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Database: PDB
Entry: 5D03
LinkDB: 5D03
Original site: 5D03 
HEADER    TRANSFERASE                             02-AUG-15   5D03              
TITLE     NEISSERIA MENINGITIDIS 3 DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE    
TITLE    2 SYNTHASE VAL223ALA VARIANT                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE;               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: 3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE SYNTHASE,DAHP   
COMPND   5 SYNTHASE,PHOSPHO-2-KETO-3-DEOXYHEPTONATE ALDOLASE;                   
COMPND   6 EC: 2.5.1.54;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS SEROGROUP B (STRAIN      
SOURCE   3 MC58);                                                               
SOURCE   4 ORGANISM_TAXID: 122586;                                              
SOURCE   5 STRAIN: MC58;                                                        
SOURCE   6 GENE: AROG, NMB0307;                                                 
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: BL21*;                                  
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7-7                                     
KEYWDS    DAH7PS, ALLOSTERY, TRANSFERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.C.HEYES,E.J.PARKER                                                  
REVDAT   2   01-NOV-17 5D03    1       HEADER REMARK                            
REVDAT   1   10-AUG-16 5D03    0                                                
JRNL        AUTH   L.C.HEYES,E.J.PARKER                                         
JRNL        TITL   NEISSERIA MENINGITIDIS 3 DEOXY-D-ARABINO-HEPTULOSONATE       
JRNL        TITL 2 7-PHOSPHATE SYNTHASE VAL223ALA VARIANT AT 1.84 ANGSTROMS     
JRNL        TITL 3 RESOLUTION                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.84 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 75.53                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 118952                         
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7865                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.84                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.89                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8825                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 564                          
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10086                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 733                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.18000                                             
REMARK   3    B22 (A**2) : 0.42000                                              
REMARK   3    B33 (A**2) : -0.30000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.29000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.116         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.112         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.093         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.197         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10375 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9869 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14066 ; 1.525 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22637 ; 0.818 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1337 ; 5.316 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   450 ;34.792 ;23.822       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1713 ;12.391 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    73 ;16.910 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1582 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11900 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2337 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5348 ; 1.299 ; 2.063       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5347 ; 1.297 ; 2.063       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6685 ; 1.834 ; 3.086       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  6686 ; 1.834 ; 3.086       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5027 ; 2.077 ; 2.332       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5027 ; 2.077 ; 2.332       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  7382 ; 3.140 ; 3.401       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 12223 ; 5.298 ;17.702       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 12224 ; 5.298 ;17.706       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    17        A   349                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.4101 -86.6278  -7.6109              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0536 T22:   0.0444                                     
REMARK   3      T33:   0.0462 T12:  -0.0120                                     
REMARK   3      T13:   0.0363 T23:  -0.0253                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5981 L22:   0.7362                                     
REMARK   3      L33:   0.5392 L12:  -0.0504                                     
REMARK   3      L13:  -0.0458 L23:  -0.3285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0367 S12:   0.0907 S13:  -0.1955                       
REMARK   3      S21:  -0.1444 S22:  -0.0362 S23:  -0.0821                       
REMARK   3      S31:   0.1435 S32:   0.0198 S33:   0.0729                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    17        B   349                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.0191 -73.5834   0.4515              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0085 T22:   0.1425                                     
REMARK   3      T33:   0.0560 T12:  -0.0242                                     
REMARK   3      T13:  -0.0097 T23:   0.0366                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1194 L22:   0.4990                                     
REMARK   3      L33:   1.0782 L12:  -0.0546                                     
REMARK   3      L13:  -0.2203 L23:  -0.3841                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0399 S12:  -0.0219 S13:   0.0737                       
REMARK   3      S21:  -0.0116 S22:   0.1472 S23:   0.0888                       
REMARK   3      S31:   0.0821 S32:  -0.2526 S33:  -0.1073                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    17        C   349                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8438 -37.0650 -30.3439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0189 T22:   0.0930                                     
REMARK   3      T33:   0.0594 T12:  -0.0015                                     
REMARK   3      T13:   0.0236 T23:   0.0491                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2808 L22:   1.9871                                     
REMARK   3      L33:   0.6793 L12:   0.5907                                     
REMARK   3      L13:  -0.0299 L23:  -0.6536                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0378 S12:   0.0502 S13:   0.0621                       
REMARK   3      S21:  -0.0652 S22:  -0.0458 S23:  -0.1597                       
REMARK   3      S31:  -0.0295 S32:   0.0279 S33:   0.0080                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    17        D   349                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.7985 -43.1168 -45.2400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0447 T22:   0.1609                                     
REMARK   3      T33:   0.0911 T12:   0.0283                                     
REMARK   3      T13:  -0.0242 T23:   0.0802                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3623 L22:   0.6099                                     
REMARK   3      L33:   0.6496 L12:   0.0478                                     
REMARK   3      L13:   0.5817 L23:  -0.2503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0951 S12:   0.1759 S13:   0.0701                       
REMARK   3      S21:  -0.1361 S22:  -0.0126 S23:   0.1619                       
REMARK   3      S31:   0.0845 S32:   0.0663 S33:  -0.0824                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5D03 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212455.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 7.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.954                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 126857                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.840                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 75.530                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.94200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: MONOCLINIC, P1211                                            
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS HCL PH 7.3, 0.2 M TRIMETHYL    
REMARK 280  -AMINO-N-OXIDE (TMAO), 0.4 MM MNSO4 AND PEG 2000MME, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 296K                           
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       67.81100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: TETRAMER BY ANALYTICAL GEL FILTRATION                        
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13200 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     TYR A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     LYS A    16                                                      
REMARK 465     ALA A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     TYR B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     ILE B    10                                                      
REMARK 465     LYS B    11                                                      
REMARK 465     ILE B    12                                                      
REMARK 465     LYS B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     ALA B   350                                                      
REMARK 465     SER B   351                                                      
REMARK 465     MET C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     TYR C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     ASP C     9                                                      
REMARK 465     ILE C    10                                                      
REMARK 465     LYS C    11                                                      
REMARK 465     ILE C    12                                                      
REMARK 465     LYS C    13                                                      
REMARK 465     GLU C    14                                                      
REMARK 465     VAL C    15                                                      
REMARK 465     LYS C    16                                                      
REMARK 465     ALA C   350                                                      
REMARK 465     SER C   351                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     HIS D     4                                                      
REMARK 465     TYR D     5                                                      
REMARK 465     PRO D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     ASP D     8                                                      
REMARK 465     ASP D     9                                                      
REMARK 465     ILE D    10                                                      
REMARK 465     LYS D    11                                                      
REMARK 465     ILE D    12                                                      
REMARK 465     LYS D    13                                                      
REMARK 465     GLU D    14                                                      
REMARK 465     VAL D    15                                                      
REMARK 465     LYS D    16                                                      
REMARK 465     ALA D   350                                                      
REMARK 465     SER D   351                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  32    CG   CD   CE   NZ                                   
REMARK 470     LYS A  83    CG   CD   CE   NZ                                   
REMARK 470     LYS A 239    CG   CD   CE   NZ                                   
REMARK 470     GLU A 246    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 274    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 275    CG   CD   CE   NZ                                   
REMARK 470     GLN A 293    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  32    CG   CD   CE   NZ                                   
REMARK 470     LYS B  80    CG   CD   CE   NZ                                   
REMARK 470     GLU B 246    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 275    CD   CE   NZ                                        
REMARK 470     ARG B 279    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 292    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 293    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 314    CG   CD   CE   NZ                                   
REMARK 470     GLU B 316    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  32    CG   CD   CE   NZ                                   
REMARK 470     GLU C  76    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  80    CD   CE   NZ                                        
REMARK 470     LYS C 239    CG   CD   CE   NZ                                   
REMARK 470     GLU C 246    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 250    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 274    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 275    CG   CD   CE   NZ                                   
REMARK 470     GLN C 293    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 314    CG   CD   CE   NZ                                   
REMARK 470     GLU C 316    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 320    CG   CD   CE   NZ                                   
REMARK 470     LYS D  32    CG   CD   CE   NZ                                   
REMARK 470     GLU D  76    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 216    CG   CD   CE   NZ                                   
REMARK 470     LYS D 239    CG   CD   CE   NZ                                   
REMARK 470     GLU D 246    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 250    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 253    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 274    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 275    CG   CD   CE   NZ                                   
REMARK 470     GLN D 293    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 314    CG   CD   CE   NZ                                   
REMARK 470     GLU D 316    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 334    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A   148     O    HOH A   501              2.13            
REMARK 500   O    HOH D   642     O    HOH D   647              2.13            
REMARK 500   O    HOH C   623     O    HOH C   655              2.14            
REMARK 500   O    HOH A   611     O    HOH A   698              2.16            
REMARK 500   O    HOH B   652     O    HOH B   677              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 262   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP A 262   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG C 167   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP C 244   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG D 101   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 103      -79.57   -126.53                                   
REMARK 500    ASP A 112       70.13   -154.41                                   
REMARK 500    ASP A 116       20.42   -145.10                                   
REMARK 500    TYR A 155       -2.24   -155.18                                   
REMARK 500    SER A 269     -153.53   -106.56                                   
REMARK 500    HIS A 270     -124.41     44.39                                   
REMARK 500    ASP A 294      -81.92   -156.09                                   
REMARK 500    THR A 323     -124.74   -112.46                                   
REMARK 500    THR B 103      -79.84   -121.01                                   
REMARK 500    ASP B 112       73.46   -157.37                                   
REMARK 500    TYR B 155        0.45   -150.66                                   
REMARK 500    SER B 269     -158.82   -104.72                                   
REMARK 500    HIS B 270     -130.57     48.31                                   
REMARK 500    ASP B 294      -83.74   -158.92                                   
REMARK 500    THR B 323     -130.67   -106.32                                   
REMARK 500    THR C 103      -87.67   -123.31                                   
REMARK 500    ASP C 112       73.86   -157.61                                   
REMARK 500    ASP C 116       16.58   -149.34                                   
REMARK 500    TYR C 155        1.92   -153.40                                   
REMARK 500    SER C 269     -158.23   -100.83                                   
REMARK 500    HIS C 270     -130.49     50.74                                   
REMARK 500    ARG C 274     -127.51     56.03                                   
REMARK 500    ASP C 294      -88.67   -168.50                                   
REMARK 500    THR C 323     -123.25   -106.71                                   
REMARK 500    THR D 103      -79.37   -125.60                                   
REMARK 500    ASP D 112       72.04   -155.34                                   
REMARK 500    ASP D 116       22.12   -144.75                                   
REMARK 500    TYR D 155       -0.46   -153.92                                   
REMARK 500    SER D 269     -159.66   -105.70                                   
REMARK 500    HIS D 270     -130.20     54.07                                   
REMARK 500    ASP D 294      -74.00   -159.54                                   
REMARK 500    THR D 323     -124.54   -109.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  63   SG                                                     
REMARK 620 2 HIS A 270   NE2 172.9                                              
REMARK 620 3 GLU A 304   OE2  87.9  85.5                                        
REMARK 620 4 ASP A 324   OD2  92.4  93.5 123.4                                  
REMARK 620 5 HOH A 549   O    82.3 102.2 149.3  86.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  63   SG                                                     
REMARK 620 2 HIS B 270   NE2 175.5                                              
REMARK 620 3 GLU B 304   OE2  87.6  88.9                                        
REMARK 620 4 ASP B 324   OD2  95.3  84.7 127.9                                  
REMARK 620 5 HOH B 639   O    80.9 103.5 150.0  80.9                            
REMARK 620 6 PEP B 402   O1  103.6  79.2  89.9 138.5  66.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  63   SG                                                     
REMARK 620 2 HIS C 270   NE2 175.7                                              
REMARK 620 3 GLU C 304   OE2  89.1  92.1                                        
REMARK 620 4 ASP C 324   OD2  92.9  89.6 128.6                                  
REMARK 620 5 HOH C 510   O    86.7  89.6 136.4  94.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  63   SG                                                     
REMARK 620 2 HIS D 270   NE2 177.3                                              
REMARK 620 3 GLU D 304   OE2  88.2  89.1                                        
REMARK 620 4 ASP D 324   OD2  87.6  93.9 126.6                                  
REMARK 620 5 PEP D 402   O2' 103.8  76.5  94.0 138.4                            
REMARK 620 6 HOH D 520   O    79.8 102.7 149.0  81.6  62.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEP A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEP B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEP C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEP D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5CZ0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CZT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5D02   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CZS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5D04   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5D05   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5D09   RELATED DB: PDB                                   
DBREF  5D03 A    1   351  UNP    Q9K169   Q9K169_NEIMB     1    351             
DBREF  5D03 B    1   351  UNP    Q9K169   Q9K169_NEIMB     1    351             
DBREF  5D03 C    1   351  UNP    Q9K169   Q9K169_NEIMB     1    351             
DBREF  5D03 D    1   351  UNP    Q9K169   Q9K169_NEIMB     1    351             
SEQADV 5D03 ALA A  223  UNP  Q9K169    VAL   223 ENGINEERED MUTATION            
SEQADV 5D03 ALA B  223  UNP  Q9K169    VAL   223 ENGINEERED MUTATION            
SEQADV 5D03 ALA C  223  UNP  Q9K169    VAL   223 ENGINEERED MUTATION            
SEQADV 5D03 ALA D  223  UNP  Q9K169    VAL   223 ENGINEERED MUTATION            
SEQRES   1 A  351  MET THR HIS HIS TYR PRO THR ASP ASP ILE LYS ILE LYS          
SEQRES   2 A  351  GLU VAL LYS GLU LEU LEU PRO PRO ILE ALA HIS LEU TYR          
SEQRES   3 A  351  GLU LEU PRO ILE SER LYS GLU ALA SER GLY LEU VAL HIS          
SEQRES   4 A  351  ARG THR ARG GLN GLU ILE SER ASP LEU VAL HIS GLY ARG          
SEQRES   5 A  351  ASP LYS ARG LEU LEU VAL ILE ILE GLY PRO CYS SER ILE          
SEQRES   6 A  351  HIS ASP PRO LYS ALA ALA LEU GLU TYR ALA GLU ARG LEU          
SEQRES   7 A  351  LEU LYS LEU ARG LYS GLN TYR GLU ASN GLU LEU LEU ILE          
SEQRES   8 A  351  VAL MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL          
SEQRES   9 A  351  GLY TRP LYS GLY LEU ILE ASN ASP PRO HIS LEU ASP GLY          
SEQRES  10 A  351  THR PHE ASP ILE ASN PHE GLY LEU ARG GLN ALA ARG SER          
SEQRES  11 A  351  LEU LEU LEU SER LEU ASN ASN MET GLY MET PRO ALA SER          
SEQRES  12 A  351  THR GLU PHE LEU ASP MET ILE THR PRO GLN TYR TYR ALA          
SEQRES  13 A  351  ASP LEU ILE SER TRP GLY ALA ILE GLY ALA ARG THR THR          
SEQRES  14 A  351  GLU SER GLN VAL HIS ARG GLU LEU ALA SER GLY LEU SER          
SEQRES  15 A  351  CYS PRO VAL GLY PHE LYS ASN GLY THR ASP GLY ASN LEU          
SEQRES  16 A  351  LYS ILE ALA ILE ASP ALA ILE GLY ALA ALA SER HIS SER          
SEQRES  17 A  351  HIS HIS PHE LEU SER VAL THR LYS ALA GLY HIS SER ALA          
SEQRES  18 A  351  ILE ALA HIS THR GLY GLY ASN PRO ASP CYS HIS VAL ILE          
SEQRES  19 A  351  LEU ARG GLY GLY LYS GLU PRO ASN TYR ASP ALA GLU HIS          
SEQRES  20 A  351  VAL SER GLU ALA ALA GLU GLN LEU ARG ALA ALA GLY VAL          
SEQRES  21 A  351  THR ASP LYS LEU MET ILE ASP CYS SER HIS ALA ASN SER          
SEQRES  22 A  351  ARG LYS ASP TYR THR ARG GLN MET GLU VAL ALA GLN ASP          
SEQRES  23 A  351  ILE ALA ALA GLN LEU GLU GLN ASP GLY GLY ASN ILE MET          
SEQRES  24 A  351  GLY VAL MET VAL GLU SER HIS LEU VAL GLU GLY ARG GLN          
SEQRES  25 A  351  ASP LYS PRO GLU VAL TYR GLY LYS SER ILE THR ASP ALA          
SEQRES  26 A  351  CYS ILE GLY TRP GLY ALA THR GLU GLU LEU LEU ALA LEU          
SEQRES  27 A  351  LEU ALA GLY ALA ASN LYS LYS ARG MET ALA ARG ALA SER          
SEQRES   1 B  351  MET THR HIS HIS TYR PRO THR ASP ASP ILE LYS ILE LYS          
SEQRES   2 B  351  GLU VAL LYS GLU LEU LEU PRO PRO ILE ALA HIS LEU TYR          
SEQRES   3 B  351  GLU LEU PRO ILE SER LYS GLU ALA SER GLY LEU VAL HIS          
SEQRES   4 B  351  ARG THR ARG GLN GLU ILE SER ASP LEU VAL HIS GLY ARG          
SEQRES   5 B  351  ASP LYS ARG LEU LEU VAL ILE ILE GLY PRO CYS SER ILE          
SEQRES   6 B  351  HIS ASP PRO LYS ALA ALA LEU GLU TYR ALA GLU ARG LEU          
SEQRES   7 B  351  LEU LYS LEU ARG LYS GLN TYR GLU ASN GLU LEU LEU ILE          
SEQRES   8 B  351  VAL MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL          
SEQRES   9 B  351  GLY TRP LYS GLY LEU ILE ASN ASP PRO HIS LEU ASP GLY          
SEQRES  10 B  351  THR PHE ASP ILE ASN PHE GLY LEU ARG GLN ALA ARG SER          
SEQRES  11 B  351  LEU LEU LEU SER LEU ASN ASN MET GLY MET PRO ALA SER          
SEQRES  12 B  351  THR GLU PHE LEU ASP MET ILE THR PRO GLN TYR TYR ALA          
SEQRES  13 B  351  ASP LEU ILE SER TRP GLY ALA ILE GLY ALA ARG THR THR          
SEQRES  14 B  351  GLU SER GLN VAL HIS ARG GLU LEU ALA SER GLY LEU SER          
SEQRES  15 B  351  CYS PRO VAL GLY PHE LYS ASN GLY THR ASP GLY ASN LEU          
SEQRES  16 B  351  LYS ILE ALA ILE ASP ALA ILE GLY ALA ALA SER HIS SER          
SEQRES  17 B  351  HIS HIS PHE LEU SER VAL THR LYS ALA GLY HIS SER ALA          
SEQRES  18 B  351  ILE ALA HIS THR GLY GLY ASN PRO ASP CYS HIS VAL ILE          
SEQRES  19 B  351  LEU ARG GLY GLY LYS GLU PRO ASN TYR ASP ALA GLU HIS          
SEQRES  20 B  351  VAL SER GLU ALA ALA GLU GLN LEU ARG ALA ALA GLY VAL          
SEQRES  21 B  351  THR ASP LYS LEU MET ILE ASP CYS SER HIS ALA ASN SER          
SEQRES  22 B  351  ARG LYS ASP TYR THR ARG GLN MET GLU VAL ALA GLN ASP          
SEQRES  23 B  351  ILE ALA ALA GLN LEU GLU GLN ASP GLY GLY ASN ILE MET          
SEQRES  24 B  351  GLY VAL MET VAL GLU SER HIS LEU VAL GLU GLY ARG GLN          
SEQRES  25 B  351  ASP LYS PRO GLU VAL TYR GLY LYS SER ILE THR ASP ALA          
SEQRES  26 B  351  CYS ILE GLY TRP GLY ALA THR GLU GLU LEU LEU ALA LEU          
SEQRES  27 B  351  LEU ALA GLY ALA ASN LYS LYS ARG MET ALA ARG ALA SER          
SEQRES   1 C  351  MET THR HIS HIS TYR PRO THR ASP ASP ILE LYS ILE LYS          
SEQRES   2 C  351  GLU VAL LYS GLU LEU LEU PRO PRO ILE ALA HIS LEU TYR          
SEQRES   3 C  351  GLU LEU PRO ILE SER LYS GLU ALA SER GLY LEU VAL HIS          
SEQRES   4 C  351  ARG THR ARG GLN GLU ILE SER ASP LEU VAL HIS GLY ARG          
SEQRES   5 C  351  ASP LYS ARG LEU LEU VAL ILE ILE GLY PRO CYS SER ILE          
SEQRES   6 C  351  HIS ASP PRO LYS ALA ALA LEU GLU TYR ALA GLU ARG LEU          
SEQRES   7 C  351  LEU LYS LEU ARG LYS GLN TYR GLU ASN GLU LEU LEU ILE          
SEQRES   8 C  351  VAL MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL          
SEQRES   9 C  351  GLY TRP LYS GLY LEU ILE ASN ASP PRO HIS LEU ASP GLY          
SEQRES  10 C  351  THR PHE ASP ILE ASN PHE GLY LEU ARG GLN ALA ARG SER          
SEQRES  11 C  351  LEU LEU LEU SER LEU ASN ASN MET GLY MET PRO ALA SER          
SEQRES  12 C  351  THR GLU PHE LEU ASP MET ILE THR PRO GLN TYR TYR ALA          
SEQRES  13 C  351  ASP LEU ILE SER TRP GLY ALA ILE GLY ALA ARG THR THR          
SEQRES  14 C  351  GLU SER GLN VAL HIS ARG GLU LEU ALA SER GLY LEU SER          
SEQRES  15 C  351  CYS PRO VAL GLY PHE LYS ASN GLY THR ASP GLY ASN LEU          
SEQRES  16 C  351  LYS ILE ALA ILE ASP ALA ILE GLY ALA ALA SER HIS SER          
SEQRES  17 C  351  HIS HIS PHE LEU SER VAL THR LYS ALA GLY HIS SER ALA          
SEQRES  18 C  351  ILE ALA HIS THR GLY GLY ASN PRO ASP CYS HIS VAL ILE          
SEQRES  19 C  351  LEU ARG GLY GLY LYS GLU PRO ASN TYR ASP ALA GLU HIS          
SEQRES  20 C  351  VAL SER GLU ALA ALA GLU GLN LEU ARG ALA ALA GLY VAL          
SEQRES  21 C  351  THR ASP LYS LEU MET ILE ASP CYS SER HIS ALA ASN SER          
SEQRES  22 C  351  ARG LYS ASP TYR THR ARG GLN MET GLU VAL ALA GLN ASP          
SEQRES  23 C  351  ILE ALA ALA GLN LEU GLU GLN ASP GLY GLY ASN ILE MET          
SEQRES  24 C  351  GLY VAL MET VAL GLU SER HIS LEU VAL GLU GLY ARG GLN          
SEQRES  25 C  351  ASP LYS PRO GLU VAL TYR GLY LYS SER ILE THR ASP ALA          
SEQRES  26 C  351  CYS ILE GLY TRP GLY ALA THR GLU GLU LEU LEU ALA LEU          
SEQRES  27 C  351  LEU ALA GLY ALA ASN LYS LYS ARG MET ALA ARG ALA SER          
SEQRES   1 D  351  MET THR HIS HIS TYR PRO THR ASP ASP ILE LYS ILE LYS          
SEQRES   2 D  351  GLU VAL LYS GLU LEU LEU PRO PRO ILE ALA HIS LEU TYR          
SEQRES   3 D  351  GLU LEU PRO ILE SER LYS GLU ALA SER GLY LEU VAL HIS          
SEQRES   4 D  351  ARG THR ARG GLN GLU ILE SER ASP LEU VAL HIS GLY ARG          
SEQRES   5 D  351  ASP LYS ARG LEU LEU VAL ILE ILE GLY PRO CYS SER ILE          
SEQRES   6 D  351  HIS ASP PRO LYS ALA ALA LEU GLU TYR ALA GLU ARG LEU          
SEQRES   7 D  351  LEU LYS LEU ARG LYS GLN TYR GLU ASN GLU LEU LEU ILE          
SEQRES   8 D  351  VAL MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL          
SEQRES   9 D  351  GLY TRP LYS GLY LEU ILE ASN ASP PRO HIS LEU ASP GLY          
SEQRES  10 D  351  THR PHE ASP ILE ASN PHE GLY LEU ARG GLN ALA ARG SER          
SEQRES  11 D  351  LEU LEU LEU SER LEU ASN ASN MET GLY MET PRO ALA SER          
SEQRES  12 D  351  THR GLU PHE LEU ASP MET ILE THR PRO GLN TYR TYR ALA          
SEQRES  13 D  351  ASP LEU ILE SER TRP GLY ALA ILE GLY ALA ARG THR THR          
SEQRES  14 D  351  GLU SER GLN VAL HIS ARG GLU LEU ALA SER GLY LEU SER          
SEQRES  15 D  351  CYS PRO VAL GLY PHE LYS ASN GLY THR ASP GLY ASN LEU          
SEQRES  16 D  351  LYS ILE ALA ILE ASP ALA ILE GLY ALA ALA SER HIS SER          
SEQRES  17 D  351  HIS HIS PHE LEU SER VAL THR LYS ALA GLY HIS SER ALA          
SEQRES  18 D  351  ILE ALA HIS THR GLY GLY ASN PRO ASP CYS HIS VAL ILE          
SEQRES  19 D  351  LEU ARG GLY GLY LYS GLU PRO ASN TYR ASP ALA GLU HIS          
SEQRES  20 D  351  VAL SER GLU ALA ALA GLU GLN LEU ARG ALA ALA GLY VAL          
SEQRES  21 D  351  THR ASP LYS LEU MET ILE ASP CYS SER HIS ALA ASN SER          
SEQRES  22 D  351  ARG LYS ASP TYR THR ARG GLN MET GLU VAL ALA GLN ASP          
SEQRES  23 D  351  ILE ALA ALA GLN LEU GLU GLN ASP GLY GLY ASN ILE MET          
SEQRES  24 D  351  GLY VAL MET VAL GLU SER HIS LEU VAL GLU GLY ARG GLN          
SEQRES  25 D  351  ASP LYS PRO GLU VAL TYR GLY LYS SER ILE THR ASP ALA          
SEQRES  26 D  351  CYS ILE GLY TRP GLY ALA THR GLU GLU LEU LEU ALA LEU          
SEQRES  27 D  351  LEU ALA GLY ALA ASN LYS LYS ARG MET ALA ARG ALA SER          
HET     MN  A 401       1                                                       
HET    PEP  A 402      10                                                       
HET     CL  A 403       1                                                       
HET    EDO  A 404       4                                                       
HET     MN  B 401       1                                                       
HET    PEP  B 402      10                                                       
HET     MN  C 401       1                                                       
HET    PEP  C 402      10                                                       
HET     CL  C 403       1                                                       
HET    SO4  C 404       5                                                       
HET     MN  D 401       1                                                       
HET    PEP  D 402      10                                                       
HET     CL  D 403       1                                                       
HET     CL  D 404       1                                                       
HET    PEG  D 405       7                                                       
HET    EDO  D 406       4                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     PEP PHOSPHOENOLPYRUVATE                                              
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   6  PEP    4(C3 H5 O6 P)                                                
FORMUL   7   CL    4(CL 1-)                                                     
FORMUL   8  EDO    2(C2 H6 O2)                                                  
FORMUL  14  SO4    O4 S 2-                                                      
FORMUL  19  PEG    C4 H10 O3                                                    
FORMUL  21  HOH   *733(H2 O)                                                    
HELIX    1 AA1 PRO A   20  LEU A   28  1                                   9    
HELIX    2 AA2 SER A   31  HIS A   50  1                                  20    
HELIX    3 AA3 ASP A   67  TYR A   85  1                                  19    
HELIX    4 AA4 ASP A  120  GLY A  139  1                                  20    
HELIX    5 AA5 ILE A  150  ILE A  159  5                                  10    
HELIX    6 AA6 SER A  171  LEU A  181  1                                  11    
HELIX    7 AA7 LEU A  195  SER A  206  1                                  12    
HELIX    8 AA8 ASP A  244  ALA A  258  1                                  15    
HELIX    9 AA9 SER A  269  ARG A  274  1                                   6    
HELIX   10 AB1 ASP A  276  THR A  278  5                                   3    
HELIX   11 AB2 ARG A  279  ASP A  294  1                                  16    
HELIX   12 AB3 GLY A  328  ARG A  349  1                                  22    
HELIX   13 AB4 PRO B   20  LEU B   28  1                                   9    
HELIX   14 AB5 SER B   31  HIS B   50  1                                  20    
HELIX   15 AB6 ASP B   67  TYR B   85  1                                  19    
HELIX   16 AB7 ASP B  120  MET B  138  1                                  19    
HELIX   17 AB8 ILE B  150  ILE B  159  5                                  10    
HELIX   18 AB9 SER B  171  LEU B  181  1                                  11    
HELIX   19 AC1 LEU B  195  SER B  206  1                                  12    
HELIX   20 AC2 ASP B  244  ALA B  258  1                                  15    
HELIX   21 AC3 SER B  269  SER B  273  5                                   5    
HELIX   22 AC4 ASP B  276  THR B  278  5                                   3    
HELIX   23 AC5 ARG B  279  ASP B  294  1                                  16    
HELIX   24 AC6 GLY B  328  ARG B  349  1                                  22    
HELIX   25 AC7 PRO C   20  LEU C   28  1                                   9    
HELIX   26 AC8 SER C   31  HIS C   50  1                                  20    
HELIX   27 AC9 ASP C   67  TYR C   85  1                                  19    
HELIX   28 AD1 ASP C  120  MET C  138  1                                  19    
HELIX   29 AD2 ILE C  150  ILE C  159  5                                  10    
HELIX   30 AD3 SER C  171  GLY C  180  1                                  10    
HELIX   31 AD4 LEU C  195  SER C  206  1                                  12    
HELIX   32 AD5 ASP C  244  GLY C  259  1                                  16    
HELIX   33 AD6 SER C  269  SER C  273  5                                   5    
HELIX   34 AD7 THR C  278  ASP C  294  1                                  17    
HELIX   35 AD8 GLY C  328  ARG C  349  1                                  22    
HELIX   36 AD9 PRO D   20  LEU D   28  1                                   9    
HELIX   37 AE1 SER D   31  HIS D   50  1                                  20    
HELIX   38 AE2 ASP D   67  TYR D   85  1                                  19    
HELIX   39 AE3 ASP D  120  MET D  138  1                                  19    
HELIX   40 AE4 ILE D  150  ILE D  159  5                                  10    
HELIX   41 AE5 SER D  171  LEU D  181  1                                  11    
HELIX   42 AE6 LEU D  195  HIS D  207  1                                  13    
HELIX   43 AE7 ASP D  244  ALA D  258  1                                  15    
HELIX   44 AE8 SER D  269  SER D  273  5                                   5    
HELIX   45 AE9 ASP D  276  THR D  278  5                                   3    
HELIX   46 AF1 ARG D  279  ASP D  294  1                                  16    
HELIX   47 AF2 GLY D  328  ARG D  349  1                                  22    
SHEET    1 AA1 9 LEU A  56  GLY A  61  0                                        
SHEET    2 AA1 9 LEU A  89  ARG A  94  1  O  LEU A  90   N  LEU A  56           
SHEET    3 AA1 9 ALA A 142  GLU A 145  1  O  SER A 143   N  MET A  93           
SHEET    4 AA1 9 TRP A 161  ILE A 164  1  O  ALA A 163   N  THR A 144           
SHEET    5 AA1 9 VAL A 185  LYS A 188  1  O  GLY A 186   N  GLY A 162           
SHEET    6 AA1 9 CYS A 231  LEU A 235  1  O  HIS A 232   N  PHE A 187           
SHEET    7 AA1 9 LEU A 264  ASP A 267  1  O  ASP A 267   N  LEU A 235           
SHEET    8 AA1 9 ILE A 298  GLU A 304  1  O  MET A 299   N  LEU A 264           
SHEET    9 AA1 9 LEU A  56  GLY A  61  1  N  LEU A  57   O  VAL A 301           
SHEET    1 AA2 2 HIS A 210  VAL A 214  0                                        
SHEET    2 AA2 2 SER A 220  HIS A 224 -1  O  ALA A 223   N  PHE A 211           
SHEET    1 AA3 9 LEU B  56  GLY B  61  0                                        
SHEET    2 AA3 9 LEU B  89  ARG B  94  1  O  LEU B  90   N  VAL B  58           
SHEET    3 AA3 9 ALA B 142  GLU B 145  1  O  SER B 143   N  MET B  93           
SHEET    4 AA3 9 TRP B 161  ILE B 164  1  O  ALA B 163   N  THR B 144           
SHEET    5 AA3 9 VAL B 185  LYS B 188  1  O  GLY B 186   N  ILE B 164           
SHEET    6 AA3 9 CYS B 231  LEU B 235  1  O  HIS B 232   N  PHE B 187           
SHEET    7 AA3 9 LEU B 264  ASP B 267  1  O  ASP B 267   N  LEU B 235           
SHEET    8 AA3 9 ILE B 298  GLU B 304  1  O  MET B 299   N  LEU B 264           
SHEET    9 AA3 9 LEU B  56  GLY B  61  1  N  LEU B  57   O  VAL B 301           
SHEET    1 AA4 2 HIS B 210  VAL B 214  0                                        
SHEET    2 AA4 2 SER B 220  HIS B 224 -1  O  ALA B 223   N  PHE B 211           
SHEET    1 AA5 9 LEU C  56  GLY C  61  0                                        
SHEET    2 AA5 9 LEU C  89  ARG C  94  1  O  LEU C  90   N  LEU C  56           
SHEET    3 AA5 9 ALA C 142  GLU C 145  1  O  SER C 143   N  MET C  93           
SHEET    4 AA5 9 TRP C 161  ILE C 164  1  O  ALA C 163   N  THR C 144           
SHEET    5 AA5 9 VAL C 185  LYS C 188  1  O  GLY C 186   N  ILE C 164           
SHEET    6 AA5 9 CYS C 231  LEU C 235  1  O  HIS C 232   N  PHE C 187           
SHEET    7 AA5 9 LEU C 264  ASP C 267  1  O  MET C 265   N  LEU C 235           
SHEET    8 AA5 9 ILE C 298  GLU C 304  1  O  MET C 299   N  LEU C 264           
SHEET    9 AA5 9 LEU C  56  GLY C  61  1  N  LEU C  57   O  MET C 299           
SHEET    1 AA6 2 HIS C 210  VAL C 214  0                                        
SHEET    2 AA6 2 SER C 220  HIS C 224 -1  O  ALA C 223   N  PHE C 211           
SHEET    1 AA7 9 LEU D  56  GLY D  61  0                                        
SHEET    2 AA7 9 LEU D  89  ARG D  94  1  O  LEU D  90   N  LEU D  56           
SHEET    3 AA7 9 ALA D 142  GLU D 145  1  O  SER D 143   N  MET D  93           
SHEET    4 AA7 9 TRP D 161  ILE D 164  1  O  ALA D 163   N  THR D 144           
SHEET    5 AA7 9 VAL D 185  LYS D 188  1  O  GLY D 186   N  ILE D 164           
SHEET    6 AA7 9 CYS D 231  LEU D 235  1  O  HIS D 232   N  PHE D 187           
SHEET    7 AA7 9 LEU D 264  ASP D 267  1  O  ASP D 267   N  LEU D 235           
SHEET    8 AA7 9 ILE D 298  GLU D 304  1  O  MET D 299   N  LEU D 264           
SHEET    9 AA7 9 LEU D  56  GLY D  61  1  N  LEU D  57   O  MET D 299           
SHEET    1 AA8 2 HIS D 210  VAL D 214  0                                        
SHEET    2 AA8 2 SER D 220  HIS D 224 -1  O  ALA D 223   N  PHE D 211           
LINK         SG  CYS A  63                MN    MN A 401     1555   1555  2.60  
LINK         NE2 HIS A 270                MN    MN A 401     1555   1555  2.36  
LINK         OE2 GLU A 304                MN    MN A 401     1555   1555  2.12  
LINK         OD2 ASP A 324                MN    MN A 401     1555   1555  2.12  
LINK         SG  CYS B  63                MN    MN B 401     1555   1555  2.60  
LINK         NE2 HIS B 270                MN    MN B 401     1555   1555  2.31  
LINK         OE2 GLU B 304                MN    MN B 401     1555   1555  1.91  
LINK         OD2 ASP B 324                MN    MN B 401     1555   1555  2.27  
LINK         SG  CYS C  63                MN    MN C 401     1555   1555  2.56  
LINK         NE2 HIS C 270                MN    MN C 401     1555   1555  2.34  
LINK         OE2 GLU C 304                MN    MN C 401     1555   1555  2.02  
LINK         OD2 ASP C 324                MN    MN C 401     1555   1555  2.24  
LINK         SG  CYS D  63                MN    MN D 401     1555   1555  2.61  
LINK         NE2 HIS D 270                MN    MN D 401     1555   1555  2.40  
LINK         OE2 GLU D 304                MN    MN D 401     1555   1555  2.12  
LINK         OD2 ASP D 324                MN    MN D 401     1555   1555  1.92  
LINK        MN    MN A 401                 O   HOH A 549     1555   1555  2.09  
LINK        MN    MN B 401                 O   HOH B 639     1555   1555  2.41  
LINK        MN    MN B 401                 O1  PEP B 402     1555   1555  2.78  
LINK        MN    MN C 401                 O   HOH C 510     1555   1555  2.11  
LINK        MN    MN D 401                 O2' PEP D 402     1555   1555  2.66  
LINK        MN    MN D 401                 O   HOH D 520     1555   1555  2.35  
SITE     1 AC1  6 CYS A  63  HIS A 270  GLU A 304  ASP A 324                    
SITE     2 AC1  6 PEP A 402  HOH A 549                                          
SITE     1 AC2 15 ARG A  94  LYS A  99  GLU A 145  GLY A 165                    
SITE     2 AC2 15 ALA A 166  ARG A 167  LYS A 188  ARG A 236                    
SITE     3 AC2 15 HIS A 270   MN A 401  HOH A 519  HOH A 523                    
SITE     4 AC2 15 HOH A 541  HOH A 549  HOH A 630                               
SITE     1 AC3  2 ARG A 101  THR A 102                                          
SITE     1 AC4  2 LEU A 115  GLY A 117                                          
SITE     1 AC5  6 CYS B  63  HIS B 270  GLU B 304  ASP B 324                    
SITE     2 AC5  6 PEP B 402  HOH B 639                                          
SITE     1 AC6 17 ARG B  94  TYR B  96  LYS B  99  GLU B 145                    
SITE     2 AC6 17 GLY B 165  ALA B 166  ARG B 167  LYS B 188                    
SITE     3 AC6 17 ARG B 236  HIS B 270  GLU B 304   MN B 401                    
SITE     4 AC6 17 HOH B 512  HOH B 517  HOH B 535  HOH B 599                    
SITE     5 AC6 17 HOH B 639                                                     
SITE     1 AC7  6 CYS C  63  HIS C 270  GLU C 304  ASP C 324                    
SITE     2 AC7  6 PEP C 402  HOH C 510                                          
SITE     1 AC8 14 ARG C  94  LYS C  99  GLU C 145  GLY C 165                    
SITE     2 AC8 14 ALA C 166  ARG C 167  LYS C 188  ARG C 236                    
SITE     3 AC8 14 HIS C 270   MN C 401  HOH C 502  HOH C 510                    
SITE     4 AC8 14 HOH C 529  HOH C 580                                          
SITE     1 AC9  5 ILE C  65  TYR C  96  PHE C  97  GLY C 108                    
SITE     2 AC9  5 LEU C 109                                                     
SITE     1 AD1  2 ARG C 101  THR C 102                                          
SITE     1 AD2  6 CYS D  63  HIS D 270  GLU D 304  ASP D 324                    
SITE     2 AD2  6 PEP D 402  HOH D 520                                          
SITE     1 AD3 17 ARG D  94  TYR D  96  LYS D  99  GLU D 145                    
SITE     2 AD3 17 GLY D 165  ALA D 166  ARG D 167  LYS D 188                    
SITE     3 AD3 17 ARG D 236  HIS D 270  GLU D 304   MN D 401                    
SITE     4 AD3 17 HOH D 502  HOH D 520  HOH D 543  HOH D 548                    
SITE     5 AD3 17 HOH D 549                                                     
SITE     1 AD4  6 ILE D  65  TYR D  96  PHE D  97  TRP D 106                    
SITE     2 AD4  6 GLY D 108  LEU D 109                                          
SITE     1 AD5  2 ARG D 101  THR D 102                                          
SITE     1 AD6  3 ARG D 279  GLU D 282  HOH D 529                               
SITE     1 AD7  1 LEU D 115                                                     
CRYST1   73.256  135.622   75.989  90.00  96.27  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      0.013651  0.000000  0.001501        0.00000                         
SCALE2      0.000000  0.007373  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013239        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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