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Database: PDB
Entry: 4EOB
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Original site: 4EOB 
HEADER    HYDROLASE                               13-APR-12   4EOB              
TITLE     STRUCTURE OF THE TYPE VI PEPTIDOGLYCAN AMIDASE EFFECTOR TSE1 FROM     
TITLE    2 PSEUDOMONAS AERUGINOSA                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYPE VI AMIDASE EFFECTOR TSE1;                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 STRAIN: PAO1;                                                        
SOURCE   5 GENE: PA1844;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SHUFFLE BL21;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET29B                                    
KEYWDS    AMIDASE, HYDROLASE, PROTEASE, BACTERIOLYTIC, PEPTIDOGLYCAN DEGRADING, 
KEYWDS   2 TSI1, PA1845                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CHOU,J.D.MOUGOUS                                                    
REVDAT   4   27-MAR-13 4EOB    1       JRNL                                     
REVDAT   3   11-JUL-12 4EOB    1       JRNL                                     
REVDAT   2   06-JUN-12 4EOB    1       JRNL   TITLE                             
REVDAT   1   30-MAY-12 4EOB    0                                                
JRNL        AUTH   S.CHOU,N.K.BUI,A.B.RUSSELL,K.W.LEXA,T.E.GARDINER,M.LEROUX,   
JRNL        AUTH 2 W.VOLLMER,J.D.MOUGOUS                                        
JRNL        TITL   STRUCTURE OF A PEPTIDOGLYCAN AMIDASE EFFECTOR TARGETED TO    
JRNL        TITL 2 GRAM-NEGATIVE BACTERIA BY THE TYPE VI SECRETION SYSTEM.      
JRNL        REF    CELL REP                      V.   1   656 2012              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   22813741                                                     
JRNL        DOI    10.1016/J.CELREP.2012.05.016                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1047)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.32                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 20654                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.710                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3732                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 45.3307 -  7.8193    0.98     1345   142  0.1863 0.2289        
REMARK   3     2  7.8193 -  6.2115    0.97     1357   145  0.1739 0.2462        
REMARK   3     3  6.2115 -  5.4278    0.97     1312   147  0.2201 0.2568        
REMARK   3     4  5.4278 -  4.9322    0.97     1328   146  0.1804 0.1941        
REMARK   3     5  4.9322 -  4.5790    0.98     1359   151  0.1556 0.2149        
REMARK   3     6  4.5790 -  4.3093    0.98     1327   147  0.1456 0.1834        
REMARK   3     7  4.3093 -  4.0936    0.98     1362   151  0.1518 0.1824        
REMARK   3     8  4.0936 -  3.9155    0.98     1354   125  0.1646 0.2526        
REMARK   3     9  3.9155 -  3.7649    0.97     1372   136  0.1597 0.2287        
REMARK   3    10  3.7649 -  3.6350    0.97     1353   176  0.1588 0.1942        
REMARK   3    11  3.6350 -  3.5214    0.96     1273   126  0.1793 0.2685        
REMARK   3    12  3.5214 -  3.4208    0.96     1338   145  0.1887 0.2410        
REMARK   3    13  3.4208 -  3.3308    0.96     1348   152  0.1860 0.2301        
REMARK   3    14  3.3308 -  3.2495    0.96     1279   129  0.1961 0.2032        
REMARK   3    15  3.2495 -  3.1757    0.94     1313   137  0.2003 0.2561        
REMARK   3    16  3.1757 -  3.1081    0.94     1324   150  0.2134 0.3028        
REMARK   3    17  3.1081 -  3.0459    0.93     1275   140  0.2195 0.2555        
REMARK   3    18  3.0459 -  2.9885    0.93     1224   115  0.2236 0.3094        
REMARK   3    19  2.9885 -  2.9351    0.92     1298   144  0.2257 0.2825        
REMARK   3    20  2.9351 -  2.8854    0.90     1272   126  0.2121 0.2436        
REMARK   3    21  2.8854 -  2.8388    0.92     1265   141  0.2050 0.3024        
REMARK   3    22  2.8388 -  2.7952    0.88     1219   112  0.2177 0.3221        
REMARK   3    23  2.7952 -  2.7541    0.90     1180   150  0.2189 0.3122        
REMARK   3    24  2.7541 -  2.7153    0.88     1216   132  0.2403 0.3163        
REMARK   3    25  2.7153 -  2.6786    0.86     1251   121  0.2370 0.3346        
REMARK   3    26  2.6786 -  2.6438    0.85     1114   139  0.2404 0.3252        
REMARK   3    27  2.6438 -  2.6108    0.76     1048   107  0.2432 0.3617        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.270           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.11                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.74750                                              
REMARK   3    B22 (A**2) : -10.29110                                            
REMARK   3    B33 (A**2) : 6.41740                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 8.04280                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           4453                                  
REMARK   3   ANGLE     :  1.130           6033                                  
REMARK   3   CHIRALITY :  0.078            652                                  
REMARK   3   PLANARITY :  0.004            784                                  
REMARK   3   DIHEDRAL  : 14.163           1569                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4EOB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071867.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : KHOZU DOUBLE FLAT CRYSTAL          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20654                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.610                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.320                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.23400                            
REMARK 200  R SYM                      (I) : 0.23400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.61                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX PHASER                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 100MM SODIUM          
REMARK 280  THIOCYANATE, 18% PEG3350, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 297K                                                    
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       53.78900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     ASP A     2                                                      
REMARK 465     LEU A   150                                                      
REMARK 465     PRO A   151                                                      
REMARK 465     ARG A   152                                                      
REMARK 465     ALA A   153                                                      
REMARK 465     SER A   154                                                      
REMARK 465     LEU A   155                                                      
REMARK 465     GLU A   156                                                      
REMARK 465     HIS A   157                                                      
REMARK 465     HIS A   158                                                      
REMARK 465     HIS A   159                                                      
REMARK 465     HIS A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     HIS A   162                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     LEU B   150                                                      
REMARK 465     PRO B   151                                                      
REMARK 465     ARG B   152                                                      
REMARK 465     ALA B   153                                                      
REMARK 465     SER B   154                                                      
REMARK 465     LEU B   155                                                      
REMARK 465     GLU B   156                                                      
REMARK 465     HIS B   157                                                      
REMARK 465     HIS B   158                                                      
REMARK 465     HIS B   159                                                      
REMARK 465     HIS B   160                                                      
REMARK 465     HIS B   161                                                      
REMARK 465     HIS B   162                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     PRO C   151                                                      
REMARK 465     ARG C   152                                                      
REMARK 465     ALA C   153                                                      
REMARK 465     SER C   154                                                      
REMARK 465     LEU C   155                                                      
REMARK 465     GLU C   156                                                      
REMARK 465     HIS C   157                                                      
REMARK 465     HIS C   158                                                      
REMARK 465     HIS C   159                                                      
REMARK 465     HIS C   160                                                      
REMARK 465     HIS C   161                                                      
REMARK 465     HIS C   162                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     LEU D   150                                                      
REMARK 465     PRO D   151                                                      
REMARK 465     ARG D   152                                                      
REMARK 465     ALA D   153                                                      
REMARK 465     SER D   154                                                      
REMARK 465     LEU D   155                                                      
REMARK 465     GLU D   156                                                      
REMARK 465     HIS D   157                                                      
REMARK 465     HIS D   158                                                      
REMARK 465     HIS D   159                                                      
REMARK 465     HIS D   160                                                      
REMARK 465     HIS D   161                                                      
REMARK 465     HIS D   162                                                      
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     ARG A 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B   4    CG   CD1  CD2                                       
REMARK 470     LYS B 104    CG   CD   CE   NZ                                   
REMARK 470     GLN C 103    CG   CD   OE1  NE2                                  
REMARK 470     ARG C 132    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 135    CG   CD   NE   CZ   NH1  NH2                        
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   O    HOH D   228     O    HOH D   237              1.91            
REMARK 500   O    ARG A    47     O    HOH A   223              2.05            
REMARK 500   O    SER A   144     O    HOH A   241              2.07            
REMARK 500   NH1  ARG D   137     O    HOH D   242              2.10            
REMARK 500   O    HOH A   231     O    HOH C   232              2.11            
REMARK 500   O    HOH B   221     O    HOH B   224              2.12            
REMARK 500   NZ   LYS B    27     O    HOH B   202              2.13            
REMARK 500   NZ   LYS D    18     O    HOH D   202              2.15            
REMARK 500   SG   CYS D    30     O    HOH D   241              2.16            
REMARK 500   O    HOH D   239     O    HOH D   243              2.16            
REMARK 500   O    VAL D   117     O    HOH D   214              2.17            
REMARK 500   OD1  ASN D    26     O    HOH D   225              2.19            
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    LEU A  84      110.55   -163.65                                   
REMARK 500    LYS A 104      -41.19   -155.90                                   
REMARK 500    SER A 112      132.84   -171.21                                   
REMARK 500    GLN A 121       41.73   -104.67                                   
REMARK 500    ASP B   5       20.53   -142.85                                   
REMARK 500    SER B  60      -13.94   -147.67                                   
REMARK 500    LEU B  84      112.27   -160.60                                   
REMARK 500    LYS B 104      -56.04   -151.76                                   
REMARK 500    ALA B 146      -62.19   -108.72                                   
REMARK 500    ARG C 102       41.06     35.44                                   
REMARK 500    LYS C 104      -38.79   -149.10                                   
REMARK 500    SER C 149     -141.14    -97.41                                   
REMARK 500    LEU D  84      112.79   -161.12                                   
REMARK 500    LYS D 104      -57.32   -145.41                                   
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 238        DISTANCE =  5.36 ANGSTROMS                       
DBREF  4EOB A    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4EOB B    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4EOB C    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
DBREF  4EOB D    1   154  UNP    Q9I2Q1   Q9I2Q1_PSEAE     1    154             
SEQADV 4EOB LEU A  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB GLU A  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS A  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS A  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS A  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS A  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS A  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS A  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB LEU B  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB GLU B  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS B  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS B  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS B  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS B  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS B  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS B  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB LEU C  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB GLU C  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS C  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS C  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS C  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS C  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS C  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS C  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB LEU D  155  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB GLU D  156  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS D  157  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS D  158  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS D  159  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS D  160  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS D  161  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQADV 4EOB HIS D  162  UNP  Q9I2Q1              EXPRESSION TAG                 
SEQRES   1 A  162  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 A  162  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 A  162  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 A  162  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 A  162  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 A  162  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 A  162  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 A  162  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 A  162  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 A  162  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 A  162  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 A  162  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER LEU GLU          
SEQRES  13 A  162  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  162  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 B  162  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 B  162  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 B  162  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 B  162  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 B  162  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 B  162  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 B  162  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 B  162  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 B  162  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 B  162  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 B  162  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER LEU GLU          
SEQRES  13 B  162  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 C  162  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 C  162  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 C  162  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 C  162  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 C  162  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 C  162  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 C  162  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 C  162  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 C  162  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 C  162  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 C  162  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 C  162  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER LEU GLU          
SEQRES  13 C  162  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 D  162  MET ASP SER LEU ASP GLN CYS ILE VAL ASN ALA CYS LYS          
SEQRES   2 D  162  ASN SER TRP ASP LYS SER TYR LEU ALA GLY THR PRO ASN          
SEQRES   3 D  162  LYS ASP ASN CYS SER GLY PHE VAL GLN SER VAL ALA ALA          
SEQRES   4 D  162  GLU LEU GLY VAL PRO MET PRO ARG GLY ASN ALA ASN ALA          
SEQRES   5 D  162  MET VAL ASP GLY LEU GLU GLN SER TRP THR LYS LEU ALA          
SEQRES   6 D  162  SER GLY ALA GLU ALA ALA GLN LYS ALA ALA GLN GLY PHE          
SEQRES   7 D  162  LEU VAL ILE ALA GLY LEU LYS GLY ARG THR TYR GLY HIS          
SEQRES   8 D  162  VAL ALA VAL VAL ILE SER GLY PRO LEU TYR ARG GLN LYS          
SEQRES   9 D  162  TYR PRO MET CYS TRP CYS GLY SER ILE ALA GLY ALA VAL          
SEQRES  10 D  162  GLY GLN SER GLN GLY LEU LYS SER VAL GLY GLN VAL TRP          
SEQRES  11 D  162  ASN ARG THR ASP ARG ASP ARG LEU ASN TYR TYR VAL TYR          
SEQRES  12 D  162  SER LEU ALA SER CYS SER LEU PRO ARG ALA SER LEU GLU          
SEQRES  13 D  162  HIS HIS HIS HIS HIS HIS                                      
FORMUL   5  HOH   *161(H2 O)                                                    
HELIX    1   1 ASP A    5  TRP A   16  1                                  12    
HELIX    2   2 PRO A   25  ASP A   28  5                                   4    
HELIX    3   3 ASN A   29  GLU A   40  1                                  12    
HELIX    4   4 ASN A   49  TRP A   61  1                                  13    
HELIX    5   5 SER A   66  GLN A   76  1                                  11    
HELIX    6   6 LEU A  100  LYS A  104  5                                   5    
HELIX    7   7 GLY A  115  GLN A  119  5                                   5    
HELIX    8   8 VAL A  126  TRP A  130  1                                   5    
HELIX    9   9 THR A  133  LEU A  138  5                                   6    
HELIX   10  10 ASP B    5  TRP B   16  1                                  12    
HELIX   11  11 PRO B   25  ASP B   28  5                                   4    
HELIX   12  12 ASN B   29  GLY B   42  1                                  14    
HELIX   13  13 ASN B   49  GLN B   59  1                                  11    
HELIX   14  14 SER B   66  GLN B   76  1                                  11    
HELIX   15  15 GLY B  115  GLN B  119  5                                   5    
HELIX   16  16 VAL B  126  TRP B  130  1                                   5    
HELIX   17  17 THR B  133  LEU B  138  5                                   6    
HELIX   18  18 ASP C    5  TRP C   16  1                                  12    
HELIX   19  19 PRO C   25  ASP C   28  5                                   4    
HELIX   20  20 ASN C   29  LEU C   41  1                                  13    
HELIX   21  21 ASN C   49  TRP C   61  1                                  13    
HELIX   22  22 SER C   66  GLN C   76  1                                  11    
HELIX   23  23 ARG C  102  LYS C  104  5                                   3    
HELIX   24  24 GLY C  115  GLN C  119  5                                   5    
HELIX   25  25 VAL C  126  TRP C  130  1                                   5    
HELIX   26  26 ASP C  134  LEU C  138  5                                   5    
HELIX   27  27 ASP D    5  TRP D   16  1                                  12    
HELIX   28  28 PRO D   25  ASP D   28  5                                   4    
HELIX   29  29 ASN D   29  GLY D   42  1                                  14    
HELIX   30  30 ASN D   49  TRP D   61  1                                  13    
HELIX   31  31 SER D   66  GLN D   76  1                                  11    
HELIX   32  32 LEU D  100  LYS D  104  5                                   5    
HELIX   33  33 VAL D  126  TRP D  130  1                                   5    
HELIX   34  34 THR D  133  ARG D  137  5                                   5    
SHEET    1   A 6 THR A  62  LEU A  64  0                                        
SHEET    2   A 6 ASN A 139  VAL A 142 -1  O  TYR A 140   N  LEU A  64           
SHEET    3   A 6 VAL A  80  LEU A  84 -1  N  ILE A  81   O  TYR A 141           
SHEET    4   A 6 HIS A  91  VAL A  95 -1  O  VAL A  95   N  VAL A  80           
SHEET    5   A 6 MET A 107  CYS A 110 -1  O  TRP A 109   N  VAL A  94           
SHEET    6   A 6 SER A 120  SER A 125 -1  O  SER A 120   N  CYS A 110           
SHEET    1   B 6 THR B  62  LYS B  63  0                                        
SHEET    2   B 6 ASN B 139  VAL B 142 -1  O  VAL B 142   N  THR B  62           
SHEET    3   B 6 VAL B  80  LEU B  84 -1  N  GLY B  83   O  ASN B 139           
SHEET    4   B 6 HIS B  91  VAL B  95 -1  O  ALA B  93   N  ALA B  82           
SHEET    5   B 6 MET B 107  CYS B 110 -1  O  TRP B 109   N  VAL B  94           
SHEET    6   B 6 SER B 120  SER B 125 -1  O  SER B 120   N  CYS B 110           
SHEET    1   C 6 THR C  62  LEU C  64  0                                        
SHEET    2   C 6 ASN C 139  VAL C 142 -1  O  VAL C 142   N  THR C  62           
SHEET    3   C 6 VAL C  80  LEU C  84 -1  N  ILE C  81   O  TYR C 141           
SHEET    4   C 6 HIS C  91  TYR C 101 -1  O  VAL C  95   N  VAL C  80           
SHEET    5   C 6 TYR C 105  CYS C 108 -1  O  TYR C 105   N  TYR C 101           
SHEET    6   C 6 LYS C 124  SER C 125 -1  O  LYS C 124   N  CYS C 108           
SHEET    1   D 6 THR D  62  LEU D  64  0                                        
SHEET    2   D 6 ASN D 139  VAL D 142 -1  O  TYR D 140   N  LEU D  64           
SHEET    3   D 6 VAL D  80  LEU D  84 -1  N  ILE D  81   O  TYR D 141           
SHEET    4   D 6 HIS D  91  VAL D  95 -1  O  ALA D  93   N  ALA D  82           
SHEET    5   D 6 MET D 107  CYS D 110 -1  O  TRP D 109   N  VAL D  94           
SHEET    6   D 6 SER D 120  SER D 125 -1  O  SER D 120   N  CYS D 110           
SSBOND   1 CYS A    7    CYS A  148                          1555   1555  2.02  
SSBOND   2 CYS B    7    CYS B  148                          1555   1555  2.03  
SSBOND   3 CYS C    7    CYS C  148                          1555   1555  2.04  
SSBOND   4 CYS D    7    CYS D  148                          1555   1555  2.04  
LINK         SG  CYS A   7                 SG  CYS A 148     1555   1555  2.02  
LINK         SG  CYS B   7                 SG  CYS B 148     1555   1555  2.03  
LINK         SG  CYS C   7                 SG  CYS C 148     1555   1555  2.04  
LINK         SG  CYS D   7                 SG  CYS D 148     1555   1555  2.04  
CISPEP   1 LEU B  145    ALA B  146          0       -24.54                     
CISPEP   2 ALA B  146    SER B  147          0        -0.08                     
CRYST1   38.662  107.578   84.396  90.00  94.23  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      0.025865  0.000000  0.001913        0.00000                         
SCALE2      0.000000  0.009296  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011881        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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