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Database: PDB
Entry: 6GZ8
LinkDB: 6GZ8
Original site: 6GZ8 
HEADER    STRUCTURAL PROTEIN                      03-JUL-18   6GZ8              
TITLE     FIRST GERMN DOMAIN OF THE SPORULATION PROTEIN GERM FROM BACILLUS      
TITLE    2 SUBTILIS                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SPORE GERMINATION PROTEIN GERM;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;     
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 GENE: GERM, BSU28380;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: RIL;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;                                  
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCR282                                    
KEYWDS    GERM, GERMN DOMAIN, LIPOPROTEIN, SPORULATION, ENDOSPORES, SECRETION   
KEYWDS   2 SYSTEMS, STRUCTURAL PROTEIN                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.TROUVE,A.MOHAMED,F.LEISICO,C.CONTRERAS-MARTEL,B.LIU,C.MAS,          
AUTHOR   2 D.Z.RUDNER,C.D.A.RODRIGUES,C.MORLOT                                  
REVDAT   2   26-DEC-18 6GZ8    1       JRNL                                     
REVDAT   1   10-OCT-18 6GZ8    0                                                
JRNL        AUTH   J.TROUVE,A.MOHAMED,F.LEISICO,C.CONTRERAS-MARTEL,B.LIU,C.MAS, 
JRNL        AUTH 2 D.Z.RUDNER,C.D.A.RODRIGUES,C.MORLOT                          
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF THE SPORULATION PROTEIN GERM  
JRNL        TITL 2 FROM BACILLUS SUBTILIS.                                      
JRNL        REF    J. STRUCT. BIOL.              V. 204   481 2018              
JRNL        REFN                   ESSN 1095-8657                               
JRNL        PMID   30266596                                                     
JRNL        DOI    10.1016/J.JSB.2018.09.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.32                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 67101                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.135                           
REMARK   3   R VALUE            (WORKING SET) : 0.135                           
REMARK   3   FREE R VALUE                     : 0.154                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1738                            
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) : 1.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.03                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4626                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 133                          
REMARK   3   BIN FREE R VALUE                    : 0.2720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1040                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 184                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 10.46                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.04000                                              
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : 0.11000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.021         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.022         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.018         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.806         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.981                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.978                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1090 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  1056 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1480 ; 1.333 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2476 ; 0.951 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   142 ; 6.685 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    46 ;33.944 ;26.087       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   209 ;12.294 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ;17.435 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   173 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1190 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   190 ; 0.003 ; 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):   541 ; 2.136 ; 1.012       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   540 ; 1.621 ; 1.007       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   677 ; 2.378 ; 1.526       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   678 ; 2.506 ; 1.530       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   549 ; 6.039 ; 1.436       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   549 ; 6.027 ; 1.436       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):   799 ; 6.053 ; 1.990       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  1307 ; 6.477 ;15.592       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1308 ; 6.477 ;15.600       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2146 ; 7.131 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   109 ;30.209 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2225 ;12.613 ; 5.000       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 6GZ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010767.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 273                                
REMARK 200  PH                             : 7.5-8.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97242                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68958                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.35600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.950                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO PHASING            
REMARK 200 SOFTWARE USED: ARCIMBOLDO                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: LARGE 3D NEEDLES                                             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE 21% PEG 3350, PH    
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       19.18000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       32.43050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.80050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       32.43050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.18000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.80050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7370 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   209                                                      
REMARK 465     ILE A   210                                                      
REMARK 465     ASN A   211                                                      
REMARK 465     LEU A   212                                                      
REMARK 465     GLU A   213                                                      
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    ASN A 155       34.50    -94.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 584        DISTANCE =  6.47 ANGSTROMS                       
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                              NA A 308  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  85   OD2                                                    
REMARK 620 2 HOH A 559   O    98.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 302  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  87   O                                                      
REMARK 620 2 HOH A 460   O   134.7                                              
REMARK 620 3 HOH A 514   O   118.2  95.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 310  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO A  98   O                                                      
REMARK 620 2 GLN A 106   OE1  78.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 304  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A  99   O                                                      
REMARK 620 2 SER A 176   O    57.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 305  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 101   O                                                      
REMARK 620 2 THR A 103   OG1 144.8                                              
REMARK 620 3 HOH A 523   O   104.0  69.2                                        
REMARK 620 4 HOH A 496   O    92.5  94.5 162.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 309  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 140   O                                                      
REMARK 620 2 SER A 177   O   114.3                                              
REMARK 620 3 HOH A 423   O   126.7 118.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 311  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 159   OE2                                                    
REMARK 620 2 HOH A 580   O   115.9                                              
REMARK 620 3 HOH A 503   O   133.2  70.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 301  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 173   O                                                      
REMARK 620 2 PHE A 175   O    97.6                                              
REMARK 620 3 ILE A 178   O    91.3  84.8                                        
REMARK 620 4 HOH A 520   O    86.4  84.4 168.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 306  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 536   O                                                      
REMARK 620 2 HOH A 556   O    92.3                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 306                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 308                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 309                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 310                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 311                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 312                 
DBREF  6GZ8 A   76   213  UNP    P39072   GERM_BACSU      76    213             
SEQRES   1 A  138  THR VAL MET ARG GLU LEU TYR LEU ILE ASP LYS ASN GLY          
SEQRES   2 A  138  TYR VAL VAL ALA GLN THR LEU PRO LEU PRO LYS SER GLU          
SEQRES   3 A  138  SER THR ALA LYS GLN ALA LEU GLU TYR LEU VAL GLN GLY          
SEQRES   4 A  138  GLY PRO VAL SER GLU ILE LEU PRO ASN GLY PHE ARG ALA          
SEQRES   5 A  138  VAL LEU PRO ALA ASP THR THR VAL ASN VAL ASP ILE LYS          
SEQRES   6 A  138  LYS ASP GLY THR ALA ILE ALA ASP PHE SER ASN GLU PHE          
SEQRES   7 A  138  LYS ASN TYR LYS LYS GLU ASP GLU GLN LYS ILE VAL GLN          
SEQRES   8 A  138  SER VAL THR TRP THR LEU THR GLN PHE SER SER ILE ASP          
SEQRES   9 A  138  LYS VAL LYS LEU ARG ILE ASN GLY HIS GLU LEU LYS GLU          
SEQRES  10 A  138  MET PRO VAL GLY GLY THR PRO ILE SER ASP ASP LEU SER          
SEQRES  11 A  138  ARG LYS ASP GLY ILE ASN LEU GLU                              
HET     NA  A 301       1                                                       
HET     NA  A 302       1                                                       
HET     NA  A 303       1                                                       
HET     NA  A 304       1                                                       
HET     NA  A 305       1                                                       
HET     NA  A 306       1                                                       
HET     NA  A 307       1                                                       
HET     NA  A 308       1                                                       
HET     NA  A 309       1                                                       
HET     NA  A 310       1                                                       
HET     NA  A 311       1                                                       
HET    EDO  A 312      10                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2   NA    11(NA 1+)                                                    
FORMUL  13  EDO    C2 H6 O2                                                     
FORMUL  14  HOH   *184(H2 O)                                                    
HELIX    1 AA1 SER A  102  TYR A  110  1                                   9    
HELIX    2 AA2 GLY A  115  LEU A  121  5                                   7    
HELIX    3 AA3 ASN A  151  ASN A  155  5                                   5    
HELIX    4 AA4 LYS A  157  GLU A  159  5                                   3    
HELIX    5 AA5 ASP A  160  GLN A  174  1                                  15    
SHEET    1 AA1 2 VAL A  77  ILE A  84  0                                        
SHEET    2 AA1 2 VAL A  90  LEU A  97 -1  O  LEU A  97   N  VAL A  77           
SHEET    1 AA2 4 VAL A 135  ILE A 139  0                                        
SHEET    2 AA2 4 THR A 144  PHE A 149 -1  O  ILE A 146   N  ASP A 138           
SHEET    3 AA2 4 LYS A 180  ILE A 185  1  O  ARG A 184   N  PHE A 149           
SHEET    4 AA2 4 HIS A 188  GLU A 189 -1  O  HIS A 188   N  ILE A 185           
LINK         OD2 ASP A  85                NA    NA A 308     1555   1555  2.67  
LINK         O   ASN A  87                NA    NA A 302     1555   1555  2.66  
LINK         O   PRO A  98                NA    NA A 310     1555   1555  2.88  
LINK         O   LYS A  99                NA    NA A 304     1555   1555  2.76  
LINK         O   LYS A  99                NA    NA A 303     1555   1555  2.84  
LINK         O   GLU A 101                NA    NA A 305     1555   1555  3.15  
LINK         OG1 THR A 103                NA    NA A 305     1555   1555  3.01  
LINK         OE1 GLN A 106                NA    NA A 310     1555   1555  2.73  
LINK         O   LYS A 140                NA    NA A 309     1555   1555  2.72  
LINK         OE2 GLU A 159                NA    NA A 311     1555   1555  2.71  
LINK         O   THR A 173                NA    NA A 301     1555   1555  2.40  
LINK         O   PHE A 175                NA    NA A 301     1555   1555  2.38  
LINK         O   SER A 177                NA    NA A 309     1555   1555  2.72  
LINK         O   ILE A 178                NA    NA A 301     1555   1555  2.33  
LINK        NA    NA A 301                 O   HOH A 520     1555   1555  2.44  
LINK        NA    NA A 302                 O   HOH A 460     1555   1555  2.76  
LINK        NA    NA A 305                 O   HOH A 523     1555   1555  3.18  
LINK        NA    NA A 305                 O   HOH A 496     1555   1555  3.07  
LINK        NA    NA A 306                 O   HOH A 536     1555   1555  2.96  
LINK        NA    NA A 306                 O   HOH A 556     1555   1555  3.00  
LINK        NA    NA A 307                 O   HOH A 559     1555   1555  2.85  
LINK        NA    NA A 308                 O   HOH A 559     1555   1555  2.88  
LINK        NA    NA A 311                 O   HOH A 580     1555   1555  3.10  
LINK         O   SER A 176                NA    NA A 304     1555   4465  2.88  
LINK        NA    NA A 302                 O   HOH A 514     1555   3644  2.70  
LINK        NA    NA A 309                 O   HOH A 423     1555   4465  2.66  
LINK        NA    NA A 311                 O   HOH A 503     1555   3644  2.73  
SITE     1 AC1  6 THR A 173  PHE A 175  ILE A 178   NA A 303                    
SITE     2 AC1  6  NA A 304  HOH A 520                                          
SITE     1 AC2  3 ASN A  87  HOH A 460  HOH A 514                               
SITE     1 AC3  5 LYS A  99  THR A 173  ILE A 178   NA A 301                    
SITE     2 AC3  5  NA A 304                                                     
SITE     1 AC4  6 LYS A  99  PHE A 175  SER A 176  ILE A 178                    
SITE     2 AC4  6  NA A 301   NA A 303                                          
SITE     1 AC5  4 GLU A 101  SER A 102  THR A 103  HOH A 496                    
SITE     1 AC6  5 GLN A 113  PRO A 130  ALA A 131  HOH A 536                    
SITE     2 AC6  5 HOH A 556                                                     
SITE     1 AC7  6 ASP A  85  LYS A  86  ASN A 123  GLY A 124                    
SITE     2 AC7  6 PHE A 125  HOH A 559                                          
SITE     1 AC8  2 ASP A  85  HOH A 559                                          
SITE     1 AC9  5 ILE A 139  LYS A 140  GLY A 143  SER A 177                    
SITE     2 AC9  5 HOH A 423                                                     
SITE     1 AD1  4 VAL A  77  ARG A  79  PRO A  98  GLN A 106                    
SITE     1 AD2  4 LYS A 105  ASN A 136  GLU A 159  HOH A 503                    
SITE     1 AD3  4 ASP A 148  LYS A 157  GLU A 159  HOH A 432                    
CRYST1   38.360   53.601   64.861  90.00  90.00  90.00 P 21 21 21    4          
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      0.026069  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018656  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015418        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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