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Database: PDB
Entry: 3N9B
LinkDB: 3N9B
Original site: 3N9B 
HEADER    LIGASE                                  28-MAY-10   3N9B              
TITLE     CRYSTAL STRUCTURE OF THE P. AERUGINOSA LIGD PHOSPHOESTERASE DOMAIN    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE ATP-DEPENDENT DNA LIGASE;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PHOSPHOESTERASE DOMAIN;                                    
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 STRAIN: PAO1;                                                        
SOURCE   5 GENE: LIGD, PA2138;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) RIL+;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    PHOSPHOESTERASE, METALLOENZYME, LIGASE, NHEJ, MANGANESE, BETA BARREL  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SHUMAN,P.NAIR,P.SMITH                                               
REVDAT   2   15-SEP-10 3N9B    1       TITLE                                    
REVDAT   1   11-AUG-10 3N9B    0                                                
JRNL        AUTH   P.A.NAIR,P.SMITH,S.SHUMAN                                    
JRNL        TITL   STRUCTURE OF BACTERIAL LIGD 3'-PHOSPHOESTERASE UNVEILS A DNA 
JRNL        TITL 2 REPAIR SUPERFAMILY                                           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107 12822 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20616014                                                     
JRNL        DOI    10.1073/PNAS.1005830107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.92 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6_289)                      
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) : 1.92                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.40                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.060                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 23992                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.153                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2387                            
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 37.4023 -  4.1348    1.00     2292   268  0.1364 0.1645        
REMARK   3     2  4.1348 -  3.2826    0.99     2325   254  0.1239 0.1807        
REMARK   3     3  3.2826 -  2.8678    1.00     2340   247  0.1507 0.1962        
REMARK   3     4  2.8678 -  2.6057    1.00     2353   223  0.1598 0.2094        
REMARK   3     5  2.6057 -  2.4189    0.99     2272   263  0.1515 0.2057        
REMARK   3     6  2.4189 -  2.2763    0.94     2195   244  0.1620 0.2095        
REMARK   3     7  2.2763 -  2.1624    0.70     1597   200  0.1725 0.2545        
REMARK   3     8  2.1624 -  2.0682    0.94     2170   239  0.1386 0.2045        
REMARK   3     9  2.0682 -  1.9886    0.92     2149   241  0.1376 0.2206        
REMARK   3    10  1.9886 -  1.9200    0.82     1912   208  0.1666 0.2438        
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              : 0.34                                          
REMARK   3   B_SOL              : 53.78                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.32120                                              
REMARK   3    B22 (A**2) : -1.63510                                             
REMARK   3    B33 (A**2) : -3.73020                                             
REMARK   3    B12 (A**2) : -1.27090                                             
REMARK   3    B13 (A**2) : -1.18420                                             
REMARK   3    B23 (A**2) : 0.47540                                              
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      :  0.010           2617                                  
REMARK   3   ANGLE     :  1.249           3556                                  
REMARK   3   CHIRALITY :  0.100            370                                  
REMARK   3   PLANARITY :  0.005            463                                  
REMARK   3   DIHEDRAL  : 14.969            993                                  
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 3N9B COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059542.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-10; 20-FEB-10; 10-FEB-10    
REMARK 200  TEMPERATURE           (KELVIN) : 130; NULL; NULL                    
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; N                            
REMARK 200  RADIATION SOURCE               : NSLS; NSLS; ROTATING ANODE         
REMARK 200  BEAMLINE                       : X12C; X25; NULL                    
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; RIGAKU RU300           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL; NULL                      
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.19 0.99 0.73; 1.19 0.99 0.73;    
REMARK 200                                   1.54                               
REMARK 200  MONOCHROMATOR                  : SEE BEAMLINE DOCUMENTATION;        
REMARK 200                                   NULL; NULL                         
REMARK 200  OPTICS                         : SEE NSLS X25 BEAMLINE              
REMARK 200                                   DESCRIPTION; SEE NSLS X12C         
REMARK 200                                   BEAMLINE DESCRIPTION; OSMIC        
REMARK 200                                   CONFOCAL MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD; IMAGE PLATE              
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC QUANTUM     
REMARK 200                                   210; RIGAKU RAXIS IV++             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24596                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.920                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL; NULL                  
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION WAS CARRIED OUT IN       
REMARK 280  SITTING-DROP VAPOR-DIFFUSION SETUPS WITH 1:1 MIXTURES OF PROTEIN    
REMARK 280  SOLUTION CONTAINING 1.3 MM PAEPEC2 AND 2MM MNCL2 AND RESERVOIR      
REMARK 280  SOLUTION CONTAINING PEG 5000 MONOMETHYLETHER (MME) (20 - 30%),      
REMARK 280  100 MM 2-(N-MORPHOLINO) ETHANESULFONIC ACID (MES) PH 6.8 - 7.0,     
REMARK 280  200 MM AMMONIUM SULFATE, AND 10 MM YTTRIUM (III) CHLORIDE AT 22     
REMARK 280  C. , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                
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 300 REMARK: PROTEIN IS MONOMER IN SOLUTION, HOWEVER, TWO PROTOMERS ARE   
REMARK 300 FOUND IN THE ASYMMETRIC UNIT,                                        
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 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     ARG A    17                                                      
REMARK 465     GLN A    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     PRO A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     ARG A    25                                                      
REMARK 465     LYS A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     ARG A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     ASP A    30                                                      
REMARK 465     SER A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     GLY A    98                                                      
REMARK 465     HIS A    99                                                      
REMARK 465     TYR A   100                                                      
REMARK 465     GLY A   101                                                      
REMARK 465     THR A   186                                                      
REMARK 465     LEU A   187                                                      
REMARK 465     ARG B    17                                                      
REMARK 465     GLN B    18                                                      
REMARK 465     THR B    19                                                      
REMARK 465     PRO B    20                                                      
REMARK 465     GLU B    21                                                      
REMARK 465     PRO B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     GLY B    24                                                      
REMARK 465     ARG B    25                                                      
REMARK 465     LYS B    26                                                      
REMARK 465     PRO B    27                                                      
REMARK 465     ARG B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     GLY B    98                                                      
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     GLN A  97    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  30    CG   OD1  OD2                                       
REMARK 470     GLN B  97    CG   CD   OE1  NE2                                  
REMARK 470     HIS B  99    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLN B    80     O    HOH B   241              2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD1  ASP A   104     O    HOH A   264     1655     2.12            
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    VAL A  81     -165.37   -124.03                                   
REMARK 500    ASP A 118      109.61    -37.38                                   
REMARK 500    ASP A 162     -168.33   -167.03                                   
REMARK 500    ALA B  44     -161.93    -78.36                                   
REMARK 500    VAL B  81     -165.48   -123.34                                   
REMARK 500    ASP B 118      108.46    -33.98                                   
REMARK 500    LYS B 151       21.77   -143.52                                   
REMARK 500    GLU B 184       42.55   -103.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 188  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  48   NE2                                                    
REMARK 620 2 ASP B  50   OD2 100.1                                              
REMARK 620 3 HIS B  42   ND1  94.8 101.0                                        
REMARK 620 4 SO4 B   1   O3  166.2  90.2  92.2                                  
REMARK 620 5 HOH B 225   O    88.2  92.1 165.8  82.2                            
REMARK 620 6 HOH B 208   O    85.7 166.4  90.6  82.3  75.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 A 191   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SO4 A   4   O4                                                     
REMARK 620 2 GLU A 184   OE2 128.8                                              
REMARK 620 3 ASP A 179   OD2  86.4  76.6                                        
REMARK 620 4 GLU A 184   OE1  78.4  56.1  95.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 188  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  48   NE2                                                    
REMARK 620 2 ASP A  50   OD2  98.2                                              
REMARK 620 3 SO4 A   2   O1  164.1  92.5                                        
REMARK 620 4 HIS A  42   ND1  95.7 100.3  93.9                                  
REMARK 620 5 HOH A 244   O    84.9  92.4  83.0 167.1                            
REMARK 620 6 HOH A 267   O    86.9 167.3  80.3  90.6  76.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 A 190   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SO4 A   3   O4                                                     
REMARK 620 2 GLU A 135   OE1 128.1                                              
REMARK 620 3 GLU A 135   OE2  79.9  51.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 A 189   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 124   OE2                                                    
REMARK 620 2 GLU A 124   OE1  48.2                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 188                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 A 189                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 A 190                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 A 191                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 188                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3N9D   RELATED DB: PDB                                   
DBREF  3N9B A   17   187  UNP    Q9I1X7   Q9I1X7_PSEAE    17    187             
DBREF  3N9B B   17   187  UNP    Q9I1X7   Q9I1X7_PSEAE    17    187             
SEQRES   1 A  171  ARG GLN THR PRO GLU PRO SER GLY ARG LYS PRO ARG LYS          
SEQRES   2 A  171  ASP SER THR GLY LEU LEU ARG TYR CYS VAL GLN LYS HIS          
SEQRES   3 A  171  ASP ALA SER ARG LEU HIS TYR ASP PHE ARG LEU GLU LEU          
SEQRES   4 A  171  ASP GLY THR LEU LYS SER TRP ALA VAL PRO LYS GLY PRO          
SEQRES   5 A  171  CYS LEU ASP PRO ALA VAL LYS ARG LEU ALA VAL GLN VAL          
SEQRES   6 A  171  GLU ASP HIS PRO LEU ASP TYR ALA ASP PHE GLU GLY SER          
SEQRES   7 A  171  ILE PRO GLN GLY HIS TYR GLY ALA GLY ASP VAL ILE VAL          
SEQRES   8 A  171  TRP ASP ARG GLY ALA TRP THR PRO LEU ASP ASP PRO ARG          
SEQRES   9 A  171  GLU GLY LEU GLU LYS GLY HIS LEU SER PHE ALA LEU ASP          
SEQRES  10 A  171  GLY GLU LYS LEU SER GLY ARG TRP HIS LEU ILE ARG THR          
SEQRES  11 A  171  ASN LEU ARG GLY LYS GLN SER GLN TRP PHE LEU VAL LYS          
SEQRES  12 A  171  ALA LYS ASP GLY GLU ALA ARG SER LEU ASP ARG PHE ASP          
SEQRES  13 A  171  VAL LEU LYS GLU ARG PRO ASP SER VAL LEU SER GLU ARG          
SEQRES  14 A  171  THR LEU                                                      
SEQRES   1 B  171  ARG GLN THR PRO GLU PRO SER GLY ARG LYS PRO ARG LYS          
SEQRES   2 B  171  ASP SER THR GLY LEU LEU ARG TYR CYS VAL GLN LYS HIS          
SEQRES   3 B  171  ASP ALA SER ARG LEU HIS TYR ASP PHE ARG LEU GLU LEU          
SEQRES   4 B  171  ASP GLY THR LEU LYS SER TRP ALA VAL PRO LYS GLY PRO          
SEQRES   5 B  171  CYS LEU ASP PRO ALA VAL LYS ARG LEU ALA VAL GLN VAL          
SEQRES   6 B  171  GLU ASP HIS PRO LEU ASP TYR ALA ASP PHE GLU GLY SER          
SEQRES   7 B  171  ILE PRO GLN GLY HIS TYR GLY ALA GLY ASP VAL ILE VAL          
SEQRES   8 B  171  TRP ASP ARG GLY ALA TRP THR PRO LEU ASP ASP PRO ARG          
SEQRES   9 B  171  GLU GLY LEU GLU LYS GLY HIS LEU SER PHE ALA LEU ASP          
SEQRES  10 B  171  GLY GLU LYS LEU SER GLY ARG TRP HIS LEU ILE ARG THR          
SEQRES  11 B  171  ASN LEU ARG GLY LYS GLN SER GLN TRP PHE LEU VAL LYS          
SEQRES  12 B  171  ALA LYS ASP GLY GLU ALA ARG SER LEU ASP ARG PHE ASP          
SEQRES  13 B  171  VAL LEU LYS GLU ARG PRO ASP SER VAL LEU SER GLU ARG          
SEQRES  14 B  171  THR LEU                                                      
HET    SO4  A   2       5                                                       
HET    SO4  A   3       5                                                       
HET    SO4  A   4       5                                                       
HET     CL  A   5       1                                                       
HET    PEG  A   6       7                                                       
HET     MN  A 188       1                                                       
HET    YT3  A   1       1                                                       
HET    YT3  A 189       1                                                       
HET    YT3  A 190       1                                                       
HET    YT3  A 191       1                                                       
HET    SO4  B   1       5                                                       
HET     MN  B 188       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     YT3 YTTRIUM (III) ION                                                
FORMUL   3  SO4    4(O4 S 2-)                                                   
FORMUL   6   CL    CL 1-                                                        
FORMUL   7  PEG    C4 H10 O3                                                    
FORMUL   8   MN    2(MN 2+)                                                     
FORMUL   9  YT3    4(Y 3+)                                                      
FORMUL  15  HOH   *358(H2 O)                                                    
HELIX    1   1 PRO A   85  PHE A   91  5                                   7    
HELIX    2   2 ASP A  118  GLY A  126  1                                   9    
HELIX    3   3 ASP A  172  ARG A  177  1                                   6    
HELIX    4   4 PRO B   85  PHE B   91  5                                   7    
HELIX    5   5 ASP B  118  GLY B  126  1                                   9    
HELIX    6   6 ASP B  172  ARG B  177  1                                   6    
SHEET    1   A10 GLY A  93  SER A  94  0                                        
SHEET    2   A10 ASP A 104  PRO A 115 -1  O  VAL A 105   N  GLY A  93           
SHEET    3   A10 HIS A 127  GLY A 134 -1  O  ASP A 133   N  ALA A 112           
SHEET    4   A10 SER A 138  ARG A 145 -1  O  TRP A 141   N  PHE A 130           
SHEET    5   A10 GLN A 154  LYS A 159 -1  O  VAL A 158   N  HIS A 142           
SHEET    6   A10 ARG A  76  HIS A  84 -1  N  ARG A  76   O  LEU A 157           
SHEET    7   A10 THR A  58  VAL A  64 -1  N  ALA A  63   O  VAL A  79           
SHEET    8   A10 LEU A  47  LEU A  55 -1  N  TYR A  49   O  VAL A  64           
SHEET    9   A10 LEU A  35  ASP A  43 -1  N  GLN A  40   O  ASP A  50           
SHEET   10   A10 ASP A 104  PRO A 115 -1  O  ASP A 109   N  VAL A  39           
SHEET    1   B10 GLY B  93  ILE B  95  0                                        
SHEET    2   B10 GLY B 103  PRO B 115 -1  O  VAL B 105   N  GLY B  93           
SHEET    3   B10 HIS B 127  GLY B 134 -1  O  ASP B 133   N  ALA B 112           
SHEET    4   B10 GLY B 139  ARG B 145 -1  O  TRP B 141   N  PHE B 130           
SHEET    5   B10 GLN B 154  LYS B 159 -1  O  VAL B 158   N  HIS B 142           
SHEET    6   B10 ARG B  76  HIS B  84 -1  N  ALA B  78   O  TRP B 155           
SHEET    7   B10 THR B  58  VAL B  64 -1  N  ALA B  63   O  VAL B  79           
SHEET    8   B10 LEU B  47  LEU B  55 -1  N  TYR B  49   O  VAL B  64           
SHEET    9   B10 ARG B  36  ASP B  43 -1  N  CYS B  38   O  ARG B  52           
SHEET   10   B10 GLY B 103  PRO B 115 -1  O  GLY B 111   N  TYR B  37           
LINK         NE2 HIS B  48                MN    MN B 188     1555   1555  2.15  
LINK         OD2 ASP B  50                MN    MN B 188     1555   1555  2.16  
LINK         O4  SO4 A   4                 Y   YT3 A 191     1555   1555  2.17  
LINK         NE2 HIS A  48                MN    MN A 188     1555   1555  2.17  
LINK         OD2 ASP A  50                MN    MN A 188     1555   1555  2.19  
LINK         ND1 HIS B  42                MN    MN B 188     1555   1555  2.20  
LINK         O1  SO4 A   2                MN    MN A 188     1555   1555  2.22  
LINK         O4  SO4 A   3                 Y   YT3 A 190     1555   1555  2.27  
LINK         OE2 GLU A 184                 Y   YT3 A 191     1555   1555  2.28  
LINK         ND1 HIS A  42                MN    MN A 188     1555   1555  2.31  
LINK         O3  SO4 B   1                MN    MN B 188     1555   1555  2.32  
LINK        MN    MN B 188                 O   HOH B 225     1555   1555  2.33  
LINK         OD2 ASP A 179                 Y   YT3 A 191     1555   1555  2.35  
LINK         Y   YT3 A 190                 O   HOH A 215     1555   1555  2.37  
LINK         Y   YT3 A 191                 O   HOH A 232     1555   1555  2.42  
LINK         OD1 ASP A 179                 Y   YT3 A   1     1555   1555  2.44  
LINK         OE1 GLU A 184                 Y   YT3 A 191     1555   1555  2.46  
LINK         Y   YT3 A   1                 O   HOH A 226     1555   1555  2.47  
LINK         OE1 GLU A 135                 Y   YT3 A 190     1555   1555  2.48  
LINK         Y   YT3 A 190                 O   HOH A 242     1555   1555  2.48  
LINK        MN    MN A 188                 O   HOH A 244     1555   1555  2.49  
LINK        MN    MN A 188                 O   HOH A 267     1555   1555  2.53  
LINK         Y   YT3 A 189                 O   HOH A 303     1555   1555  2.54  
LINK         OE2 GLU A 135                 Y   YT3 A 190     1555   1555  2.59  
LINK         OE2 GLU A 124                 Y   YT3 A 189     1555   1555  2.59  
LINK         Y   YT3 A 191                 O   HOH A 333     1555   1555  2.60  
LINK         Y   YT3 A   1                 O   HOH A 304     1555   1555  2.66  
LINK        MN    MN B 188                 O   HOH B 208     1555   1555  2.66  
LINK         Y   YT3 A   1                 O   HOH A 198     1555   1555  2.69  
LINK         OE1 GLU A 124                 Y   YT3 A 189     1555   1555  2.79  
LINK         Y   YT3 A 190                 O   HOH A 300     1555   1555  2.82  
SITE     1 AC1 10 HIS A  42  ASP A  50  HIS A  84   MN A 188                    
SITE     2 AC1 10 HOH A 239  HOH A 267  HOH A 332  HOH A 364                    
SITE     3 AC1 10 LYS B  75  HOH B 197                                          
SITE     1 AC2  9 GLU A 135  ARG A 177  YT3 A 190  HOH A 193                    
SITE     2 AC2  9 LYS B 136  ARG B 177  PRO B 178  ASP B 179                    
SITE     3 AC2  9 HOH B 203                                                     
SITE     1 AC3  9 LYS A 136  ARG A 177  PRO A 178  ASP A 179                    
SITE     2 AC3  9 GLU A 184  YT3 A 191  HOH A 333  GLU B 135                    
SITE     3 AC3  9 ARG B 177                                                     
SITE     1 AC4  1 ARG A 140                                                     
SITE     1 AC5  7 LYS A 161  ASP A 162  GLY A 163  ALA A 165                    
SITE     2 AC5  7 HOH A 292  HOH A 318  HOH B 217                               
SITE     1 AC6  6 SO4 A   2  HIS A  42  HIS A  48  ASP A  50                    
SITE     2 AC6  6 HOH A 244  HOH A 267                                          
SITE     1 AC7  7 ASP A 117  ASP A 179  HOH A 198  HOH A 226                    
SITE     2 AC7  7 HOH A 294  HOH A 304  HOH A 352                               
SITE     1 AC8  5 ASP A 104  GLU A 124  HOH A 209  HOH A 303                    
SITE     2 AC8  5 HOH A 335                                                     
SITE     1 AC9  6 SO4 A   3  GLU A 135  HOH A 215  HOH A 242                    
SITE     2 AC9  6 HOH A 300  ASP B 179                                          
SITE     1 BC1  6 SO4 A   4  ASP A 179  GLU A 184  HOH A 232                    
SITE     2 BC1  6 HOH A 333  GLU B 135                                          
SITE     1 BC2 11 LYS A  75  HOH A 248  HIS B  42  ASP B  50                    
SITE     2 BC2 11 HIS B  84  TYR B 100   MN B 188  HOH B 208                    
SITE     3 BC2 11 HOH B 211  HOH B 225  HOH B 266                               
SITE     1 BC3  6 SO4 B   1  HIS B  42  HIS B  48  ASP B  50                    
SITE     2 BC3  6 HOH B 208  HOH B 225                                          
CRYST1   41.583   45.550   53.384 102.32 109.43 104.59 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      0.024048  0.006258  0.011129        0.00000                         
SCALE2      0.000000  0.022685  0.007813        0.00000                         
SCALE3      0.000000  0.000000  0.021009        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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