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Database: PDB
Entry: 6MBZ
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Original site: 6MBZ 
HEADER    TRANSCRIPTION ACTIVATOR                 30-AUG-18   6MBZ              
TITLE     STRUCTURE OF TRANSCRIPTION FACTOR                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 5B;       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: STAT5B;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    TRANSCRIPTION FACTOR, TRANSCRIPTION ACTIVATOR                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.-S.SEO,S.DHE-PAGANON                                                
REVDAT   1   19-JUN-19 6MBZ    0                                                
JRNL        AUTH   E.D.DE ARAUJO,F.ERDOGAN,H.A.NEUBAUER,D.MENEKSEDAG-EROL,      
JRNL        AUTH 2 P.MANASWIYOUNGKUL,M.S.ERAM,H.S.SEO,A.K.QADREE,J.ISRAELIAN,   
JRNL        AUTH 3 A.ORLOVA,T.SUSKE,H.T.T.PHAM,A.BOERSMA,S.TANGERMANN,L.KENNER, 
JRNL        AUTH 4 T.RULICKE,A.DONG,M.RAVICHANDRAN,P.J.BROWN,G.F.AUDETTE,       
JRNL        AUTH 5 S.RAUSCHER,S.DHE-PAGANON,R.MORIGGL,P.T.GUNNING               
JRNL        TITL   STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF THE                
JRNL        TITL 2 STAT5BN642HDRIVER MUTATION.                                  
JRNL        REF    NAT COMMUN                    V.  10  2517 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   31175292                                                     
JRNL        DOI    10.1038/S41467-019-10422-7                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.14_3260: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 23022                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.266                           
REMARK   3   R VALUE            (WORKING SET) : 0.265                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1143                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 70.7171 -  6.4186    1.00     2906   147  0.2279 0.2600        
REMARK   3     2  6.4186 -  5.0951    1.00     2786   122  0.2785 0.2480        
REMARK   3     3  5.0951 -  4.4512    1.00     2725   154  0.2237 0.2696        
REMARK   3     4  4.4512 -  4.0442    1.00     2717   131  0.2563 0.2602        
REMARK   3     5  4.0442 -  3.7544    1.00     2745   118  0.2929 0.2791        
REMARK   3     6  3.7544 -  3.5330    1.00     2672   157  0.3171 0.3717        
REMARK   3     7  3.5330 -  3.3561    1.00     2674   152  0.3426 0.3617        
REMARK   3     8  3.3561 -  3.2100    1.00     2654   162  0.3857 0.4275        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.530            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.780           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 95.95                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           8072                                  
REMARK   3   ANGLE     :  0.793          11019                                  
REMARK   3   CHIRALITY :  0.046           1279                                  
REMARK   3   PLANARITY :  0.006           1431                                  
REMARK   3   DIHEDRAL  :  4.572           4785                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 349 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.9016  59.5186  66.7131              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9316 T22:   0.7782                                     
REMARK   3      T33:   0.9052 T12:   0.1235                                     
REMARK   3      T13:  -0.0080 T23:   0.1117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0024 L22:   4.3061                                     
REMARK   3      L33:   0.7441 L12:  -3.9137                                     
REMARK   3      L13:   1.0780 L23:  -1.6631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2536 S12:  -0.6057 S13:  -0.1359                       
REMARK   3      S21:   0.0957 S22:   0.3878 S23:   0.2528                       
REMARK   3      S31:   0.1236 S32:  -0.1139 S33:  -0.1104                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 350 THROUGH 488 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6522  41.4519  68.3785              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7697 T22:   0.5658                                     
REMARK   3      T33:   0.7174 T12:   0.0609                                     
REMARK   3      T13:   0.0785 T23:   0.0766                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7539 L22:   3.5305                                     
REMARK   3      L33:   6.5005 L12:  -1.0123                                     
REMARK   3      L13:   0.0169 L23:  -1.3434                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1549 S12:   0.1762 S13:   0.2736                       
REMARK   3      S21:   0.3231 S22:   0.0693 S23:  -0.1166                       
REMARK   3      S31:  -0.1874 S32:   0.2534 S33:   0.2144                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 489 THROUGH 685 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3495   9.6072  89.9028              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7559 T22:   0.8129                                     
REMARK   3      T33:   0.7191 T12:   0.0577                                     
REMARK   3      T13:  -0.0099 T23:   0.0899                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5936 L22:   7.5649                                     
REMARK   3      L33:   1.2538 L12:  -0.7540                                     
REMARK   3      L13:  -0.3841 L23:  -0.3408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0815 S12:  -0.2528 S13:  -0.1481                       
REMARK   3      S21:   0.2449 S22:   0.3666 S23:   0.5401                       
REMARK   3      S31:  -0.0875 S32:  -0.5319 S33:  -0.2650                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 138 THROUGH 249 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.4267  34.9590 115.5223              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9816 T22:   0.8151                                     
REMARK   3      T33:   1.2776 T12:   0.1851                                     
REMARK   3      T13:  -0.0418 T23:  -0.1526                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0700 L22:   0.5887                                     
REMARK   3      L33:   1.5617 L12:  -2.4196                                     
REMARK   3      L13:   3.3693 L23:  -0.6449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3300 S12:   0.5632 S13:  -0.5859                       
REMARK   3      S21:  -0.1460 S22:  -0.2073 S23:   0.0983                       
REMARK   3      S31:   0.3958 S32:   0.2397 S33:  -0.2222                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 250 THROUGH 349 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8112  52.6675 111.3304              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8971 T22:   0.7914                                     
REMARK   3      T33:   0.8116 T12:   0.0350                                     
REMARK   3      T13:  -0.0612 T23:  -0.0300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3799 L22:   2.1317                                     
REMARK   3      L33:   0.9806 L12:  -3.4211                                     
REMARK   3      L13:   1.9442 L23:  -0.8807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0710 S12:  -0.0400 S13:  -0.5268                       
REMARK   3      S21:  -0.1497 S22:   0.0022 S23:  -0.0768                       
REMARK   3      S31:   0.1010 S32:  -0.0756 S33:  -0.1069                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 350 THROUGH 503 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5891  67.7191 109.9029              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6527 T22:   0.6401                                     
REMARK   3      T33:   0.6301 T12:  -0.0322                                     
REMARK   3      T13:   0.0963 T23:   0.0469                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5332 L22:   4.2983                                     
REMARK   3      L33:   3.8686 L12:  -2.0094                                     
REMARK   3      L13:   0.6374 L23:   0.6154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1637 S12:   0.1470 S13:   0.2562                       
REMARK   3      S21:   0.4925 S22:  -0.0070 S23:  -0.4163                       
REMARK   3      S31:  -0.1256 S32:   0.4677 S33:   0.2699                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 504 THROUGH 685 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -50.4787  62.9531  92.0551              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6817 T22:   1.0562                                     
REMARK   3      T33:   0.5189 T12:  -0.0222                                     
REMARK   3      T13:  -0.0366 T23:   0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5056 L22:   2.2970                                     
REMARK   3      L33:   1.6842 L12:  -1.3176                                     
REMARK   3      L13:   1.4565 L23:   0.2265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1176 S12:   0.1941 S13:  -0.1585                       
REMARK   3      S21:  -0.1512 S22:  -0.0120 S23:  -0.1126                       
REMARK   3      S31:   0.1716 S32:  -0.2871 S33:  -0.0927                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6MBZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000236612.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23029                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.210                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.7900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.21                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.15200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1Y1U                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, VAPOR DIFFUSION, SITTING       
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       66.19000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.70000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       66.19000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.70000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 810  LIES ON A SPECIAL POSITION.                          
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     SER A   132                                                      
REMARK 465     THR A   133                                                      
REMARK 465     GLY A   134                                                      
REMARK 465     SER A   135                                                      
REMARK 465     ALA A   136                                                      
REMARK 465     MET A   137                                                      
REMARK 465     GLN A   185                                                      
REMARK 465     PHE A   186                                                      
REMARK 465     GLY A   187                                                      
REMARK 465     ARG A   389                                                      
REMARK 465     ASN A   390                                                      
REMARK 465     ASP A   391                                                      
REMARK 465     SER A   427                                                      
REMARK 465     ASP A   428                                                      
REMARK 465     ARG A   429                                                      
REMARK 465     ARG A   430                                                      
REMARK 465     GLY A   431                                                      
REMARK 465     ALA A   432                                                      
REMARK 465     VAL A   686                                                      
REMARK 465     PRO A   687                                                      
REMARK 465     CYS A   688                                                      
REMARK 465     GLU A   689                                                      
REMARK 465     SER A   690                                                      
REMARK 465     ALA A   691                                                      
REMARK 465     THR A   692                                                      
REMARK 465     ALA A   693                                                      
REMARK 465     LYS A   694                                                      
REMARK 465     ALA A   695                                                      
REMARK 465     VAL A   696                                                      
REMARK 465     ASP A   697                                                      
REMARK 465     GLY A   698                                                      
REMARK 465     TYR A   699                                                      
REMARK 465     VAL A   700                                                      
REMARK 465     LYS A   701                                                      
REMARK 465     PRO A   702                                                      
REMARK 465     GLN A   703                                                      
REMARK 465     SER B   132                                                      
REMARK 465     THR B   133                                                      
REMARK 465     GLY B   134                                                      
REMARK 465     SER B   135                                                      
REMARK 465     ALA B   136                                                      
REMARK 465     MET B   137                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     LEU B   189                                                      
REMARK 465     ALA B   190                                                      
REMARK 465     GLN B   191                                                      
REMARK 465     LEU B   192                                                      
REMARK 465     SER B   193                                                      
REMARK 465     PRO B   194                                                      
REMARK 465     GLN B   195                                                      
REMARK 465     GLU B   196                                                      
REMARK 465     ARG B   197                                                      
REMARK 465     LEU B   198                                                      
REMARK 465     SER B   199                                                      
REMARK 465     GLU B   386                                                      
REMARK 465     ASN B   387                                                      
REMARK 465     THR B   388                                                      
REMARK 465     ARG B   389                                                      
REMARK 465     ASN B   390                                                      
REMARK 465     ASP B   428                                                      
REMARK 465     ARG B   429                                                      
REMARK 465     ARG B   430                                                      
REMARK 465     GLY B   431                                                      
REMARK 465     ALA B   432                                                      
REMARK 465     GLU B   433                                                      
REMARK 465     SER B   434                                                      
REMARK 465     VAL B   435                                                      
REMARK 465     VAL B   686                                                      
REMARK 465     PRO B   687                                                      
REMARK 465     CYS B   688                                                      
REMARK 465     GLU B   689                                                      
REMARK 465     SER B   690                                                      
REMARK 465     ALA B   691                                                      
REMARK 465     THR B   692                                                      
REMARK 465     ALA B   693                                                      
REMARK 465     LYS B   694                                                      
REMARK 465     ALA B   695                                                      
REMARK 465     VAL B   696                                                      
REMARK 465     ASP B   697                                                      
REMARK 465     GLY B   698                                                      
REMARK 465     TYR B   699                                                      
REMARK 465     VAL B   700                                                      
REMARK 465     LYS B   701                                                      
REMARK 465     PRO B   702                                                      
REMARK 465     GLN B   703                                                      
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 A 182    CG1  CG2  CD1                                       
REMARK 470     LEU A 189    CG   CD1  CD2                                       
REMARK 470     GLN A 191    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 192    CG   CD1  CD2                                       
REMARK 470     GLN A 195    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 198    CG   CD1  CD2                                       
REMARK 470     SER A 199    OG                                                  
REMARK 470     ARG A 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 202    OG1  CG2                                            
REMARK 470     GLN A 206    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 303    CG   CD1  CD2                                       
REMARK 470     GLU A 311    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 315    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 343    CG   CD   CE   NZ                                   
REMARK 470     ASN A 361    CG   OD1  ND2                                       
REMARK 470     MET A 364    CG   SD   CE                                        
REMARK 470     GLN A 368    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     GLN A 377    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 378    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 380    CG   CD   CE   NZ                                   
REMARK 470     GLU A 386    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 387    CG   OD1  ND2                                       
REMARK 470     THR A 388    OG1  CG2                                            
REMARK 470     TYR A 392    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 395    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 407    CG   CD   OE1  NE2                                  
REMARK 470     THR A 409    OG1  CG2                                            
REMARK 470     ARG A 417    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 425    CG   CD   CE   NZ                                   
REMARK 470     GLU A 433    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 454    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 460    CG   CD   CE   NZ                                   
REMARK 470     GLN A 474    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 490    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 501    CG   CD   CE   NZ                                   
REMARK 470     GLN A 506    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 509    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 527    CG   CD   CE   NZ                                   
REMARK 470     LYS A 536    CG   CD   CE   NZ                                   
REMARK 470     ASN A 540    CG   OD1  ND2                                       
REMARK 470     LEU A 545    CG   CD1  CD2                                       
REMARK 470     GLU A 546    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 560    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 563    CG   CD1  CD2                                       
REMARK 470     ARG A 566    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 568    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR A 569    OG1  CG2                                            
REMARK 470     GLN A 572    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 579    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 582    CG   CD   CE   NZ                                   
REMARK 470     LYS A 586    CG   CD   CE   NZ                                   
REMARK 470     VAL A 598    CG1  CG2                                            
REMARK 470     LYS A 600    CG   CD   CE   NZ                                   
REMARK 470     GLN A 601    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 610    CG   CD   CE   NZ                                   
REMARK 470     GLU A 623    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 624    CG1  CG2  CD1                                       
REMARK 470     LYS A 632    CG   CD   CE   NZ                                   
REMARK 470     ASP A 634    CG   OD1  OD2                                       
REMARK 470     SER A 635    OG                                                  
REMARK 470     ARG A 638    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 664    CG   OD1  ND2                                       
REMARK 470     LEU A 666    CG   CD1  CD2                                       
REMARK 470     ARG A 673    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 139    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 140    CG   CD   CE   NZ                                   
REMARK 470     LEU B 142    CG   CD1  CD2                                       
REMARK 470     GLN B 143    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 145    CG   OD1  ND2                                       
REMARK 470     GLN B 146    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 149    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 150    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 153    CG   CD1  CD2                                       
REMARK 470     GLN B 156    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 157    CG   OD1  OD2                                       
REMARK 470     THR B 158    OG1  CG2                                            
REMARK 470     GLU B 161    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 163    CG   CD   CE   NZ                                   
REMARK 470     LYS B 164    CG   CD   CE   NZ                                   
REMARK 470     GLN B 167    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 180    CG   CD1  CD2                                       
REMARK 470     ILE B 182    CG1  CG2  CD1                                       
REMARK 470     GLN B 183    CG   CD   OE1  NE2                                  
REMARK 470     PHE B 186    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 201    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 204    CG   CD1  CD2                                       
REMARK 470     GLN B 205    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 207    CG   CD   CE   NZ                                   
REMARK 470     GLN B 216    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 217    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 220    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 231    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 234    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 235    CG   CD   CE   NZ                                   
REMARK 470     GLN B 238    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 242    CG   CD   CE   NZ                                   
REMARK 470     ARG B 294    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 297    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 299    CG   CD1  CD2                                       
REMARK 470     GLU B 311    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 313    CG   CD1  CD2                                       
REMARK 470     LYS B 336    CG   CD   CE   NZ                                   
REMARK 470     LYS B 359    CG   CD   CE   NZ                                   
REMARK 470     LEU B 360    CG   CD1  CD2                                       
REMARK 470     ASN B 361    CG   OD1  ND2                                       
REMARK 470     VAL B 362    CG1  CG2                                            
REMARK 470     HIS B 363    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET B 364    CG   SD   CE                                        
REMARK 470     ASN B 365    CG   OD1  ND2                                       
REMARK 470     GLN B 368    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 370    CG   CD   CE   NZ                                   
REMARK 470     GLN B 378    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 384    CG   CD   CE   NZ                                   
REMARK 470     GLU B 395    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 404    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 405    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS B 406    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B 407    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 423    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 425    CG   CD   CE   NZ                                   
REMARK 470     GLU B 438    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 453    CG   OD1  ND2                                       
REMARK 470     GLU B 454    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 455    CG   CD1  CD2                                       
REMARK 470     VAL B 456    CG1  CG2                                            
REMARK 470     HIS B 471    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER B 473    OG                                                  
REMARK 470     GLN B 474    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 475    CG   OD1  OD2                                       
REMARK 470     ASN B 476    CG   OD1  ND2                                       
REMARK 470     GLU B 490    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 494    CG1  CG2                                            
REMARK 470     ASP B 500    CG   OD1  OD2                                       
REMARK 470     LYS B 501    CG   CD   CE   NZ                                   
REMARK 470     LYS B 527    CG   CD   CE   NZ                                   
REMARK 470     GLN B 535    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 536    CG   CD   CE   NZ                                   
REMARK 470     PHE B 538    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN B 539    CG   OD1  ND2                                       
REMARK 470     ASN B 540    CG   OD1  ND2                                       
REMARK 470     SER B 541    OG                                                  
REMARK 470     HIS B 544    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU B 545    CG   CD1  CD2                                       
REMARK 470     GLU B 546    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 547    CG   OD1  OD2                                       
REMARK 470     GLN B 557    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 560    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 563    CG   CD1  CD2                                       
REMARK 470     ARG B 566    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 568    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR B 569    OG1  CG2                                            
REMARK 470     GLN B 572    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 582    CG   CD   CE   NZ                                   
REMARK 470     LYS B 583    CG   CD   CE   NZ                                   
REMARK 470     LEU B 585    CG   CD1  CD2                                       
REMARK 470     LYS B 586    CG   CD   CE   NZ                                   
REMARK 470     VAL B 598    CG1  CG2                                            
REMARK 470     LYS B 600    CG   CD   CE   NZ                                   
REMARK 470     GLN B 601    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 602    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 606    CG   CD1  CD2                                       
REMARK 470     ILE B 608    CG1  CG2  CD1                                       
REMARK 470     ASN B 609    CG   OD1  ND2                                       
REMARK 470     LYS B 610    CG   CD   CE   NZ                                   
REMARK 470     ASP B 612    CG   OD1  OD2                                       
REMARK 470     GLU B 623    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 624    CG1  CG2  CD1                                       
REMARK 470     LYS B 632    CG   CD   CE   NZ                                   
REMARK 470     ASP B 634    CG   OD1  OD2                                       
REMARK 470     GLN B 636    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 637    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 656    CG   CD1  CD2                                       
REMARK 470     LEU B 663    CG   CD1  CD2                                       
REMARK 470     ASN B 664    CG   OD1  ND2                                       
REMARK 470     ILE B 667    CG1  CG2  CD1                                       
REMARK 470     ASP B 672    CG   OD1  OD2                                       
REMARK 470     ARG B 673    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 677    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 678    CG1  CG2                                            
REMARK 470     TYR B 682    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR B 683    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR B 684    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NE2  GLN B   288     O    HOH B   801              1.43            
REMARK 500   CB   LEU B   663     CD1  LEU B   666              1.65            
REMARK 500   O    SER A   210     O    HOH A   801              1.88            
REMARK 500   O    LEU B   666     NZ   LYS B   675              1.97            
REMARK 500   O    ASP A   676     OG   SER A   680              2.08            
REMARK 500   O    ASN B   540     OH   TYR B   548              2.09            
REMARK 500   N    VAL A   502     O    HOH A   802              2.15            
REMARK 500   O    LEU B   663     CD1  LEU B   666              2.17            
REMARK 500   O    TYR B   679     O    HOH B   802              2.18            
REMARK 500   O    ASN A   399     O    HOH A   803              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LEU A 464   C     PRO A 465   N       0.154                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 465   C   -  N   -  CA  ANGL. DEV. =  13.4 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    LEU A 189     -166.81   -167.44                                   
REMARK 500    ALA A 190     -161.32   -103.22                                   
REMARK 500    ASP A 250      -63.11   -125.11                                   
REMARK 500    PRO A 306      -92.33    -54.18                                   
REMARK 500    VAL A 341       74.69     54.98                                   
REMARK 500    LYS A 359     -148.17   -106.79                                   
REMARK 500    GLU A 395     -154.13     60.11                                   
REMARK 500    CYS A 400      142.66    176.34                                   
REMARK 500    LYS A 425      -78.59    -71.13                                   
REMARK 500    LYS A 501      -77.58    -91.99                                   
REMARK 500    VAL A 502      131.76     49.73                                   
REMARK 500    LEU A 537      -72.75    -73.18                                   
REMARK 500    ASN A 539       95.18    -61.91                                   
REMARK 500    LEU A 551      129.80     67.45                                   
REMARK 500    ASN A 559       11.47   -145.03                                   
REMARK 500    TYR A 568       63.17    -59.45                                   
REMARK 500    THR A 569      176.35     71.17                                   
REMARK 500    HIS A 584      -39.31   -133.46                                   
REMARK 500    HIS A 604      -72.58    -65.03                                   
REMARK 500    GLN A 636      -80.44     29.42                                   
REMARK 500    PHE A 640     -104.60    -87.71                                   
REMARK 500    TRP A 641       94.92     53.39                                   
REMARK 500    THR A 647     -167.60   -113.26                                   
REMARK 500    SER A 655      151.41     75.12                                   
REMARK 500    PHE A 670      -83.78      4.16                                   
REMARK 500    PRO A 671      -87.81    -77.00                                   
REMARK 500    GLU B 201       48.90    -99.78                                   
REMARK 500    ASP B 250      -62.79   -124.36                                   
REMARK 500    PRO B 306      -85.09    -53.51                                   
REMARK 500    VAL B 341       73.58     50.91                                   
REMARK 500    LYS B 359       57.27   -103.58                                   
REMARK 500    LEU B 360     -152.68   -161.74                                   
REMARK 500    ASN B 361       55.61    -90.02                                   
REMARK 500    HIS B 363      -38.68   -136.61                                   
REMARK 500    ALA B 408      -59.80     60.91                                   
REMARK 500    ARG B 423      157.34     62.60                                   
REMARK 500    LYS B 425      -72.98    -67.33                                   
REMARK 500    ARG B 426      154.94     68.76                                   
REMARK 500    ILE B 469      139.28     68.26                                   
REMARK 500    HIS B 471      -94.31   -157.50                                   
REMARK 500    LYS B 501      -84.95    -93.36                                   
REMARK 500    VAL B 502      132.98     61.08                                   
REMARK 500    LEU B 537      -76.80    -75.12                                   
REMARK 500    ASN B 539       95.63    -67.69                                   
REMARK 500    LEU B 545      -77.03     53.25                                   
REMARK 500    LEU B 551      133.86     68.34                                   
REMARK 500    ASN B 562      150.35     66.14                                   
REMARK 500    TYR B 568       67.16    -54.86                                   
REMARK 500    THR B 569      178.06     70.65                                   
REMARK 500    HIS B 584      -38.10   -134.22                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6MBZ A  136   703  UNP    P51692   STA5B_HUMAN    136    703             
DBREF  6MBZ B  136   703  UNP    P51692   STA5B_HUMAN    136    703             
SEQADV 6MBZ SER A  132  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBZ THR A  133  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBZ GLY A  134  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBZ SER A  135  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBZ HIS A  642  UNP  P51692    ASN   642 ENGINEERED MUTATION            
SEQADV 6MBZ SER B  132  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBZ THR B  133  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBZ GLY B  134  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBZ SER B  135  UNP  P51692              EXPRESSION TAG                 
SEQADV 6MBZ HIS B  642  UNP  P51692    ASN   642 ENGINEERED MUTATION            
SEQRES   1 A  572  SER THR GLY SER ALA MET SER GLN LYS HIS LEU GLN ILE          
SEQRES   2 A  572  ASN GLN THR PHE GLU GLU LEU ARG LEU VAL THR GLN ASP          
SEQRES   3 A  572  THR GLU ASN GLU LEU LYS LYS LEU GLN GLN THR GLN GLU          
SEQRES   4 A  572  TYR PHE ILE ILE GLN TYR GLN GLU SER LEU ARG ILE GLN          
SEQRES   5 A  572  ALA GLN PHE GLY PRO LEU ALA GLN LEU SER PRO GLN GLU          
SEQRES   6 A  572  ARG LEU SER ARG GLU THR ALA LEU GLN GLN LYS GLN VAL          
SEQRES   7 A  572  SER LEU GLU ALA TRP LEU GLN ARG GLU ALA GLN THR LEU          
SEQRES   8 A  572  GLN GLN TYR ARG VAL GLU LEU ALA GLU LYS HIS GLN LYS          
SEQRES   9 A  572  THR LEU GLN LEU LEU ARG LYS GLN GLN THR ILE ILE LEU          
SEQRES  10 A  572  ASP ASP GLU LEU ILE GLN TRP LYS ARG ARG GLN GLN LEU          
SEQRES  11 A  572  ALA GLY ASN GLY GLY PRO PRO GLU GLY SER LEU ASP VAL          
SEQRES  12 A  572  LEU GLN SER TRP CYS GLU LYS LEU ALA GLU ILE ILE TRP          
SEQRES  13 A  572  GLN ASN ARG GLN GLN ILE ARG ARG ALA GLU HIS LEU CYS          
SEQRES  14 A  572  GLN GLN LEU PRO ILE PRO GLY PRO VAL GLU GLU MET LEU          
SEQRES  15 A  572  ALA GLU VAL ASN ALA THR ILE THR ASP ILE ILE SER ALA          
SEQRES  16 A  572  LEU VAL THR SER THR PHE ILE ILE GLU LYS GLN PRO PRO          
SEQRES  17 A  572  GLN VAL LEU LYS THR GLN THR LYS PHE ALA ALA THR VAL          
SEQRES  18 A  572  ARG LEU LEU VAL GLY GLY LYS LEU ASN VAL HIS MET ASN          
SEQRES  19 A  572  PRO PRO GLN VAL LYS ALA THR ILE ILE SER GLU GLN GLN          
SEQRES  20 A  572  ALA LYS SER LEU LEU LYS ASN GLU ASN THR ARG ASN ASP          
SEQRES  21 A  572  TYR SER GLY GLU ILE LEU ASN ASN CYS CYS VAL MET GLU          
SEQRES  22 A  572  TYR HIS GLN ALA THR GLY THR LEU SER ALA HIS PHE ARG          
SEQRES  23 A  572  ASN MET SER LEU LYS ARG ILE LYS ARG SER ASP ARG ARG          
SEQRES  24 A  572  GLY ALA GLU SER VAL THR GLU GLU LYS PHE THR ILE LEU          
SEQRES  25 A  572  PHE GLU SER GLN PHE SER VAL GLY GLY ASN GLU LEU VAL          
SEQRES  26 A  572  PHE GLN VAL LYS THR LEU SER LEU PRO VAL VAL VAL ILE          
SEQRES  27 A  572  VAL HIS GLY SER GLN ASP ASN ASN ALA THR ALA THR VAL          
SEQRES  28 A  572  LEU TRP ASP ASN ALA PHE ALA GLU PRO GLY ARG VAL PRO          
SEQRES  29 A  572  PHE ALA VAL PRO ASP LYS VAL LEU TRP PRO GLN LEU CYS          
SEQRES  30 A  572  GLU ALA LEU ASN MET LYS PHE LYS ALA GLU VAL GLN SER          
SEQRES  31 A  572  ASN ARG GLY LEU THR LYS GLU ASN LEU VAL PHE LEU ALA          
SEQRES  32 A  572  GLN LYS LEU PHE ASN ASN SER SER SER HIS LEU GLU ASP          
SEQRES  33 A  572  TYR SER GLY LEU SER VAL SER TRP SER GLN PHE ASN ARG          
SEQRES  34 A  572  GLU ASN LEU PRO GLY ARG ASN TYR THR PHE TRP GLN TRP          
SEQRES  35 A  572  PHE ASP GLY VAL MET GLU VAL LEU LYS LYS HIS LEU LYS          
SEQRES  36 A  572  PRO HIS TRP ASN ASP GLY ALA ILE LEU GLY PHE VAL ASN          
SEQRES  37 A  572  LYS GLN GLN ALA HIS ASP LEU LEU ILE ASN LYS PRO ASP          
SEQRES  38 A  572  GLY THR PHE LEU LEU ARG PHE SER ASP SER GLU ILE GLY          
SEQRES  39 A  572  GLY ILE THR ILE ALA TRP LYS PHE ASP SER GLN GLU ARG          
SEQRES  40 A  572  MET PHE TRP HIS LEU MET PRO PHE THR THR ARG ASP PHE          
SEQRES  41 A  572  SER ILE ARG SER LEU ALA ASP ARG LEU GLY ASP LEU ASN          
SEQRES  42 A  572  TYR LEU ILE TYR VAL PHE PRO ASP ARG PRO LYS ASP GLU          
SEQRES  43 A  572  VAL TYR SER LYS TYR TYR THR PRO VAL PRO CYS GLU SER          
SEQRES  44 A  572  ALA THR ALA LYS ALA VAL ASP GLY TYR VAL LYS PRO GLN          
SEQRES   1 B  572  SER THR GLY SER ALA MET SER GLN LYS HIS LEU GLN ILE          
SEQRES   2 B  572  ASN GLN THR PHE GLU GLU LEU ARG LEU VAL THR GLN ASP          
SEQRES   3 B  572  THR GLU ASN GLU LEU LYS LYS LEU GLN GLN THR GLN GLU          
SEQRES   4 B  572  TYR PHE ILE ILE GLN TYR GLN GLU SER LEU ARG ILE GLN          
SEQRES   5 B  572  ALA GLN PHE GLY PRO LEU ALA GLN LEU SER PRO GLN GLU          
SEQRES   6 B  572  ARG LEU SER ARG GLU THR ALA LEU GLN GLN LYS GLN VAL          
SEQRES   7 B  572  SER LEU GLU ALA TRP LEU GLN ARG GLU ALA GLN THR LEU          
SEQRES   8 B  572  GLN GLN TYR ARG VAL GLU LEU ALA GLU LYS HIS GLN LYS          
SEQRES   9 B  572  THR LEU GLN LEU LEU ARG LYS GLN GLN THR ILE ILE LEU          
SEQRES  10 B  572  ASP ASP GLU LEU ILE GLN TRP LYS ARG ARG GLN GLN LEU          
SEQRES  11 B  572  ALA GLY ASN GLY GLY PRO PRO GLU GLY SER LEU ASP VAL          
SEQRES  12 B  572  LEU GLN SER TRP CYS GLU LYS LEU ALA GLU ILE ILE TRP          
SEQRES  13 B  572  GLN ASN ARG GLN GLN ILE ARG ARG ALA GLU HIS LEU CYS          
SEQRES  14 B  572  GLN GLN LEU PRO ILE PRO GLY PRO VAL GLU GLU MET LEU          
SEQRES  15 B  572  ALA GLU VAL ASN ALA THR ILE THR ASP ILE ILE SER ALA          
SEQRES  16 B  572  LEU VAL THR SER THR PHE ILE ILE GLU LYS GLN PRO PRO          
SEQRES  17 B  572  GLN VAL LEU LYS THR GLN THR LYS PHE ALA ALA THR VAL          
SEQRES  18 B  572  ARG LEU LEU VAL GLY GLY LYS LEU ASN VAL HIS MET ASN          
SEQRES  19 B  572  PRO PRO GLN VAL LYS ALA THR ILE ILE SER GLU GLN GLN          
SEQRES  20 B  572  ALA LYS SER LEU LEU LYS ASN GLU ASN THR ARG ASN ASP          
SEQRES  21 B  572  TYR SER GLY GLU ILE LEU ASN ASN CYS CYS VAL MET GLU          
SEQRES  22 B  572  TYR HIS GLN ALA THR GLY THR LEU SER ALA HIS PHE ARG          
SEQRES  23 B  572  ASN MET SER LEU LYS ARG ILE LYS ARG SER ASP ARG ARG          
SEQRES  24 B  572  GLY ALA GLU SER VAL THR GLU GLU LYS PHE THR ILE LEU          
SEQRES  25 B  572  PHE GLU SER GLN PHE SER VAL GLY GLY ASN GLU LEU VAL          
SEQRES  26 B  572  PHE GLN VAL LYS THR LEU SER LEU PRO VAL VAL VAL ILE          
SEQRES  27 B  572  VAL HIS GLY SER GLN ASP ASN ASN ALA THR ALA THR VAL          
SEQRES  28 B  572  LEU TRP ASP ASN ALA PHE ALA GLU PRO GLY ARG VAL PRO          
SEQRES  29 B  572  PHE ALA VAL PRO ASP LYS VAL LEU TRP PRO GLN LEU CYS          
SEQRES  30 B  572  GLU ALA LEU ASN MET LYS PHE LYS ALA GLU VAL GLN SER          
SEQRES  31 B  572  ASN ARG GLY LEU THR LYS GLU ASN LEU VAL PHE LEU ALA          
SEQRES  32 B  572  GLN LYS LEU PHE ASN ASN SER SER SER HIS LEU GLU ASP          
SEQRES  33 B  572  TYR SER GLY LEU SER VAL SER TRP SER GLN PHE ASN ARG          
SEQRES  34 B  572  GLU ASN LEU PRO GLY ARG ASN TYR THR PHE TRP GLN TRP          
SEQRES  35 B  572  PHE ASP GLY VAL MET GLU VAL LEU LYS LYS HIS LEU LYS          
SEQRES  36 B  572  PRO HIS TRP ASN ASP GLY ALA ILE LEU GLY PHE VAL ASN          
SEQRES  37 B  572  LYS GLN GLN ALA HIS ASP LEU LEU ILE ASN LYS PRO ASP          
SEQRES  38 B  572  GLY THR PHE LEU LEU ARG PHE SER ASP SER GLU ILE GLY          
SEQRES  39 B  572  GLY ILE THR ILE ALA TRP LYS PHE ASP SER GLN GLU ARG          
SEQRES  40 B  572  MET PHE TRP HIS LEU MET PRO PHE THR THR ARG ASP PHE          
SEQRES  41 B  572  SER ILE ARG SER LEU ALA ASP ARG LEU GLY ASP LEU ASN          
SEQRES  42 B  572  TYR LEU ILE TYR VAL PHE PRO ASP ARG PRO LYS ASP GLU          
SEQRES  43 B  572  VAL TYR SER LYS TYR TYR THR PRO VAL PRO CYS GLU SER          
SEQRES  44 B  572  ALA THR ALA LYS ALA VAL ASP GLY TYR VAL LYS PRO GLN          
FORMUL   3  HOH   *36(H2 O)                                                     
HELIX    1 AA1 LYS A  140  GLN A  183  1                                  44    
HELIX    2 AA2 SER A  193  ASP A  250  1                                  58    
HELIX    3 AA3 ASP A  250  GLY A  263  1                                  14    
HELIX    4 AA4 LEU A  272  LEU A  303  1                                  32    
HELIX    5 AA5 PRO A  308  THR A  331  1                                  24    
HELIX    6 AA6 GLU A  376  LYS A  384  1                                   9    
HELIX    7 AA7 HIS A  471  ALA A  489  1                                  19    
HELIX    8 AA8 LEU A  503  GLN A  520  1                                  18    
HELIX    9 AA9 THR A  526  PHE A  538  1                                  13    
HELIX   10 AB1 HIS A  544  SER A  549  5                                   6    
HELIX   11 AB2 SER A  554  ARG A  560  1                                   7    
HELIX   12 AB3 TYR A  568  HIS A  584  1                                  17    
HELIX   13 AB4 LEU A  585  ASP A  591  1                                   7    
HELIX   14 AB5 ASN A  599  ASN A  609  1                                  11    
HELIX   15 AB6 SER A  635  MET A  639  5                                   5    
HELIX   16 AB7 THR A  647  ARG A  654  1                                   8    
HELIX   17 AB8 SER A  655  LEU A  663  1                                   9    
HELIX   18 AB9 PRO A  674  SER A  680  1                                   7    
HELIX   19 AC1 LYS B  140  ALA B  184  1                                  45    
HELIX   20 AC2 THR B  202  ASP B  250  1                                  49    
HELIX   21 AC3 ASP B  250  GLY B  263  1                                  14    
HELIX   22 AC4 LEU B  272  LEU B  303  1                                  32    
HELIX   23 AC5 PRO B  308  THR B  331  1                                  24    
HELIX   24 AC6 VAL B  356  LEU B  360  5                                   5    
HELIX   25 AC7 GLU B  376  ASN B  385  1                                  10    
HELIX   26 AC8 ASP B  475  ALA B  489  1                                  15    
HELIX   27 AC9 LEU B  503  GLN B  520  1                                  18    
HELIX   28 AD1 THR B  526  PHE B  538  1                                  13    
HELIX   29 AD2 LEU B  545  SER B  549  5                                   5    
HELIX   30 AD3 SER B  554  ARG B  560  1                                   7    
HELIX   31 AD4 TYR B  568  HIS B  584  1                                  17    
HELIX   32 AD5 LEU B  585  ASP B  591  1                                   7    
HELIX   33 AD6 ASN B  599  ASN B  609  1                                  11    
HELIX   34 AD7 THR B  647  ARG B  654  1                                   8    
HELIX   35 AD8 SER B  655  LEU B  663  1                                   9    
HELIX   36 AD9 PRO B  674  SER B  680  1                                   7    
SHEET    1 AA1 4 PHE A 332  LYS A 336  0                                        
SHEET    2 AA1 4 LYS A 347  LEU A 354 -1  O  ARG A 353   N  ILE A 333           
SHEET    3 AA1 4 THR A 411  SER A 420 -1  O  ALA A 414   N  VAL A 352           
SHEET    4 AA1 4 GLU A 404  HIS A 406 -1  N  GLU A 404   O  SER A 413           
SHEET    1 AA2 2 LEU A 342  LYS A 343  0                                        
SHEET    2 AA2 2 VAL A 468  ILE A 469  1  O  ILE A 469   N  LEU A 342           
SHEET    1 AA3 4 CYS A 401  VAL A 402  0                                        
SHEET    2 AA3 4 GLN A 368  SER A 375 -1  N  VAL A 369   O  CYS A 401           
SHEET    3 AA3 4 PHE A 440  SER A 449 -1  O  LEU A 443   N  THR A 372           
SHEET    4 AA3 4 VAL A 456  LEU A 462 -1  O  PHE A 457   N  PHE A 448           
SHEET    1 AA4 3 ILE A 627  TRP A 631  0                                        
SHEET    2 AA4 3 THR A 614  PHE A 619 -1  N  LEU A 616   O  ALA A 630           
SHEET    3 AA4 3 TYR A 668  VAL A 669  1  O  TYR A 668   N  PHE A 615           
SHEET    1 AA5 4 PHE B 332  LYS B 336  0                                        
SHEET    2 AA5 4 LYS B 347  LEU B 354 -1  O  ARG B 353   N  ILE B 333           
SHEET    3 AA5 4 THR B 411  ILE B 424 -1  O  MET B 419   N  PHE B 348           
SHEET    4 AA5 4 GLY B 394  LEU B 397 -1  N  LEU B 397   O  SER B 420           
SHEET    1 AA6 4 PHE B 332  LYS B 336  0                                        
SHEET    2 AA6 4 LYS B 347  LEU B 354 -1  O  ARG B 353   N  ILE B 333           
SHEET    3 AA6 4 THR B 411  ILE B 424 -1  O  MET B 419   N  PHE B 348           
SHEET    4 AA6 4 GLU B 404  HIS B 406 -1  N  GLU B 404   O  SER B 413           
SHEET    1 AA7 4 CYS B 400  VAL B 402  0                                        
SHEET    2 AA7 4 GLN B 368  SER B 375 -1  N  VAL B 369   O  CYS B 401           
SHEET    3 AA7 4 PHE B 440  SER B 449 -1  O  LEU B 443   N  THR B 372           
SHEET    4 AA7 4 VAL B 456  LEU B 462 -1  O  PHE B 457   N  PHE B 448           
SHEET    1 AA8 3 LEU B 617  PHE B 619  0                                        
SHEET    2 AA8 3 ILE B 627  LYS B 632 -1  O  THR B 628   N  ARG B 618           
SHEET    3 AA8 3 PHE B 640  PHE B 646 -1  O  PHE B 646   N  ILE B 627           
CRYST1  132.380  141.400   72.850  90.00  90.00  90.00 P 21 21 2     8          
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      0.007554  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007072  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013727        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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