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Database: PDB
Entry: 5CZT
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Original site: 5CZT 
HEADER    TRANSFERASE                             01-AUG-15   5CZT              
TITLE     NEISSERIA MENINGITIDIS 3 DEXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE     
TITLE    2 SYNTHASE GLU176ALA 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                                                      
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 5CZT    1       HEADER REMARK                            
REVDAT   1   10-AUG-16 5CZT    0                                                
JRNL        AUTH   L.C.HEYES,E.J.PARKER                                         
JRNL        TITL   NEISSERIA MENINGITIDIS 3 DEXY-D-ARABINO-HEPTULOSONATE        
JRNL        TITL 2 7-PHOSPHATE SYNTHASE GLU176ALA VARIANT AT 2.04 ANGSTROMS     
JRNL        TITL 3 RESOLUTION                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
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) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 76.41                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 95084                          
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) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6322                            
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) : 2.04                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.09                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6897                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 483                          
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10503                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 55                                      
REMARK   3   SOLVENT ATOMS            : 745                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.16000                                              
REMARK   3    B22 (A**2) : 1.23000                                              
REMARK   3    B33 (A**2) : -1.16000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.63000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.170         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.148         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.113         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.059         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10803 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 10353 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14633 ; 1.391 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 23773 ; 0.807 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1385 ; 5.557 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   467 ;32.985 ;23.683       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1818 ;13.592 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    75 ;14.860 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1646 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12332 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2437 ; 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):  5555 ; 1.284 ; 2.132       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5554 ; 1.284 ; 2.132       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6935 ; 2.030 ; 3.188       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  6936 ; 2.029 ; 3.188       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5248 ; 1.664 ; 2.318       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5248 ; 1.664 ; 2.318       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  7699 ; 2.614 ; 3.401       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 12741 ; 5.029 ;17.819       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 12742 ; 5.029 ;17.819       
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     4        A   349                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5771 -11.9248 -40.0227              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0085 T22:   0.1046                                     
REMARK   3      T33:   0.1156 T12:   0.0147                                     
REMARK   3      T13:   0.0034 T23:   0.0662                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2150 L22:   0.8758                                     
REMARK   3      L33:   1.2181 L12:  -0.1979                                     
REMARK   3      L13:   0.0411 L23:   0.0336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0226 S12:   0.0894 S13:  -0.0063                       
REMARK   3      S21:  -0.0269 S22:  -0.1400 S23:  -0.1570                       
REMARK   3      S31:  -0.0465 S32:   0.1820 S33:   0.1173                       
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     4        B   349                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1235  -9.6737  -7.9745              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1018 T22:   0.0748                                     
REMARK   3      T33:   0.0741 T12:   0.0055                                     
REMARK   3      T13:  -0.0377 T23:   0.0393                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0563 L22:   0.3946                                     
REMARK   3      L33:   1.6683 L12:  -0.4277                                     
REMARK   3      L13:   0.9020 L23:  -0.0440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0375 S12:   0.0679 S13:  -0.0797                       
REMARK   3      S21:   0.1071 S22:   0.0645 S23:   0.0253                       
REMARK   3      S31:  -0.0582 S32:   0.2036 S33:  -0.0270                       
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     4        C   349                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.4209  36.6974 -32.1863              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0550 T22:   0.0368                                     
REMARK   3      T33:   0.0300 T12:  -0.0222                                     
REMARK   3      T13:  -0.0148 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3501 L22:   0.5877                                     
REMARK   3      L33:   0.6554 L12:  -0.0230                                     
REMARK   3      L13:   0.0274 L23:  -0.0972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0090 S12:   0.0118 S13:   0.0349                       
REMARK   3      S21:   0.0015 S22:  -0.0221 S23:  -0.0011                       
REMARK   3      S31:   0.0121 S32:  -0.0108 S33:   0.0312                       
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     4        D   349                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.6915  25.7628  -1.9161              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0853 T22:   0.0677                                     
REMARK   3      T33:   0.0191 T12:  -0.0111                                     
REMARK   3      T13:   0.0198 T23:   0.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4356 L22:   0.3013                                     
REMARK   3      L33:   0.6646 L12:  -0.0085                                     
REMARK   3      L13:  -0.0670 L23:   0.0171                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0067 S12:  -0.0660 S13:   0.0142                       
REMARK   3      S21:   0.0783 S22:   0.0334 S23:   0.0535                       
REMARK   3      S31:   0.0820 S32:  -0.1055 S33:  -0.0402                       
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 5CZT 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_1000212437.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUN-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                       : MX1                                
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 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 101442                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.410                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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   (%): 54.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS HCL (PH 7.3), 0.2 M            
REMARK 280  TRIMETHYL-AMINO-N-OXIDE (TMAO), 0.4 MM MNSO4 AND PEG 2000MME,       
REMARK 280  VAPOR 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       70.41400            
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: 15320 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 45330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -134.0 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     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     THR B   102                                                      
REMARK 465     THR B   103                                                      
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     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     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  16    CG   CD   CE   NZ                                   
REMARK 470     LYS A  69    CG   CD   CE   NZ                                   
REMARK 470     GLU A  76    OE1  OE2                                            
REMARK 470     ARG A 101    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 102    OG1  CG2                                            
REMARK 470     THR A 103    OG1  CG2                                            
REMARK 470     VAL A 104    CG1  CG2                                            
REMARK 470     LYS A 107    CG   CD   CE   NZ                                   
REMARK 470     ASP A 192    CG   OD1  OD2                                       
REMARK 470     LYS A 239    CG   CD   CE   NZ                                   
REMARK 470     GLU A 246    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 250    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 253    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 275    CG   CD   CE   NZ                                   
REMARK 470     GLN A 293    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 316    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  32    CG   CD   CE   NZ                                   
REMARK 470     LYS B  69    CG   CD   CE   NZ                                   
REMARK 470     GLU B  76    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  99    CD   CE   NZ                                        
REMARK 470     LYS B 107    CG   CD   CE   NZ                                   
REMARK 470     LYS B 239    CG   CD   CE   NZ                                   
REMARK 470     GLU B 240    OE1  OE2                                            
REMARK 470     ARG B 279    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 292    OE1  OE2                                            
REMARK 470     ASP B 313    OD1  OD2                                            
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     ARG C 101    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR C 102    OG1  CG2                                            
REMARK 470     THR C 103    OG1  CG2                                            
REMARK 470     VAL C 104    CG1  CG2                                            
REMARK 470     LYS C 107    CE   NZ                                             
REMARK 470     GLN C 172    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 239    CG   CD   CE   NZ                                   
REMARK 470     GLU C 240    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 246    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 250    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 253    OE1  OE2                                            
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 D  32    CG   CD   CE   NZ                                   
REMARK 470     ASP D 192    CG   OD1  OD2                                       
REMARK 470     LYS D 239    CG   CD   CE   NZ                                   
REMARK 470     GLU D 240    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 246    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 293    CG   CD   OE1  NE2                                  
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   NH1  ARG C   279     O    HOH C   501              1.58            
REMARK 500   OD1  ASP A   112     O    THR A   118              1.67            
REMARK 500   OD1  ASP A   116     OG1  THR A   118              1.76            
REMARK 500   ND1  HIS C   219     O    HOH C   502              1.93            
REMARK 500   OE2  GLU C    27     O    HOH C   503              2.14            
REMARK 500   OE1  GLU A    17     O    HOH A   501              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 103       73.52   -153.46                                   
REMARK 500    SER A 213     -161.41   -161.02                                   
REMARK 500    SER A 269     -166.55   -101.64                                   
REMARK 500    HIS A 270     -133.91     53.85                                   
REMARK 500    LYS A 275       -1.34     64.89                                   
REMARK 500    ASP A 294      -82.03   -161.64                                   
REMARK 500    THR A 323     -127.03   -112.78                                   
REMARK 500    SER B 213     -161.12   -167.10                                   
REMARK 500    ASP B 230       50.60   -112.53                                   
REMARK 500    HIS B 270     -130.18     57.11                                   
REMARK 500    ASP B 294      -86.78   -155.02                                   
REMARK 500    THR B 323     -124.29   -117.14                                   
REMARK 500    PRO C 100      102.17    -58.11                                   
REMARK 500    SER C 213     -162.37   -163.28                                   
REMARK 500    ASP C 230       50.39   -114.20                                   
REMARK 500    SER C 269     -158.83   -107.79                                   
REMARK 500    HIS C 270     -126.22     46.82                                   
REMARK 500    ASP C 294      -80.26   -160.15                                   
REMARK 500    THR C 323     -126.05   -113.26                                   
REMARK 500    TYR D 155       14.01   -146.61                                   
REMARK 500    SER D 213     -160.88   -164.30                                   
REMARK 500    HIS D 270     -133.48     62.91                                   
REMARK 500    ASP D 294      -76.07   -164.58                                   
REMARK 500    THR D 323     -124.08   -119.15                                   
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 171.9                                              
REMARK 620 3 GLU A 304   OE2  92.3  80.5                                        
REMARK 620 4 ASP A 324   OD2  93.6  93.4 122.8                                  
REMARK 620 5 HOH A 642   O    85.3  96.0 126.4 110.8                            
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 171.7                                              
REMARK 620 3 GLU B 304   OE2  88.6  94.2                                        
REMARK 620 4 ASP B 324   OD2  95.6  88.6 129.7                                  
REMARK 620 5 HOH B 601   O    91.0  80.9 122.9 107.1                            
REMARK 620 N                    1     2     3     4                             
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 176.4                                              
REMARK 620 3 GLU C 304   OE2  91.7  88.1                                        
REMARK 620 4 ASP C 324   OD2  92.0  90.7 132.7                                  
REMARK 620 5 HOH C 669   O    90.5  86.8 125.9 101.2                            
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 173.4                                              
REMARK 620 3 GLU D 304   OE2  91.5  86.8                                        
REMARK 620 4 ASP D 324   OD2  94.8  90.6 139.5                                  
REMARK 620 5 HOH D 639   O    90.6  84.3 115.0 104.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHE A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHE B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHE C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHE D 404                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5CZS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CZ0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5D02   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5D03   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  5CZT A    1   351  UNP    Q9K169   Q9K169_NEIMB     1    351             
DBREF  5CZT B    1   351  UNP    Q9K169   Q9K169_NEIMB     1    351             
DBREF  5CZT C    1   351  UNP    Q9K169   Q9K169_NEIMB     1    351             
DBREF  5CZT D    1   351  UNP    Q9K169   Q9K169_NEIMB     1    351             
SEQADV 5CZT ALA A  176  UNP  Q9K169    GLU   176 ENGINEERED MUTATION            
SEQADV 5CZT ALA B  176  UNP  Q9K169    GLU   176 ENGINEERED MUTATION            
SEQADV 5CZT ALA C  176  UNP  Q9K169    GLU   176 ENGINEERED MUTATION            
SEQADV 5CZT ALA D  176  UNP  Q9K169    GLU   176 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 ALA 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 VAL 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 ALA 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 VAL 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 ALA 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 VAL 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 ALA 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 VAL 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    PHE  A 402      12                                                       
HET     MN  B 401       1                                                       
HET    PHE  B 402      12                                                       
HET     MN  C 401       1                                                       
HET     CL  C 402       1                                                       
HET    PHE  C 403      12                                                       
HET     MN  D 401       1                                                       
HET     CL  D 402       1                                                       
HET     CL  D 403       1                                                       
HET    PHE  D 404      12                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     PHE PHENYLALANINE                                                    
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   6  PHE    4(C9 H11 N O2)                                               
FORMUL  10   CL    3(CL 1-)                                                     
FORMUL  16  HOH   *745(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 LYS A  107  ASP A  112  1                                   6    
HELIX    5 AA5 ASP A  120  GLY A  139  1                                  20    
HELIX    6 AA6 THR A  151  ALA A  156  1                                   6    
HELIX    7 AA7 ASP A  157  ILE A  159  5                                   3    
HELIX    8 AA8 SER A  171  SER A  179  1                                   9    
HELIX    9 AA9 LEU A  195  SER A  206  1                                  12    
HELIX   10 AB1 ASP A  244  ALA A  258  1                                  15    
HELIX   11 AB2 SER A  269  ARG A  274  5                                   6    
HELIX   12 AB3 ASP A  276  THR A  278  5                                   3    
HELIX   13 AB4 ARG A  279  ASP A  294  1                                  16    
HELIX   14 AB5 GLY A  328  ARG A  349  1                                  22    
HELIX   15 AB6 PRO B   20  LEU B   28  1                                   9    
HELIX   16 AB7 SER B   31  HIS B   50  1                                  20    
HELIX   17 AB8 ASP B   67  TYR B   85  1                                  19    
HELIX   18 AB9 LYS B  107  ASP B  112  1                                   6    
HELIX   19 AC1 ASP B  120  GLY B  139  1                                  20    
HELIX   20 AC2 THR B  151  ALA B  156  1                                   6    
HELIX   21 AC3 ASP B  157  ILE B  159  5                                   3    
HELIX   22 AC4 SER B  171  SER B  179  1                                   9    
HELIX   23 AC5 LEU B  195  SER B  206  1                                  12    
HELIX   24 AC6 ASP B  244  ALA B  258  1                                  15    
HELIX   25 AC7 SER B  269  ARG B  274  5                                   6    
HELIX   26 AC8 ASP B  276  THR B  278  5                                   3    
HELIX   27 AC9 ARG B  279  ASP B  294  1                                  16    
HELIX   28 AD1 GLY B  328  ARG B  349  1                                  22    
HELIX   29 AD2 PRO C   20  LEU C   28  1                                   9    
HELIX   30 AD3 SER C   31  HIS C   50  1                                  20    
HELIX   31 AD4 ASP C   67  TYR C   85  1                                  19    
HELIX   32 AD5 LYS C  107  ASP C  112  1                                   6    
HELIX   33 AD6 ASP C  120  MET C  138  1                                  19    
HELIX   34 AD7 THR C  151  ALA C  156  1                                   6    
HELIX   35 AD8 SER C  171  SER C  179  1                                   9    
HELIX   36 AD9 LEU C  195  SER C  206  1                                  12    
HELIX   37 AE1 ASP C  244  ALA C  258  1                                  15    
HELIX   38 AE2 SER C  269  SER C  273  5                                   5    
HELIX   39 AE3 ASP C  276  THR C  278  5                                   3    
HELIX   40 AE4 ARG C  279  ASP C  294  1                                  16    
HELIX   41 AE5 GLY C  328  ARG C  349  1                                  22    
HELIX   42 AE6 PRO D   20  LEU D   28  1                                   9    
HELIX   43 AE7 SER D   31  HIS D   50  1                                  20    
HELIX   44 AE8 ASP D   67  TYR D   85  1                                  19    
HELIX   45 AE9 LYS D  107  ASP D  112  1                                   6    
HELIX   46 AF1 ASP D  120  MET D  138  1                                  19    
HELIX   47 AF2 THR D  151  ALA D  156  1                                   6    
HELIX   48 AF3 SER D  171  LEU D  181  1                                  11    
HELIX   49 AF4 LEU D  195  SER D  206  1                                  12    
HELIX   50 AF5 ASP D  244  ALA D  258  1                                  15    
HELIX   51 AF6 SER D  269  ARG D  274  5                                   6    
HELIX   52 AF7 ASP D  276  THR D  278  5                                   3    
HELIX   53 AF8 ARG D  279  ASP D  294  1                                  16    
HELIX   54 AF9 GLY D  328  ARG D  349  1                                  22    
SHEET    1 AA1 3 ILE A  12  GLU A  17  0                                        
SHEET    2 AA1 3 SER B 220  THR B 225 -1  O  HIS B 224   N  GLU A  14           
SHEET    3 AA1 3 HIS B 210  VAL B 214 -1  N  SER B 213   O  ALA B 221           
SHEET    1 AA2 9 LEU A  56  GLY A  61  0                                        
SHEET    2 AA2 9 LEU A  89  ARG A  94  1  O  LEU A  90   N  LEU A  56           
SHEET    3 AA2 9 ALA A 142  GLU A 145  1  O  SER A 143   N  MET A  93           
SHEET    4 AA2 9 TRP A 161  ILE A 164  1  O  ALA A 163   N  THR A 144           
SHEET    5 AA2 9 VAL A 185  LYS A 188  1  O  GLY A 186   N  GLY A 162           
SHEET    6 AA2 9 CYS A 231  LEU A 235  1  O  HIS A 232   N  PHE A 187           
SHEET    7 AA2 9 LEU A 264  ASP A 267  1  O  ASP A 267   N  LEU A 235           
SHEET    8 AA2 9 ILE A 298  GLU A 304  1  O  MET A 299   N  LEU A 264           
SHEET    9 AA2 9 LEU A  56  GLY A  61  1  N  ILE A  59   O  VAL A 301           
SHEET    1 AA3 3 HIS A 210  VAL A 214  0                                        
SHEET    2 AA3 3 SER A 220  THR A 225 -1  O  ALA A 221   N  SER A 213           
SHEET    3 AA3 3 ILE B  12  GLU B  17 -1  O  GLU B  14   N  HIS A 224           
SHEET    1 AA4 2 VAL A 308  ARG A 311  0                                        
SHEET    2 AA4 2 LYS A 320  SER A 321  1  N  SER A 321   O  GLY A 310           
SHEET    1 AA5 9 LEU B  56  GLY B  61  0                                        
SHEET    2 AA5 9 LEU B  89  ARG B  94  1  O  LEU B  90   N  LEU B  56           
SHEET    3 AA5 9 ALA B 142  GLU B 145  1  O  SER B 143   N  MET B  93           
SHEET    4 AA5 9 TRP B 161  ILE B 164  1  O  ALA B 163   N  THR B 144           
SHEET    5 AA5 9 VAL B 185  LYS B 188  1  O  GLY B 186   N  GLY B 162           
SHEET    6 AA5 9 CYS B 231  LEU B 235  1  O  HIS B 232   N  PHE B 187           
SHEET    7 AA5 9 LEU B 264  ASP B 267  1  O  MET B 265   N  LEU B 235           
SHEET    8 AA5 9 ILE B 298  GLU B 304  1  O  MET B 299   N  LEU B 264           
SHEET    9 AA5 9 LEU B  56  GLY B  61  1  N  LEU B  57   O  MET B 299           
SHEET    1 AA6 3 ILE C  12  GLU C  17  0                                        
SHEET    2 AA6 3 SER D 220  THR D 225 -1  O  HIS D 224   N  GLU C  14           
SHEET    3 AA6 3 HIS D 210  VAL D 214 -1  N  SER D 213   O  ALA D 221           
SHEET    1 AA7 9 LEU C  56  GLY C  61  0                                        
SHEET    2 AA7 9 LEU C  89  ARG C  94  1  O  LEU C  90   N  LEU C  56           
SHEET    3 AA7 9 ALA C 142  GLU C 145  1  O  SER C 143   N  MET C  93           
SHEET    4 AA7 9 ILE C 159  ILE C 164  1  O  SER C 160   N  ALA C 142           
SHEET    5 AA7 9 VAL C 185  LYS C 188  1  O  GLY C 186   N  GLY C 162           
SHEET    6 AA7 9 CYS C 231  LEU C 235  1  O  HIS C 232   N  PHE C 187           
SHEET    7 AA7 9 LEU C 264  ASP C 267  1  O  ASP C 267   N  LEU C 235           
SHEET    8 AA7 9 ILE C 298  GLU C 304  1  O  MET C 299   N  LEU C 264           
SHEET    9 AA7 9 LEU C  56  GLY C  61  1  N  ILE C  59   O  VAL C 301           
SHEET    1 AA8 3 HIS C 210  VAL C 214  0                                        
SHEET    2 AA8 3 SER C 220  THR C 225 -1  O  VAL C 223   N  PHE C 211           
SHEET    3 AA8 3 ILE D  12  GLU D  17 -1  O  GLU D  14   N  HIS C 224           
SHEET    1 AA9 2 VAL C 308  ARG C 311  0                                        
SHEET    2 AA9 2 LYS C 320  SER C 321  1  N  SER C 321   O  GLY C 310           
SHEET    1 AB1 9 LEU D  56  GLY D  61  0                                        
SHEET    2 AB1 9 LEU D  89  ARG D  94  1  O  LEU D  90   N  LEU D  56           
SHEET    3 AB1 9 ALA D 142  GLU D 145  1  O  SER D 143   N  MET D  93           
SHEET    4 AB1 9 ILE D 159  ILE D 164  1  O  SER D 160   N  ALA D 142           
SHEET    5 AB1 9 VAL D 185  LYS D 188  1  O  GLY D 186   N  GLY D 162           
SHEET    6 AB1 9 CYS D 231  LEU D 235  1  O  HIS D 232   N  PHE D 187           
SHEET    7 AB1 9 LEU D 264  ASP D 267  1  O  ASP D 267   N  LEU D 235           
SHEET    8 AB1 9 ILE D 298  GLU D 304  1  O  MET D 299   N  LEU D 264           
SHEET    9 AB1 9 LEU D  56  GLY D  61  1  N  ILE D  59   O  VAL D 303           
SHEET    1 AB2 2 VAL D 308  ARG D 311  0                                        
SHEET    2 AB2 2 LYS D 320  SER D 321  1  N  SER D 321   O  GLY D 310           
LINK         SG  CYS A  63                MN    MN A 401     1555   1555  2.56  
LINK         NE2 HIS A 270                MN    MN A 401     1555   1555  2.36  
LINK         OE2 GLU A 304                MN    MN A 401     1555   1555  1.95  
LINK         OD2 ASP A 324                MN    MN A 401     1555   1555  2.25  
LINK         SG  CYS B  63                MN    MN B 401     1555   1555  2.52  
LINK         NE2 HIS B 270                MN    MN B 401     1555   1555  2.33  
LINK         OE2 GLU B 304                MN    MN B 401     1555   1555  2.03  
LINK         OD2 ASP B 324                MN    MN B 401     1555   1555  2.16  
LINK         SG  CYS C  63                MN    MN C 401     1555   1555  2.57  
LINK         NE2 HIS C 270                MN    MN C 401     1555   1555  2.22  
LINK         OE2 GLU C 304                MN    MN C 401     1555   1555  2.04  
LINK         OD2 ASP C 324                MN    MN C 401     1555   1555  2.10  
LINK         SG  CYS D  63                MN    MN D 401     1555   1555  2.51  
LINK         NE2 HIS D 270                MN    MN D 401     1555   1555  2.24  
LINK         OE2 GLU D 304                MN    MN D 401     1555   1555  2.17  
LINK         OD2 ASP D 324                MN    MN D 401     1555   1555  2.02  
LINK        MN    MN A 401                 O   HOH A 642     1555   1555  1.81  
LINK        MN    MN B 401                 O   HOH B 601     1555   1555  2.15  
LINK        MN    MN C 401                 O   HOH C 669     1555   1555  2.01  
LINK        MN    MN D 401                 O   HOH D 639     1555   1555  2.15  
SITE     1 AC1  5 CYS A  63  HIS A 270  GLU A 304  ASP A 324                    
SITE     2 AC1  5 HOH A 642                                                     
SITE     1 AC2 12 MET A 149  GLN A 153  ALA A 156  GLY A 180                    
SITE     2 AC2 12 LEU A 181  SER A 182  PHE A 211  SER A 213                    
SITE     3 AC2 12 VAL A 223  ASP B   8  ASP B   9  HOH B 544                    
SITE     1 AC3  5 CYS B  63  HIS B 270  GLU B 304  ASP B 324                    
SITE     2 AC3  5 HOH B 601                                                     
SITE     1 AC4 12 ASP A   8  ASP A   9  HOH A 557  GLN B 153                    
SITE     2 AC4 12 ALA B 156  GLY B 180  LEU B 181  SER B 182                    
SITE     3 AC4 12 PHE B 211  SER B 213  LYS B 216  HOH B 605                    
SITE     1 AC5  5 CYS C  63  HIS C 270  GLU C 304  ASP C 324                    
SITE     2 AC5  5 HOH C 669                                                     
SITE     1 AC6  3 LYS C 188  ARG C 236  HIS C 270                               
SITE     1 AC7 14 MET C 149  GLN C 153  ALA C 156  GLY C 180                    
SITE     2 AC7 14 LEU C 181  SER C 182  PHE C 211  SER C 213                    
SITE     3 AC7 14 LYS C 216  VAL C 223  HOH C 687  ASP D   8                    
SITE     4 AC7 14 ASP D   9  HOH D 551                                          
SITE     1 AC8  5 CYS D  63  HIS D 270  GLU D 304  ASP D 324                    
SITE     2 AC8  5 HOH D 639                                                     
SITE     1 AC9  4 ARG D  94  LYS D 188  HIS D 270  HOH D 520                    
SITE     1 AD1  2 ALA D 166  ARG D 167                                          
SITE     1 AD2 11 ASP C   8  ASP C   9  HOH C 547  MET D 149                    
SITE     2 AD2 11 GLN D 153  ALA D 156  GLY D 180  LEU D 181                    
SITE     3 AD2 11 SER D 182  SER D 213  VAL D 223                               
CRYST1   75.647  140.828   77.266  90.00  98.56  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      0.013219  0.000000  0.001990        0.00000                         
SCALE2      0.000000  0.007101  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013088        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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