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Database: PDB
Entry: 3ZK7
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HEADER    METAL TRANSPORT                         22-JAN-13   3ZK7              
TITLE     CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA IN THE METAL-  
TITLE    2 FREE, OPEN STATE                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MANGANESE ABC TRANSPORTER SUBSTRATE-BINDING LIPOPROTEIN;   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 23-309;                                           
COMPND   5 SYNONYM: PNEUMOCOCCAL SURFACE ADHESIN A, PSAA;                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_COMMON: PNEUMOCOCCUS;                                       
SOURCE   4 ORGANISM_TAXID: 1313;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    METAL TRANSPORT, ATP-BINDING CASSETTE TRANSPORTERS, LIPOPROTEIN,      
KEYWDS   2 MEMBRANE TRANSPORT PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.M.COUNAGO,M.P.WEEN,M.BAJAJ,J.ZUEGG,M.A.COOPER,A.G.MCEWAN,J.C.PATON, 
AUTHOR   2 B.KOBE,C.A.MCDEVITT                                                  
REVDAT   7   20-DEC-23 3ZK7    1       REMARK                                   
REVDAT   6   06-MAR-19 3ZK7    1       REMARK                                   
REVDAT   5   28-MAR-18 3ZK7    1       JRNL   ATOM                              
REVDAT   4   08-JAN-14 3ZK7    1       JRNL                                     
REVDAT   3   20-NOV-13 3ZK7    1       JRNL                                     
REVDAT   2   13-NOV-13 3ZK7    1       JRNL                                     
REVDAT   1   06-NOV-13 3ZK7    0                                                
JRNL        AUTH   R.M.COUNAGO,M.P.WEEN,S.L.BEGG,M.BAJAJ,J.ZUEGG,M.L.O'MARA,    
JRNL        AUTH 2 M.A.COOPER,A.G.MCEWAN,J.C.PATON,B.KOBE,C.A.MCDEVITT          
JRNL        TITL   IMPERFECT COORDINATION CHEMISTRY FACILITATES METAL ION       
JRNL        TITL 2 RELEASE IN THE PSA PERMEASE.                                 
JRNL        REF    NAT. CHEM. BIOL.              V.  10    35 2014              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   24212134                                                     
JRNL        DOI    10.1038/NCHEMBIO.1382                                        
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.C.LAWRENCE,P.A.PILLING,V.C.EPA,A.M.BERRY,A.D.OGUNNIYI,     
REMARK   1  AUTH 2 J.C.PATON                                                    
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA   
REMARK   1  TITL 2 REVEALS A METAL-BINDING SITE AND A NOVEL STRUCTURE FOR A     
REMARK   1  TITL 3 PUTATIVE ABC-TYPE BINDING PROTEIN.                           
REMARK   1  REF    STRUCTURE                     V.   6  1553 1998              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1  PMID   9862808                                                      
REMARK   1  DOI    10.1016/S0969-2126(98)00153-1                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.A.MCDEVITT,A.D.OGUNNIYI,E.VALKOV,M.C.LAWRENCE,B.KOBE,      
REMARK   1  AUTH 2 A.G.MCEWAN,J.C.PATON                                         
REMARK   1  TITL   A MOLECULAR MECHANISM FOR BACTERIAL SUSCEPTIBILITY TO ZINC.  
REMARK   1  REF    PLOS PATHOG.                  V.   7 02357 2011              
REMARK   1  REFN                   ISSN 1553-7366                               
REMARK   1  PMID   22072971                                                     
REMARK   1  DOI    10.1371/JOURNAL.PPAT.1002357                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 57796                          
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)  : 0.163                          
REMARK   3   R VALUE            (WORKING SET)  : 0.161                          
REMARK   3   FREE R VALUE                      : 0.192                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.070                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2930                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.69                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.73                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.56                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4069                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2041                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3861                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2031                   
REMARK   3   BIN FREE R VALUE                        : 0.2241                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.11                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 208                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4432                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 667                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.88                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.77460                                             
REMARK   3    B22 (A**2) : 0.29820                                              
REMARK   3    B33 (A**2) : 1.47650                                              
REMARK   3    B12 (A**2) : -1.07260                                             
REMARK   3    B13 (A**2) : 0.16740                                              
REMARK   3    B23 (A**2) : -0.48550                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.194               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.103               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.097               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.142               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.098               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 9004   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 16380  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2570   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 148    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1226   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 9004   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 602    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 9973   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.05                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.26                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 3.02                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|32 - 123 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):    1.1117  -18.3272   36.7110           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0225 T22:   -0.0695                                    
REMARK   3     T33:   -0.0563 T12:    0.0247                                    
REMARK   3     T13:    0.0299 T23:   -0.0246                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5050 L22:    2.2364                                    
REMARK   3     L33:    0.7251 L12:   -0.0636                                    
REMARK   3     L13:   -0.0866 L23:    0.4325                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0139 S12:    0.0074 S13:   -0.0652                     
REMARK   3     S21:   -0.0533 S22:   -0.0240 S23:    0.0005                     
REMARK   3     S31:    0.0716 S32:   -0.0009 S33:    0.0380                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|124 - 145 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   -4.2923   -3.1507   47.4210           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0258 T22:   -0.0529                                    
REMARK   3     T33:   -0.0461 T12:    0.0108                                    
REMARK   3     T13:    0.0177 T23:   -0.0277                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.3971 L22:    1.5810                                    
REMARK   3     L33:    3.4711 L12:   -0.6402                                    
REMARK   3     L13:   -3.4272 L23:    0.1503                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1007 S12:    0.0780 S13:   -0.1036                     
REMARK   3     S21:    0.2212 S22:    0.0501 S23:    0.0815                     
REMARK   3     S31:    0.1524 S32:   -0.1749 S33:    0.0506                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|146 - 196 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   15.3198   -7.8880   45.0847           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0288 T22:    0.0330                                    
REMARK   3     T33:    0.0738 T12:    0.0455                                    
REMARK   3     T13:   -0.0319 T23:   -0.0420                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4953 L22:    2.4540                                    
REMARK   3     L33:    0.5035 L12:   -0.0698                                    
REMARK   3     L13:   -0.0715 L23:    0.1506                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0665 S12:   -0.1280 S13:   -0.0089                     
REMARK   3     S21:    0.1287 S22:    0.0767 S23:   -0.4825                     
REMARK   3     S31:    0.0552 S32:    0.1280 S33:   -0.0101                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { A|197 - 309 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.7245    8.8984   34.9286           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0342 T22:   -0.0596                                    
REMARK   3     T33:   -0.0469 T12:    0.0035                                    
REMARK   3     T13:    0.0148 T23:   -0.0423                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7561 L22:    1.7698                                    
REMARK   3     L33:    1.3660 L12:   -0.2217                                    
REMARK   3     L13:    0.5090 L23:   -0.4084                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0927 S12:   -0.0646 S13:    0.0504                     
REMARK   3     S21:   -0.1198 S22:    0.0498 S23:   -0.0226                     
REMARK   3     S31:   -0.1612 S32:   -0.0696 S33:    0.0429                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { B|32 - 123 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):    0.7988   -5.2281   11.0108           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0446 T22:   -0.0634                                    
REMARK   3     T33:   -0.0371 T12:   -0.0110                                    
REMARK   3     T13:   -0.0226 T23:   -0.0246                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5648 L22:    2.4524                                    
REMARK   3     L33:    1.0659 L12:   -0.1549                                    
REMARK   3     L13:   -0.3596 L23:    0.0570                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0288 S12:    0.0261 S13:    0.0426                     
REMARK   3     S21:    0.0946 S22:   -0.0717 S23:   -0.0713                     
REMARK   3     S31:   -0.0908 S32:   -0.0098 S33:    0.0429                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { B|124 - 145 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.4783  -20.3834    0.1873           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0207 T22:   -0.0306                                    
REMARK   3     T33:    0.0029 T12:    0.0167                                    
REMARK   3     T13:   -0.0219 T23:   -0.0411                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9575 L22:    0.8311                                    
REMARK   3     L33:    3.6013 L12:    0.1418                                    
REMARK   3     L13:    2.0435 L23:    0.6269                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0139 S12:   -0.1715 S13:    0.0308                     
REMARK   3     S21:   -0.1462 S22:   -0.1414 S23:    0.0556                     
REMARK   3     S31:   -0.0646 S32:   -0.2689 S33:    0.1553                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { B|146 - 196 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   15.8630  -14.5426    2.6527           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1070 T22:    0.0201                                    
REMARK   3     T33:    0.1143 T12:   -0.0001                                    
REMARK   3     T13:    0.0539 T23:    0.0158                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2572 L22:    4.1951                                    
REMARK   3     L33:    0.8650 L12:   -0.5760                                    
REMARK   3     L13:   -0.0035 L23:    0.3157                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0321 S12:    0.1203 S13:    0.1208                     
REMARK   3     S21:   -0.2440 S22:   -0.0254 S23:   -0.7581                     
REMARK   3     S31:   -0.0548 S32:    0.1330 S33:   -0.0067                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { B|197 - 309 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):    1.0056  -32.5192   12.3719           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0620 T22:   -0.0567                                    
REMARK   3     T33:   -0.0363 T12:    0.0120                                    
REMARK   3     T13:   -0.0075 T23:   -0.0303                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5454 L22:    2.8560                                    
REMARK   3     L33:    0.7845 L12:   -0.0898                                    
REMARK   3     L13:    0.0427 L23:   -0.1231                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0051 S12:    0.0102 S13:   -0.0342                     
REMARK   3     S21:    0.1276 S22:   -0.0157 S23:    0.0081                     
REMARK   3     S31:    0.0946 S32:   -0.0033 S33:    0.0209                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ZK7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290055509.                                   
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                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95369                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                   (SI111)                            
REMARK 200  OPTICS                         : SILICON MIRRORS (ADAPTIVE AND U    
REMARK 200                                   -BENT)                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57796                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 17.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1PSZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5% W/V PEG 1,000 12.5% W/V PEG        
REMARK 280  3,350, 12.5% V/V MPD; 0.1 M TRIZMA/BICINE PH 8.7 AFTER 7-10 DAYS    
REMARK 280  AT 293 K, FOLLOWING STREAK-SEEDING OF PRE-EQUILIBRATED (24 HOURS)   
REMARK 280  DROPS                                                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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    ILE A  90       47.40     38.27                                   
REMARK 500    LYS A 113      -59.20   -127.82                                   
REMARK 500    HIS A 139       46.70    -84.38                                   
REMARK 500    LYS B 113      -59.11   -128.81                                   
REMARK 500    HIS B 139       40.14    -84.41                                   
REMARK 500    THR B 279      -70.05   -120.18                                   
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 A2013        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH A2329        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH A2330        DISTANCE =  6.45 ANGSTROMS                       
REMARK 525    HOH B2128        DISTANCE =  7.29 ANGSTROMS                       
REMARK 525    HOH B2338        DISTANCE =  6.16 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 1310                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 1310                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 1311                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 1311                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ZK8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA E205Q IN THE  
REMARK 900 METAL-FREE, OPEN STATE                                               
REMARK 900 RELATED ID: 3ZK9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA D280N IN THE  
REMARK 900 METAL-FREE, OPEN STATE                                               
REMARK 900 RELATED ID: 3ZKA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA D280N IN THE  
REMARK 900 METAL-BOUND, OPEN STATE                                              
REMARK 900 RELATED ID: 3ZTT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA WITH          
REMARK 900 MANGANESE                                                            
DBREF  3ZK7 A   32   309  UNP    P0A4G2   MTSA_STRPN      32    309             
DBREF  3ZK7 B   32   309  UNP    P0A4G2   MTSA_STRPN      32    309             
SEQRES   1 A  278  LYS LEU LYS VAL VAL ALA THR ASN SER ILE ILE ALA ASP          
SEQRES   2 A  278  ILE THR LYS ASN ILE ALA GLY ASP LYS ILE ASP LEU HIS          
SEQRES   3 A  278  SER ILE VAL PRO ILE GLY GLN ASP PRO HIS GLU TYR GLU          
SEQRES   4 A  278  PRO LEU PRO GLU ASP VAL LYS LYS THR SER GLU ALA ASP          
SEQRES   5 A  278  LEU ILE PHE TYR ASN GLY ILE ASN LEU GLU THR GLY GLY          
SEQRES   6 A  278  ASN ALA TRP PHE THR LYS LEU VAL GLU ASN ALA LYS LYS          
SEQRES   7 A  278  THR GLU ASN LYS ASP TYR PHE ALA VAL SER ASP GLY VAL          
SEQRES   8 A  278  ASP VAL ILE TYR LEU GLU GLY GLN ASN GLU LYS GLY LYS          
SEQRES   9 A  278  GLU ASP PRO HIS ALA TRP LEU ASN LEU GLU ASN GLY ILE          
SEQRES  10 A  278  ILE PHE ALA LYS ASN ILE ALA LYS GLN LEU SER ALA LYS          
SEQRES  11 A  278  ASP PRO ASN ASN LYS GLU PHE TYR GLU LYS ASN LEU LYS          
SEQRES  12 A  278  GLU TYR THR ASP LYS LEU ASP LYS LEU ASP LYS GLU SER          
SEQRES  13 A  278  LYS ASP LYS PHE ASN LYS ILE PRO ALA GLU LYS LYS LEU          
SEQRES  14 A  278  ILE VAL THR SER GLU GLY ALA PHE LYS TYR PHE SER LYS          
SEQRES  15 A  278  ALA TYR GLY VAL PRO SER ALA TYR ILE TRP GLU ILE ASN          
SEQRES  16 A  278  THR GLU GLU GLU GLY THR PRO GLU GLN ILE LYS THR LEU          
SEQRES  17 A  278  VAL GLU LYS LEU ARG GLN THR LYS VAL PRO SER LEU PHE          
SEQRES  18 A  278  VAL GLU SER SER VAL ASP ASP ARG PRO MET LYS THR VAL          
SEQRES  19 A  278  SER GLN ASP THR ASN ILE PRO ILE TYR ALA GLN ILE PHE          
SEQRES  20 A  278  THR ASP SER ILE ALA GLU GLN GLY LYS GLU GLY ASP SER          
SEQRES  21 A  278  TYR TYR SER MET MET LYS TYR ASN LEU ASP LYS ILE ALA          
SEQRES  22 A  278  GLU GLY LEU ALA LYS                                          
SEQRES   1 B  278  LYS LEU LYS VAL VAL ALA THR ASN SER ILE ILE ALA ASP          
SEQRES   2 B  278  ILE THR LYS ASN ILE ALA GLY ASP LYS ILE ASP LEU HIS          
SEQRES   3 B  278  SER ILE VAL PRO ILE GLY GLN ASP PRO HIS GLU TYR GLU          
SEQRES   4 B  278  PRO LEU PRO GLU ASP VAL LYS LYS THR SER GLU ALA ASP          
SEQRES   5 B  278  LEU ILE PHE TYR ASN GLY ILE ASN LEU GLU THR GLY GLY          
SEQRES   6 B  278  ASN ALA TRP PHE THR LYS LEU VAL GLU ASN ALA LYS LYS          
SEQRES   7 B  278  THR GLU ASN LYS ASP TYR PHE ALA VAL SER ASP GLY VAL          
SEQRES   8 B  278  ASP VAL ILE TYR LEU GLU GLY GLN ASN GLU LYS GLY LYS          
SEQRES   9 B  278  GLU ASP PRO HIS ALA TRP LEU ASN LEU GLU ASN GLY ILE          
SEQRES  10 B  278  ILE PHE ALA LYS ASN ILE ALA LYS GLN LEU SER ALA LYS          
SEQRES  11 B  278  ASP PRO ASN ASN LYS GLU PHE TYR GLU LYS ASN LEU LYS          
SEQRES  12 B  278  GLU TYR THR ASP LYS LEU ASP LYS LEU ASP LYS GLU SER          
SEQRES  13 B  278  LYS ASP LYS PHE ASN LYS ILE PRO ALA GLU LYS LYS LEU          
SEQRES  14 B  278  ILE VAL THR SER GLU GLY ALA PHE LYS TYR PHE SER LYS          
SEQRES  15 B  278  ALA TYR GLY VAL PRO SER ALA TYR ILE TRP GLU ILE ASN          
SEQRES  16 B  278  THR GLU GLU GLU GLY THR PRO GLU GLN ILE LYS THR LEU          
SEQRES  17 B  278  VAL GLU LYS LEU ARG GLN THR LYS VAL PRO SER LEU PHE          
SEQRES  18 B  278  VAL GLU SER SER VAL ASP ASP ARG PRO MET LYS THR VAL          
SEQRES  19 B  278  SER GLN ASP THR ASN ILE PRO ILE TYR ALA GLN ILE PHE          
SEQRES  20 B  278  THR ASP SER ILE ALA GLU GLN GLY LYS GLU GLY ASP SER          
SEQRES  21 B  278  TYR TYR SER MET MET LYS TYR ASN LEU ASP LYS ILE ALA          
SEQRES  22 B  278  GLU GLY LEU ALA LYS                                          
HET    TRS  A1310      20                                                       
HET    TRS  A1311      20                                                       
HET    TRS  B1310      20                                                       
HET    TRS  B1311      20                                                       
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   3  TRS    4(C4 H12 N O3 1+)                                            
FORMUL   7  HOH   *667(H2 O)                                                    
HELIX    1   1 ASN A   39  GLY A   51  1                                  13    
HELIX    2   2 LEU A   72  ALA A   82  1                                  11    
HELIX    3   3 ALA A   98  ALA A  107  1                                  10    
HELIX    4   4 LEU A  127  GLN A  130  5                                   4    
HELIX    5   5 HIS A  139  LEU A  142  5                                   4    
HELIX    6   6 ASN A  143  ASP A  162  1                                  20    
HELIX    7   7 ASN A  165  ILE A  194  1                                  30    
HELIX    8   8 PRO A  195  LYS A  199  5                                   5    
HELIX    9   9 PHE A  208  GLY A  216  1                                   9    
HELIX   10  10 THR A  232  ARG A  244  1                                  13    
HELIX   11  11 ASP A  259  ASN A  270  1                                  12    
HELIX   12  12 SER A  291  LYS A  309  1                                  19    
HELIX   13  13 ASN B   39  GLY B   51  1                                  13    
HELIX   14  14 LEU B   72  ALA B   82  1                                  11    
HELIX   15  15 ASN B   91  GLU B   93  5                                   3    
HELIX   16  16 THR B   94  ALA B  107  1                                  14    
HELIX   17  17 LEU B  127  GLN B  130  5                                   4    
HELIX   18  18 HIS B  139  LEU B  142  5                                   4    
HELIX   19  19 ASN B  143  ASP B  162  1                                  20    
HELIX   20  20 ASN B  165  ILE B  194  1                                  30    
HELIX   21  21 PRO B  195  LYS B  199  5                                   5    
HELIX   22  22 PHE B  208  GLY B  216  1                                   9    
HELIX   23  23 THR B  232  ARG B  244  1                                  13    
HELIX   24  24 ASP B  259  ASN B  270  1                                  12    
HELIX   25  25 SER B  291  LYS B  309  1                                  19    
SHEET    1  AA 4 ILE A  54  SER A  58  0                                        
SHEET    2  AA 4 LEU A  33  ALA A  37  1  O  LEU A  33   N  ASP A  55           
SHEET    3  AA 4 LEU A  84  TYR A  87  1  O  LEU A  84   N  VAL A  36           
SHEET    4  AA 4 TYR A 115  ALA A 117  1  O  PHE A 116   N  TYR A  87           
SHEET    1  AB 2 ILE A 201  GLU A 205  0                                        
SHEET    2  AB 2 SER A 219  TRP A 223  1  O  ALA A 220   N  THR A 203           
SHEET    1  AC 2 LEU A 251  GLU A 254  0                                        
SHEET    2  AC 2 ILE A 273  ILE A 277  1  N  TYR A 274   O  LEU A 251           
SHEET    1  BA 4 ILE B  54  SER B  58  0                                        
SHEET    2  BA 4 LEU B  33  ALA B  37  1  O  LEU B  33   N  ASP B  55           
SHEET    3  BA 4 LEU B  84  TYR B  87  1  O  LEU B  84   N  VAL B  36           
SHEET    4  BA 4 TYR B 115  ALA B 117  1  O  PHE B 116   N  TYR B  87           
SHEET    1  BB 2 ILE B 201  GLU B 205  0                                        
SHEET    2  BB 2 SER B 219  TRP B 223  1  O  ALA B 220   N  THR B 203           
SHEET    1  BC 2 LEU B 251  GLU B 254  0                                        
SHEET    2  BC 2 ILE B 273  ILE B 277  1  N  TYR B 274   O  LEU B 251           
SITE     1 AC1  9 ILE A  62  GLY A  63  GLN A  64  HIS B  57                    
SITE     2 AC1  9 SER B  58  ILE B  59  TYR B  69  GLU B  74                    
SITE     3 AC1  9 ASP B  75                                                     
SITE     1 AC2 10 HIS A  57  SER A  58  ILE A  59  TYR A  69                    
SITE     2 AC2 10 GLU A  74  ASP A  75  HOH A2032  ILE B  62                    
SITE     3 AC2 10 GLY B  63  GLN B  64                                          
SITE     1 AC3  6 ASP B  65  HIS B  67  HIS B 139  GLU B 205                    
SITE     2 AC3  6 ASP B 280  HOH B2293                                          
SITE     1 AC4  5 ASP A  65  HIS A  67  HIS A 139  GLU A 205                    
SITE     2 AC4  5 ASP A 280                                                     
CRYST1   40.940   59.910   62.630 107.02 103.90  96.96 P 1           2          
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      0.024426  0.002982  0.007470        0.00000                         
SCALE2      0.000000  0.016816  0.005958        0.00000                         
SCALE3      0.000000  0.000000  0.017450        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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