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Database: PDB
Entry: 4IZ5
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HEADER    TRANSFERASE                             29-JAN-13   4IZ5              
TITLE     STRUCTURE OF THE COMPLEX BETWEEN ERK2 PHOSPHOMIMETIC MUTANT AND PEA-15
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 8-360;                                        
COMPND   5 SYNONYM: MAP KINASE 1, MAPK 1, ERT1, EXTRACELLULAR SIGNAL-REGULATED  
COMPND   6 KINASE 2, ERK-2, MAP KINASE ISOFORM P42, P42-MAPK, MITOGEN-ACTIVATED 
COMPND   7 PROTEIN KINASE 2, MAP KINASE 2, MAPK 2;                              
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: ASTROCYTIC PHOSPHOPROTEIN PEA-15;                          
COMPND  13 CHAIN: E, F, G, H;                                                   
COMPND  14 FRAGMENT: UNP RESIDUES 1-130;                                        
COMPND  15 SYNONYM: 15 KDA PHOSPHOPROTEIN ENRICHED IN ASTROCYTES, PHOSPHOPROTEIN
COMPND  16 ENRICHED IN DIABETES, PED;                                           
COMPND  17 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: MAPK1, ERK2, PRKM1, PRKM2;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: PEA15;                                                         
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    MAP KINASE, DEATH EFFECTOR DOMAIN, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.D.MACE,H.ROBINSON,S.J.RIEDL                                         
REVDAT   2   24-APR-13 4IZ5    1       JRNL                                     
REVDAT   1   10-APR-13 4IZ5    0                                                
JRNL        AUTH   P.D.MACE,Y.WALLEZ,M.F.EGGER,M.K.DOBACZEWSKA,H.ROBINSON,      
JRNL        AUTH 2 E.B.PASQUALE,S.J.RIEDL                                       
JRNL        TITL   STRUCTURE OF ERK2 BOUND TO PEA-15 REVEALS A MECHANISM FOR    
JRNL        TITL 2 RAPID RELEASE OF ACTIVATED MAPK.                             
JRNL        REF    NAT COMMUN                    V.   4  1681 2013              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   23575685                                                     
JRNL        DOI    10.1038/NCOMMS2687                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0107                                      
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) : 3.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 36572                          
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) : 0.245                           
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1930                            
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) : 3.19                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.27                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2244                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.31                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 117                          
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14061                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 188                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.87000                                              
REMARK   3    B22 (A**2) : -6.18000                                             
REMARK   3    B33 (A**2) : -0.70000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.85000                                             
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): 0.594         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.483         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 62.307        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.885                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.839                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14559 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 19752 ; 1.070 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1711 ; 5.570 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   702 ;35.741 ;24.416       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2578 ;19.302 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;17.135 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2209 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10880 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    11        A   357                          
REMARK   3    RESIDUE RANGE :   A   900        A   904                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4090   4.6720   8.6900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0273 T22:   0.1146                                     
REMARK   3      T33:   0.0474 T12:  -0.0167                                     
REMARK   3      T13:  -0.0043 T23:   0.0703                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9804 L22:   3.3884                                     
REMARK   3      L33:   1.8418 L12:  -1.8124                                     
REMARK   3      L13:  -0.5482 L23:   0.6775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0411 S12:  -0.1344 S13:  -0.1653                       
REMARK   3      S21:   0.0301 S22:   0.1086 S23:   0.1677                       
REMARK   3      S31:  -0.1584 S32:  -0.1037 S33:  -0.0676                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    11        B   357                          
REMARK   3    RESIDUE RANGE :   B   900        B   904                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.1020  23.1970 -17.0050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0953 T22:   0.1800                                     
REMARK   3      T33:   0.1191 T12:   0.0881                                     
REMARK   3      T13:  -0.0639 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6202 L22:   3.9546                                     
REMARK   3      L33:   1.6599 L12:   0.9152                                     
REMARK   3      L13:   0.1777 L23:   0.2512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2128 S12:   0.1628 S13:  -0.0418                       
REMARK   3      S21:  -0.1088 S22:  -0.0142 S23:   0.0197                       
REMARK   3      S31:   0.1563 S32:   0.1277 S33:  -0.1987                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    11        C   357                          
REMARK   3    RESIDUE RANGE :   C   900        C   904                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.4370  75.9880  57.9430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1965 T22:   0.2360                                     
REMARK   3      T33:   0.0725 T12:  -0.0183                                     
REMARK   3      T13:   0.0067 T23:  -0.1143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4409 L22:   2.8904                                     
REMARK   3      L33:   2.5594 L12:  -1.5420                                     
REMARK   3      L13:   0.4005 L23:   0.1752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0320 S12:   0.0900 S13:  -0.0052                       
REMARK   3      S21:   0.1597 S22:  -0.2329 S23:   0.2560                       
REMARK   3      S31:   0.0195 S32:  -0.2000 S33:   0.2009                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    11        D   357                          
REMARK   3    RESIDUE RANGE :   D   900        D   904                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.8900  56.3290  32.6030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1590 T22:   0.1424                                     
REMARK   3      T33:   0.1162 T12:   0.0499                                     
REMARK   3      T13:   0.0997 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1775 L22:   6.2218                                     
REMARK   3      L33:   1.5361 L12:   0.3030                                     
REMARK   3      L13:   0.2989 L23:  -0.7004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1553 S12:   0.1262 S13:  -0.1708                       
REMARK   3      S21:  -0.4241 S22:  -0.0753 S23:  -0.1230                       
REMARK   3      S31:   0.0100 S32:  -0.0541 S33:  -0.0801                       
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     1        E    86                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0290  40.7150  58.4450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2908 T22:   0.2517                                     
REMARK   3      T33:   0.2149 T12:   0.0055                                     
REMARK   3      T13:  -0.0594 T23:   0.1585                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1369 L22:   9.1451                                     
REMARK   3      L33:   5.2230 L12:  -0.5213                                     
REMARK   3      L13:   0.3097 L23:   1.2289                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1634 S12:  -0.3477 S13:  -0.3878                       
REMARK   3      S21:   0.9713 S22:   0.2861 S23:  -0.3906                       
REMARK   3      S31:   0.0358 S32:   0.3187 S33:  -0.1226                       
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     1        F    86                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.5970  96.7260  35.3290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5116 T22:   0.0462                                     
REMARK   3      T33:   0.2393 T12:   0.1195                                     
REMARK   3      T13:  -0.0968 T23:  -0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.0876 L22:   8.8017                                     
REMARK   3      L33:   7.0388 L12:   0.1793                                     
REMARK   3      L13:  -4.8050 L23:  -0.1985                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0212 S12:  -0.0395 S13:   0.7709                       
REMARK   3      S21:  -0.0959 S22:   0.0714 S23:  -0.5285                       
REMARK   3      S31:  -1.1246 S32:  -0.0475 S33:  -0.0926                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     1        G    86                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0000 -17.2500 -12.1090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4498 T22:   0.1637                                     
REMARK   3      T33:   0.2865 T12:   0.0146                                     
REMARK   3      T13:  -0.2362 T23:   0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.7055 L22:   9.7777                                     
REMARK   3      L33:   4.3430 L12:  -0.7971                                     
REMARK   3      L13:   5.3001 L23:   3.5773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4820 S12:   0.0886 S13:  -0.4478                       
REMARK   3      S21:  -0.2863 S22:  -0.3741 S23:   0.6225                       
REMARK   3      S31:   0.3277 S32:  -0.1185 S33:  -0.1079                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H    86                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.7060  40.7450   8.0380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0927 T22:   0.1761                                     
REMARK   3      T33:   0.0516 T12:   0.0058                                     
REMARK   3      T13:   0.0214 T23:  -0.0591                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9731 L22:  10.2955                                     
REMARK   3      L33:   4.7468 L12:  -1.4346                                     
REMARK   3      L13:  -2.2137 L23:  -1.7333                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3358 S12:  -0.1765 S13:   0.0515                       
REMARK   3      S21:   0.7204 S22:   0.4490 S23:   0.2003                       
REMARK   3      S31:   0.2558 S32:  -0.2871 S33:  -0.1133                       
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 USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4IZ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077392.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36572                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS AND 2.0 M AMMONIUM        
REMARK 280  SULFATE, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K    
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       74.56450            
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                                              
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: 3570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     TYR A   358                                                      
REMARK 465     ARG A   359                                                      
REMARK 465     SER A   360                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     TYR B   358                                                      
REMARK 465     ARG B   359                                                      
REMARK 465     SER B   360                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     GLY C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     GLY C    10                                                      
REMARK 465     TYR C   358                                                      
REMARK 465     ARG C   359                                                      
REMARK 465     SER C   360                                                      
REMARK 465     GLY D     5                                                      
REMARK 465     PRO D     6                                                      
REMARK 465     GLY D     7                                                      
REMARK 465     GLY D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     GLY D    10                                                      
REMARK 465     TYR D   358                                                      
REMARK 465     ARG D   359                                                      
REMARK 465     SER D   360                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     SER E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     ILE E    31                                                      
REMARK 465     PRO E    32                                                      
REMARK 465     SER E    33                                                      
REMARK 465     GLU E    34                                                      
REMARK 465     LYS E    35                                                      
REMARK 465     SER E    36                                                      
REMARK 465     LEU E    87                                                      
REMARK 465     LYS E    88                                                      
REMARK 465     ILE E    89                                                      
REMARK 465     SER E    90                                                      
REMARK 465     GLU E    91                                                      
REMARK 465     GLU E    92                                                      
REMARK 465     ASP E    93                                                      
REMARK 465     GLU E    94                                                      
REMARK 465     LEU E    95                                                      
REMARK 465     ASP E    96                                                      
REMARK 465     THR E    97                                                      
REMARK 465     LYS E    98                                                      
REMARK 465     LEU E    99                                                      
REMARK 465     THR E   100                                                      
REMARK 465     ARG E   101                                                      
REMARK 465     ILE E   102                                                      
REMARK 465     PRO E   103                                                      
REMARK 465     SER E   104                                                      
REMARK 465     ALA E   105                                                      
REMARK 465     LYS E   106                                                      
REMARK 465     LYS E   107                                                      
REMARK 465     TYR E   108                                                      
REMARK 465     LYS E   109                                                      
REMARK 465     ASP E   110                                                      
REMARK 465     ILE E   111                                                      
REMARK 465     ILE E   112                                                      
REMARK 465     ARG E   113                                                      
REMARK 465     GLN E   114                                                      
REMARK 465     PRO E   115                                                      
REMARK 465     SER E   116                                                      
REMARK 465     GLU E   117                                                      
REMARK 465     GLU E   118                                                      
REMARK 465     GLU E   119                                                      
REMARK 465     ILE E   120                                                      
REMARK 465     ILE E   121                                                      
REMARK 465     LYS E   128                                                      
REMARK 465     LYS E   129                                                      
REMARK 465     ALA E   130                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     ILE F    31                                                      
REMARK 465     PRO F    32                                                      
REMARK 465     SER F    33                                                      
REMARK 465     GLU F    34                                                      
REMARK 465     LYS F    35                                                      
REMARK 465     SER F    36                                                      
REMARK 465     LEU F    87                                                      
REMARK 465     LYS F    88                                                      
REMARK 465     ILE F    89                                                      
REMARK 465     SER F    90                                                      
REMARK 465     GLU F    91                                                      
REMARK 465     GLU F    92                                                      
REMARK 465     ASP F    93                                                      
REMARK 465     GLU F    94                                                      
REMARK 465     LEU F    95                                                      
REMARK 465     ASP F    96                                                      
REMARK 465     THR F    97                                                      
REMARK 465     LYS F    98                                                      
REMARK 465     LEU F    99                                                      
REMARK 465     THR F   100                                                      
REMARK 465     ARG F   101                                                      
REMARK 465     ILE F   102                                                      
REMARK 465     PRO F   103                                                      
REMARK 465     SER F   104                                                      
REMARK 465     ALA F   105                                                      
REMARK 465     LYS F   106                                                      
REMARK 465     LYS F   107                                                      
REMARK 465     TYR F   108                                                      
REMARK 465     LYS F   109                                                      
REMARK 465     ASP F   110                                                      
REMARK 465     ILE F   111                                                      
REMARK 465     ILE F   112                                                      
REMARK 465     ARG F   113                                                      
REMARK 465     GLN F   114                                                      
REMARK 465     PRO F   115                                                      
REMARK 465     SER F   116                                                      
REMARK 465     GLU F   117                                                      
REMARK 465     GLU F   118                                                      
REMARK 465     GLU F   119                                                      
REMARK 465     ILE F   120                                                      
REMARK 465     ILE F   121                                                      
REMARK 465     LYS F   128                                                      
REMARK 465     LYS F   129                                                      
REMARK 465     ALA F   130                                                      
REMARK 465     GLY G    -2                                                      
REMARK 465     SER G    -1                                                      
REMARK 465     HIS G     0                                                      
REMARK 465     ILE G    31                                                      
REMARK 465     PRO G    32                                                      
REMARK 465     SER G    33                                                      
REMARK 465     GLU G    34                                                      
REMARK 465     LYS G    35                                                      
REMARK 465     SER G    36                                                      
REMARK 465     LEU G    87                                                      
REMARK 465     LYS G    88                                                      
REMARK 465     ILE G    89                                                      
REMARK 465     SER G    90                                                      
REMARK 465     GLU G    91                                                      
REMARK 465     GLU G    92                                                      
REMARK 465     ASP G    93                                                      
REMARK 465     GLU G    94                                                      
REMARK 465     LEU G    95                                                      
REMARK 465     ASP G    96                                                      
REMARK 465     THR G    97                                                      
REMARK 465     LYS G    98                                                      
REMARK 465     LEU G    99                                                      
REMARK 465     THR G   100                                                      
REMARK 465     ARG G   101                                                      
REMARK 465     ILE G   102                                                      
REMARK 465     PRO G   103                                                      
REMARK 465     SER G   104                                                      
REMARK 465     ALA G   105                                                      
REMARK 465     LYS G   106                                                      
REMARK 465     LYS G   107                                                      
REMARK 465     TYR G   108                                                      
REMARK 465     LYS G   109                                                      
REMARK 465     ASP G   110                                                      
REMARK 465     ILE G   111                                                      
REMARK 465     ILE G   112                                                      
REMARK 465     ARG G   113                                                      
REMARK 465     GLN G   114                                                      
REMARK 465     PRO G   115                                                      
REMARK 465     SER G   116                                                      
REMARK 465     GLU G   117                                                      
REMARK 465     GLU G   118                                                      
REMARK 465     GLU G   119                                                      
REMARK 465     ILE G   120                                                      
REMARK 465     ILE G   121                                                      
REMARK 465     LYS G   128                                                      
REMARK 465     LYS G   129                                                      
REMARK 465     ALA G   130                                                      
REMARK 465     GLY H    -2                                                      
REMARK 465     SER H    -1                                                      
REMARK 465     HIS H     0                                                      
REMARK 465     ILE H    31                                                      
REMARK 465     PRO H    32                                                      
REMARK 465     SER H    33                                                      
REMARK 465     GLU H    34                                                      
REMARK 465     LYS H    35                                                      
REMARK 465     SER H    36                                                      
REMARK 465     LEU H    87                                                      
REMARK 465     LYS H    88                                                      
REMARK 465     ILE H    89                                                      
REMARK 465     SER H    90                                                      
REMARK 465     GLU H    91                                                      
REMARK 465     GLU H    92                                                      
REMARK 465     ASP H    93                                                      
REMARK 465     GLU H    94                                                      
REMARK 465     LEU H    95                                                      
REMARK 465     ASP H    96                                                      
REMARK 465     THR H    97                                                      
REMARK 465     LYS H    98                                                      
REMARK 465     LEU H    99                                                      
REMARK 465     THR H   100                                                      
REMARK 465     ARG H   101                                                      
REMARK 465     ILE H   102                                                      
REMARK 465     PRO H   103                                                      
REMARK 465     SER H   104                                                      
REMARK 465     ALA H   105                                                      
REMARK 465     LYS H   106                                                      
REMARK 465     LYS H   107                                                      
REMARK 465     TYR H   108                                                      
REMARK 465     LYS H   109                                                      
REMARK 465     ASP H   110                                                      
REMARK 465     ILE H   111                                                      
REMARK 465     ILE H   112                                                      
REMARK 465     ARG H   113                                                      
REMARK 465     GLN H   114                                                      
REMARK 465     PRO H   115                                                      
REMARK 465     SER H   116                                                      
REMARK 465     GLU H   117                                                      
REMARK 465     GLU H   118                                                      
REMARK 465     GLU H   119                                                      
REMARK 465     ILE H   120                                                      
REMARK 465     ILE H   121                                                      
REMARK 465     LYS H   122                                                      
REMARK 465     LEU H   123                                                      
REMARK 465     ALA H   124                                                      
REMARK 465     PRO H   125                                                      
REMARK 465     PRO H   126                                                      
REMARK 465     PRO H   127                                                      
REMARK 465     LYS H   128                                                      
REMARK 465     LYS H   129                                                      
REMARK 465     ALA H   130                                                      
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     GLU B 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 330    CG   CD   CE   NZ                                   
REMARK 470     GLU D 326    CG   CD   OE1  OE2                                  
REMARK 470     ARG E  85    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG F  85    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G  85    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG H  85    CG   CD   NE   CZ   NH1  NH2                        
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 A 157   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    LEU B 157   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    LEU C 157   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    LEU D 157   CA  -  CB  -  CG  ANGL. DEV. =  15.0 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    VAL A  21       31.51    -97.25                                   
REMARK 500    SER A  57     -133.30   -115.94                                   
REMARK 500    PRO A  58      119.83    -33.11                                   
REMARK 500    PHE A  59       41.69    -95.25                                   
REMARK 500    ARG A 148       -6.05     76.22                                   
REMARK 500    ASP A 167       96.87     61.68                                   
REMARK 500    ALA A 174      106.33    -59.41                                   
REMARK 500    SER A 202      -14.44     89.90                                   
REMARK 500    ASN A 224      -24.54     64.26                                   
REMARK 500    PRO A 229       42.13    -86.37                                   
REMARK 500    LEU A 294       51.51   -108.67                                   
REMARK 500    ALA A 327       67.95   -111.49                                   
REMARK 500    ASP A 332       96.64     62.88                                   
REMARK 500    GLU A 334      -33.78     79.08                                   
REMARK 500    LEU A 335       64.76     25.72                                   
REMARK 500    ASP A 336     -141.15    -76.15                                   
REMARK 500    PRO A 356      -27.01    -37.32                                   
REMARK 500    VAL B  21       31.46    -95.39                                   
REMARK 500    SER B  57     -131.49   -115.99                                   
REMARK 500    PRO B  58      118.88    -33.86                                   
REMARK 500    PHE B  59       41.32    -94.28                                   
REMARK 500    ARG B 148       -4.59     74.21                                   
REMARK 500    ASP B 167       96.88     63.18                                   
REMARK 500    ALA B 174      106.13    -59.70                                   
REMARK 500    SER B 202      -13.98     89.25                                   
REMARK 500    ASN B 224      -24.25     63.51                                   
REMARK 500    PRO B 229       41.38    -85.32                                   
REMARK 500    LEU B 294       51.28   -107.91                                   
REMARK 500    ALA B 327       68.53   -111.00                                   
REMARK 500    ASP B 332       95.89     63.31                                   
REMARK 500    GLU B 334      -33.57     80.25                                   
REMARK 500    LEU B 335       64.63     25.02                                   
REMARK 500    ASP B 336     -139.56    -75.25                                   
REMARK 500    PRO B 356      -27.98    -36.57                                   
REMARK 500    VAL C  21       31.47    -97.41                                   
REMARK 500    SER C  57     -131.62   -115.03                                   
REMARK 500    PRO C  58      119.32    -33.83                                   
REMARK 500    PHE C  59       41.22    -94.42                                   
REMARK 500    ARG C 148       -6.00     75.48                                   
REMARK 500    ASP C 167       96.83     62.04                                   
REMARK 500    ALA C 174      106.10    -58.60                                   
REMARK 500    SER C 202      -15.06     90.34                                   
REMARK 500    ASN C 224      -23.83     64.49                                   
REMARK 500    PRO C 229       40.90    -85.91                                   
REMARK 500    LEU C 294       50.52   -108.65                                   
REMARK 500    ALA C 327       67.55   -111.70                                   
REMARK 500    ASP C 332       95.74     63.27                                   
REMARK 500    GLU C 334      -33.69     79.36                                   
REMARK 500    LEU C 335       64.87     24.63                                   
REMARK 500    ASP C 336     -140.49    -74.94                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      85 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER A   57     PRO A   58                 -148.34                    
REMARK 500 SER C   57     PRO C   58                 -149.63                    
REMARK 500 SER D   57     PRO D   58                 -149.04                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 904                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IZ7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IZA   RELATED DB: PDB                                   
DBREF  4IZ5 A    8   360  UNP    P28482   MK01_HUMAN       8    360             
DBREF  4IZ5 B    8   360  UNP    P28482   MK01_HUMAN       8    360             
DBREF  4IZ5 C    8   360  UNP    P28482   MK01_HUMAN       8    360             
DBREF  4IZ5 D    8   360  UNP    P28482   MK01_HUMAN       8    360             
DBREF  4IZ5 E    1   130  UNP    Q15121   PEA15_HUMAN      1    130             
DBREF  4IZ5 F    1   130  UNP    Q15121   PEA15_HUMAN      1    130             
DBREF  4IZ5 G    1   130  UNP    Q15121   PEA15_HUMAN      1    130             
DBREF  4IZ5 H    1   130  UNP    Q15121   PEA15_HUMAN      1    130             
SEQADV 4IZ5 GLY A    5  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 PRO A    6  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 GLY A    7  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 GLU A  185  UNP  P28482    THR   185 ENGINEERED MUTATION            
SEQADV 4IZ5 GLY B    5  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 PRO B    6  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 GLY B    7  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 GLU B  185  UNP  P28482    THR   185 ENGINEERED MUTATION            
SEQADV 4IZ5 GLY C    5  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 PRO C    6  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 GLY C    7  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 GLU C  185  UNP  P28482    THR   185 ENGINEERED MUTATION            
SEQADV 4IZ5 GLY D    5  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 PRO D    6  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 GLY D    7  UNP  P28482              EXPRESSION TAG                 
SEQADV 4IZ5 GLU D  185  UNP  P28482    THR   185 ENGINEERED MUTATION            
SEQADV 4IZ5 GLY E   -2  UNP  Q15121              EXPRESSION TAG                 
SEQADV 4IZ5 SER E   -1  UNP  Q15121              EXPRESSION TAG                 
SEQADV 4IZ5 HIS E    0  UNP  Q15121              EXPRESSION TAG                 
SEQADV 4IZ5 GLY F   -2  UNP  Q15121              EXPRESSION TAG                 
SEQADV 4IZ5 SER F   -1  UNP  Q15121              EXPRESSION TAG                 
SEQADV 4IZ5 HIS F    0  UNP  Q15121              EXPRESSION TAG                 
SEQADV 4IZ5 GLY G   -2  UNP  Q15121              EXPRESSION TAG                 
SEQADV 4IZ5 SER G   -1  UNP  Q15121              EXPRESSION TAG                 
SEQADV 4IZ5 HIS G    0  UNP  Q15121              EXPRESSION TAG                 
SEQADV 4IZ5 GLY H   -2  UNP  Q15121              EXPRESSION TAG                 
SEQADV 4IZ5 SER H   -1  UNP  Q15121              EXPRESSION TAG                 
SEQADV 4IZ5 HIS H    0  UNP  Q15121              EXPRESSION TAG                 
SEQRES   1 A  356  GLY PRO GLY GLY ALA GLY PRO GLU MET VAL ARG GLY GLN          
SEQRES   2 A  356  VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU SER TYR          
SEQRES   3 A  356  ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER ALA TYR          
SEQRES   4 A  356  ASP ASN VAL ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE          
SEQRES   5 A  356  SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU          
SEQRES   6 A  356  ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN          
SEQRES   7 A  356  ILE ILE GLY ILE ASN ASP ILE ILE ARG ALA PRO THR ILE          
SEQRES   8 A  356  GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP LEU MET          
SEQRES   9 A  356  GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN HIS LEU          
SEQRES  10 A  356  SER ASN ASP HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU          
SEQRES  11 A  356  ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS          
SEQRES  12 A  356  ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN THR THR          
SEQRES  13 A  356  CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL          
SEQRES  14 A  356  ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU GLU GLU          
SEQRES  15 A  356  TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET          
SEQRES  16 A  356  LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP          
SEQRES  17 A  356  SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG          
SEQRES  18 A  356  PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN          
SEQRES  19 A  356  HIS ILE LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP          
SEQRES  20 A  356  LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU          
SEQRES  21 A  356  LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG          
SEQRES  22 A  356  LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP LEU LEU          
SEQRES  23 A  356  ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG ILE GLU          
SEQRES  24 A  356  VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR          
SEQRES  25 A  356  TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA PRO PHE          
SEQRES  26 A  356  LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS GLU LYS          
SEQRES  27 A  356  LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG PHE GLN          
SEQRES  28 A  356  PRO GLY TYR ARG SER                                          
SEQRES   1 B  356  GLY PRO GLY GLY ALA GLY PRO GLU MET VAL ARG GLY GLN          
SEQRES   2 B  356  VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU SER TYR          
SEQRES   3 B  356  ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER ALA TYR          
SEQRES   4 B  356  ASP ASN VAL ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE          
SEQRES   5 B  356  SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU          
SEQRES   6 B  356  ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN          
SEQRES   7 B  356  ILE ILE GLY ILE ASN ASP ILE ILE ARG ALA PRO THR ILE          
SEQRES   8 B  356  GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP LEU MET          
SEQRES   9 B  356  GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN HIS LEU          
SEQRES  10 B  356  SER ASN ASP HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU          
SEQRES  11 B  356  ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS          
SEQRES  12 B  356  ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN THR THR          
SEQRES  13 B  356  CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL          
SEQRES  14 B  356  ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU GLU GLU          
SEQRES  15 B  356  TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET          
SEQRES  16 B  356  LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP          
SEQRES  17 B  356  SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG          
SEQRES  18 B  356  PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN          
SEQRES  19 B  356  HIS ILE LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP          
SEQRES  20 B  356  LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU          
SEQRES  21 B  356  LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG          
SEQRES  22 B  356  LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP LEU LEU          
SEQRES  23 B  356  ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG ILE GLU          
SEQRES  24 B  356  VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR          
SEQRES  25 B  356  TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA PRO PHE          
SEQRES  26 B  356  LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS GLU LYS          
SEQRES  27 B  356  LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG PHE GLN          
SEQRES  28 B  356  PRO GLY TYR ARG SER                                          
SEQRES   1 C  356  GLY PRO GLY GLY ALA GLY PRO GLU MET VAL ARG GLY GLN          
SEQRES   2 C  356  VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU SER TYR          
SEQRES   3 C  356  ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER ALA TYR          
SEQRES   4 C  356  ASP ASN VAL ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE          
SEQRES   5 C  356  SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU          
SEQRES   6 C  356  ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN          
SEQRES   7 C  356  ILE ILE GLY ILE ASN ASP ILE ILE ARG ALA PRO THR ILE          
SEQRES   8 C  356  GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP LEU MET          
SEQRES   9 C  356  GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN HIS LEU          
SEQRES  10 C  356  SER ASN ASP HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU          
SEQRES  11 C  356  ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS          
SEQRES  12 C  356  ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN THR THR          
SEQRES  13 C  356  CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL          
SEQRES  14 C  356  ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU GLU GLU          
SEQRES  15 C  356  TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET          
SEQRES  16 C  356  LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP          
SEQRES  17 C  356  SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG          
SEQRES  18 C  356  PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN          
SEQRES  19 C  356  HIS ILE LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP          
SEQRES  20 C  356  LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU          
SEQRES  21 C  356  LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG          
SEQRES  22 C  356  LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP LEU LEU          
SEQRES  23 C  356  ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG ILE GLU          
SEQRES  24 C  356  VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR          
SEQRES  25 C  356  TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA PRO PHE          
SEQRES  26 C  356  LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS GLU LYS          
SEQRES  27 C  356  LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG PHE GLN          
SEQRES  28 C  356  PRO GLY TYR ARG SER                                          
SEQRES   1 D  356  GLY PRO GLY GLY ALA GLY PRO GLU MET VAL ARG GLY GLN          
SEQRES   2 D  356  VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU SER TYR          
SEQRES   3 D  356  ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER ALA TYR          
SEQRES   4 D  356  ASP ASN VAL ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE          
SEQRES   5 D  356  SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU          
SEQRES   6 D  356  ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN          
SEQRES   7 D  356  ILE ILE GLY ILE ASN ASP ILE ILE ARG ALA PRO THR ILE          
SEQRES   8 D  356  GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP LEU MET          
SEQRES   9 D  356  GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN HIS LEU          
SEQRES  10 D  356  SER ASN ASP HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU          
SEQRES  11 D  356  ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS          
SEQRES  12 D  356  ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN THR THR          
SEQRES  13 D  356  CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL          
SEQRES  14 D  356  ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU GLU GLU          
SEQRES  15 D  356  TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET          
SEQRES  16 D  356  LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP          
SEQRES  17 D  356  SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG          
SEQRES  18 D  356  PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN          
SEQRES  19 D  356  HIS ILE LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP          
SEQRES  20 D  356  LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU          
SEQRES  21 D  356  LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG          
SEQRES  22 D  356  LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP LEU LEU          
SEQRES  23 D  356  ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG ILE GLU          
SEQRES  24 D  356  VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR          
SEQRES  25 D  356  TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA PRO PHE          
SEQRES  26 D  356  LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS GLU LYS          
SEQRES  27 D  356  LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG PHE GLN          
SEQRES  28 D  356  PRO GLY TYR ARG SER                                          
SEQRES   1 E  133  GLY SER HIS MET ALA GLU TYR GLY THR LEU LEU GLN ASP          
SEQRES   2 E  133  LEU THR ASN ASN ILE THR LEU GLU ASP LEU GLU GLN LEU          
SEQRES   3 E  133  LYS SER ALA CYS LYS GLU ASP ILE PRO SER GLU LYS SER          
SEQRES   4 E  133  GLU GLU ILE THR THR GLY SER ALA TRP PHE SER PHE LEU          
SEQRES   5 E  133  GLU SER HIS ASN LYS LEU ASP LYS ASP ASN LEU SER TYR          
SEQRES   6 E  133  ILE GLU HIS ILE PHE GLU ILE SER ARG ARG PRO ASP LEU          
SEQRES   7 E  133  LEU THR MET VAL VAL ASP TYR ARG THR ARG VAL LEU LYS          
SEQRES   8 E  133  ILE SER GLU GLU ASP GLU LEU ASP THR LYS LEU THR ARG          
SEQRES   9 E  133  ILE PRO SER ALA LYS LYS TYR LYS ASP ILE ILE ARG GLN          
SEQRES  10 E  133  PRO SER GLU GLU GLU ILE ILE LYS LEU ALA PRO PRO PRO          
SEQRES  11 E  133  LYS LYS ALA                                                  
SEQRES   1 F  133  GLY SER HIS MET ALA GLU TYR GLY THR LEU LEU GLN ASP          
SEQRES   2 F  133  LEU THR ASN ASN ILE THR LEU GLU ASP LEU GLU GLN LEU          
SEQRES   3 F  133  LYS SER ALA CYS LYS GLU ASP ILE PRO SER GLU LYS SER          
SEQRES   4 F  133  GLU GLU ILE THR THR GLY SER ALA TRP PHE SER PHE LEU          
SEQRES   5 F  133  GLU SER HIS ASN LYS LEU ASP LYS ASP ASN LEU SER TYR          
SEQRES   6 F  133  ILE GLU HIS ILE PHE GLU ILE SER ARG ARG PRO ASP LEU          
SEQRES   7 F  133  LEU THR MET VAL VAL ASP TYR ARG THR ARG VAL LEU LYS          
SEQRES   8 F  133  ILE SER GLU GLU ASP GLU LEU ASP THR LYS LEU THR ARG          
SEQRES   9 F  133  ILE PRO SER ALA LYS LYS TYR LYS ASP ILE ILE ARG GLN          
SEQRES  10 F  133  PRO SER GLU GLU GLU ILE ILE LYS LEU ALA PRO PRO PRO          
SEQRES  11 F  133  LYS LYS ALA                                                  
SEQRES   1 G  133  GLY SER HIS MET ALA GLU TYR GLY THR LEU LEU GLN ASP          
SEQRES   2 G  133  LEU THR ASN ASN ILE THR LEU GLU ASP LEU GLU GLN LEU          
SEQRES   3 G  133  LYS SER ALA CYS LYS GLU ASP ILE PRO SER GLU LYS SER          
SEQRES   4 G  133  GLU GLU ILE THR THR GLY SER ALA TRP PHE SER PHE LEU          
SEQRES   5 G  133  GLU SER HIS ASN LYS LEU ASP LYS ASP ASN LEU SER TYR          
SEQRES   6 G  133  ILE GLU HIS ILE PHE GLU ILE SER ARG ARG PRO ASP LEU          
SEQRES   7 G  133  LEU THR MET VAL VAL ASP TYR ARG THR ARG VAL LEU LYS          
SEQRES   8 G  133  ILE SER GLU GLU ASP GLU LEU ASP THR LYS LEU THR ARG          
SEQRES   9 G  133  ILE PRO SER ALA LYS LYS TYR LYS ASP ILE ILE ARG GLN          
SEQRES  10 G  133  PRO SER GLU GLU GLU ILE ILE LYS LEU ALA PRO PRO PRO          
SEQRES  11 G  133  LYS LYS ALA                                                  
SEQRES   1 H  133  GLY SER HIS MET ALA GLU TYR GLY THR LEU LEU GLN ASP          
SEQRES   2 H  133  LEU THR ASN ASN ILE THR LEU GLU ASP LEU GLU GLN LEU          
SEQRES   3 H  133  LYS SER ALA CYS LYS GLU ASP ILE PRO SER GLU LYS SER          
SEQRES   4 H  133  GLU GLU ILE THR THR GLY SER ALA TRP PHE SER PHE LEU          
SEQRES   5 H  133  GLU SER HIS ASN LYS LEU ASP LYS ASP ASN LEU SER TYR          
SEQRES   6 H  133  ILE GLU HIS ILE PHE GLU ILE SER ARG ARG PRO ASP LEU          
SEQRES   7 H  133  LEU THR MET VAL VAL ASP TYR ARG THR ARG VAL LEU LYS          
SEQRES   8 H  133  ILE SER GLU GLU ASP GLU LEU ASP THR LYS LEU THR ARG          
SEQRES   9 H  133  ILE PRO SER ALA LYS LYS TYR LYS ASP ILE ILE ARG GLN          
SEQRES  10 H  133  PRO SER GLU GLU GLU ILE ILE LYS LEU ALA PRO PRO PRO          
SEQRES  11 H  133  LYS LYS ALA                                                  
HET    ADP  A 900      27                                                       
HET    SO4  A 901       5                                                       
HET    SO4  A 902       5                                                       
HET    SO4  A 903       5                                                       
HET    SO4  A 904       5                                                       
HET    ADP  B 900      27                                                       
HET    SO4  B 901       5                                                       
HET    SO4  B 902       5                                                       
HET    SO4  B 903       5                                                       
HET    SO4  B 904       5                                                       
HET    ADP  C 900      27                                                       
HET    SO4  C 901       5                                                       
HET    SO4  C 902       5                                                       
HET    SO4  C 903       5                                                       
HET    SO4  C 904       5                                                       
HET    ADP  D 900      27                                                       
HET    SO4  D 901       5                                                       
HET    SO4  D 902       5                                                       
HET    SO4  D 903       5                                                       
HET    SO4  D 904       5                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   9  ADP    4(C10 H15 N5 O10 P2)                                         
FORMUL  10  SO4    16(O4 S 2-)                                                  
HELIX    1   1 HIS A   61  ARG A   77  1                                  17    
HELIX    2   2 LEU A  112  GLN A  119  1                                   8    
HELIX    3   3 SER A  122  ALA A  143  1                                  22    
HELIX    4   4 LYS A  151  SER A  153  5                                   3    
HELIX    5   5 GLY A  182  VAL A  188  1                                   7    
HELIX    6   6 ALA A  195  ASN A  201  1                                   7    
HELIX    7   7 LYS A  207  ASN A  224  1                                  18    
HELIX    8   8 HIS A  232  GLY A  245  1                                  14    
HELIX    9   9 ASP A  251  ILE A  255  5                                   5    
HELIX   10  10 ASN A  257  LEU A  267  1                                  11    
HELIX   11  11 PRO A  274  PHE A  279  1                                   6    
HELIX   12  12 ASP A  283  LEU A  294  1                                  12    
HELIX   13  13 GLU A  303  ALA A  309  1                                   7    
HELIX   14  14 HIS A  310  GLU A  314  5                                   5    
HELIX   15  15 ASP A  318  GLU A  322  5                                   5    
HELIX   16  16 PRO A  339  THR A  351  1                                  13    
HELIX   17  17 ALA A  352  GLN A  355  5                                   4    
HELIX   18  18 HIS B   61  ARG B   77  1                                  17    
HELIX   19  19 LEU B  112  GLN B  119  1                                   8    
HELIX   20  20 SER B  122  ALA B  143  1                                  22    
HELIX   21  21 LYS B  151  SER B  153  5                                   3    
HELIX   22  22 GLY B  182  VAL B  188  1                                   7    
HELIX   23  23 ALA B  195  ASN B  201  1                                   7    
HELIX   24  24 LYS B  207  ASN B  224  1                                  18    
HELIX   25  25 HIS B  232  GLY B  245  1                                  14    
HELIX   26  26 ASP B  251  ILE B  255  5                                   5    
HELIX   27  27 ASN B  257  LEU B  267  1                                  11    
HELIX   28  28 PRO B  274  PHE B  279  1                                   6    
HELIX   29  29 ASP B  283  LEU B  294  1                                  12    
HELIX   30  30 GLU B  303  ALA B  309  1                                   7    
HELIX   31  31 HIS B  310  GLU B  314  5                                   5    
HELIX   32  32 ASP B  318  GLU B  322  5                                   5    
HELIX   33  33 PRO B  339  THR B  351  1                                  13    
HELIX   34  34 ALA B  352  GLN B  355  5                                   4    
HELIX   35  35 HIS C   61  ARG C   77  1                                  17    
HELIX   36  36 LEU C  112  LYS C  117  1                                   6    
HELIX   37  37 SER C  122  ALA C  143  1                                  22    
HELIX   38  38 LYS C  151  SER C  153  5                                   3    
HELIX   39  39 GLY C  182  VAL C  188  1                                   7    
HELIX   40  40 ALA C  195  ASN C  201  1                                   7    
HELIX   41  41 LYS C  207  ASN C  224  1                                  18    
HELIX   42  42 HIS C  232  GLY C  245  1                                  14    
HELIX   43  43 ASP C  251  ILE C  255  5                                   5    
HELIX   44  44 ASN C  257  LEU C  267  1                                  11    
HELIX   45  45 PRO C  274  PHE C  279  1                                   6    
HELIX   46  46 ASP C  283  LEU C  294  1                                  12    
HELIX   47  47 GLU C  303  ALA C  309  1                                   7    
HELIX   48  48 HIS C  310  GLU C  314  5                                   5    
HELIX   49  49 ASP C  318  GLU C  322  5                                   5    
HELIX   50  50 PRO C  339  THR C  351  1                                  13    
HELIX   51  51 ALA C  352  GLN C  355  5                                   4    
HELIX   52  52 HIS D   61  ARG D   77  1                                  17    
HELIX   53  53 LEU D  112  LYS D  117  1                                   6    
HELIX   54  54 SER D  122  ALA D  143  1                                  22    
HELIX   55  55 LYS D  151  SER D  153  5                                   3    
HELIX   56  56 GLY D  182  VAL D  188  1                                   7    
HELIX   57  57 ALA D  195  ASN D  201  1                                   7    
HELIX   58  58 LYS D  207  ASN D  224  1                                  18    
HELIX   59  59 HIS D  232  GLY D  245  1                                  14    
HELIX   60  60 ASP D  251  ILE D  255  5                                   5    
HELIX   61  61 ASN D  257  LEU D  267  1                                  11    
HELIX   62  62 PRO D  274  PHE D  279  1                                   6    
HELIX   63  63 ASP D  283  LEU D  294  1                                  12    
HELIX   64  64 GLU D  303  ALA D  309  1                                   7    
HELIX   65  65 HIS D  310  GLU D  314  5                                   5    
HELIX   66  66 ASP D  318  GLU D  322  5                                   5    
HELIX   67  67 PRO D  339  THR D  351  1                                  13    
HELIX   68  68 ALA D  352  GLN D  355  5                                   4    
HELIX   69  69 ALA E    2  ASN E   13  1                                  12    
HELIX   70  70 THR E   16  CYS E   27  1                                  12    
HELIX   71  71 GLY E   42  SER E   51  1                                  10    
HELIX   72  72 LEU E   60  SER E   70  1                                  11    
HELIX   73  73 ARG E   72  ARG E   85  1                                  14    
HELIX   74  74 ALA F    2  ASN F   13  1                                  12    
HELIX   75  75 THR F   16  CYS F   27  1                                  12    
HELIX   76  76 GLY F   42  SER F   51  1                                  10    
HELIX   77  77 LEU F   60  SER F   70  1                                  11    
HELIX   78  78 ARG F   72  ARG F   85  1                                  14    
HELIX   79  79 ALA G    2  ASN G   13  1                                  12    
HELIX   80  80 THR G   16  CYS G   27  1                                  12    
HELIX   81  81 GLY G   42  SER G   51  1                                  10    
HELIX   82  82 LEU G   60  SER G   70  1                                  11    
HELIX   83  83 ARG G   72  ARG G   85  1                                  14    
HELIX   84  84 ALA H    2  ASN H   13  1                                  12    
HELIX   85  85 THR H   16  CYS H   27  1                                  12    
HELIX   86  86 GLY H   42  SER H   51  1                                  10    
HELIX   87  87 LEU H   60  SER H   70  1                                  11    
HELIX   88  88 ARG H   72  ARG H   85  1                                  14    
SHEET    1   A 2 MET A  13  VAL A  14  0                                        
SHEET    2   A 2 GLN A  17  VAL A  18 -1  O  GLN A  17   N  VAL A  14           
SHEET    1   B 5 TYR A  25  GLU A  33  0                                        
SHEET    2   B 5 MET A  38  ASP A  44 -1  O  TYR A  43   N  THR A  26           
SHEET    3   B 5 VAL A  49  ILE A  56 -1  O  ILE A  53   N  CYS A  40           
SHEET    4   B 5 VAL A 101  ASP A 106 -1  O  VAL A 101   N  ILE A  56           
SHEET    5   B 5 ILE A  86  ILE A  90 -1  N  ASN A  87   O  VAL A 104           
SHEET    1   C 3 THR A 110  ASP A 111  0                                        
SHEET    2   C 3 LEU A 155  ASN A 158 -1  O  LEU A 157   N  THR A 110           
SHEET    3   C 3 ASP A 162  ILE A 165 -1  O  LYS A 164   N  LEU A 156           
SHEET    1   D 2 VAL A 145  LEU A 146  0                                        
SHEET    2   D 2 ARG A 172  VAL A 173 -1  O  ARG A 172   N  LEU A 146           
SHEET    1   E 5 TYR B  25  GLU B  33  0                                        
SHEET    2   E 5 MET B  38  ASP B  44 -1  O  TYR B  43   N  THR B  26           
SHEET    3   E 5 VAL B  49  ILE B  56 -1  O  ILE B  53   N  CYS B  40           
SHEET    4   E 5 VAL B 101  ASP B 106 -1  O  VAL B 101   N  ILE B  56           
SHEET    5   E 5 ILE B  86  ILE B  90 -1  N  ASN B  87   O  VAL B 104           
SHEET    1   F 3 THR B 110  ASP B 111  0                                        
SHEET    2   F 3 LEU B 155  LEU B 157 -1  O  LEU B 157   N  THR B 110           
SHEET    3   F 3 LEU B 163  ILE B 165 -1  O  LYS B 164   N  LEU B 156           
SHEET    1   G 2 VAL B 145  LEU B 146  0                                        
SHEET    2   G 2 ARG B 172  VAL B 173 -1  O  ARG B 172   N  LEU B 146           
SHEET    1   H 2 MET C  13  VAL C  14  0                                        
SHEET    2   H 2 GLN C  17  VAL C  18 -1  O  GLN C  17   N  VAL C  14           
SHEET    1   I 5 TYR C  25  GLU C  33  0                                        
SHEET    2   I 5 MET C  38  ASP C  44 -1  O  TYR C  43   N  THR C  26           
SHEET    3   I 5 VAL C  49  ILE C  56 -1  O  VAL C  51   N  ALA C  42           
SHEET    4   I 5 VAL C 101  ASP C 106 -1  O  VAL C 101   N  ILE C  56           
SHEET    5   I 5 ILE C  86  ILE C  90 -1  N  ASN C  87   O  VAL C 104           
SHEET    1   J 3 THR C 110  ASP C 111  0                                        
SHEET    2   J 3 LEU C 155  ASN C 158 -1  O  LEU C 157   N  THR C 110           
SHEET    3   J 3 ASP C 162  ILE C 165 -1  O  LYS C 164   N  LEU C 156           
SHEET    1   K 2 VAL C 145  LEU C 146  0                                        
SHEET    2   K 2 ARG C 172  VAL C 173 -1  O  ARG C 172   N  LEU C 146           
SHEET    1   L 2 MET D  13  VAL D  14  0                                        
SHEET    2   L 2 GLN D  17  VAL D  18 -1  O  GLN D  17   N  VAL D  14           
SHEET    1   M 5 TYR D  25  GLU D  33  0                                        
SHEET    2   M 5 MET D  38  ASP D  44 -1  O  TYR D  43   N  THR D  26           
SHEET    3   M 5 VAL D  49  ILE D  56 -1  O  VAL D  51   N  ALA D  42           
SHEET    4   M 5 VAL D 101  ASP D 106 -1  O  VAL D 101   N  ILE D  56           
SHEET    5   M 5 ILE D  86  ILE D  90 -1  N  ASN D  87   O  VAL D 104           
SHEET    1   N 3 THR D 110  ASP D 111  0                                        
SHEET    2   N 3 LEU D 155  LEU D 157 -1  O  LEU D 157   N  THR D 110           
SHEET    3   N 3 LEU D 163  ILE D 165 -1  O  LYS D 164   N  LEU D 156           
SHEET    1   O 2 VAL D 145  LEU D 146  0                                        
SHEET    2   O 2 ARG D 172  VAL D 173 -1  O  ARG D 172   N  LEU D 146           
SITE     1 AC1 11 GLY A  34  ALA A  35  VAL A  39  ALA A  52                    
SITE     2 AC1 11 LYS A  54  ASP A 106  LEU A 107  MET A 108                    
SITE     3 AC1 11 ASP A 111  LYS A 114  LEU A 156                               
SITE     1 AC2  7 ARG A  70  ARG A 172  VAL A 173  MET A 333                    
SITE     2 AC2  7 GLU A 334  LEU A 335  ASP A 336                               
SITE     1 AC3  8 ARG A 148  ARG A 172  HIS A 178  HIS A 180                    
SITE     2 AC3  8 THR A 181  GLY A 182  PHE A 183  LEU A 184                    
SITE     1 AC4  4 VAL A 188  ALA A 189  THR A 190  ARG B  15                    
SITE     1 AC5  3 ARG A 191  LYS A 231  HIS A 232                               
SITE     1 AC6 11 GLY B  34  ALA B  35  VAL B  39  ALA B  52                    
SITE     2 AC6 11 LYS B  54  GLN B 105  ASP B 106  MET B 108                    
SITE     3 AC6 11 ASP B 111  LYS B 114  LEU B 156                               
SITE     1 AC7  7 ARG B  70  ARG B 172  VAL B 173  MET B 333                    
SITE     2 AC7  7 GLU B 334  LEU B 335  ASP B 336                               
SITE     1 AC8  8 ARG B 148  ARG B 172  HIS B 178  HIS B 180                    
SITE     2 AC8  8 THR B 181  GLY B 182  PHE B 183  LEU B 184                    
SITE     1 AC9  4 ARG A  15  VAL B 188  ALA B 189  THR B 190                    
SITE     1 BC1  2 ARG B 191  HIS B 232                                          
SITE     1 BC2 12 GLY C  34  ALA C  35  VAL C  39  ALA C  52                    
SITE     2 BC2 12 LYS C  54  GLN C 105  ASP C 106  MET C 108                    
SITE     3 BC2 12 ASP C 111  LYS C 114  SER C 153  LEU C 156                    
SITE     1 BC3  7 ARG C  70  ARG C 172  VAL C 173  MET C 333                    
SITE     2 BC3  7 GLU C 334  LEU C 335  ASP C 336                               
SITE     1 BC4  8 ARG C 148  ARG C 172  HIS C 178  HIS C 180                    
SITE     2 BC4  8 THR C 181  GLY C 182  PHE C 183  LEU C 184                    
SITE     1 BC5  5 TYR C 187  VAL C 188  ALA C 189  THR C 190                    
SITE     2 BC5  5 ARG D  15                                                     
SITE     1 BC6  3 ARG C 191  LYS C 231  HIS C 232                               
SITE     1 BC7 12 GLY D  34  ALA D  35  VAL D  39  ALA D  52                    
SITE     2 BC7 12 LYS D  54  GLN D 105  ASP D 106  LEU D 107                    
SITE     3 BC7 12 MET D 108  ASP D 111  LYS D 114  SER D 153                    
SITE     1 BC8  7 ARG D  70  ARG D 172  VAL D 173  MET D 333                    
SITE     2 BC8  7 GLU D 334  LEU D 335  ASP D 336                               
SITE     1 BC9  8 ARG D 148  ARG D 172  HIS D 178  HIS D 180                    
SITE     2 BC9  8 THR D 181  GLY D 182  PHE D 183  LEU D 184                    
SITE     1 CC1  4 ARG C  15  VAL D 188  ALA D 189  THR D 190                    
SITE     1 CC2  2 ARG D 191  HIS D 232                                          
CRYST1   80.801  149.129   98.869  90.00  90.41  90.00 P 1 21 1      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      0.012376  0.000000  0.000088        0.00000                         
SCALE2      0.000000  0.006706  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010115        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.667906  0.514880 -0.537401      -10.92135    1                    
MTRIX2   2  0.530014 -0.835977 -0.142219       28.61932    1                    
MTRIX3   2 -0.522481 -0.189841 -0.831248       -7.94119    1                    
MTRIX1   3 -0.997086 -0.050848  0.056866      -40.33215    1                    
MTRIX2   3  0.053678 -0.997336  0.049398       79.88192    1                    
MTRIX3   3  0.054203  0.052306  0.997159      -50.76248    1                    
MTRIX1   4 -0.663440 -0.582288 -0.469881       30.36577    1                    
MTRIX2   4 -0.574483  0.798767 -0.178720      -51.08615    1                    
MTRIX3   4  0.479392  0.151369 -0.864448       42.16953    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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