JSB    1       REMARK                                   
REVDAT   3   20-SEP-17 5JSB    1       REMARK                                   
REVDAT   2   07-DEC-16 5JSB    1       REMARK                                   
REVDAT   1   16-NOV-16 5JSB    0                                                
JRNL        AUTH   S.BERGER,E.PROCKO,D.MARGINEANTU,E.F.LEE,B.W.SHEN,A.ZELTER,   
JRNL        AUTH 2 D.A.SILVA,K.CHAWLA,M.J.HEROLD,J.M.GARNIER,R.JOHNSON,         
JRNL        AUTH 3 M.J.MACCOSS,G.LESSENE,T.N.DAVIS,P.S.STAYTON,B.L.STODDARD,    
JRNL        AUTH 4 W.D.FAIRLIE,D.M.HOCKENBERY,D.BAKER                           
JRNL        TITL   COMPUTATIONALLY DESIGNED HIGH SPECIFICITY INHIBITORS         
JRNL        TITL 2 DELINEATE THE ROLES OF BCL2 FAMILY PROTEINS IN CANCER.       
JRNL        REF    ELIFE                         V.   5       2016              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   27805565                                                     
JRNL        DOI    10.7554/ELIFE.20352                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 161.86                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 43236                          
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2316                            
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) : 2.74                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1908                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 56.50                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 105                          
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13038                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 22                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 58.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 92.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.21000                                             
REMARK   3    B22 (A**2) : 1.72000                                              
REMARK   3    B33 (A**2) : 1.59000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.26000                                             
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): 0.360         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.301         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.027        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13205 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 13212 ; 0.011 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17677 ; 1.987 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 30313 ; 2.084 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1592 ; 6.469 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   679 ;38.197 ;23.814       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2682 ;21.560 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   144 ;17.285 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1943 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14788 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  3040 ; 0.009 ; 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):  6401 ; 3.250 ; 5.027       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6400 ; 3.250 ; 5.026       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7982 ; 5.101 ; 7.538       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  7983 ; 5.101 ; 7.539       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6804 ; 4.374 ; 5.557       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  6804 ; 4.374 ; 5.557       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  9695 ; 7.003 ; 8.115       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 15082 ; 9.362 ;38.601       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 15083 ; 9.361 ;38.605       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 30                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A   172    322       C   172    322   18044  0.09  0.05     
REMARK   3    2     A   172    322       E   172    322   17838  0.09  0.05     
REMARK   3    3     A   172    322       G   172    322   17968  0.10  0.05     
REMARK   3    4     A   172    322       I   172    322   18412  0.07  0.05     
REMARK   3    5     A   172    322       K   172    322   17878  0.09  0.05     
REMARK   3    6     B     2    117       D     2    117   14244  0.07  0.05     
REMARK   3    7     B     2    117       F     2    117   14122  0.07  0.05     
REMARK   3    8     B     2    117       H     2    117   13900  0.10  0.05     
REMARK   3    9     B     2    117       J     2    117   13746  0.10  0.05     
REMARK   3   10     B     2    117       L     2    117   13798  0.10  0.05     
REMARK   3   11     C   172    322       E   172    322   17578  0.11  0.05     
REMARK   3   12     C   172    322       G   172    322   17902  0.10  0.05     
REMARK   3   13     C   172    322       I   172    322   17740  0.10  0.05     
REMARK   3   14     C   172    322       K   172    322   17680  0.10  0.05     
REMARK   3   15     D     2    117       F     2    117   14412  0.07  0.05     
REMARK   3   16     D     2    117       H     2    117   14186  0.09  0.05     
REMARK   3   17     D     2    117       J     2    117   14036  0.09  0.05     
REMARK   3   18     D     2    117       L     2    117   14076  0.10  0.05     
REMARK   3   19     E   172    322       G   172    322   17814  0.09  0.05     
REMARK   3   20     E   172    322       I   172    322   17936  0.09  0.05     
REMARK   3   21     E   172    322       K   172    322   17252  0.10  0.05     
REMARK   3   22     F     2    117       H     2    117   14186  0.09  0.05     
REMARK   3   23     F     2    117       J     2    117   13930  0.09  0.05     
REMARK   3   24     F     2    117       L     2    117   13968  0.10  0.05     
REMARK   3   25     G   172    322       I   172    322   18104  0.08  0.05     
REMARK   3   26     G   172    322       K   172    322   17750  0.10  0.05     
REMARK   3   27     H     2    117       J     2    117   13924  0.10  0.05     
REMARK   3   28     H     2    117       L     2    117   13828  0.10  0.05     
REMARK   3   29     I   172    322       K   172    322   17630  0.09  0.05     
REMARK   3   30     J     2    117       L     2    117   13868  0.10  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
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   172        A   322                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3242 -60.9835 -50.2056              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1028 T22:   0.1093                                     
REMARK   3      T33:   0.2999 T12:   0.0713                                     
REMARK   3      T13:  -0.0215 T23:   0.0258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7018 L22:   4.9427                                     
REMARK   3      L33:   5.1615 L12:  -0.7961                                     
REMARK   3      L13:   0.6549 L23:  -0.6959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2943 S12:   0.7134 S13:   0.8583                       
REMARK   3      S21:  -0.3512 S22:  -0.2681 S23:   0.8613                       
REMARK   3      S31:  -0.4997 S32:  -0.2664 S33:  -0.0263                       
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     2        B   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0519 -73.7095 -35.9951              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1534 T22:   0.2219                                     
REMARK   3      T33:   0.2727 T12:  -0.1203                                     
REMARK   3      T13:   0.1239 T23:   0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9424 L22:  10.8124                                     
REMARK   3      L33:   6.1395 L12:  -1.9671                                     
REMARK   3      L13:   0.0093 L23:   4.3868                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0010 S12:  -0.4701 S13:  -0.3202                       
REMARK   3      S21:   0.7536 S22:  -0.0366 S23:   0.5923                       
REMARK   3      S31:   0.5291 S32:  -0.3204 S33:   0.0376                       
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   172        C   322                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1395 -35.2649  -9.1235              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3219 T22:   0.2228                                     
REMARK   3      T33:   0.2409 T12:   0.1628                                     
REMARK   3      T13:   0.0971 T23:   0.2072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5236 L22:   5.2255                                     
REMARK   3      L33:   5.1068 L12:  -1.3087                                     
REMARK   3      L13:   1.7449 L23:  -0.0998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:  -0.9689 S13:  -1.3407                       
REMARK   3      S21:   0.2761 S22:  -0.0977 S23:   0.2096                       
REMARK   3      S31:   1.2145 S32:   0.4842 S33:   0.1033                       
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     2        D   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.1779 -17.5308 -13.0037              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0556 T22:   0.2175                                     
REMARK   3      T33:   0.2475 T12:  -0.0605                                     
REMARK   3      T13:  -0.0163 T23:  -0.0165                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9567 L22:   4.3042                                     
REMARK   3      L33:  12.4850 L12:  -0.7337                                     
REMARK   3      L13:  -0.3985 L23:   1.7651                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0779 S12:  -0.1312 S13:   0.4375                       
REMARK   3      S21:  -0.1776 S22:   0.1341 S23:  -0.2918                       
REMARK   3      S31:  -0.7649 S32:   0.6245 S33:  -0.0562                       
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   172        E   322                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.9206 -31.9108 -71.5417              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2002 T22:   0.1613                                     
REMARK   3      T33:   0.1424 T12:  -0.1137                                     
REMARK   3      T13:  -0.0478 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0551 L22:   4.7840                                     
REMARK   3      L33:   3.7393 L12:  -0.3368                                     
REMARK   3      L13:   2.3245 L23:  -0.3666                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1413 S12:  -0.1082 S13:  -0.7673                       
REMARK   3      S21:  -0.5232 S22:   0.0478 S23:   0.4001                       
REMARK   3      S31:   0.6174 S32:  -0.6474 S33:  -0.1890                       
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     2        F   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.0968 -13.5853 -65.7539              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1840 T22:   0.2052                                     
REMARK   3      T33:   0.2167 T12:   0.1642                                     
REMARK   3      T13:  -0.0511 T23:  -0.0455                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9589 L22:   3.1499                                     
REMARK   3      L33:  11.1344 L12:   0.5046                                     
REMARK   3      L13:  -0.1069 L23:  -1.4159                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0064 S12:  -0.3244 S13:   0.3013                       
REMARK   3      S21:   0.1112 S22:   0.0413 S23:   0.3020                       
REMARK   3      S31:  -0.8658 S32:  -0.4629 S33:  -0.0350                       
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   172        G   322                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.1464 -55.8408 -31.4621              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2654 T22:   0.1946                                     
REMARK   3      T33:   0.3555 T12:  -0.1803                                     
REMARK   3      T13:  -0.0439 T23:  -0.1128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6636 L22:   5.2190                                     
REMARK   3      L33:   5.3282 L12:   1.4248                                     
REMARK   3      L13:  -0.3819 L23:   0.7293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4059 S12:  -0.8736 S13:   1.3465                       
REMARK   3      S21:   0.7674 S22:  -0.5198 S23:  -0.2818                       
REMARK   3      S31:  -0.7539 S32:   0.4026 S33:   0.1139                       
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     2        H   117                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0273 -68.7345 -44.2784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0360 T22:   0.2883                                     
REMARK   3      T33:   0.2652 T12:   0.0115                                     
REMARK   3      T13:   0.0689 T23:   0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2471 L22:   9.2621                                     
REMARK   3      L33:   8.6148 L12:   0.1186                                     
REMARK   3      L13:   0.5244 L23:  -4.4671                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0369 S12:   0.2059 S13:  -0.1940                       
REMARK   3      S21:  -0.3458 S22:  -0.3706 S23:  -0.7552                       
REMARK   3      S31:   0.4402 S32:   0.5445 S33:   0.3336                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   172        I   322                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.1081 -21.4827 -78.7220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2572 T22:   0.2234                                     
REMARK   3      T33:   0.1095 T12:  -0.0609                                     
REMARK   3      T13:   0.0861 T23:   0.0370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9152 L22:   3.5348                                     
REMARK   3      L33:   4.1594 L12:  -1.9902                                     
REMARK   3      L13:  -0.3964 L23:   0.0537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1553 S12:   1.0199 S13:   0.4369                       
REMARK   3      S21:  -0.8755 S22:  -0.0392 S23:  -0.3223                       
REMARK   3      S31:  -0.1199 S32:   0.3952 S33:  -0.1161                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     2        J   117                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.0470 -27.0181 -60.4258              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0699 T22:   0.1555                                     
REMARK   3      T33:   0.1056 T12:   0.0268                                     
REMARK   3      T13:  -0.0199 T23:   0.0639                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9267 L22:  10.1820                                     
REMARK   3      L33:   4.9383 L12:   1.3457                                     
REMARK   3      L13:   0.2814 L23:   2.9492                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1451 S12:  -0.4281 S13:  -0.0280                       
REMARK   3      S21:   0.6883 S22:  -0.0576 S23:  -0.3440                       
REMARK   3      S31:   0.3273 S32:   0.1777 S33:  -0.0875                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   172        K   322                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.3402 -17.7805  -2.1847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1284 T22:   0.6698                                     
REMARK   3      T33:   0.0791 T12:   0.0773                                     
REMARK   3      T13:   0.0182 T23:  -0.1348                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5494 L22:   4.4407                                     
REMARK   3      L33:   6.4106 L12:   0.5143                                     
REMARK   3      L13:  -1.9210 L23:   0.1551                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0603 S12:  -1.7141 S13:   0.6826                       
REMARK   3      S21:   0.7439 S22:   0.1943 S23:   0.1980                       
REMARK   3      S31:  -0.0008 S32:  -0.9428 S33:  -0.1340                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     2        L   117                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.7526 -21.0410 -21.0056              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1070 T22:   0.2963                                     
REMARK   3      T33:   0.0948 T12:  -0.0430                                     
REMARK   3      T13:  -0.0426 T23:   0.0311                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1179 L22:  10.9875                                     
REMARK   3      L33:   5.8585 L12:  -0.4796                                     
REMARK   3      L13:  -0.2821 L23:  -2.9782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0661 S12:   0.4513 S13:   0.3417                       
REMARK   3      S21:  -1.0045 S22:   0.2160 S23:   0.1634                       
REMARK   3      S31:   0.1910 S32:  -0.6804 S33:  -0.1499                       
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                                                           
REMARK   4                                                                      
REMARK   4 5JSB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221046.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5 - 10.5                         
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000 708                       
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000 708                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.740                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 161.860                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 8.000                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : 0.09400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.090                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.7                                          
REMARK 200 STARTING MODEL: COMPUTATION DESIGNED                                 
REMARK 200                                                                      
REMARK 200 REMARK: IRREGULAR                                                    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.27 M SODIUM CITRATE, CAPS PH 10.5 OR   
REMARK 280  CHES PH 9.5, EVAPORATION, TEMPERATURE 298K                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       46.12300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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: 3010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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: 2940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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: 2940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
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: 2920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
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: 6                                                       
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: 2960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     GLU A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     GLY A   327                                                      
REMARK 465     ILE A   328                                                      
REMARK 465     ARG A   329                                                      
REMARK 465     ASN A   330                                                      
REMARK 465     VAL A   331                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     LEU A   333                                                      
REMARK 465     ALA A   334                                                      
REMARK 465     PHE A   335                                                      
REMARK 465     ALA A   336                                                      
REMARK 465     GLY A   337                                                      
REMARK 465     VAL A   338                                                      
REMARK 465     ALA A   339                                                      
REMARK 465     GLY A   340                                                      
REMARK 465     VAL A   341                                                      
REMARK 465     GLY A   342                                                      
REMARK 465     ALA A   343                                                      
REMARK 465     GLY A   344                                                      
REMARK 465     LEU A   345                                                      
REMARK 465     ALA A   346                                                      
REMARK 465     TYR A   347                                                      
REMARK 465     LEU A   348                                                      
REMARK 465     ILE A   349                                                      
REMARK 465     ARG A   350                                                      
REMARK 465     ASP C   323                                                      
REMARK 465     LEU C   324                                                      
REMARK 465     GLU C   325                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLY C   327                                                      
REMARK 465     ILE C   328                                                      
REMARK 465     ARG C   329                                                      
REMARK 465     ASN C   330                                                      
REMARK 465     VAL C   331                                                      
REMARK 465     LEU C   332                                                      
REMARK 465     LEU C   333                                                      
REMARK 465     ALA C   334                                                      
REMARK 465     PHE C   335                                                      
REMARK 465     ALA C   336                                                      
REMARK 465     GLY C   337                                                      
REMARK 465     VAL C   338                                                      
REMARK 465     ALA C   339                                                      
REMARK 465     GLY C   340                                                      
REMARK 465     VAL C   341                                                      
REMARK 465     GLY C   342                                                      
REMARK 465     ALA C   343                                                      
REMARK 465     GLY C   344                                                      
REMARK 465     LEU C   345                                                      
REMARK 465     ALA C   346                                                      
REMARK 465     TYR C   347                                                      
REMARK 465     LEU C   348                                                      
REMARK 465     ILE C   349                                                      
REMARK 465     ARG C   350                                                      
REMARK 465     ASP E   323                                                      
REMARK 465     LEU E   324                                                      
REMARK 465     GLU E   325                                                      
REMARK 465     GLY E   326                                                      
REMARK 465     GLY E   327                                                      
REMARK 465     ILE E   328                                                      
REMARK 465     ARG E   329                                                      
REMARK 465     ASN E   330                                                      
REMARK 465     VAL E   331                                                      
REMARK 465     LEU E   332                                                      
REMARK 465     LEU E   333                                                      
REMARK 465     ALA E   334                                                      
REMARK 465     PHE E   335                                                      
REMARK 465     ALA E   336                                                      
REMARK 465     GLY E   337                                                      
REMARK 465     VAL E   338                                                      
REMARK 465     ALA E   339                                                      
REMARK 465     GLY E   340                                                      
REMARK 465     VAL E   341                                                      
REMARK 465     GLY E   342                                                      
REMARK 465     ALA E   343                                                      
REMARK 465     GLY E   344                                                      
REMARK 465     LEU E   345                                                      
REMARK 465     ALA E   346                                                      
REMARK 465     TYR E   347                                                      
REMARK 465     LEU E   348                                                      
REMARK 465     ILE E   349                                                      
REMARK 465     ARG E   350                                                      
REMARK 465     ASP G   323                                                      
REMARK 465     LEU G   324                                                      
REMARK 465     GLU G   325                                                      
REMARK 465     GLY G   326                                                      
REMARK 465     GLY G   327                                                      
REMARK 465     ILE G   328                                                      
REMARK 465     ARG G   329                                                      
REMARK 465     ASN G   330                                                      
REMARK 465     VAL G   331                                                      
REMARK 465     LEU G   332                                                      
REMARK 465     LEU G   333                                                      
REMARK 465     ALA G   334                                                      
REMARK 465     PHE G   335                                                      
REMARK 465     ALA G   336                                                      
REMARK 465     GLY G   337                                                      
REMARK 465     VAL G   338                                                      
REMARK 465     ALA G   339                                                      
REMARK 465     GLY G   340                                                      
REMARK 465     VAL G   341                                                      
REMARK 465     GLY G   342                                                      
REMARK 465     ALA G   343                                                      
REMARK 465     GLY G   344                                                      
REMARK 465     LEU G   345                                                      
REMARK 465     ALA G   346                                                      
REMARK 465     TYR G   347                                                      
REMARK 465     LEU G   348                                                      
REMARK 465     ILE G   349                                                      
REMARK 465     ARG G   350                                                      
REMARK 465     ASP I   323                                                      
REMARK 465     LEU I   324                                                      
REMARK 465     GLU I   325                                                      
REMARK 465     GLY I   326                                                      
REMARK 465     GLY I   327                                                      
REMARK 465     ILE I   328                                                      
REMARK 465     ARG I   329                                                      
REMARK 465     ASN I   330                                                      
REMARK 465     VAL I   331                                                      
REMARK 465     LEU I   332                                                      
REMARK 465     LEU I   333                                                      
REMARK 465     ALA I   334                                                      
REMARK 465     PHE I   335                                                      
REMARK 465     ALA I   336                                                      
REMARK 465     GLY I   337                                                      
REMARK 465     VAL I   338                                                      
REMARK 465     ALA I   339                                                      
REMARK 465     GLY I   340                                                      
REMARK 465     VAL I   341                                                      
REMARK 465     GLY I   342                                                      
REMARK 465     ALA I   343                                                      
REMARK 465     GLY I   344                                                      
REMARK 465     LEU I   345                                                      
REMARK 465     ALA I   346                                                      
REMARK 465     TYR I   347                                                      
REMARK 465     LEU I   348                                                      
REMARK 465     ILE I   349                                                      
REMARK 465     ARG I   350                                                      
REMARK 465     ASP K   323                                                      
REMARK 465     LEU K   324                                                      
REMARK 465     GLU K   325                                                      
REMARK 465     GLY K   326                                                      
REMARK 465     GLY K   327                                                      
REMARK 465     ILE K   328                                                      
REMARK 465     ARG K   329                                                      
REMARK 465     ASN K   330                                                      
REMARK 465     VAL K   331                                                      
REMARK 465     LEU K   332                                                      
REMARK 465     LEU K   333                                                      
REMARK 465     ALA K   334                                                      
REMARK 465     PHE K   335                                                      
REMARK 465     ALA K   336                                                      
REMARK 465     GLY K   337                                                      
REMARK 465     VAL K   338                                                      
REMARK 465     ALA K   339                                                      
REMARK 465     GLY K   340                                                      
REMARK 465     VAL K   341                                                      
REMARK 465     GLY K   342                                                      
REMARK 465     ALA K   343                                                      
REMARK 465     GLY K   344                                                      
REMARK 465     LEU K   345                                                      
REMARK 465     ALA K   346                                                      
REMARK 465     TYR K   347                                                      
REMARK 465     LEU K   348                                                      
REMARK 465     ILE K   349                                                      
REMARK 465     ARG K   350                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE K 181    CB   CG1  CG2  CD1                                  
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   OE2  GLU A   288     NZ   LYS J    34     1655     1.86            
REMARK 500   N    ARG E   201     OD2  ASP F    36     2544     1.89            
REMARK 500   OG1  THR K   196     OD1  ASP L    36     2455     2.09            
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  98   CB    GLU B  98   CG      0.161                       
REMARK 500    PRO I 198   CA    PRO I 198   C       0.199                       
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    ARG A 176   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG B  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    LEU B  28   CA  -  CB  -  CG  ANGL. DEV. =  16.7 DEGREES          
REMARK 500    LEU B  28   CB  -  CG  -  CD2 ANGL. DEV. =  21.9 DEGREES          
REMARK 500    ARG B  42   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B  90   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    GLU B  98   CB  -  CA  -  C   ANGL. DEV. =  15.7 DEGREES          
REMARK 500    ASP C 172   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    SER C 255   CB  -  CA  -  C   ANGL. DEV. = -15.7 DEGREES          
REMARK 500    ARG D  33   CG  -  CD  -  NE  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    ARG D  33   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG D  90   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG D  90   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG E 184   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG E 184   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP E 195   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG E 207   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG E 303   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG F  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG F 101   CD  -  NE  -  CZ  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ARG F 101   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG F 101   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG F 108   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG G 184   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG G 187   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG G 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    MET G 199   CG  -  SD  -  CE  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ARG G 207   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG G 207   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    GLU H  87   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    ARG H 108   CG  -  CD  -  NE  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    LEU H 114   CB  -  CG  -  CD2 ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ARG I 176   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    MET I 199   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG I 201   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG J 108   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    LEU J 114   CB  -  CG  -  CD2 ANGL. DEV. =  13.3 DEGREES          
REMARK 500    MET K 199   N   -  CA  -  C   ANGL. DEV. =  22.8 DEGREES          
REMARK 500    ARG K 201   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG L  42   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG L  55   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    LEU L  88   CB  -  CG  -  CD2 ANGL. DEV. =  15.3 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    ALA A 204     -124.97   -122.37                                   
REMARK 500    ASN A 239     -148.27   -141.38                                   
REMARK 500    ALA B  77       37.69    -97.03                                   
REMARK 500    SER C 202       42.03    -84.17                                   
REMARK 500    ALA C 204     -125.00   -123.97                                   
REMARK 500    ASN C 239     -148.90   -140.42                                   
REMARK 500    ALA D  77       36.64    -95.05                                   
REMARK 500    MET E 199     -100.57    -79.81                                   
REMARK 500    SER E 202       57.17     35.73                                   
REMARK 500    ASN E 239     -149.63   -141.85                                   
REMARK 500    ALA F  77       37.37    -96.32                                   
REMARK 500    LYS G 197      159.30    -44.89                                   
REMARK 500    MET G 199       47.76   -101.58                                   
REMARK 500    SER G 202       55.90     37.46                                   
REMARK 500    ASN G 239     -148.43   -141.40                                   
REMARK 500    ALA H  77       36.32    -95.01                                   
REMARK 500    LYS I 194       49.57    -97.37                                   
REMARK 500    LYS I 197      163.70    171.31                                   
REMARK 500    MET I 199     -111.20     64.28                                   
REMARK 500    SER I 202       65.03     33.60                                   
REMARK 500    ASN I 239     -148.77   -141.04                                   
REMARK 500    ALA J  77       36.37    -95.72                                   
REMARK 500    SER K 202       40.38    -86.01                                   
REMARK 500    ALA K 204     -125.69   -122.02                                   
REMARK 500    ASN K 239     -148.04   -140.30                                   
REMARK 500    ALA L  77       38.09    -96.83                                   
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 MET A  199     GLY A  200                  147.90                    
REMARK 500 MET C  199     GLY C  200                  147.93                    
REMARK 500 MET K  199     GLY K  200                 -142.69                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5JSN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OYD   RELATED DB: PDB                                   
DBREF  5JSB A  172   350  UNP    Q07820   MCL1_HUMAN     172    350             
DBREF  5JSB B    2   117  PDB    5JSB     5JSB             2    117             
DBREF  5JSB C  172   350  UNP    Q07820   MCL1_HUMAN     172    350             
DBREF  5JSB D    2   117  PDB    5JSB     5JSB             2    117             
DBREF  5JSB E  172   350  UNP    Q07820   MCL1_HUMAN     172    350             
DBREF  5JSB F    2   117  PDB    5JSB     5JSB             2    117             
DBREF  5JSB G  172   350  UNP    Q07820   MCL1_HUMAN     172    350             
DBREF  5JSB H    2   117  PDB    5JSB     5JSB             2    117             
DBREF  5JSB I  172   350  UNP    Q07820   MCL1_HUMAN     172    350             
DBREF  5JSB J    2   117  PDB    5JSB     5JSB             2    117             
DBREF  5JSB K  172   350  UNP    Q07820   MCL1_HUMAN     172    350             
DBREF  5JSB L    2   117  PDB    5JSB     5JSB             2    117             
SEQRES   1 A  179  ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER ARG          
SEQRES   2 A  179  TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR LYS          
SEQRES   3 A  179  PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA LEU          
SEQRES   4 A  179  GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG ASN          
SEQRES   5 A  179  HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU ASP          
SEQRES   6 A  179  ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG VAL          
SEQRES   7 A  179  MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP GLY          
SEQRES   8 A  179  ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL ALA          
SEQRES   9 A  179  LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE GLU          
SEQRES  10 A  179  PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG THR          
SEQRES  11 A  179  LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP GLY          
SEQRES  12 A  179  PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY GLY          
SEQRES  13 A  179  ILE ARG ASN VAL LEU LEU ALA PHE ALA GLY VAL ALA GLY          
SEQRES  14 A  179  VAL GLY ALA GLY LEU ALA TYR LEU ILE ARG                      
SEQRES   1 B  116  ASP PRO LYS LYS VAL LEU ASP LYS ALA LYS ASP GLN ALA          
SEQRES   2 B  116  GLU ASN ARG VAL ARG GLU LEU LYS GLN VAL LEU GLU GLU          
SEQRES   3 B  116  LEU TYR LYS GLU ALA ARG LYS LEU ASP LEU THR GLN GLU          
SEQRES   4 B  116  MET ARG LYS LYS LEU ILE GLU ARG TYR ALA ALA ALA ILE          
SEQRES   5 B  116  ILE ARG ALA ILE GLY ASP ILE ASN ASN ALA ILE TYR GLN          
SEQRES   6 B  116  ALA LYS GLN GLU ALA GLU LYS LEU LYS LYS ALA GLY LEU          
SEQRES   7 B  116  VAL ASN SER GLN GLN LEU ASP GLU LEU LEU ARG ARG LEU          
SEQRES   8 B  116  ASP GLU LEU GLN LYS GLU ALA SER ARG LYS ALA ASN GLU          
SEQRES   9 B  116  TYR GLY ARG GLU PHE GLU LEU LYS LEU GLU TYR GLY              
SEQRES   1 C  179  ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER ARG          
SEQRES   2 C  179  TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR LYS          
SEQRES   3 C  179  PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA LEU          
SEQRES   4 C  179  GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG ASN          
SEQRES   5 C  179  HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU ASP          
SEQRES   6 C  179  ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG VAL          
SEQRES   7 C  179  MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP GLY          
SEQRES   8 C  179  ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL ALA          
SEQRES   9 C  179  LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE GLU          
SEQRES  10 C  179  PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG THR          
SEQRES  11 C  179  LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP GLY          
SEQRES  12 C  179  PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY GLY          
SEQRES  13 C  179  ILE ARG ASN VAL LEU LEU ALA PHE ALA GLY VAL ALA GLY          
SEQRES  14 C  179  VAL GLY ALA GLY LEU ALA TYR LEU ILE ARG                      
SEQRES   1 D  116  ASP PRO LYS LYS VAL LEU ASP LYS ALA LYS ASP GLN ALA          
SEQRES   2 D  116  GLU ASN ARG VAL ARG GLU LEU LYS GLN VAL LEU GLU GLU          
SEQRES   3 D  116  LEU TYR LYS GLU ALA ARG LYS LEU ASP LEU THR GLN GLU          
SEQRES   4 D  116  MET ARG LYS LYS LEU ILE GLU ARG TYR ALA ALA ALA ILE          
SEQRES   5 D  116  ILE ARG ALA ILE GLY ASP ILE ASN ASN ALA ILE TYR GLN          
SEQRES   6 D  116  ALA LYS GLN GLU ALA GLU LYS LEU LYS LYS ALA GLY LEU          
SEQRES   7 D  116  VAL ASN SER GLN GLN LEU ASP GLU LEU LEU ARG ARG LEU          
SEQRES   8 D  116  ASP GLU LEU GLN LYS GLU ALA SER ARG LYS ALA ASN GLU          
SEQRES   9 D  116  TYR GLY ARG GLU PHE GLU LEU LYS LEU GLU TYR GLY              
SEQRES   1 E  179  ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER ARG          
SEQRES   2 E  179  TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR LYS          
SEQRES   3 E  179  PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA LEU          
SEQRES   4 E  179  GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG ASN          
SEQRES   5 E  179  HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU ASP          
SEQRES   6 E  179  ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG VAL          
SEQRES   7 E  179  MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP GLY          
SEQRES   8 E  179  ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL ALA          
SEQRES   9 E  179  LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE GLU          
SEQRES  10 E  179  PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG THR          
SEQRES  11 E  179  LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP GLY          
SEQRES  12 E  179  PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY GLY          
SEQRES  13 E  179  ILE ARG ASN VAL LEU LEU ALA PHE ALA GLY VAL ALA GLY          
SEQRES  14 E  179  VAL GLY ALA GLY LEU ALA TYR LEU ILE ARG                      
SEQRES   1 F  116  ASP PRO LYS LYS VAL LEU ASP LYS ALA LYS ASP GLN ALA          
SEQRES   2 F  116  GLU ASN ARG VAL ARG GLU LEU LYS GLN VAL LEU GLU GLU          
SEQRES   3 F  116  LEU TYR LYS GLU ALA ARG LYS LEU ASP LEU THR GLN GLU          
SEQRES   4 F  116  MET ARG LYS LYS LEU ILE GLU ARG TYR ALA ALA ALA ILE          
SEQRES   5 F  116  ILE ARG ALA ILE GLY ASP ILE ASN ASN ALA ILE TYR GLN          
SEQRES   6 F  116  ALA LYS GLN GLU ALA GLU LYS LEU LYS LYS ALA GLY LEU          
SEQRES   7 F  116  VAL ASN SER GLN GLN LEU ASP GLU LEU LEU ARG ARG LEU          
SEQRES   8 F  116  ASP GLU LEU GLN LYS GLU ALA SER ARG LYS ALA ASN GLU          
SEQRES   9 F  116  TYR GLY ARG GLU PHE GLU LEU LYS LEU GLU TYR GLY              
SEQRES   1 G  179  ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER ARG          
SEQRES   2 G  179  TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR LYS          
SEQRES   3 G  179  PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA LEU          
SEQRES   4 G  179  GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG ASN          
SEQRES   5 G  179  HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU ASP          
SEQRES   6 G  179  ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG VAL          
SEQRES   7 G  179  MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP GLY          
SEQRES   8 G  179  ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL ALA          
SEQRES   9 G  179  LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE GLU          
SEQRES  10 G  179  PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG THR          
SEQRES  11 G  179  LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP GLY          
SEQRES  12 G  179  PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY GLY          
SEQRES  13 G  179  ILE ARG ASN VAL LEU LEU ALA PHE ALA GLY VAL ALA GLY          
SEQRES  14 G  179  VAL GLY ALA GLY LEU ALA TYR LEU ILE ARG                      
SEQRES   1 H  116  ASP PRO LYS LYS VAL LEU ASP LYS ALA LYS ASP GLN ALA          
SEQRES   2 H  116  GLU ASN ARG VAL ARG GLU LEU LYS GLN VAL LEU GLU GLU          
SEQRES   3 H  116  LEU TYR LYS GLU ALA ARG LYS LEU ASP LEU THR GLN GLU          
SEQRES   4 H  116  MET ARG LYS LYS LEU ILE GLU ARG TYR ALA ALA ALA ILE          
SEQRES   5 H  116  ILE ARG ALA ILE GLY ASP ILE ASN ASN ALA ILE TYR GLN          
SEQRES   6 H  116  ALA LYS GLN GLU ALA GLU LYS LEU LYS LYS ALA GLY LEU          
SEQRES   7 H  116  VAL ASN SER GLN GLN LEU ASP GLU LEU LEU ARG ARG LEU          
SEQRES   8 H  116  ASP GLU LEU GLN LYS GLU ALA SER ARG LYS ALA ASN GLU          
SEQRES   9 H  116  TYR GLY ARG GLU PHE GLU LEU LYS LEU GLU TYR GLY              
SEQRES   1 I  179  ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER ARG          
SEQRES   2 I  179  TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR LYS          
SEQRES   3 I  179  PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA LEU          
SEQRES   4 I  179  GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG ASN          
SEQRES   5 I  179  HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU ASP          
SEQRES   6 I  179  ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG VAL          
SEQRES   7 I  179  MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP GLY          
SEQRES   8 I  179  ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL ALA          
SEQRES   9 I  179  LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE GLU          
SEQRES  10 I  179  PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG THR          
SEQRES  11 I  179  LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP GLY          
SEQRES  12 I  179  PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY GLY          
SEQRES  13 I  179  ILE ARG ASN VAL LEU LEU ALA PHE ALA GLY VAL ALA GLY          
SEQRES  14 I  179  VAL GLY ALA GLY LEU ALA TYR LEU ILE ARG                      
SEQRES   1 J  116  ASP PRO LYS LYS VAL LEU ASP LYS ALA LYS ASP GLN ALA          
SEQRES   2 J  116  GLU ASN ARG VAL ARG GLU LEU LYS GLN VAL LEU GLU GLU          
SEQRES   3 J  116  LEU TYR LYS GLU ALA ARG LYS LEU ASP LEU THR GLN GLU          
SEQRES   4 J  116  MET ARG LYS LYS LEU ILE GLU ARG TYR ALA ALA ALA ILE          
SEQRES   5 J  116  ILE ARG ALA ILE GLY ASP ILE ASN ASN ALA ILE TYR GLN          
SEQRES   6 J  116  ALA LYS GLN GLU ALA GLU LYS LEU LYS LYS ALA GLY LEU          
SEQRES   7 J  116  VAL ASN SER GLN GLN LEU ASP GLU LEU LEU ARG ARG LEU          
SEQRES   8 J  116  ASP GLU LEU GLN LYS GLU ALA SER ARG LYS ALA ASN GLU          
SEQRES   9 J  116  TYR GLY ARG GLU PHE GLU LEU LYS LEU GLU TYR GLY              
SEQRES   1 K  179  ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER ARG          
SEQRES   2 K  179  TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR LYS          
SEQRES   3 K  179  PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA LEU          
SEQRES   4 K  179  GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG ASN          
SEQRES   5 K  179  HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU ASP          
SEQRES   6 K  179  ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG VAL          
SEQRES   7 K  179  MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP GLY          
SEQRES   8 K  179  ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL ALA          
SEQRES   9 K  179  LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE GLU          
SEQRES  10 K  179  PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG THR          
SEQRES  11 K  179  LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP GLY          
SEQRES  12 K  179  PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY GLY          
SEQRES  13 K  179  ILE ARG ASN VAL LEU LEU ALA PHE ALA GLY VAL ALA GLY          
SEQRES  14 K  179  VAL GLY ALA GLY LEU ALA TYR LEU ILE ARG                      
SEQRES   1 L  116  ASP PRO LYS LYS VAL LEU ASP LYS ALA LYS ASP GLN ALA          
SEQRES   2 L  116  GLU ASN ARG VAL ARG GLU LEU LYS GLN VAL LEU GLU GLU          
SEQRES   3 L  116  LEU TYR LYS GLU ALA ARG LYS LEU ASP LEU THR GLN GLU          
SEQRES   4 L  116  MET ARG LYS LYS LEU ILE GLU ARG TYR ALA ALA ALA ILE          
SEQRES   5 L  116  ILE ARG ALA ILE GLY ASP ILE ASN ASN ALA ILE TYR GLN          
SEQRES   6 L  116  ALA LYS GLN GLU ALA GLU LYS LEU LYS LYS ALA GLY LEU          
SEQRES   7 L  116  VAL ASN SER GLN GLN LEU ASP GLU LEU LEU ARG ARG LEU          
SEQRES   8 L  116  ASP GLU LEU GLN LYS GLU ALA SER ARG LYS ALA ASN GLU          
SEQRES   9 L  116  TYR GLY ARG GLU PHE GLU LEU LYS LEU GLU TYR GLY              
FORMUL  13  HOH   *22(H2 O)                                                     
HELIX    1 AA1 ASP A  172  GLY A  192  1                                  21    
HELIX    2 AA2 ALA A  204  HIS A  224  1                                  21    
HELIX    3 AA3 HIS A  224  ASP A  236  1                                  13    
HELIX    4 AA4 GLU A  240  SER A  255  1                                  16    
HELIX    5 AA5 ASN A  260  ILE A  281  1                                  22    
HELIX    6 AA6 ASN A  282  SER A  285  5                                   4    
HELIX    7 AA7 CYS A  286  GLN A  309  1                                  24    
HELIX    8 AA8 ARG A  310  HIS A  320  1                                  11    
HELIX    9 AA9 PRO B    3  LEU B   35  1                                  33    
HELIX   10 AB1 THR B   38  ALA B   77  1                                  40    
HELIX   11 AB2 ASN B   81  TYR B  116  1                                  36    
HELIX   12 AB3 GLU C  173  GLY C  192  1                                  20    
HELIX   13 AB4 ALA C  204  HIS C  224  1                                  21    
HELIX   14 AB5 HIS C  224  ASP C  236  1                                  13    
HELIX   15 AB6 GLU C  240  SER C  255  1                                  16    
HELIX   16 AB7 ASN C  260  ILE C  281  1                                  22    
HELIX   17 AB8 GLN C  283  SER C  285  5                                   3    
HELIX   18 AB9 CYS C  286  GLN C  309  1                                  24    
HELIX   19 AC1 ARG C  310  HIS C  320  1                                  11    
HELIX   20 AC2 PRO D    3  LEU D   35  1                                  33    
HELIX   21 AC3 THR D   38  ALA D   77  1                                  40    
HELIX   22 AC4 ASN D   81  TYR D  116  1                                  36    
HELIX   23 AC5 GLU E  173  GLY E  192  1                                  20    
HELIX   24 AC6 SER E  202  HIS E  224  1                                  23    
HELIX   25 AC7 HIS E  224  ASP E  236  1                                  13    
HELIX   26 AC8 GLU E  240  SER E  255  1                                  16    
HELIX   27 AC9 ASN E  260  ILE E  281  1                                  22    
HELIX   28 AD1 ASN E  282  SER E  285  5                                   4    
HELIX   29 AD2 CYS E  286  GLN E  309  1                                  24    
HELIX   30 AD3 ARG E  310  HIS E  320  1                                  11    
HELIX   31 AD4 PRO F    3  LEU F   35  1                                  33    
HELIX   32 AD5 THR F   38  ALA F   77  1                                  40    
HELIX   33 AD6 ASN F   81  GLY F  117  1                                  37    
HELIX   34 AD7 GLU G  173  GLY G  192  1                                  20    
HELIX   35 AD8 SER G  202  HIS G  224  1                                  23    
HELIX   36 AD9 HIS G  224  ASP G  236  1                                  13    
HELIX   37 AE1 GLU G  240  SER G  255  1                                  16    
HELIX   38 AE2 ASN G  260  ILE G  281  1                                  22    
HELIX   39 AE3 ASN G  282  SER G  285  5                                   4    
HELIX   40 AE4 CYS G  286  GLN G  309  1                                  24    
HELIX   41 AE5 ARG G  310  HIS G  320  1                                  11    
HELIX   42 AE6 PRO H    3  LEU H   35  1                                  33    
HELIX   43 AE7 THR H   38  ALA H   77  1                                  40    
HELIX   44 AE8 ASN H   81  GLY H  117  1                                  37    
HELIX   45 AE9 GLU I  173  GLY I  192  1                                  20    
HELIX   46 AF1 SER I  202  HIS I  224  1                                  23    
HELIX   47 AF2 HIS I  224  ASP I  236  1                                  13    
HELIX   48 AF3 GLU I  240  SER I  255  1                                  16    
HELIX   49 AF4 ASN I  260  ILE I  281  1                                  22    
HELIX   50 AF5 ASN I  282  SER I  285  5                                   4    
HELIX   51 AF6 CYS I  286  GLN I  309  1                                  24    
HELIX   52 AF7 ARG I  310  HIS I  320  1                                  11    
HELIX   53 AF8 PRO J    3  LEU J   35  1                                  33    
HELIX   54 AF9 THR J   38  ALA J   77  1                                  40    
HELIX   55 AG1 ASN J   81  TYR J  116  1                                  36    
HELIX   56 AG2 GLU K  173  GLY K  192  1                                  20    
HELIX   57 AG3 ALA K  204  HIS K  224  1                                  21    
HELIX   58 AG4 HIS K  224  ASP K  236  1                                  13    
HELIX   59 AG5 GLU K  240  SER K  255  1                                  16    
HELIX   60 AG6 ASN K  260  ILE K  281  1                                  22    
HELIX   61 AG7 GLN K  283  SER K  285  5                                   3    
HELIX   62 AG8 CYS K  286  GLN K  309  1                                  24    
HELIX   63 AG9 ARG K  310  HIS K  320  1                                  11    
HELIX   64 AH1 PRO L    3  LEU L   35  1                                  33    
HELIX   65 AH2 THR L   38  ALA L   77  1                                  40    
HELIX   66 AH3 ASN L   81  GLY L  117  1                                  37    
CRYST1   61.917   92.246  162.005  90.00  92.39  90.00 P 1 21 1     12          
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      0.016151  0.000000  0.000674        0.00000                         
SCALE2      0.000000  0.010841  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006178        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system