GenomeNet

Database: PDB
Entry: 5D7N
LinkDB: 5D7N
Original site: 5D7N 
HEADER    HYDROLASE                               14-AUG-15   5D7N              
TITLE     CRYSTAL STRUCTURE OF HUMAN SIRT3 AT AN IMPROVED RESOLUTION            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-3, MITOCHONDRIAL;
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: UNP RESIDUES 118-395;                                      
COMPND   5 SYNONYM: HSIRT3,REGULATORY PROTEIN SIR2 HOMOLOG 3,SIR2-LIKE PROTEIN  
COMPND   6 3;                                                                   
COMPND   7 EC: 3.5.1.-;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: GLY1 ORIGINATES FROM TEV CLEAVAGE SITE HIS2/MET3      
COMPND  10 ORIGINATE FROM NDEI RESTRICTION SITE OF THE VECTOR                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SIRT3, SIR2L3;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, SIRTUIN 3, DEACYLASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.RUMPF,S.GERHARDT,O.EINSLE,M.JUNG                                    
REVDAT   2   09-DEC-15 5D7N    1       JRNL                                     
REVDAT   1   02-DEC-15 5D7N    0                                                
JRNL        AUTH   T.RUMPF,S.GERHARDT,O.EINSLE,M.JUNG                           
JRNL        TITL   SEEDING FOR SIRTUINS: MICROSEED MATRIX SEEDING TO OBTAIN     
JRNL        TITL 2 CRYSTALS OF HUMAN SIRT3 AND SIRT2 SUITABLE FOR SOAKING.      
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  71  1498 2015              
JRNL        REFN                   ESSN 2053-230X                               
JRNL        PMID   26625292                                                     
JRNL        DOI    10.1107/S2053230X15019986                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.83 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0071                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 160291                         
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8479                            
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) : 1.83                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.88                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 11866                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 627                          
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12775                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 94                                      
REMARK   3   SOLVENT ATOMS            : 1257                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.09000                                             
REMARK   3    B33 (A**2) : 0.15000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.12000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.121         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.113         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.089         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.862         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13439 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 13096 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18337 ; 1.336 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 30150 ; 0.816 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1703 ; 5.380 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   587 ;32.949 ;22.879       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2172 ;13.105 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   116 ;14.013 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2083 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15033 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3043 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6588 ; 1.063 ; 1.592       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6587 ; 1.063 ; 1.592       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8245 ; 1.791 ; 2.378       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  8246 ; 1.791 ; 2.379       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6851 ; 1.454 ; 1.842       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  6851 ; 1.454 ; 1.842       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 10052 ; 2.427 ; 2.662       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 15919 ; 5.369 ;14.098       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 15361 ; 5.201 ;13.501       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
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   121        A   400                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1594  -0.5309   3.3116              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0734 T22:   0.1094                                     
REMARK   3      T33:   0.0183 T12:  -0.0040                                     
REMARK   3      T13:  -0.0124 T23:   0.0366                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1627 L22:   0.5479                                     
REMARK   3      L33:   0.4644 L12:  -0.1365                                     
REMARK   3      L13:   0.2732 L23:  -0.2035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0246 S12:   0.0291 S13:  -0.0035                       
REMARK   3      S21:   0.0459 S22:   0.0387 S23:  -0.0060                       
REMARK   3      S31:  -0.0384 S32:   0.0330 S33:  -0.0141                       
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   122        B   400                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.6409  39.5913 -15.1259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0438 T22:   0.1041                                     
REMARK   3      T33:   0.0750 T12:  -0.0028                                     
REMARK   3      T13:  -0.0158 T23:   0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2554 L22:   0.3474                                     
REMARK   3      L33:   0.2399 L12:   0.1338                                     
REMARK   3      L13:   0.1846 L23:   0.0561                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0228 S12:  -0.0040 S13:   0.0486                       
REMARK   3      S21:  -0.0172 S22:   0.0115 S23:  -0.0154                       
REMARK   3      S31:   0.0402 S32:   0.0433 S33:   0.0113                       
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   121        C   400                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1875  68.0387 -35.8475              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0665 T22:   0.0969                                     
REMARK   3      T33:   0.0520 T12:  -0.0390                                     
REMARK   3      T13:   0.0118 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1588 L22:   0.1473                                     
REMARK   3      L33:   0.4675 L12:  -0.1309                                     
REMARK   3      L13:  -0.1530 L23:   0.0275                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0315 S12:  -0.0131 S13:  -0.0066                       
REMARK   3      S21:  -0.0156 S22:  -0.0251 S23:   0.0156                       
REMARK   3      S31:  -0.0464 S32:   0.0316 S33:  -0.0064                       
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   121        D   400                          
REMARK   3    ORIGIN FOR THE GROUP (A):  59.2454  49.6916 -43.1295              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0627 T22:   0.0904                                     
REMARK   3      T33:   0.0544 T12:  -0.0196                                     
REMARK   3      T13:  -0.0262 T23:  -0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9628 L22:   0.1857                                     
REMARK   3      L33:   0.0491 L12:   0.0204                                     
REMARK   3      L13:  -0.2072 L23:  -0.0271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0244 S12:   0.0758 S13:  -0.0214                       
REMARK   3      S21:   0.0187 S22:   0.0211 S23:  -0.0152                       
REMARK   3      S31:  -0.0056 S32:  -0.0193 S33:   0.0033                       
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   122        E   400                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9803 -35.2375  -9.7161              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0374 T22:   0.1746                                     
REMARK   3      T33:   0.0019 T12:  -0.0037                                     
REMARK   3      T13:  -0.0030 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8146 L22:   0.3190                                     
REMARK   3      L33:   0.0099 L12:  -0.0412                                     
REMARK   3      L13:  -0.0394 L23:  -0.0353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0188 S12:   0.1382 S13:  -0.0241                       
REMARK   3      S21:   0.0358 S22:   0.0177 S23:   0.0053                       
REMARK   3      S31:   0.0010 S32:   0.0117 S33:   0.0012                       
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   122        F   400                          
REMARK   3    ORIGIN FOR THE GROUP (A):  75.2952  18.4263 -32.5147              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0946 T22:   0.0485                                     
REMARK   3      T33:   0.0643 T12:  -0.0018                                     
REMARK   3      T13:  -0.0376 T23:  -0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3398 L22:   0.1123                                     
REMARK   3      L33:   0.8579 L12:  -0.1747                                     
REMARK   3      L13:  -0.1590 L23:   0.0062                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0206 S12:  -0.0113 S13:  -0.0416                       
REMARK   3      S21:  -0.0296 S22:   0.0338 S23:   0.0346                       
REMARK   3      S31:   0.0595 S32:  -0.0049 S33:  -0.0544                       
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 5D7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211692.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 168813                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.830                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.660                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.81500                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 3GLS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 25 % (W/V)     
REMARK 280  PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K           
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       71.92500            
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: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     GLY A   115                                                      
REMARK 465     HIS A   116                                                      
REMARK 465     MET A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     ASP A   119                                                      
REMARK 465     LYS A   120                                                      
REMARK 465     GLY A   392                                                      
REMARK 465     LYS A   393                                                      
REMARK 465     LEU A   394                                                      
REMARK 465     ASP A   395                                                      
REMARK 465     GLY B   115                                                      
REMARK 465     HIS B   116                                                      
REMARK 465     MET B   117                                                      
REMARK 465     SER B   118                                                      
REMARK 465     ASP B   119                                                      
REMARK 465     LYS B   120                                                      
REMARK 465     GLY B   121                                                      
REMARK 465     LEU B   394                                                      
REMARK 465     ASP B   395                                                      
REMARK 465     GLY C   115                                                      
REMARK 465     HIS C   116                                                      
REMARK 465     MET C   117                                                      
REMARK 465     SER C   118                                                      
REMARK 465     ASP C   119                                                      
REMARK 465     LYS C   120                                                      
REMARK 465     LYS C   393                                                      
REMARK 465     LEU C   394                                                      
REMARK 465     ASP C   395                                                      
REMARK 465     GLY D   115                                                      
REMARK 465     HIS D   116                                                      
REMARK 465     MET D   117                                                      
REMARK 465     SER D   118                                                      
REMARK 465     ASP D   119                                                      
REMARK 465     LYS D   120                                                      
REMARK 465     LYS D   393                                                      
REMARK 465     LEU D   394                                                      
REMARK 465     ASP D   395                                                      
REMARK 465     GLY E   115                                                      
REMARK 465     HIS E   116                                                      
REMARK 465     MET E   117                                                      
REMARK 465     SER E   118                                                      
REMARK 465     ASP E   119                                                      
REMARK 465     LYS E   120                                                      
REMARK 465     GLY E   121                                                      
REMARK 465     LYS E   393                                                      
REMARK 465     LEU E   394                                                      
REMARK 465     ASP E   395                                                      
REMARK 465     GLY F   115                                                      
REMARK 465     HIS F   116                                                      
REMARK 465     MET F   117                                                      
REMARK 465     SER F   118                                                      
REMARK 465     ASP F   119                                                      
REMARK 465     LYS F   120                                                      
REMARK 465     GLY F   121                                                      
REMARK 465     GLY F   392                                                      
REMARK 465     LYS F   393                                                      
REMARK 465     LEU F   394                                                      
REMARK 465     ASP F   395                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   505     O    HOH A   705              2.18            
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    ASP A 172       62.89    -66.99                                   
REMARK 500    VAL A 258      -60.52   -101.05                                   
REMARK 500    ASP B 290       49.48    -81.10                                   
REMARK 500    VAL C 258      -61.88   -100.92                                   
REMARK 500    LEU C 322       65.28     72.03                                   
REMARK 500    GLN D 138       14.20   -142.90                                   
REMARK 500    ASP D 172       51.03    -91.10                                   
REMARK 500    ASP D 290       47.97    -78.14                                   
REMARK 500    ASP E 172       37.71    -99.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 256   SG                                                     
REMARK 620 2 CYS A 259   SG  108.4                                              
REMARK 620 3 CYS A 280   SG  107.3 110.3                                        
REMARK 620 4 CYS A 283   SG   92.7 120.6 115.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 256   SG                                                     
REMARK 620 2 CYS B 259   SG  106.8                                              
REMARK 620 3 CYS B 280   SG  109.0 109.8                                        
REMARK 620 4 CYS B 283   SG   95.6 121.6 112.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 256   SG                                                     
REMARK 620 2 CYS C 259   SG  106.9                                              
REMARK 620 3 CYS C 280   SG  108.6 108.3                                        
REMARK 620 4 CYS C 283   SG   95.6 121.3 114.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 256   SG                                                     
REMARK 620 2 CYS D 259   SG  107.5                                              
REMARK 620 3 CYS D 280   SG  106.8 111.0                                        
REMARK 620 4 CYS D 283   SG   95.9 119.6 113.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 256   SG                                                     
REMARK 620 2 CYS E 259   SG  107.0                                              
REMARK 620 3 CYS E 280   SG  108.9 109.3                                        
REMARK 620 4 CYS E 283   SG   96.0 119.7 114.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 256   SG                                                     
REMARK 620 2 CYS F 259   SG  108.6                                              
REMARK 620 3 CYS F 280   SG  109.2 111.6                                        
REMARK 620 4 CYS F 283   SG   91.4 117.3 116.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 405  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 680   O                                                      
REMARK 620 2 GLU F 375   OE2  95.6                                              
REMARK 620 3 HOH F 571   O    91.8  70.4                                        
REMARK 620 4 HOH F 628   O    96.1 106.8 171.9                                  
REMARK 620 5 HOH F 645   O    92.1  16.9  87.0  90.8                            
REMARK 620 6 HOH F 584   O    87.7 160.8  90.6  91.6 177.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE E 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 F 402                 
DBREF  5D7N A  118   395  UNP    Q9NTG7   SIR3_HUMAN     118    395             
DBREF  5D7N B  118   395  UNP    Q9NTG7   SIR3_HUMAN     118    395             
DBREF  5D7N C  118   395  UNP    Q9NTG7   SIR3_HUMAN     118    395             
DBREF  5D7N D  118   395  UNP    Q9NTG7   SIR3_HUMAN     118    395             
DBREF  5D7N E  118   395  UNP    Q9NTG7   SIR3_HUMAN     118    395             
DBREF  5D7N F  118   395  UNP    Q9NTG7   SIR3_HUMAN     118    395             
SEQADV 5D7N GLY A  115  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N HIS A  116  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N MET A  117  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N GLY B  115  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N HIS B  116  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N MET B  117  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N GLY C  115  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N HIS C  116  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N MET C  117  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N GLY D  115  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N HIS D  116  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N MET D  117  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N GLY E  115  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N HIS E  116  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N MET E  117  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N GLY F  115  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N HIS F  116  UNP  Q9NTG7              EXPRESSION TAG                 
SEQADV 5D7N MET F  117  UNP  Q9NTG7              EXPRESSION TAG                 
SEQRES   1 A  281  GLY HIS MET SER ASP LYS GLY LYS LEU SER LEU GLN ASP          
SEQRES   2 A  281  VAL ALA GLU LEU ILE ARG ALA ARG ALA CYS GLN ARG VAL          
SEQRES   3 A  281  VAL VAL MET VAL GLY ALA GLY ILE SER THR PRO SER GLY          
SEQRES   4 A  281  ILE PRO ASP PHE ARG SER PRO GLY SER GLY LEU TYR SER          
SEQRES   5 A  281  ASN LEU GLN GLN TYR ASP LEU PRO TYR PRO GLU ALA ILE          
SEQRES   6 A  281  PHE GLU LEU PRO PHE PHE PHE HIS ASN PRO LYS PRO PHE          
SEQRES   7 A  281  PHE THR LEU ALA LYS GLU LEU TYR PRO GLY ASN TYR LYS          
SEQRES   8 A  281  PRO ASN VAL THR HIS TYR PHE LEU ARG LEU LEU HIS ASP          
SEQRES   9 A  281  LYS GLY LEU LEU LEU ARG LEU TYR THR GLN ASN ILE ASP          
SEQRES  10 A  281  GLY LEU GLU ARG VAL SER GLY ILE PRO ALA SER LYS LEU          
SEQRES  11 A  281  VAL GLU ALA HIS GLY THR PHE ALA SER ALA THR CYS THR          
SEQRES  12 A  281  VAL CYS GLN ARG PRO PHE PRO GLY GLU ASP ILE ARG ALA          
SEQRES  13 A  281  ASP VAL MET ALA ASP ARG VAL PRO ARG CYS PRO VAL CYS          
SEQRES  14 A  281  THR GLY VAL VAL LYS PRO ASP ILE VAL PHE PHE GLY GLU          
SEQRES  15 A  281  PRO LEU PRO GLN ARG PHE LEU LEU HIS VAL VAL ASP PHE          
SEQRES  16 A  281  PRO MET ALA ASP LEU LEU LEU ILE LEU GLY THR SER LEU          
SEQRES  17 A  281  GLU VAL GLU PRO PHE ALA SER LEU THR GLU ALA VAL ARG          
SEQRES  18 A  281  SER SER VAL PRO ARG LEU LEU ILE ASN ARG ASP LEU VAL          
SEQRES  19 A  281  GLY PRO LEU ALA TRP HIS PRO ARG SER ARG ASP VAL ALA          
SEQRES  20 A  281  GLN LEU GLY ASP VAL VAL HIS GLY VAL GLU SER LEU VAL          
SEQRES  21 A  281  GLU LEU LEU GLY TRP THR GLU GLU MET ARG ASP LEU VAL          
SEQRES  22 A  281  GLN ARG GLU THR GLY LYS LEU ASP                              
SEQRES   1 B  281  GLY HIS MET SER ASP LYS GLY LYS LEU SER LEU GLN ASP          
SEQRES   2 B  281  VAL ALA GLU LEU ILE ARG ALA ARG ALA CYS GLN ARG VAL          
SEQRES   3 B  281  VAL VAL MET VAL GLY ALA GLY ILE SER THR PRO SER GLY          
SEQRES   4 B  281  ILE PRO ASP PHE ARG SER PRO GLY SER GLY LEU TYR SER          
SEQRES   5 B  281  ASN LEU GLN GLN TYR ASP LEU PRO TYR PRO GLU ALA ILE          
SEQRES   6 B  281  PHE GLU LEU PRO PHE PHE PHE HIS ASN PRO LYS PRO PHE          
SEQRES   7 B  281  PHE THR LEU ALA LYS GLU LEU TYR PRO GLY ASN TYR LYS          
SEQRES   8 B  281  PRO ASN VAL THR HIS TYR PHE LEU ARG LEU LEU HIS ASP          
SEQRES   9 B  281  LYS GLY LEU LEU LEU ARG LEU TYR THR GLN ASN ILE ASP          
SEQRES  10 B  281  GLY LEU GLU ARG VAL SER GLY ILE PRO ALA SER LYS LEU          
SEQRES  11 B  281  VAL GLU ALA HIS GLY THR PHE ALA SER ALA THR CYS THR          
SEQRES  12 B  281  VAL CYS GLN ARG PRO PHE PRO GLY GLU ASP ILE ARG ALA          
SEQRES  13 B  281  ASP VAL MET ALA ASP ARG VAL PRO ARG CYS PRO VAL CYS          
SEQRES  14 B  281  THR GLY VAL VAL LYS PRO ASP ILE VAL PHE PHE GLY GLU          
SEQRES  15 B  281  PRO LEU PRO GLN ARG PHE LEU LEU HIS VAL VAL ASP PHE          
SEQRES  16 B  281  PRO MET ALA ASP LEU LEU LEU ILE LEU GLY THR SER LEU          
SEQRES  17 B  281  GLU VAL GLU PRO PHE ALA SER LEU THR GLU ALA VAL ARG          
SEQRES  18 B  281  SER SER VAL PRO ARG LEU LEU ILE ASN ARG ASP LEU VAL          
SEQRES  19 B  281  GLY PRO LEU ALA TRP HIS PRO ARG SER ARG ASP VAL ALA          
SEQRES  20 B  281  GLN LEU GLY ASP VAL VAL HIS GLY VAL GLU SER LEU VAL          
SEQRES  21 B  281  GLU LEU LEU GLY TRP THR GLU GLU MET ARG ASP LEU VAL          
SEQRES  22 B  281  GLN ARG GLU THR GLY LYS LEU ASP                              
SEQRES   1 C  281  GLY HIS MET SER ASP LYS GLY LYS LEU SER LEU GLN ASP          
SEQRES   2 C  281  VAL ALA GLU LEU ILE ARG ALA ARG ALA CYS GLN ARG VAL          
SEQRES   3 C  281  VAL VAL MET VAL GLY ALA GLY ILE SER THR PRO SER GLY          
SEQRES   4 C  281  ILE PRO ASP PHE ARG SER PRO GLY SER GLY LEU TYR SER          
SEQRES   5 C  281  ASN LEU GLN GLN TYR ASP LEU PRO TYR PRO GLU ALA ILE          
SEQRES   6 C  281  PHE GLU LEU PRO PHE PHE PHE HIS ASN PRO LYS PRO PHE          
SEQRES   7 C  281  PHE THR LEU ALA LYS GLU LEU TYR PRO GLY ASN TYR LYS          
SEQRES   8 C  281  PRO ASN VAL THR HIS TYR PHE LEU ARG LEU LEU HIS ASP          
SEQRES   9 C  281  LYS GLY LEU LEU LEU ARG LEU TYR THR GLN ASN ILE ASP          
SEQRES  10 C  281  GLY LEU GLU ARG VAL SER GLY ILE PRO ALA SER LYS LEU          
SEQRES  11 C  281  VAL GLU ALA HIS GLY THR PHE ALA SER ALA THR CYS THR          
SEQRES  12 C  281  VAL CYS GLN ARG PRO PHE PRO GLY GLU ASP ILE ARG ALA          
SEQRES  13 C  281  ASP VAL MET ALA ASP ARG VAL PRO ARG CYS PRO VAL CYS          
SEQRES  14 C  281  THR GLY VAL VAL LYS PRO ASP ILE VAL PHE PHE GLY GLU          
SEQRES  15 C  281  PRO LEU PRO GLN ARG PHE LEU LEU HIS VAL VAL ASP PHE          
SEQRES  16 C  281  PRO MET ALA ASP LEU LEU LEU ILE LEU GLY THR SER LEU          
SEQRES  17 C  281  GLU VAL GLU PRO PHE ALA SER LEU THR GLU ALA VAL ARG          
SEQRES  18 C  281  SER SER VAL PRO ARG LEU LEU ILE ASN ARG ASP LEU VAL          
SEQRES  19 C  281  GLY PRO LEU ALA TRP HIS PRO ARG SER ARG ASP VAL ALA          
SEQRES  20 C  281  GLN LEU GLY ASP VAL VAL HIS GLY VAL GLU SER LEU VAL          
SEQRES  21 C  281  GLU LEU LEU GLY TRP THR GLU GLU MET ARG ASP LEU VAL          
SEQRES  22 C  281  GLN ARG GLU THR GLY LYS LEU ASP                              
SEQRES   1 D  281  GLY HIS MET SER ASP LYS GLY LYS LEU SER LEU GLN ASP          
SEQRES   2 D  281  VAL ALA GLU LEU ILE ARG ALA ARG ALA CYS GLN ARG VAL          
SEQRES   3 D  281  VAL VAL MET VAL GLY ALA GLY ILE SER THR PRO SER GLY          
SEQRES   4 D  281  ILE PRO ASP PHE ARG SER PRO GLY SER GLY LEU TYR SER          
SEQRES   5 D  281  ASN LEU GLN GLN TYR ASP LEU PRO TYR PRO GLU ALA ILE          
SEQRES   6 D  281  PHE GLU LEU PRO PHE PHE PHE HIS ASN PRO LYS PRO PHE          
SEQRES   7 D  281  PHE THR LEU ALA LYS GLU LEU TYR PRO GLY ASN TYR LYS          
SEQRES   8 D  281  PRO ASN VAL THR HIS TYR PHE LEU ARG LEU LEU HIS ASP          
SEQRES   9 D  281  LYS GLY LEU LEU LEU ARG LEU TYR THR GLN ASN ILE ASP          
SEQRES  10 D  281  GLY LEU GLU ARG VAL SER GLY ILE PRO ALA SER LYS LEU          
SEQRES  11 D  281  VAL GLU ALA HIS GLY THR PHE ALA SER ALA THR CYS THR          
SEQRES  12 D  281  VAL CYS GLN ARG PRO PHE PRO GLY GLU ASP ILE ARG ALA          
SEQRES  13 D  281  ASP VAL MET ALA ASP ARG VAL PRO ARG CYS PRO VAL CYS          
SEQRES  14 D  281  THR GLY VAL VAL LYS PRO ASP ILE VAL PHE PHE GLY GLU          
SEQRES  15 D  281  PRO LEU PRO GLN ARG PHE LEU LEU HIS VAL VAL ASP PHE          
SEQRES  16 D  281  PRO MET ALA ASP LEU LEU LEU ILE LEU GLY THR SER LEU          
SEQRES  17 D  281  GLU VAL GLU PRO PHE ALA SER LEU THR GLU ALA VAL ARG          
SEQRES  18 D  281  SER SER VAL PRO ARG LEU LEU ILE ASN ARG ASP LEU VAL          
SEQRES  19 D  281  GLY PRO LEU ALA TRP HIS PRO ARG SER ARG ASP VAL ALA          
SEQRES  20 D  281  GLN LEU GLY ASP VAL VAL HIS GLY VAL GLU SER LEU VAL          
SEQRES  21 D  281  GLU LEU LEU GLY TRP THR GLU GLU MET ARG ASP LEU VAL          
SEQRES  22 D  281  GLN ARG GLU THR GLY LYS LEU ASP                              
SEQRES   1 E  281  GLY HIS MET SER ASP LYS GLY LYS LEU SER LEU GLN ASP          
SEQRES   2 E  281  VAL ALA GLU LEU ILE ARG ALA ARG ALA CYS GLN ARG VAL          
SEQRES   3 E  281  VAL VAL MET VAL GLY ALA GLY ILE SER THR PRO SER GLY          
SEQRES   4 E  281  ILE PRO ASP PHE ARG SER PRO GLY SER GLY LEU TYR SER          
SEQRES   5 E  281  ASN LEU GLN GLN TYR ASP LEU PRO TYR PRO GLU ALA ILE          
SEQRES   6 E  281  PHE GLU LEU PRO PHE PHE PHE HIS ASN PRO LYS PRO PHE          
SEQRES   7 E  281  PHE THR LEU ALA LYS GLU LEU TYR PRO GLY ASN TYR LYS          
SEQRES   8 E  281  PRO ASN VAL THR HIS TYR PHE LEU ARG LEU LEU HIS ASP          
SEQRES   9 E  281  LYS GLY LEU LEU LEU ARG LEU TYR THR GLN ASN ILE ASP          
SEQRES  10 E  281  GLY LEU GLU ARG VAL SER GLY ILE PRO ALA SER LYS LEU          
SEQRES  11 E  281  VAL GLU ALA HIS GLY THR PHE ALA SER ALA THR CYS THR          
SEQRES  12 E  281  VAL CYS GLN ARG PRO PHE PRO GLY GLU ASP ILE ARG ALA          
SEQRES  13 E  281  ASP VAL MET ALA ASP ARG VAL PRO ARG CYS PRO VAL CYS          
SEQRES  14 E  281  THR GLY VAL VAL LYS PRO ASP ILE VAL PHE PHE GLY GLU          
SEQRES  15 E  281  PRO LEU PRO GLN ARG PHE LEU LEU HIS VAL VAL ASP PHE          
SEQRES  16 E  281  PRO MET ALA ASP LEU LEU LEU ILE LEU GLY THR SER LEU          
SEQRES  17 E  281  GLU VAL GLU PRO PHE ALA SER LEU THR GLU ALA VAL ARG          
SEQRES  18 E  281  SER SER VAL PRO ARG LEU LEU ILE ASN ARG ASP LEU VAL          
SEQRES  19 E  281  GLY PRO LEU ALA TRP HIS PRO ARG SER ARG ASP VAL ALA          
SEQRES  20 E  281  GLN LEU GLY ASP VAL VAL HIS GLY VAL GLU SER LEU VAL          
SEQRES  21 E  281  GLU LEU LEU GLY TRP THR GLU GLU MET ARG ASP LEU VAL          
SEQRES  22 E  281  GLN ARG GLU THR GLY LYS LEU ASP                              
SEQRES   1 F  281  GLY HIS MET SER ASP LYS GLY LYS LEU SER LEU GLN ASP          
SEQRES   2 F  281  VAL ALA GLU LEU ILE ARG ALA ARG ALA CYS GLN ARG VAL          
SEQRES   3 F  281  VAL VAL MET VAL GLY ALA GLY ILE SER THR PRO SER GLY          
SEQRES   4 F  281  ILE PRO ASP PHE ARG SER PRO GLY SER GLY LEU TYR SER          
SEQRES   5 F  281  ASN LEU GLN GLN TYR ASP LEU PRO TYR PRO GLU ALA ILE          
SEQRES   6 F  281  PHE GLU LEU PRO PHE PHE PHE HIS ASN PRO LYS PRO PHE          
SEQRES   7 F  281  PHE THR LEU ALA LYS GLU LEU TYR PRO GLY ASN TYR LYS          
SEQRES   8 F  281  PRO ASN VAL THR HIS TYR PHE LEU ARG LEU LEU HIS ASP          
SEQRES   9 F  281  LYS GLY LEU LEU LEU ARG LEU TYR THR GLN ASN ILE ASP          
SEQRES  10 F  281  GLY LEU GLU ARG VAL SER GLY ILE PRO ALA SER LYS LEU          
SEQRES  11 F  281  VAL GLU ALA HIS GLY THR PHE ALA SER ALA THR CYS THR          
SEQRES  12 F  281  VAL CYS GLN ARG PRO PHE PRO GLY GLU ASP ILE ARG ALA          
SEQRES  13 F  281  ASP VAL MET ALA ASP ARG VAL PRO ARG CYS PRO VAL CYS          
SEQRES  14 F  281  THR GLY VAL VAL LYS PRO ASP ILE VAL PHE PHE GLY GLU          
SEQRES  15 F  281  PRO LEU PRO GLN ARG PHE LEU LEU HIS VAL VAL ASP PHE          
SEQRES  16 F  281  PRO MET ALA ASP LEU LEU LEU ILE LEU GLY THR SER LEU          
SEQRES  17 F  281  GLU VAL GLU PRO PHE ALA SER LEU THR GLU ALA VAL ARG          
SEQRES  18 F  281  SER SER VAL PRO ARG LEU LEU ILE ASN ARG ASP LEU VAL          
SEQRES  19 F  281  GLY PRO LEU ALA TRP HIS PRO ARG SER ARG ASP VAL ALA          
SEQRES  20 F  281  GLN LEU GLY ASP VAL VAL HIS GLY VAL GLU SER LEU VAL          
SEQRES  21 F  281  GLU LEU LEU GLY TRP THR GLU GLU MET ARG ASP LEU VAL          
SEQRES  22 F  281  GLN ARG GLU THR GLY LYS LEU ASP                              
HET     ZN  A 401       1                                                       
HET    PEG  A 402       7                                                       
HET    PEG  A 403       7                                                       
HET    PEG  A 404       7                                                       
HET     MG  A 405       1                                                       
HET     ZN  B 401       1                                                       
HET    PEG  B 402       7                                                       
HET     ZN  C 401       1                                                       
HET    PEG  C 402       7                                                       
HET     ZN  D 401       1                                                       
HET    PEG  D 402       7                                                       
HET    1PE  D 403      16                                                       
HET    GOL  D 404       6                                                       
HET     ZN  E 401       1                                                       
HET    PGE  E 402      10                                                       
HET     ZN  F 401       1                                                       
HET    PG4  F 402      13                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     GOL GLYCEROL                                                         
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETSYN     1PE PEG400                                                           
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   7   ZN    6(ZN 2+)                                                     
FORMUL   8  PEG    6(C4 H10 O3)                                                 
FORMUL  11   MG    MG 2+                                                        
FORMUL  18  1PE    C10 H22 O6                                                   
FORMUL  19  GOL    C3 H8 O3                                                     
FORMUL  21  PGE    C6 H14 O4                                                    
FORMUL  23  PG4    C8 H18 O5                                                    
FORMUL  24  HOH   *1257(H2 O)                                                   
HELIX    1 AA1 SER A  124  ALA A  134  1                                  11    
HELIX    2 AA2 ALA A  146  GLY A  153  5                                   8    
HELIX    3 AA3 SER A  162  GLN A  169  1                                   8    
HELIX    4 AA4 TYR A  175  PHE A  180  5                                   6    
HELIX    5 AA5 GLU A  181  PHE A  186  1                                   6    
HELIX    6 AA6 PRO A  189  TYR A  200  1                                  12    
HELIX    7 AA7 ASN A  207  LYS A  219  1                                  13    
HELIX    8 AA8 GLY A  232  SER A  237  1                                   6    
HELIX    9 AA9 PRO A  240  SER A  242  5                                   3    
HELIX   10 AB1 ILE A  268  ALA A  274  1                                   7    
HELIX   11 AB2 PRO A  299  LEU A  303  5                                   5    
HELIX   12 AB3 LEU A  304  ALA A  312  1                                   9    
HELIX   13 AB4 PHE A  327  VAL A  334  5                                   8    
HELIX   14 AB5 VAL A  348  HIS A  354  1                                   7    
HELIX   15 AB6 ASP A  365  GLY A  378  1                                  14    
HELIX   16 AB7 TRP A  379  THR A  391  1                                  13    
HELIX   17 AB8 SER B  124  ALA B  134  1                                  11    
HELIX   18 AB9 ALA B  146  GLY B  153  5                                   8    
HELIX   19 AC1 SER B  162  GLN B  169  1                                   8    
HELIX   20 AC2 TYR B  175  PHE B  180  5                                   6    
HELIX   21 AC3 GLU B  181  ASN B  188  1                                   8    
HELIX   22 AC4 PRO B  189  TYR B  200  1                                  12    
HELIX   23 AC5 ASN B  207  LYS B  219  1                                  13    
HELIX   24 AC6 GLY B  232  SER B  237  1                                   6    
HELIX   25 AC7 PRO B  240  SER B  242  5                                   3    
HELIX   26 AC8 ILE B  268  ALA B  274  1                                   7    
HELIX   27 AC9 PRO B  299  LEU B  303  5                                   5    
HELIX   28 AD1 LEU B  304  ALA B  312  1                                   9    
HELIX   29 AD2 PHE B  327  ALA B  333  5                                   7    
HELIX   30 AD3 VAL B  348  HIS B  354  1                                   7    
HELIX   31 AD4 ASP B  365  GLY B  378  1                                  14    
HELIX   32 AD5 TRP B  379  GLY B  392  1                                  14    
HELIX   33 AD6 SER C  124  ALA C  134  1                                  11    
HELIX   34 AD7 ALA C  146  GLY C  153  5                                   8    
HELIX   35 AD8 SER C  162  GLN C  170  1                                   9    
HELIX   36 AD9 TYR C  175  PHE C  180  5                                   6    
HELIX   37 AE1 GLU C  181  ASN C  188  1                                   8    
HELIX   38 AE2 PRO C  189  TYR C  200  1                                  12    
HELIX   39 AE3 ASN C  207  LYS C  219  1                                  13    
HELIX   40 AE4 GLY C  232  SER C  237  1                                   6    
HELIX   41 AE5 PRO C  240  SER C  242  5                                   3    
HELIX   42 AE6 ILE C  268  ALA C  274  1                                   7    
HELIX   43 AE7 PRO C  299  LEU C  303  5                                   5    
HELIX   44 AE8 LEU C  304  ALA C  312  1                                   9    
HELIX   45 AE9 PRO C  326  THR C  331  1                                   6    
HELIX   46 AF1 GLY C  349  HIS C  354  1                                   6    
HELIX   47 AF2 ASP C  365  GLY C  378  1                                  14    
HELIX   48 AF3 TRP C  379  GLY C  392  1                                  14    
HELIX   49 AF4 SER D  124  ALA D  134  1                                  11    
HELIX   50 AF5 ALA D  146  GLY D  153  5                                   8    
HELIX   51 AF6 SER D  162  GLN D  170  1                                   9    
HELIX   52 AF7 TYR D  175  PHE D  180  5                                   6    
HELIX   53 AF8 GLU D  181  PHE D  186  1                                   6    
HELIX   54 AF9 PRO D  189  TYR D  200  1                                  12    
HELIX   55 AG1 ASN D  207  LYS D  219  1                                  13    
HELIX   56 AG2 GLY D  232  SER D  237  1                                   6    
HELIX   57 AG3 PRO D  240  SER D  242  5                                   3    
HELIX   58 AG4 ILE D  268  ALA D  274  1                                   7    
HELIX   59 AG5 PRO D  299  LEU D  303  5                                   5    
HELIX   60 AG6 LEU D  304  ALA D  312  1                                   9    
HELIX   61 AG7 PHE D  327  ALA D  333  5                                   7    
HELIX   62 AG8 VAL D  348  HIS D  354  1                                   7    
HELIX   63 AG9 ASP D  365  GLY D  378  1                                  14    
HELIX   64 AH1 TRP D  379  GLY D  392  1                                  14    
HELIX   65 AH2 SER E  124  ALA E  134  1                                  11    
HELIX   66 AH3 ALA E  146  GLY E  153  5                                   8    
HELIX   67 AH4 SER E  162  GLN E  170  1                                   9    
HELIX   68 AH5 TYR E  175  PHE E  180  5                                   6    
HELIX   69 AH6 GLU E  181  ASN E  188  1                                   8    
HELIX   70 AH7 PRO E  189  TYR E  200  1                                  12    
HELIX   71 AH8 ASN E  207  LYS E  219  1                                  13    
HELIX   72 AH9 GLY E  232  SER E  237  1                                   6    
HELIX   73 AI1 PRO E  240  SER E  242  5                                   3    
HELIX   74 AI2 ILE E  268  ALA E  274  1                                   7    
HELIX   75 AI3 PRO E  299  LEU E  303  5                                   5    
HELIX   76 AI4 LEU E  304  ALA E  312  1                                   9    
HELIX   77 AI5 PHE E  327  ALA E  333  5                                   7    
HELIX   78 AI6 VAL E  348  HIS E  354  1                                   7    
HELIX   79 AI7 ASP E  365  GLY E  378  1                                  14    
HELIX   80 AI8 TRP E  379  GLY E  392  1                                  14    
HELIX   81 AI9 SER F  124  ALA F  134  1                                  11    
HELIX   82 AJ1 ALA F  146  GLY F  153  5                                   8    
HELIX   83 AJ2 SER F  162  GLN F  170  1                                   9    
HELIX   84 AJ3 TYR F  175  PHE F  180  5                                   6    
HELIX   85 AJ4 GLU F  181  ASN F  188  1                                   8    
HELIX   86 AJ5 PRO F  189  TYR F  200  1                                  12    
HELIX   87 AJ6 ASN F  207  LYS F  219  1                                  13    
HELIX   88 AJ7 GLY F  232  SER F  237  1                                   6    
HELIX   89 AJ8 PRO F  240  SER F  242  5                                   3    
HELIX   90 AJ9 ILE F  268  ALA F  274  1                                   7    
HELIX   91 AK1 PRO F  299  LEU F  303  5                                   5    
HELIX   92 AK2 LEU F  304  ALA F  312  1                                   9    
HELIX   93 AK3 PHE F  327  ALA F  333  5                                   7    
HELIX   94 AK4 VAL F  348  HIS F  354  1                                   7    
HELIX   95 AK5 ASP F  365  GLY F  378  1                                  14    
HELIX   96 AK6 TRP F  379  THR F  391  1                                  13    
SHEET    1 AA1 6 LEU A 244  GLU A 246  0                                        
SHEET    2 AA1 6 LEU A 222  THR A 227  1  N  LEU A 225   O  VAL A 245           
SHEET    3 AA1 6 VAL A 140  VAL A 144  1  N  VAL A 142   O  TYR A 226           
SHEET    4 AA1 6 LEU A 314  LEU A 318  1  O  LEU A 316   N  MET A 143           
SHEET    5 AA1 6 ARG A 340  ASN A 344  1  O  LEU A 341   N  ILE A 317           
SHEET    6 AA1 6 ASP A 359  LEU A 363  1  O  GLN A 362   N  LEU A 342           
SHEET    1 AA2 3 PRO A 262  PRO A 264  0                                        
SHEET    2 AA2 3 GLY A 249  CYS A 256 -1  N  ALA A 254   O  PHE A 263           
SHEET    3 AA2 3 VAL A 287  ILE A 291 -1  O  ASP A 290   N  SER A 253           
SHEET    1 AA3 6 LEU B 244  GLU B 246  0                                        
SHEET    2 AA3 6 LEU B 222  THR B 227  1  N  LEU B 225   O  VAL B 245           
SHEET    3 AA3 6 VAL B 140  VAL B 144  1  N  VAL B 142   O  TYR B 226           
SHEET    4 AA3 6 LEU B 314  LEU B 318  1  O  LEU B 316   N  MET B 143           
SHEET    5 AA3 6 ARG B 340  ASN B 344  1  O  LEU B 341   N  LEU B 315           
SHEET    6 AA3 6 ASP B 359  LEU B 363  1  O  GLN B 362   N  LEU B 342           
SHEET    1 AA4 3 PRO B 262  PRO B 264  0                                        
SHEET    2 AA4 3 GLY B 249  CYS B 256 -1  N  ALA B 254   O  PHE B 263           
SHEET    3 AA4 3 VAL B 287  ILE B 291 -1  O  ASP B 290   N  SER B 253           
SHEET    1 AA5 6 LEU C 244  GLU C 246  0                                        
SHEET    2 AA5 6 LEU C 222  THR C 227  1  N  THR C 227   O  VAL C 245           
SHEET    3 AA5 6 VAL C 140  VAL C 144  1  N  VAL C 142   O  TYR C 226           
SHEET    4 AA5 6 LEU C 314  LEU C 318  1  O  LEU C 316   N  MET C 143           
SHEET    5 AA5 6 ARG C 340  ASN C 344  1  O  LEU C 341   N  LEU C 315           
SHEET    6 AA5 6 ASP C 359  LEU C 363  1  O  GLN C 362   N  LEU C 342           
SHEET    1 AA6 3 PRO C 262  PRO C 264  0                                        
SHEET    2 AA6 3 GLY C 249  CYS C 256 -1  N  ALA C 254   O  PHE C 263           
SHEET    3 AA6 3 VAL C 287  ILE C 291 -1  O  ASP C 290   N  SER C 253           
SHEET    1 AA7 6 LEU D 244  GLU D 246  0                                        
SHEET    2 AA7 6 LEU D 222  THR D 227  1  N  THR D 227   O  VAL D 245           
SHEET    3 AA7 6 VAL D 140  VAL D 144  1  N  VAL D 142   O  TYR D 226           
SHEET    4 AA7 6 LEU D 314  LEU D 318  1  O  LEU D 318   N  MET D 143           
SHEET    5 AA7 6 ARG D 340  ASN D 344  1  O  ILE D 343   N  ILE D 317           
SHEET    6 AA7 6 ASP D 359  LEU D 363  1  O  VAL D 360   N  LEU D 342           
SHEET    1 AA8 3 PRO D 262  PRO D 264  0                                        
SHEET    2 AA8 3 GLY D 249  CYS D 256 -1  N  ALA D 254   O  PHE D 263           
SHEET    3 AA8 3 VAL D 287  ILE D 291 -1  O  ASP D 290   N  SER D 253           
SHEET    1 AA9 6 LEU E 244  GLU E 246  0                                        
SHEET    2 AA9 6 LEU E 222  THR E 227  1  N  THR E 227   O  VAL E 245           
SHEET    3 AA9 6 VAL E 140  VAL E 144  1  N  VAL E 142   O  TYR E 226           
SHEET    4 AA9 6 LEU E 314  LEU E 318  1  O  LEU E 318   N  MET E 143           
SHEET    5 AA9 6 ARG E 340  ASN E 344  1  O  LEU E 341   N  LEU E 315           
SHEET    6 AA9 6 ASP E 359  LEU E 363  1  O  GLN E 362   N  LEU E 342           
SHEET    1 AB1 3 PRO E 262  PRO E 264  0                                        
SHEET    2 AB1 3 GLY E 249  CYS E 256 -1  N  ALA E 254   O  PHE E 263           
SHEET    3 AB1 3 VAL E 287  ILE E 291 -1  O  ASP E 290   N  SER E 253           
SHEET    1 AB2 6 LEU F 244  GLU F 246  0                                        
SHEET    2 AB2 6 LEU F 222  THR F 227  1  N  LEU F 225   O  VAL F 245           
SHEET    3 AB2 6 VAL F 140  VAL F 144  1  N  VAL F 142   O  TYR F 226           
SHEET    4 AB2 6 LEU F 314  LEU F 318  1  O  LEU F 318   N  MET F 143           
SHEET    5 AB2 6 ARG F 340  ASN F 344  1  O  LEU F 341   N  LEU F 315           
SHEET    6 AB2 6 ASP F 359  LEU F 363  1  O  GLN F 362   N  LEU F 342           
SHEET    1 AB3 3 PRO F 262  PRO F 264  0                                        
SHEET    2 AB3 3 GLY F 249  CYS F 256 -1  N  ALA F 254   O  PHE F 263           
SHEET    3 AB3 3 VAL F 287  ILE F 291 -1  O  ASP F 290   N  SER F 253           
LINK         SG  CYS A 256                ZN    ZN A 401     1555   1555  2.32  
LINK         SG  CYS A 259                ZN    ZN A 401     1555   1555  2.32  
LINK         SG  CYS A 280                ZN    ZN A 401     1555   1555  2.29  
LINK         SG  CYS A 283                ZN    ZN A 401     1555   1555  2.33  
LINK         SG  CYS B 256                ZN    ZN B 401     1555   1555  2.35  
LINK         SG  CYS B 259                ZN    ZN B 401     1555   1555  2.33  
LINK         SG  CYS B 280                ZN    ZN B 401     1555   1555  2.35  
LINK         SG  CYS B 283                ZN    ZN B 401     1555   1555  2.32  
LINK         SG  CYS C 256                ZN    ZN C 401     1555   1555  2.33  
LINK         SG  CYS C 259                ZN    ZN C 401     1555   1555  2.33  
LINK         SG  CYS C 280                ZN    ZN C 401     1555   1555  2.31  
LINK         SG  CYS C 283                ZN    ZN C 401     1555   1555  2.33  
LINK         SG  CYS D 256                ZN    ZN D 401     1555   1555  2.33  
LINK         SG  CYS D 259                ZN    ZN D 401     1555   1555  2.30  
LINK         SG  CYS D 280                ZN    ZN D 401     1555   1555  2.30  
LINK         SG  CYS D 283                ZN    ZN D 401     1555   1555  2.34  
LINK         SG  CYS E 256                ZN    ZN E 401     1555   1555  2.34  
LINK         SG  CYS E 259                ZN    ZN E 401     1555   1555  2.30  
LINK         SG  CYS E 280                ZN    ZN E 401     1555   1555  2.33  
LINK         SG  CYS E 283                ZN    ZN E 401     1555   1555  2.30  
LINK         SG  CYS F 256                ZN    ZN F 401     1555   1555  2.35  
LINK         SG  CYS F 259                ZN    ZN F 401     1555   1555  2.29  
LINK         SG  CYS F 280                ZN    ZN F 401     1555   1555  2.32  
LINK         SG  CYS F 283                ZN    ZN F 401     1555   1555  2.28  
LINK        MG    MG A 405                 O   HOH A 680     1555   1555  2.01  
LINK         OE2 GLU F 375                MG    MG A 405     1555   1554  2.17  
LINK        MG    MG A 405                 O   HOH F 571     1555   1556  2.02  
LINK        MG    MG A 405                 O   HOH F 628     1555   1556  2.01  
LINK        MG    MG A 405                 O   HOH F 645     1555   1556  2.04  
LINK        MG    MG A 405                 O   HOH F 584     1555   1556  2.11  
CISPEP   1 GLU A  325    PRO A  326          0         0.05                     
CISPEP   2 GLU B  325    PRO B  326          0         1.67                     
CISPEP   3 GLU C  325    PRO C  326          0        -2.72                     
CISPEP   4 GLU D  325    PRO D  326          0         1.05                     
CISPEP   5 GLU E  325    PRO E  326          0         4.47                     
CISPEP   6 GLU F  325    PRO F  326          0         3.18                     
SITE     1 AC1  4 CYS A 256  CYS A 259  CYS A 280  CYS A 283                    
SITE     1 AC2  3 VAL A 292  PHE A 293  HOH A 633                               
SITE     1 AC3  2 CYS A 259  GLN A 260                                          
SITE     1 AC4  6 HOH A 680  GLU F 375  HOH F 571  HOH F 584                    
SITE     2 AC4  6 HOH F 628  HOH F 645                                          
SITE     1 AC5  4 CYS B 256  CYS B 259  CYS B 280  CYS B 283                    
SITE     1 AC6  6 HIS B 248  VAL B 292  PHE B 293  PHE B 294                    
SITE     2 AC6  6 HOH B 502  HOH B 561                                          
SITE     1 AC7  4 CYS C 256  CYS C 259  CYS C 280  CYS C 283                    
SITE     1 AC8  4 PHE C 180  HIS C 248  VAL C 292  HOH C 650                    
SITE     1 AC9  4 CYS D 256  CYS D 259  CYS D 280  CYS D 283                    
SITE     1 AD1  4 GLU D 323  GOL D 404  HOH D 690  GLU F 181                    
SITE     1 AD2  5 GLN D 228  HIS D 248  VAL D 292  PHE D 294                    
SITE     2 AD2  5 GLY D 295                                                     
SITE     1 AD3  6 LEU D 322  GLU D 323  GLU D 325  PEG D 402                    
SITE     2 AD3  6 TYR F 175  GLU F 177                                          
SITE     1 AD4  4 CYS E 256  CYS E 259  CYS E 280  CYS E 283                    
SITE     1 AD5  6 ARG E 158  PHE E 180  HIS E 248  VAL E 292                    
SITE     2 AD5  6 PHE E 294  GLY E 295                                          
SITE     1 AD6  4 CYS F 256  CYS F 259  CYS F 280  CYS F 283                    
SITE     1 AD7 10 ARG F 158  GLN F 228  HIS F 248  VAL F 292                    
SITE     2 AD7 10 PHE F 294  HOH F 502  HOH F 505  HOH F 570                    
SITE     3 AD7 10 HOH F 617  HOH F 636                                          
CRYST1   84.990  143.850   89.460  90.00 116.33  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      0.011766  0.000000  0.005823        0.00000                         
SCALE2      0.000000  0.006952  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012472        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system