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Database: PDB
Entry: 3HNF
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Original site: 3HNF 
HEADER    OXIDOREDUCTASE                          31-MAY-09   3HNF              
TITLE     CRYSTAL STRUCTURE OF HUMAN RIBONUCLEOTIDE REDUCTASE 1 BOUND TO THE    
TITLE    2 EFFECTORS TTP AND DATP                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT;        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M1,            
COMPND   5 RIBONUCLEOTIDE REDUCTASE LARGE SUBUNIT;                              
COMPND   6 EC: 1.17.4.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RR1, RRM1;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21                                     
KEYWDS    OXIDOREDUCTASE, RIBONUCLEOTIDE REDUCTASE, ALLOSTERIC ENZYME, ATP-     
KEYWDS   2 BINDING, DNA REPLICATION, NUCLEOTIDE-BINDING                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.W.FAIRMAN,S.R.WIJERATHNA,H.XU,C.G.DEALWIS                           
REVDAT   4   01-NOV-17 3HNF    1       REMARK                                   
REVDAT   3   23-MAR-11 3HNF    1       JRNL                                     
REVDAT   2   09-MAR-11 3HNF    1       JRNL                                     
REVDAT   1   23-FEB-11 3HNF    0                                                
JRNL        AUTH   J.W.FAIRMAN,S.R.WIJERATHNA,M.F.AHMAD,H.XU,R.NAKANO,S.JHA,    
JRNL        AUTH 2 J.PRENDERGAST,R.M.WELIN,S.FLODIN,A.ROOS,P.NORDLUND,Z.LI,     
JRNL        AUTH 3 T.WALZ,C.G.DEALWIS                                           
JRNL        TITL   STRUCTURAL BASIS FOR ALLOSTERIC REGULATION OF HUMAN          
JRNL        TITL 2 RIBONUCLEOTIDE REDUCTASE BY NUCLEOTIDE-INDUCED               
JRNL        TITL 3 OLIGOMERIZATION.                                             
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18   316 2011              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   21336276                                                     
JRNL        DOI    10.1038/NSMB.2007                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.16 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 3.16                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 26016                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1335                            
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) : 3.16                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.24                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1792                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 101                          
REMARK   3   BIN FREE R VALUE                    : 0.3410                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11391                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 110                                     
REMARK   3   SOLVENT ATOMS            : 48                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.50000                                              
REMARK   3    B22 (A**2) : -3.54000                                             
REMARK   3    B33 (A**2) : 2.03000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.578         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.403         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 48.662        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.883                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11741 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15971 ; 1.458 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1442 ; 6.549 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   515 ;41.031 ;24.447       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1950 ;21.412 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    55 ;17.083 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1791 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8792 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6005 ; 0.236 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  8061 ; 0.316 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   477 ; 0.167 ; 0.200       
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):    65 ; 0.225 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.122 ; 0.200       
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):  7353 ; 0.408 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11626 ; 0.754 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5010 ; 1.024 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4345 ; 1.703 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     742      4                      
REMARK   3           1     B      1       B     742      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   5350 ; 0.480 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   5350 ; 0.450 ; 2.000           
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    14        A   288                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.6320  30.8550  -9.7560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3776 T22:  -0.1669                                     
REMARK   3      T33:  -0.0425 T12:  -0.0117                                     
REMARK   3      T13:  -0.0394 T23:   0.0341                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1728 L22:   3.1759                                     
REMARK   3      L33:   1.8371 L12:   0.7059                                     
REMARK   3      L13:   0.3510 L23:   0.8591                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0713 S12:  -0.0771 S13:   0.0069                       
REMARK   3      S21:   0.4484 S22:  -0.2141 S23:   0.3268                       
REMARK   3      S31:   0.0688 S32:  -0.0541 S33:   0.2854                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   295        A   316                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8480  15.2210 -39.6960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0026 T22:  -0.0329                                     
REMARK   3      T33:  -0.0525 T12:   0.0884                                     
REMARK   3      T13:  -0.0175 T23:  -0.1530                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6530 L22:   5.0795                                     
REMARK   3      L33:   3.8503 L12:   0.1655                                     
REMARK   3      L13:   0.6770 L23:  -3.8110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2951 S12:   0.2310 S13:   0.5899                       
REMARK   3      S21:   0.2644 S22:   0.2281 S23:   0.9279                       
REMARK   3      S31:  -0.1292 S32:  -0.9442 S33:   0.0669                       
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 :   A   326        A   742                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0100  33.0750 -34.5090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0803 T22:  -0.1157                                     
REMARK   3      T33:  -0.2165 T12:  -0.0852                                     
REMARK   3      T13:  -0.0159 T23:   0.0911                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9089 L22:   1.6631                                     
REMARK   3      L33:   1.6774 L12:   0.2908                                     
REMARK   3      L13:   0.5662 L23:   0.7447                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2049 S12:   0.1292 S13:   0.1140                       
REMARK   3      S21:  -0.3927 S22:   0.0819 S23:   0.0094                       
REMARK   3      S31:  -0.2749 S32:   0.1252 S33:   0.1230                       
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 :   B     1        B   287                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.2420 -22.6030 -39.2270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0827 T22:  -0.0061                                     
REMARK   3      T33:  -0.1723 T12:  -0.0179                                     
REMARK   3      T13:   0.0018 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3460 L22:   1.4358                                     
REMARK   3      L33:   2.1384 L12:  -0.0710                                     
REMARK   3      L13:   0.0188 L23:   0.9909                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1156 S12:   0.4460 S13:   0.0142                       
REMARK   3      S21:  -0.3834 S22:   0.1538 S23:   0.1189                       
REMARK   3      S31:  -0.0723 S32:   0.0353 S33:  -0.0382                       
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 :   B   294        B   629                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.9560 -20.6670 -11.5420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2514 T22:  -0.3290                                     
REMARK   3      T33:  -0.2855 T12:   0.0244                                     
REMARK   3      T13:  -0.0319 T23:   0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8755 L22:   2.7201                                     
REMARK   3      L33:   1.9765 L12:   0.3329                                     
REMARK   3      L13:  -0.1249 L23:   1.3559                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0468 S12:   0.1062 S13:   0.0344                       
REMARK   3      S21:  -0.0130 S22:  -0.0384 S23:   0.0551                       
REMARK   3      S31:   0.0982 S32:  -0.0423 S33:  -0.0085                       
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 :   B   632        B   742                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.9250 -24.1910 -16.7550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2291 T22:  -0.1565                                     
REMARK   3      T33:  -0.0445 T12:  -0.0252                                     
REMARK   3      T13:   0.0010 T23:   0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6437 L22:   3.1091                                     
REMARK   3      L33:   2.7912 L12:   1.5325                                     
REMARK   3      L13:   0.4771 L23:   1.6462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1766 S12:   0.2382 S13:   0.3233                       
REMARK   3      S21:  -0.2088 S22:  -0.2486 S23:   0.7108                       
REMARK   3      S31:   0.0138 S32:  -0.7254 S33:   0.0721                       
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 3HNF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053348.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31793                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.15500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6510                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64400                            
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: PDB ENTRY 3HNC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL PH 7.9, 0.2 M LISO4,      
REMARK 280  19% PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       34.42800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      110.00150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.19400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      110.00150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.42800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.19400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 52380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     GLY A   289                                                      
REMARK 465     GLY A   290                                                      
REMARK 465     ASN A   291                                                      
REMARK 465     LYS A   292                                                      
REMARK 465     ARG A   293                                                      
REMARK 465     ASN A   317                                                      
REMARK 465     THR A   318                                                      
REMARK 465     GLY A   319                                                      
REMARK 465     LYS A   320                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     GLN A   323                                                      
REMARK 465     ARG A   324                                                      
REMARK 465     ALA A   325                                                      
REMARK 465     PRO A   743                                                      
REMARK 465     ALA A   744                                                      
REMARK 465     ALA A   745                                                      
REMARK 465     ASN A   746                                                      
REMARK 465     PRO A   747                                                      
REMARK 465     ILE A   748                                                      
REMARK 465     GLN A   749                                                      
REMARK 465     PHE A   750                                                      
REMARK 465     THR A   751                                                      
REMARK 465     LEU A   752                                                      
REMARK 465     ASN A   753                                                      
REMARK 465     LYS A   754                                                      
REMARK 465     GLU A   755                                                      
REMARK 465     LYS A   756                                                      
REMARK 465     LEU A   757                                                      
REMARK 465     LYS A   758                                                      
REMARK 465     ASP A   759                                                      
REMARK 465     LYS A   760                                                      
REMARK 465     GLU A   761                                                      
REMARK 465     LYS A   762                                                      
REMARK 465     VAL A   763                                                      
REMARK 465     SER A   764                                                      
REMARK 465     LYS A   765                                                      
REMARK 465     GLU A   766                                                      
REMARK 465     GLU A   767                                                      
REMARK 465     GLU A   768                                                      
REMARK 465     GLU A   769                                                      
REMARK 465     LYS A   770                                                      
REMARK 465     GLU A   771                                                      
REMARK 465     ARG A   772                                                      
REMARK 465     ASN A   773                                                      
REMARK 465     THR A   774                                                      
REMARK 465     ALA A   775                                                      
REMARK 465     ALA A   776                                                      
REMARK 465     MET A   777                                                      
REMARK 465     VAL A   778                                                      
REMARK 465     CYS A   779                                                      
REMARK 465     SER A   780                                                      
REMARK 465     LEU A   781                                                      
REMARK 465     GLU A   782                                                      
REMARK 465     ASN A   783                                                      
REMARK 465     ARG A   784                                                      
REMARK 465     ASP A   785                                                      
REMARK 465     GLU A   786                                                      
REMARK 465     CYS A   787                                                      
REMARK 465     LEU A   788                                                      
REMARK 465     MET A   789                                                      
REMARK 465     CYS A   790                                                      
REMARK 465     GLY A   791                                                      
REMARK 465     SER A   792                                                      
REMARK 465     GLY B   289                                                      
REMARK 465     GLY B   290                                                      
REMARK 465     ASN B   291                                                      
REMARK 465     LEU B   630                                                      
REMARK 465     SER B   631                                                      
REMARK 465     PRO B   743                                                      
REMARK 465     ALA B   744                                                      
REMARK 465     ALA B   745                                                      
REMARK 465     ASN B   746                                                      
REMARK 465     PRO B   747                                                      
REMARK 465     ILE B   748                                                      
REMARK 465     GLN B   749                                                      
REMARK 465     PHE B   750                                                      
REMARK 465     THR B   751                                                      
REMARK 465     LEU B   752                                                      
REMARK 465     ASN B   753                                                      
REMARK 465     LYS B   754                                                      
REMARK 465     GLU B   755                                                      
REMARK 465     LYS B   756                                                      
REMARK 465     LEU B   757                                                      
REMARK 465     LYS B   758                                                      
REMARK 465     ASP B   759                                                      
REMARK 465     LYS B   760                                                      
REMARK 465     GLU B   761                                                      
REMARK 465     LYS B   762                                                      
REMARK 465     VAL B   763                                                      
REMARK 465     SER B   764                                                      
REMARK 465     LYS B   765                                                      
REMARK 465     GLU B   766                                                      
REMARK 465     GLU B   767                                                      
REMARK 465     GLU B   768                                                      
REMARK 465     GLU B   769                                                      
REMARK 465     LYS B   770                                                      
REMARK 465     GLU B   771                                                      
REMARK 465     ARG B   772                                                      
REMARK 465     ASN B   773                                                      
REMARK 465     THR B   774                                                      
REMARK 465     ALA B   775                                                      
REMARK 465     ALA B   776                                                      
REMARK 465     MET B   777                                                      
REMARK 465     VAL B   778                                                      
REMARK 465     CYS B   779                                                      
REMARK 465     SER B   780                                                      
REMARK 465     LEU B   781                                                      
REMARK 465     GLU B   782                                                      
REMARK 465     ASN B   783                                                      
REMARK 465     ARG B   784                                                      
REMARK 465     ASP B   785                                                      
REMARK 465     GLU B   786                                                      
REMARK 465     CYS B   787                                                      
REMARK 465     LEU B   788                                                      
REMARK 465     MET B   789                                                      
REMARK 465     CYS B   790                                                      
REMARK 465     GLY B   791                                                      
REMARK 465     SER B   792                                                      
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     LYS A  17    CG   CD   CE   NZ                                   
REMARK 470     ARG A  21    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  42    CG   CD   CE   NZ                                   
REMARK 470     GLU A  55    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  57    CG   OD1  OD2                                       
REMARK 470     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     GLU A  89    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 111    CG   CD   CE   NZ                                   
REMARK 470     ARG A 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 162    CG   CD   CE   NZ                                   
REMARK 470     GLU A 181    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 212    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 244    OG                                                  
REMARK 470     LYS A 315    CG   CD   CE   NZ                                   
REMARK 470     LYS A 316    CG   CD   CE   NZ                                   
REMARK 470     LYS A 369    CG   CD   CE   NZ                                   
REMARK 470     LYS A 376    CG   CD   CE   NZ                                   
REMARK 470     LYS A 385    CG   CD   CE   NZ                                   
REMARK 470     LYS A 438    CG   CD   CE   NZ                                   
REMARK 470     LYS A 464    CG   CD   CE   NZ                                   
REMARK 470     ASP A 580    CG   OD1  OD2                                       
REMARK 470     LYS A 582    CG   CD   CE   NZ                                   
REMARK 470     GLU A 586    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 590    CG   CD   CE   NZ                                   
REMARK 470     ARG A 627    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 628    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 675    CG   OD1  OD2                                       
REMARK 470     LYS A 689    CG   CD   CE   NZ                                   
REMARK 470     LYS A 719    CG   CD   CE   NZ                                   
REMARK 470     LYS B  24    CG   CD   CE   NZ                                   
REMARK 470     LYS B  42    CG   CD   CE   NZ                                   
REMARK 470     ASP B  57    CG   OD1  OD2                                       
REMARK 470     HIS B 108    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN B 109    CG   OD1  ND2                                       
REMARK 470     LYS B 111    CG   CD   CE   NZ                                   
REMARK 470     LYS B 118    CG   CD   CE   NZ                                   
REMARK 470     LYS B 162    CG   CD   CE   NZ                                   
REMARK 470     GLU B 181    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 236    CG   CD   CE   NZ                                   
REMARK 470     GLN B 288    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 317    CG   OD1  ND2                                       
REMARK 470     THR B 318    OG1  CG2                                            
REMARK 470     LYS B 320    CG   CD   CE   NZ                                   
REMARK 470     GLU B 321    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 322    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 376    CG   CD   CE   NZ                                   
REMARK 470     LYS B 385    CG   CD   CE   NZ                                   
REMARK 470     LYS B 438    CG   CD   CE   NZ                                   
REMARK 470     GLU B 458    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 609    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 628    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 633    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 647    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 653    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 654    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 656    CG   CD   CE   NZ                                   
REMARK 470     GLN B 658    CG   CD   OE1  NE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     CYS A  218   CA   CB   SG                                        
REMARK 480     CYS A  444   CA   CB   SG                                        
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   OD1  ASN B   416     CG2  VAL B   561              2.09            
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    LEU B  47   CA  -  CB  -  CG  ANGL. DEV. =  16.5 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    SER A  20       -8.61    -51.26                                   
REMARK 500    ASN A  30       96.93    -69.34                                   
REMARK 500    ILE A  44       -2.28    -55.14                                   
REMARK 500    THR A  52     -147.05   -146.81                                   
REMARK 500    THR A  53      -51.09    -24.72                                   
REMARK 500    LYS A  88        1.68    -65.91                                   
REMARK 500    GLU A  89       22.57   -142.54                                   
REMARK 500    TYR A 104       96.88    -18.52                                   
REMARK 500    ASN A 106       95.70    -61.62                                   
REMARK 500    ASN A 127       34.83   -142.80                                   
REMARK 500    SER A 154      -21.07   -143.77                                   
REMARK 500    ASN A 160      103.89     22.25                                   
REMARK 500    LYS A 162      119.67    -14.03                                   
REMARK 500    LYS A 180     -112.09     24.20                                   
REMARK 500    ARG A 196       30.98     70.64                                   
REMARK 500    ARG A 212       76.74   -114.77                                   
REMARK 500    SER A 217       24.16   -148.25                                   
REMARK 500    CYS A 218      140.26    162.00                                   
REMARK 500    LEU A 221      106.81   -165.48                                   
REMARK 500    SER A 244       35.76    -82.59                                   
REMARK 500    ALA A 245      -54.69     92.19                                   
REMARK 500    TYR A 285      -99.82    -81.52                                   
REMARK 500    ASP A 287      -68.67   -121.12                                   
REMARK 500    ALA A 296       85.94    166.68                                   
REMARK 500    LEU A 312       22.39    -71.34                                   
REMARK 500    ASP A 327        8.08    178.73                                   
REMARK 500    TRP A 333       74.63   -100.79                                   
REMARK 500    THR A 344       44.41   -104.20                                   
REMARK 500    ASN A 345       87.44     17.17                                   
REMARK 500    ARG A 379       70.18    -48.14                                   
REMARK 500    LYS A 382      134.47   -174.89                                   
REMARK 500    CYS A 425     -168.14   -173.74                                   
REMARK 500    SER A 457       24.03    -67.98                                   
REMARK 500    ARG A 499       59.70     34.10                                   
REMARK 500    ARG A 516       20.51     96.84                                   
REMARK 500    ASP A 577        7.84    -69.15                                   
REMARK 500    LEU A 598      -43.42   -131.52                                   
REMARK 500    ALA A 600       96.04   -167.41                                   
REMARK 500    SER A 616     -127.23     42.74                                   
REMARK 500    PRO A 619      173.99    -54.22                                   
REMARK 500    ARG A 627      120.90   -173.35                                   
REMARK 500    LEU A 630     -119.40     48.58                                   
REMARK 500    ASN A 638      116.72    -37.56                                   
REMARK 500    GLU A 653      -77.43    -53.30                                   
REMARK 500    CYS A 662       34.83    -98.98                                   
REMARK 500    ASN A 663       17.77     45.08                                   
REMARK 500    GLU A 697      -70.16    -51.16                                   
REMARK 500    GLN A 704     -104.11   -112.49                                   
REMARK 500    ALA A 713      -80.65    -59.05                                   
REMARK 500    TYR A 737      -98.07    -79.37                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      98 RAMACHANDRAN OUTLIERS.                        
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                              MG A 801  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP A 804   O2B                                                    
REMARK 620 2 TTP A 804   O2A  66.7                                              
REMARK 620 3 TTP A 804   O3G  87.8 105.2                                        
REMARK 620 4 TTP A 804   O1G  66.7 126.8  49.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 802  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP B 803   O2A                                                    
REMARK 620 2 TTP B 803   O3B  70.2                                              
REMARK 620 3 TTP B 803   O3G 125.5  64.5                                        
REMARK 620 4 TTP B 803   O2B  66.9  56.9 108.2                                  
REMARK 620 5 TTP B 803   O1G 119.7  56.1  52.0  62.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTP B 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 809                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3HNC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN RIBONUCLEOTIDE REDUCTASE 1 BOUND TO THE   
REMARK 900 EFFECTOR TTP                                                         
REMARK 900 RELATED ID: 3HND   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN RIBONUCLEOTIDE REDUCTASE 1 BOUND TO THE   
REMARK 900 EFFECTOR TTP AND SUBSTRATE GDP                                       
REMARK 900 RELATED ID: 3HNE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN RIBONUCLEOTIDE REDUCTASE 1 BOUND TO THE   
REMARK 900 EFFECTORS TTP AND ATP                                                
DBREF  3HNF A    1   792  UNP    P23921   RIR1_HUMAN       1    792             
DBREF  3HNF B    1   792  UNP    P23921   RIR1_HUMAN       1    792             
SEQRES   1 A  792  MET HIS VAL ILE LYS ARG ASP GLY ARG GLN GLU ARG VAL          
SEQRES   2 A  792  MET PHE ASP LYS ILE THR SER ARG ILE GLN LYS LEU CYS          
SEQRES   3 A  792  TYR GLY LEU ASN MET ASP PHE VAL ASP PRO ALA GLN ILE          
SEQRES   4 A  792  THR MET LYS VAL ILE GLN GLY LEU TYR SER GLY VAL THR          
SEQRES   5 A  792  THR VAL GLU LEU ASP THR LEU ALA ALA GLU THR ALA ALA          
SEQRES   6 A  792  THR LEU THR THR LYS HIS PRO ASP TYR ALA ILE LEU ALA          
SEQRES   7 A  792  ALA ARG ILE ALA VAL SER ASN LEU HIS LYS GLU THR LYS          
SEQRES   8 A  792  LYS VAL PHE SER ASP VAL MET GLU ASP LEU TYR ASN TYR          
SEQRES   9 A  792  ILE ASN PRO HIS ASN GLY LYS HIS SER PRO MET VAL ALA          
SEQRES  10 A  792  LYS SER THR LEU ASP ILE VAL LEU ALA ASN LYS ASP ARG          
SEQRES  11 A  792  LEU ASN SER ALA ILE ILE TYR ASP ARG ASP PHE SER TYR          
SEQRES  12 A  792  ASN TYR PHE GLY PHE LYS THR LEU GLU ARG SER TYR LEU          
SEQRES  13 A  792  LEU LYS ILE ASN GLY LYS VAL ALA GLU ARG PRO GLN HIS          
SEQRES  14 A  792  MET LEU MET ARG VAL SER VAL GLY ILE HIS LYS GLU ASP          
SEQRES  15 A  792  ILE ASP ALA ALA ILE GLU THR TYR ASN LEU LEU SER GLU          
SEQRES  16 A  792  ARG TRP PHE THR HIS ALA SER PRO THR LEU PHE ASN ALA          
SEQRES  17 A  792  GLY THR ASN ARG PRO GLN LEU SER SER CYS PHE LEU LEU          
SEQRES  18 A  792  SER MET LYS ASP ASP SER ILE GLU GLY ILE TYR ASP THR          
SEQRES  19 A  792  LEU LYS GLN CYS ALA LEU ILE SER LYS SER ALA GLY GLY          
SEQRES  20 A  792  ILE GLY VAL ALA VAL SER CYS ILE ARG ALA THR GLY SER          
SEQRES  21 A  792  TYR ILE ALA GLY THR ASN GLY ASN SER ASN GLY LEU VAL          
SEQRES  22 A  792  PRO MET LEU ARG VAL TYR ASN ASN THR ALA ARG TYR VAL          
SEQRES  23 A  792  ASP GLN GLY GLY ASN LYS ARG PRO GLY ALA PHE ALA ILE          
SEQRES  24 A  792  TYR LEU GLU PRO TRP HIS LEU ASP ILE PHE GLU PHE LEU          
SEQRES  25 A  792  ASP LEU LYS LYS ASN THR GLY LYS GLU GLU GLN ARG ALA          
SEQRES  26 A  792  ARG ASP LEU PHE PHE ALA LEU TRP ILE PRO ASP LEU PHE          
SEQRES  27 A  792  MET LYS ARG VAL GLU THR ASN GLN ASP TRP SER LEU MET          
SEQRES  28 A  792  CYS PRO ASN GLU CYS PRO GLY LEU ASP GLU VAL TRP GLY          
SEQRES  29 A  792  GLU GLU PHE GLU LYS LEU TYR ALA SER TYR GLU LYS GLN          
SEQRES  30 A  792  GLY ARG VAL ARG LYS VAL VAL LYS ALA GLN GLN LEU TRP          
SEQRES  31 A  792  TYR ALA ILE ILE GLU SER GLN THR GLU THR GLY THR PRO          
SEQRES  32 A  792  TYR MET LEU TYR LYS ASP SER CYS ASN ARG LYS SER ASN          
SEQRES  33 A  792  GLN GLN ASN LEU GLY THR ILE LYS CYS SER ASN LEU CYS          
SEQRES  34 A  792  THR GLU ILE VAL GLU TYR THR SER LYS ASP GLU VAL ALA          
SEQRES  35 A  792  VAL CYS ASN LEU ALA SER LEU ALA LEU ASN MET TYR VAL          
SEQRES  36 A  792  THR SER GLU HIS THR TYR ASP PHE LYS LYS LEU ALA GLU          
SEQRES  37 A  792  VAL THR LYS VAL VAL VAL ARG ASN LEU ASN LYS ILE ILE          
SEQRES  38 A  792  ASP ILE ASN TYR TYR PRO VAL PRO GLU ALA CYS LEU SER          
SEQRES  39 A  792  ASN LYS ARG HIS ARG PRO ILE GLY ILE GLY VAL GLN GLY          
SEQRES  40 A  792  LEU ALA ASP ALA PHE ILE LEU MET ARG TYR PRO PHE GLU          
SEQRES  41 A  792  SER ALA GLU ALA GLN LEU LEU ASN LYS GLN ILE PHE GLU          
SEQRES  42 A  792  THR ILE TYR TYR GLY ALA LEU GLU ALA SER CYS ASP LEU          
SEQRES  43 A  792  ALA LYS GLU GLN GLY PRO TYR GLU THR TYR GLU GLY SER          
SEQRES  44 A  792  PRO VAL SER LYS GLY ILE LEU GLN TYR ASP MET TRP ASN          
SEQRES  45 A  792  VAL THR PRO THR ASP LEU TRP ASP TRP LYS VAL LEU LYS          
SEQRES  46 A  792  GLU LYS ILE ALA LYS TYR GLY ILE ARG ASN SER LEU LEU          
SEQRES  47 A  792  ILE ALA PRO MET PRO THR ALA SER THR ALA GLN ILE LEU          
SEQRES  48 A  792  GLY ASN ASN GLU SER ILE GLU PRO TYR THR SER ASN ILE          
SEQRES  49 A  792  TYR THR ARG ARG VAL LEU SER GLY GLU PHE GLN ILE VAL          
SEQRES  50 A  792  ASN PRO HIS LEU LEU LYS ASP LEU THR GLU ARG GLY LEU          
SEQRES  51 A  792  TRP HIS GLU GLU MET LYS ASN GLN ILE ILE ALA CYS ASN          
SEQRES  52 A  792  GLY SER ILE GLN SER ILE PRO GLU ILE PRO ASP ASP LEU          
SEQRES  53 A  792  LYS GLN LEU TYR LYS THR VAL TRP GLU ILE SER GLN LYS          
SEQRES  54 A  792  THR VAL LEU LYS MET ALA ALA GLU ARG GLY ALA PHE ILE          
SEQRES  55 A  792  ASP GLN SER GLN SER LEU ASN ILE HIS ILE ALA GLU PRO          
SEQRES  56 A  792  ASN TYR GLY LYS LEU THR SER MET HIS PHE TYR GLY TRP          
SEQRES  57 A  792  LYS GLN GLY LEU LYS THR GLY MET TYR TYR LEU ARG THR          
SEQRES  58 A  792  ARG PRO ALA ALA ASN PRO ILE GLN PHE THR LEU ASN LYS          
SEQRES  59 A  792  GLU LYS LEU LYS ASP LYS GLU LYS VAL SER LYS GLU GLU          
SEQRES  60 A  792  GLU GLU LYS GLU ARG ASN THR ALA ALA MET VAL CYS SER          
SEQRES  61 A  792  LEU GLU ASN ARG ASP GLU CYS LEU MET CYS GLY SER              
SEQRES   1 B  792  MET HIS VAL ILE LYS ARG ASP GLY ARG GLN GLU ARG VAL          
SEQRES   2 B  792  MET PHE ASP LYS ILE THR SER ARG ILE GLN LYS LEU CYS          
SEQRES   3 B  792  TYR GLY LEU ASN MET ASP PHE VAL ASP PRO ALA GLN ILE          
SEQRES   4 B  792  THR MET LYS VAL ILE GLN GLY LEU TYR SER GLY VAL THR          
SEQRES   5 B  792  THR VAL GLU LEU ASP THR LEU ALA ALA GLU THR ALA ALA          
SEQRES   6 B  792  THR LEU THR THR LYS HIS PRO ASP TYR ALA ILE LEU ALA          
SEQRES   7 B  792  ALA ARG ILE ALA VAL SER ASN LEU HIS LYS GLU THR LYS          
SEQRES   8 B  792  LYS VAL PHE SER ASP VAL MET GLU ASP LEU TYR ASN TYR          
SEQRES   9 B  792  ILE ASN PRO HIS ASN GLY LYS HIS SER PRO MET VAL ALA          
SEQRES  10 B  792  LYS SER THR LEU ASP ILE VAL LEU ALA ASN LYS ASP ARG          
SEQRES  11 B  792  LEU ASN SER ALA ILE ILE TYR ASP ARG ASP PHE SER TYR          
SEQRES  12 B  792  ASN TYR PHE GLY PHE LYS THR LEU GLU ARG SER TYR LEU          
SEQRES  13 B  792  LEU LYS ILE ASN GLY LYS VAL ALA GLU ARG PRO GLN HIS          
SEQRES  14 B  792  MET LEU MET ARG VAL SER VAL GLY ILE HIS LYS GLU ASP          
SEQRES  15 B  792  ILE ASP ALA ALA ILE GLU THR TYR ASN LEU LEU SER GLU          
SEQRES  16 B  792  ARG TRP PHE THR HIS ALA SER PRO THR LEU PHE ASN ALA          
SEQRES  17 B  792  GLY THR ASN ARG PRO GLN LEU SER SER CYS PHE LEU LEU          
SEQRES  18 B  792  SER MET LYS ASP ASP SER ILE GLU GLY ILE TYR ASP THR          
SEQRES  19 B  792  LEU LYS GLN CYS ALA LEU ILE SER LYS SER ALA GLY GLY          
SEQRES  20 B  792  ILE GLY VAL ALA VAL SER CYS ILE ARG ALA THR GLY SER          
SEQRES  21 B  792  TYR ILE ALA GLY THR ASN GLY ASN SER ASN GLY LEU VAL          
SEQRES  22 B  792  PRO MET LEU ARG VAL TYR ASN ASN THR ALA ARG TYR VAL          
SEQRES  23 B  792  ASP GLN GLY GLY ASN LYS ARG PRO GLY ALA PHE ALA ILE          
SEQRES  24 B  792  TYR LEU GLU PRO TRP HIS LEU ASP ILE PHE GLU PHE LEU          
SEQRES  25 B  792  ASP LEU LYS LYS ASN THR GLY LYS GLU GLU GLN ARG ALA          
SEQRES  26 B  792  ARG ASP LEU PHE PHE ALA LEU TRP ILE PRO ASP LEU PHE          
SEQRES  27 B  792  MET LYS ARG VAL GLU THR ASN GLN ASP TRP SER LEU MET          
SEQRES  28 B  792  CYS PRO ASN GLU CYS PRO GLY LEU ASP GLU VAL TRP GLY          
SEQRES  29 B  792  GLU GLU PHE GLU LYS LEU TYR ALA SER TYR GLU LYS GLN          
SEQRES  30 B  792  GLY ARG VAL ARG LYS VAL VAL LYS ALA GLN GLN LEU TRP          
SEQRES  31 B  792  TYR ALA ILE ILE GLU SER GLN THR GLU THR GLY THR PRO          
SEQRES  32 B  792  TYR MET LEU TYR LYS ASP SER CYS ASN ARG LYS SER ASN          
SEQRES  33 B  792  GLN GLN ASN LEU GLY THR ILE LYS CYS SER ASN LEU CYS          
SEQRES  34 B  792  THR GLU ILE VAL GLU TYR THR SER LYS ASP GLU VAL ALA          
SEQRES  35 B  792  VAL CYS ASN LEU ALA SER LEU ALA LEU ASN MET TYR VAL          
SEQRES  36 B  792  THR SER GLU HIS THR TYR ASP PHE LYS LYS LEU ALA GLU          
SEQRES  37 B  792  VAL THR LYS VAL VAL VAL ARG ASN LEU ASN LYS ILE ILE          
SEQRES  38 B  792  ASP ILE ASN TYR TYR PRO VAL PRO GLU ALA CYS LEU SER          
SEQRES  39 B  792  ASN LYS ARG HIS ARG PRO ILE GLY ILE GLY VAL GLN GLY          
SEQRES  40 B  792  LEU ALA ASP ALA PHE ILE LEU MET ARG TYR PRO PHE GLU          
SEQRES  41 B  792  SER ALA GLU ALA GLN LEU LEU ASN LYS GLN ILE PHE GLU          
SEQRES  42 B  792  THR ILE TYR TYR GLY ALA LEU GLU ALA SER CYS ASP LEU          
SEQRES  43 B  792  ALA LYS GLU GLN GLY PRO TYR GLU THR TYR GLU GLY SER          
SEQRES  44 B  792  PRO VAL SER LYS GLY ILE LEU GLN TYR ASP MET TRP ASN          
SEQRES  45 B  792  VAL THR PRO THR ASP LEU TRP ASP TRP LYS VAL LEU LYS          
SEQRES  46 B  792  GLU LYS ILE ALA LYS TYR GLY ILE ARG ASN SER LEU LEU          
SEQRES  47 B  792  ILE ALA PRO MET PRO THR ALA SER THR ALA GLN ILE LEU          
SEQRES  48 B  792  GLY ASN ASN GLU SER ILE GLU PRO TYR THR SER ASN ILE          
SEQRES  49 B  792  TYR THR ARG ARG VAL LEU SER GLY GLU PHE GLN ILE VAL          
SEQRES  50 B  792  ASN PRO HIS LEU LEU LYS ASP LEU THR GLU ARG GLY LEU          
SEQRES  51 B  792  TRP HIS GLU GLU MET LYS ASN GLN ILE ILE ALA CYS ASN          
SEQRES  52 B  792  GLY SER ILE GLN SER ILE PRO GLU ILE PRO ASP ASP LEU          
SEQRES  53 B  792  LYS GLN LEU TYR LYS THR VAL TRP GLU ILE SER GLN LYS          
SEQRES  54 B  792  THR VAL LEU LYS MET ALA ALA GLU ARG GLY ALA PHE ILE          
SEQRES  55 B  792  ASP GLN SER GLN SER LEU ASN ILE HIS ILE ALA GLU PRO          
SEQRES  56 B  792  ASN TYR GLY LYS LEU THR SER MET HIS PHE TYR GLY TRP          
SEQRES  57 B  792  LYS GLN GLY LEU LYS THR GLY MET TYR TYR LEU ARG THR          
SEQRES  58 B  792  ARG PRO ALA ALA ASN PRO ILE GLN PHE THR LEU ASN LYS          
SEQRES  59 B  792  GLU LYS LEU LYS ASP LYS GLU LYS VAL SER LYS GLU GLU          
SEQRES  60 B  792  GLU GLU LYS GLU ARG ASN THR ALA ALA MET VAL CYS SER          
SEQRES  61 B  792  LEU GLU ASN ARG ASP GLU CYS LEU MET CYS GLY SER              
HET     MG  A 801       1                                                       
HET    TTP  A 804      29                                                       
HET    SO4  A 807       5                                                       
HET    SO4  A 808       5                                                       
HET     MG  B 802       1                                                       
HET    TTP  B 803      29                                                       
HET    DTP  B 805      30                                                       
HET    SO4  B 806       5                                                       
HET    SO4  B 809       5                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     TTP THYMIDINE-5'-TRIPHOSPHATE                                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE                                
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4  TTP    2(C10 H17 N2 O14 P3)                                         
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   9  DTP    C10 H16 N5 O12 P3                                            
FORMUL  12  HOH   *48(H2 O)                                                     
HELIX    1   1 MET A   14  GLN A   23  1                                  10    
HELIX    2   2 LYS A   24  TYR A   27  5                                   4    
HELIX    3   3 ASP A   35  ILE A   44  1                                  10    
HELIX    4   4 THR A   52  LEU A   67  1                                  16    
HELIX    5   5 THR A   68  HIS A   71  5                                   4    
HELIX    6   6 PRO A   72  LYS A   88  1                                  17    
HELIX    7   7 VAL A   93  TYR A  104  1                                  12    
HELIX    8   8 ALA A  117  ALA A  126  1                                  10    
HELIX    9   9 ASN A  127  SER A  133  1                                   7    
HELIX   10  10 ALA A  134  ILE A  135  5                                   2    
HELIX   11  11 ILE A  136  SER A  142  5                                   7    
HELIX   12  12 ASN A  144  TYR A  155  1                                  12    
HELIX   13  13 ARG A  166  LYS A  180  1                                  15    
HELIX   14  14 ASP A  182  GLU A  195  1                                  14    
HELIX   15  15 ALA A  201  ALA A  208  1                                   8    
HELIX   16  16 SER A  227  SER A  244  1                                  18    
HELIX   17  17 GLY A  271  VAL A  286  1                                  16    
HELIX   18  18 ASP A  307  LEU A  312  1                                   6    
HELIX   19  19 PRO A  335  THR A  344  1                                  10    
HELIX   20  20 TRP A  363  LYS A  376  1                                  14    
HELIX   21  21 ALA A  386  GLY A  401  1                                  16    
HELIX   22  22 LYS A  408  LYS A  414  1                                   7    
HELIX   23  23 GLN A  417  GLY A  421  5                                   5    
HELIX   24  24 ASN A  452  TYR A  454  5                                   3    
HELIX   25  25 ASP A  462  ASN A  484  1                                  23    
HELIX   26  26 VAL A  488  ARG A  499  1                                  12    
HELIX   27  27 GLY A  507  ARG A  516  1                                  10    
HELIX   28  28 SER A  521  GLY A  551  1                                  31    
HELIX   29  29 LEU A  566  TRP A  571  1                                   6    
HELIX   30  30 ASP A  580  GLY A  592  1                                  13    
HELIX   31  31 THR A  604  LEU A  611  1                                   8    
HELIX   32  32 ASN A  638  ARG A  648  1                                  11    
HELIX   33  33 HIS A  652  CYS A  662  1                                  11    
HELIX   34  34 PRO A  673  TYR A  680  1                                   8    
HELIX   35  35 THR A  682  ILE A  686  5                                   5    
HELIX   36  36 SER A  687  GLY A  699  1                                  13    
HELIX   37  37 ASN A  716  GLY A  731  1                                  16    
HELIX   38  38 PHE B   15  LYS B   24  1                                  10    
HELIX   39  39 PRO B   36  ILE B   44  1                                   9    
HELIX   40  40 VAL B   54  THR B   66  1                                  13    
HELIX   41  41 PRO B   72  GLU B   89  1                                  18    
HELIX   42  42 VAL B   93  TYR B  104  1                                  12    
HELIX   43  43 ALA B  117  ASN B  127  1                                  11    
HELIX   44  44 ASN B  127  ILE B  135  1                                   9    
HELIX   45  45 ILE B  136  TYR B  143  5                                   8    
HELIX   46  46 ASN B  144  TYR B  155  1                                  12    
HELIX   47  47 ARG B  166  LYS B  180  1                                  15    
HELIX   48  48 ASP B  182  GLU B  195  1                                  14    
HELIX   49  49 ALA B  201  ALA B  208  1                                   8    
HELIX   50  50 SER B  227  SER B  244  1                                  18    
HELIX   51  51 ILE B  262  ASN B  266  5                                   5    
HELIX   52  52 GLY B  271  VAL B  286  1                                  16    
HELIX   53  53 ASP B  307  LEU B  314  1                                   8    
HELIX   54  54 LYS B  320  ARG B  324  5                                   5    
HELIX   55  55 PRO B  335  THR B  344  1                                  10    
HELIX   56  56 TRP B  363  GLN B  377  1                                  15    
HELIX   57  57 ALA B  386  THR B  400  1                                  15    
HELIX   58  58 TYR B  407  LYS B  414  1                                   8    
HELIX   59  59 GLN B  417  GLY B  421  5                                   5    
HELIX   60  60 ASP B  462  ASN B  484  1                                  23    
HELIX   61  61 VAL B  488  ARG B  499  1                                  12    
HELIX   62  62 GLY B  507  ARG B  516  1                                  10    
HELIX   63  63 SER B  521  GLY B  551  1                                  31    
HELIX   64  64 PRO B  560  GLY B  564  5                                   5    
HELIX   65  65 LEU B  566  MET B  570  5                                   5    
HELIX   66  66 ASP B  580  GLY B  592  1                                  13    
HELIX   67  67 SER B  606  GLY B  612  1                                   7    
HELIX   68  68 ASN B  638  ARG B  648  1                                  11    
HELIX   69  69 HIS B  652  CYS B  662  1                                  11    
HELIX   70  70 PRO B  673  TYR B  680  1                                   8    
HELIX   71  71 THR B  682  ILE B  686  5                                   5    
HELIX   72  72 SER B  687  ALA B  700  1                                  14    
HELIX   73  73 ASN B  716  GLN B  730  1                                  15    
SHEET    1   A 3 PHE A 198  HIS A 200  0                                        
SHEET    2   A 3 LEU A 446  ALA A 450 -1  O  SER A 448   N  THR A 199           
SHEET    3   A 3 GLY A 502  GLN A 506  1  O  GLY A 504   N  ALA A 447           
SHEET    1   B 6 PHE A 219  SER A 222  0                                        
SHEET    2   B 6 ILE A 248  ALA A 251  1  O  ALA A 251   N  LEU A 221           
SHEET    3   B 6 PHE A 297  LEU A 301  1  O  ALA A 298   N  VAL A 250           
SHEET    4   B 6 LEU A 328  ILE A 334  1  O  PHE A 329   N  PHE A 297           
SHEET    5   B 6 TYR A 404  TYR A 407  1  O  TYR A 404   N  LEU A 332           
SHEET    6   B 6 THR A 734  MET A 736 -1  O  GLY A 735   N  MET A 405           
SHEET    1   C 2 TYR A 261  ILE A 262  0                                        
SHEET    2   C 2 GLY A 267  ASN A 268 -1  O  GLY A 267   N  ILE A 262           
SHEET    1   D 2 ASP A 347  LEU A 350  0                                        
SHEET    2   D 2 LYS A 382  LYS A 385 -1  O  LYS A 382   N  LEU A 350           
SHEET    1   E 2 ILE A 624  TYR A 625  0                                        
SHEET    2   E 2 ILE A 636  VAL A 637 -1  O  ILE A 636   N  TYR A 625           
SHEET    1   F 2 ILE A 710  HIS A 711  0                                        
SHEET    2   F 2 LEU A 739  ARG A 740  1  O  ARG A 740   N  ILE A 710           
SHEET    1   G 2 HIS B   2  ILE B   4  0                                        
SHEET    2   G 2 GLN B  10  ARG B  12 -1  O  GLU B  11   N  VAL B   3           
SHEET    1   H 2 LYS B 158  ILE B 159  0                                        
SHEET    2   H 2 LYS B 162  VAL B 163 -1  O  LYS B 162   N  ILE B 159           
SHEET    1   I 3 PHE B 198  HIS B 200  0                                        
SHEET    2   I 3 LEU B 446  ALA B 450 -1  O  SER B 448   N  THR B 199           
SHEET    3   I 3 GLY B 502  GLN B 506  1  O  GLY B 504   N  ALA B 447           
SHEET    1   J 7 ALA B 442  CYS B 444  0                                        
SHEET    2   J 7 CYS B 218  SER B 222 -1  N  LEU B 220   O  ALA B 442           
SHEET    3   J 7 GLY B 247  ALA B 251  1  O  ALA B 251   N  LEU B 221           
SHEET    4   J 7 PHE B 297  LEU B 301  1  O  ALA B 298   N  VAL B 250           
SHEET    5   J 7 LEU B 328  TRP B 333  1  O  PHE B 329   N  ILE B 299           
SHEET    6   J 7 TYR B 404  LEU B 406  1  O  LEU B 406   N  LEU B 332           
SHEET    7   J 7 THR B 734  MET B 736 -1  O  GLY B 735   N  MET B 405           
SHEET    1   K 2 ASP B 347  LEU B 350  0                                        
SHEET    2   K 2 LYS B 382  LYS B 385 -1  O  LYS B 382   N  LEU B 350           
SHEET    1   L 2 ILE B 624  ARG B 627  0                                        
SHEET    2   L 2 PHE B 634  VAL B 637 -1  O  ILE B 636   N  TYR B 625           
SHEET    1   M 2 ILE B 710  HIS B 711  0                                        
SHEET    2   M 2 LEU B 739  ARG B 740  1  O  ARG B 740   N  ILE B 710           
LINK        MG    MG A 801                 O2B TTP A 804     1555   1555  2.22  
LINK        MG    MG A 801                 O2A TTP A 804     1555   1555  2.49  
LINK        MG    MG B 802                 O2A TTP B 803     1555   1555  2.49  
LINK        MG    MG B 802                 O3B TTP B 803     1555   1555  2.42  
LINK        MG    MG B 802                 O3G TTP B 803     1555   1555  2.40  
LINK        MG    MG A 801                 O3G TTP A 804     1555   1555  2.83  
LINK        MG    MG B 802                 O2B TTP B 803     1555   1555  2.90  
LINK        MG    MG A 801                 O1G TTP A 804     1555   1555  2.97  
LINK        MG    MG B 802                 O1G TTP B 803     1555   1555  2.98  
CISPEP   1 THR A  402    PRO A  403          0        -3.61                     
CISPEP   2 THR B  402    PRO B  403          0         8.80                     
SITE     1 AC1  1 TTP A 804                                                     
SITE     1 AC2 11 ASP A 226  SER A 227  ILE A 228  ARG A 256                    
SITE     2 AC2 11 ILE A 262  ALA A 263  GLY A 264  THR A 265                    
SITE     3 AC2 11  MG A 801  LYS B 243  ASP B 287                               
SITE     1 AC3  5 SER A 202  THR A 604  ALA A 605  SER A 606                    
SITE     2 AC3  5 THR A 607                                                     
SITE     1 AC4  4 ILE A 136  TYR A 137  ASP A 138  LYS B 382                    
SITE     1 AC5  2 ASP B 226  TTP B 803                                          
SITE     1 AC6 13 LYS A 243  VAL A 286  ASP A 287  ASP B 226                    
SITE     2 AC6 13 SER B 227  ILE B 228  ARG B 256  ILE B 262                    
SITE     3 AC6 13 ALA B 263  GLY B 264  THR B 265   MG B 802                    
SITE     4 AC6 13 HOH B 822                                                     
SITE     1 AC7  9 LYS B   5  ARG B   6  ARG B  12  MET B  14                    
SITE     2 AC7  9 ILE B  18  ARG B  21  THR B  53  LEU B  56                    
SITE     3 AC7  9 LYS B  88                                                     
SITE     1 AC8  6 SER B 202  PRO B 603  THR B 604  ALA B 605                    
SITE     2 AC8  6 SER B 606  THR B 607                                          
SITE     1 AC9  3 SER B 687  GLN B 688  LYS B 689                               
CRYST1   68.856  114.388  220.003  90.00  90.00  90.00 P 21 21 21    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      0.014523  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008742  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004545        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system