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Database: PDB
Entry: 4MP6
LinkDB: 4MP6
Original site: 4MP6 
HEADER    OXIDOREDUCTASE                          12-SEP-13   4MP6              
TITLE     STAPHYLOFERRIN B PRECURSOR BIOSYNTHETIC ENZYME SBNB BOUND TO CITRATE  
TITLE    2 AND NAD+                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE ORNITHINE CYCLODEAMINASE;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;            
SOURCE   3 ORGANISM_TAXID: 196620;                                              
SOURCE   4 STRAIN: NEWMAN;                                                      
SOURCE   5 GENE: SBNB;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    SIDEROPHORE, L-DAP SYNTHESIS, ACEGA DEHYDROGENASE, OXIDOREDUCTASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.GRIGG,M.J.KOBYLARZ,D.K.RAI,M.E.P.MURPHY                           
REVDAT   4   28-FEB-24 4MP6    1       REMARK SEQADV                            
REVDAT   3   15-NOV-17 4MP6    1       REMARK                                   
REVDAT   2   09-APR-14 4MP6    1       JRNL                                     
REVDAT   1   05-MAR-14 4MP6    0                                                
JRNL        AUTH   M.J.KOBYLARZ,J.C.GRIGG,S.J.TAKAYAMA,D.K.RAI,D.E.HEINRICHS,   
JRNL        AUTH 2 M.E.MURPHY                                                   
JRNL        TITL   SYNTHESIS OF L-2,3-DIAMINOPROPIONIC ACID, A SIDEROPHORE AND  
JRNL        TITL 2 ANTIBIOTIC PRECURSOR.                                        
JRNL        REF    CHEM.BIOL.                    V.  21   379 2014              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   24485762                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2013.12.011                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 19067                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 981                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1289                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2637                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 57                                      
REMARK   3   SOLVENT ATOMS            : 129                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.52000                                             
REMARK   3    B22 (A**2) : -0.52000                                             
REMARK   3    B33 (A**2) : 1.05000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.264         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.204         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.152         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.844        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2802 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3811 ; 1.468 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   344 ; 6.496 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   138 ;40.247 ;25.290       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   482 ;16.609 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;20.323 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   419 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2150 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1364 ; 0.800 ; 0.978       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1712 ; 1.440 ; 1.464       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1438 ; 0.826 ; 1.178       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A    45                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1204   4.5618 -11.1264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2396 T22:   0.2104                                     
REMARK   3      T33:   0.2230 T12:  -0.0226                                     
REMARK   3      T13:   0.0045 T23:  -0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8872 L22:   0.4626                                     
REMARK   3      L33:   0.5128 L12:  -0.1754                                     
REMARK   3      L13:   0.4548 L23:   0.0738                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0434 S12:   0.2202 S13:   0.2699                       
REMARK   3      S21:  -0.0269 S22:   0.0086 S23:  -0.0130                       
REMARK   3      S31:   0.0771 S32:   0.0351 S33:   0.0348                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    46        A    97                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.6797  -0.6829   4.6248              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2101 T22:   0.3109                                     
REMARK   3      T33:   0.2469 T12:   0.0654                                     
REMARK   3      T13:   0.0261 T23:  -0.0594                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3326 L22:   1.3163                                     
REMARK   3      L33:   2.7244 L12:   0.5357                                     
REMARK   3      L13:  -0.0207 L23:   1.0391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0080 S12:  -0.0059 S13:   0.1143                       
REMARK   3      S21:  -0.0601 S22:  -0.0920 S23:   0.2493                       
REMARK   3      S31:  -0.0066 S32:  -0.3334 S33:   0.1001                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    98        A   168                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.9408   9.5846  -8.4410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2723 T22:   0.2496                                     
REMARK   3      T33:   0.2494 T12:  -0.0224                                     
REMARK   3      T13:  -0.0515 T23:  -0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0770 L22:   0.5636                                     
REMARK   3      L33:   0.2197 L12:  -1.1848                                     
REMARK   3      L13:  -0.2237 L23:   0.0022                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2632 S12:   0.0453 S13:   0.3409                       
REMARK   3      S21:   0.0522 S22:   0.1392 S23:  -0.1721                       
REMARK   3      S31:   0.0782 S32:  -0.0641 S33:   0.1240                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   169        A   258                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.4723  10.9383  -0.8285              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2640 T22:   0.2880                                     
REMARK   3      T33:   0.2175 T12:   0.0483                                     
REMARK   3      T13:  -0.0072 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7075 L22:   1.3182                                     
REMARK   3      L33:   0.5480 L12:  -1.2455                                     
REMARK   3      L13:  -0.0082 L23:   0.4591                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6096 S12:  -0.1918 S13:   0.0264                       
REMARK   3      S21:   0.2822 S22:   0.3919 S23:   0.1537                       
REMARK   3      S31:   0.0475 S32:  -0.0085 S33:   0.2177                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   259        A   274                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.6425 -11.5748  -0.9167              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2935 T22:   0.0471                                     
REMARK   3      T33:   0.9416 T12:   0.0929                                     
REMARK   3      T13:   0.4321 T23:   0.1810                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3281 L22:  23.7804                                     
REMARK   3      L33:   0.0013 L12:  -2.7690                                     
REMARK   3      L13:   0.0191 L23:  -0.1525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2126 S12:  -0.0439 S13:  -0.0519                       
REMARK   3      S21:   1.3602 S22:   0.2482 S23:  -0.1696                       
REMARK   3      S31:  -0.0167 S32:  -0.0052 S33:  -0.0356                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   275        A   336                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4381   1.7208 -12.9418              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2541 T22:   0.2311                                     
REMARK   3      T33:   0.2288 T12:  -0.0331                                     
REMARK   3      T13:   0.0065 T23:  -0.0641                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9774 L22:   0.3031                                     
REMARK   3      L33:   0.1440 L12:  -0.4651                                     
REMARK   3      L13:   0.2495 L23:  -0.0072                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1772 S12:   0.2467 S13:  -0.3053                       
REMARK   3      S21:  -0.0644 S22:   0.0537 S23:   0.0611                       
REMARK   3      S31:  -0.0052 S32:   0.0352 S33:   0.1235                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 4MP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000082191.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SIDE SCATTERING I-BEAM BENT        
REMARK 200                                   SINGLE CRYSTAL; ASYMMETRIC CUT     
REMARK 200                                   4.9650 DEG.                        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19090                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM CITRATE TRIBASIC, PH      
REMARK 280  7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.53950            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.33000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.33000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       39.26975            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.33000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.33000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      117.80925            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.33000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.33000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       39.26975            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.33000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.33000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      117.80925            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       78.53950            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
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   NH2  ARG A    10     OG   SER A   116              2.07            
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    GLN A  42       86.55   -154.13                                   
REMARK 500    ASN A 234       59.87    -92.73                                   
REMARK 500    ILE A 237      -56.39     73.21                                   
REMARK 500    ASN A 260       31.40    -88.46                                   
REMARK 500    LYS A 263       47.50    -87.95                                   
REMARK 500    GLU A 272     -167.21    -73.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4M54   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH N-(1-AMINO-1-CARBOXYL-2-ETHYL)-      
REMARK 900 GLUTAMIC ACID AND NADH                                               
REMARK 900 RELATED ID: 4MP3   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN APO SELENOMETHIONINE                                
REMARK 900 RELATED ID: 4MP8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4MPD   RELATED DB: PDB                                   
DBREF  4MP6 A    1   336  UNP    Q8NYS7   Q8NYS7_STAAW     1    336             
SEQADV 4MP6 GLY A   -2  UNP  Q8NYS7              EXPRESSION TAG                 
SEQADV 4MP6 SER A   -1  UNP  Q8NYS7              EXPRESSION TAG                 
SEQADV 4MP6 HIS A    0  UNP  Q8NYS7              EXPRESSION TAG                 
SEQRES   1 A  339  GLY SER HIS MET ASN ARG GLU MET LEU TYR LEU ASN ARG          
SEQRES   2 A  339  SER ASP ILE GLU GLN ALA GLY GLY ASN HIS SER GLN VAL          
SEQRES   3 A  339  TYR VAL ASP ALA LEU THR GLU ALA LEU THR ALA HIS ALA          
SEQRES   4 A  339  HIS ASN ASP PHE VAL GLN PRO LEU LYS PRO TYR LEU ARG          
SEQRES   5 A  339  GLN ASP PRO GLU ASN GLY HIS ILE ALA ASP ARG ILE ILE          
SEQRES   6 A  339  ALA MET PRO SER HIS ILE GLY GLY GLU HIS ALA ILE SER          
SEQRES   7 A  339  GLY ILE LYS TRP ILE GLY SER LYS HIS ASP ASN PRO SER          
SEQRES   8 A  339  LYS ARG ASN MET GLU ARG ALA SER GLY VAL ILE ILE LEU          
SEQRES   9 A  339  ASN ASP PRO GLU THR ASN TYR PRO ILE ALA VAL MET GLU          
SEQRES  10 A  339  ALA SER LEU ILE SER SER MET ARG THR ALA ALA VAL SER          
SEQRES  11 A  339  VAL ILE ALA ALA LYS HIS LEU ALA LYS LYS GLY PHE LYS          
SEQRES  12 A  339  ASP LEU THR ILE ILE GLY CYS GLY LEU ILE GLY ASP LYS          
SEQRES  13 A  339  GLN LEU GLN SER MET LEU GLU GLN PHE ASP HIS ILE GLU          
SEQRES  14 A  339  ARG VAL PHE VAL TYR ASP GLN PHE SER GLU ALA CYS ALA          
SEQRES  15 A  339  ARG PHE VAL ASP ARG TRP GLN GLN GLN ARG PRO GLU ILE          
SEQRES  16 A  339  ASN PHE ILE ALA THR GLU ASN ALA LYS GLU ALA VAL SER          
SEQRES  17 A  339  ASN GLY GLU VAL VAL ILE THR CYS THR VAL THR ASP GLN          
SEQRES  18 A  339  PRO TYR ILE GLU TYR ASP TRP LEU GLN LYS GLY ALA PHE          
SEQRES  19 A  339  ILE SER ASN ILE SER ILE MET ASP VAL HIS LYS GLU VAL          
SEQRES  20 A  339  PHE ILE LYS ALA ASP LYS VAL VAL VAL ASP ASP TRP SER          
SEQRES  21 A  339  GLN CYS ASN ARG GLU LYS LYS THR ILE ASN GLN LEU VAL          
SEQRES  22 A  339  LEU GLU GLY LYS PHE SER LYS GLU ALA LEU HIS ALA GLU          
SEQRES  23 A  339  LEU GLY GLN LEU VAL THR GLY ASP ILE PRO GLY ARG GLU          
SEQRES  24 A  339  ASP ASP ASP GLU ILE ILE LEU LEU ASN PRO MET GLY MET          
SEQRES  25 A  339  ALA ILE GLU ASP ILE SER SER ALA TYR PHE ILE TYR GLN          
SEQRES  26 A  339  GLN ALA GLN GLN GLN ASN ILE GLY THR THR LEU ASN LEU          
SEQRES  27 A  339  TYR                                                          
HET    NAD  A 400      44                                                       
HET    CIT  A 401      13                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     CIT CITRIC ACID                                                      
FORMUL   2  NAD    C21 H27 N7 O14 P2                                            
FORMUL   3  CIT    C6 H8 O7                                                     
FORMUL   4  HOH   *129(H2 O)                                                    
HELIX    1   1 ASN A    9  ALA A   16  1                                   8    
HELIX    2   2 SER A   21  HIS A   37  1                                  17    
HELIX    3   3 ASP A   85  ASN A   91  1                                   7    
HELIX    4   4 ALA A  115  ALA A  135  1                                  21    
HELIX    5   5 GLY A  148  PHE A  162  1                                  15    
HELIX    6   6 PHE A  174  ARG A  189  1                                  16    
HELIX    7   7 ASN A  199  ASN A  206  1                                   8    
HELIX    8   8 GLU A  222  LEU A  226  5                                   5    
HELIX    9   9 HIS A  241  ALA A  248  1                                   8    
HELIX   10  10 LYS A  264  GLU A  272  1                                   9    
HELIX   11  11 LEU A  284  THR A  289  1                                   6    
HELIX   12  12 MET A  309  GLN A  327  1                                  19    
SHEET    1   A 3 PHE A  40  VAL A  41  0                                        
SHEET    2   A 3 ARG A  60  ILE A  68 -1  O  HIS A  67   N  VAL A  41           
SHEET    3   A 3 TYR A  47  LEU A  48 -1  N  LEU A  48   O  ILE A  61           
SHEET    1   B 7 PHE A  40  VAL A  41  0                                        
SHEET    2   B 7 ARG A  60  ILE A  68 -1  O  HIS A  67   N  VAL A  41           
SHEET    3   B 7 ILE A  74  SER A  82 -1  O  GLY A  76   N  SER A  66           
SHEET    4   B 7 ALA A  95  ASN A 102 -1  O  VAL A  98   N  TRP A  79           
SHEET    5   B 7 PRO A 109  GLU A 114 -1  O  ILE A 110   N  LEU A 101           
SHEET    6   B 7 GLU A   4  LEU A   8  1  N  LEU A   8   O  GLU A 114           
SHEET    7   B 7 THR A 331  ASN A 334 -1  O  THR A 331   N  TYR A   7           
SHEET    1   C 8 ASN A 193  ALA A 196  0                                        
SHEET    2   C 8 ARG A 167  TYR A 171  1  N  VAL A 170   O  ILE A 195           
SHEET    3   C 8 ASP A 141  ILE A 145  1  N  LEU A 142   O  PHE A 169           
SHEET    4   C 8 VAL A 209  THR A 212  1  O  VAL A 209   N  THR A 143           
SHEET    5   C 8 PHE A 231  SER A 233  1  O  SER A 233   N  VAL A 210           
SHEET    6   C 8 ILE A 302  ASN A 305  1  O  LEU A 304   N  ILE A 232           
SHEET    7   C 8 LYS A 250  VAL A 253  1  N  VAL A 252   O  LEU A 303           
SHEET    8   C 8 ALA A 282  GLU A 283  1  O  ALA A 282   N  VAL A 253           
SITE     1 AC1 25 HIS A  37  ARG A  94  ARG A 122  THR A 123                    
SITE     2 AC1 25 GLY A 146  GLY A 148  LEU A 149  ILE A 150                    
SITE     3 AC1 25 ASP A 172  GLN A 173  CYS A 213  THR A 214                    
SITE     4 AC1 25 VAL A 215  ILE A 235  PRO A 306  GLY A 308                    
SITE     5 AC1 25 CIT A 401  HOH A 505  HOH A 529  HOH A 535                    
SITE     6 AC1 25 HOH A 540  HOH A 549  HOH A 572  HOH A 597                    
SITE     7 AC1 25 HOH A 618                                                     
SITE     1 AC2 11 LYS A  45  ARG A  60  ILE A  62  MET A  64                    
SITE     2 AC2 11 LYS A  78  ARG A  94  ARG A 122  GLY A 308                    
SITE     3 AC2 11 NAD A 400  HOH A 603  HOH A 628                               
CRYST1   62.660   62.660  157.079  90.00  90.00  90.00 P 41 21 2     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      0.015959  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015959  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006366        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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