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Database: PDB
Entry: 4R73
LinkDB: 4R73
Original site: 4R73 
HEADER    TRANSPORT PROTEIN                       26-AUG-14   4R73              
TITLE     STRUCTURE OF THE PERIPLASMIC BINDING PROTEIN AFUA FROM ACTINOBACILLUS 
TITLE    2 PLEUROPNEUMONIAE (ENDOGENOUS GLUCOSE-6-PHOSPHATE AND MANNOSE-6-      
TITLE    3 PHOSPHATE BOUND)                                                     
CAVEAT     4R73    SUGARS A G6P 401 AND B G6P 401 HAVE INCORRECT                
CAVEAT   2 4R73     STEREOCHEMISTRY AT THEIR C1 CHIRAL CENTERS.                 
CAVEAT     4R73    SUGARS A M6P 402 AND B M6P 402 HAVE INCORRECT                
CAVEAT   2 4R73     STEREOCHEMISTRY AT THEIR C1, C3, AND C4 CHIRAL CENTERS.     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ABC-TYPE FE3+ TRANSPORT SYSTEM, PERIPLASMIC COMPONENT;     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 28-346;                                       
COMPND   5 SYNONYM: AFUA;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ACTINOBACILLUS PLEUROPNEUMONIAE;                
SOURCE   3 ORGANISM_TAXID: 715;                                                 
SOURCE   4 GENE: AFUA, APL_1446;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ABC TRANSPORTER, SUGAR TRANSPORTER, GLUCOSE-6-PHOSPHATE, FRUCTOSE-6-  
KEYWDS   2 PHOSPHATE, SEDOHEPTULOSE-7-PHOSPHATE, TRANSPORT PROTEIN              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CALMETTES,C.TANG,B.SIT,T.F.MORAES                                   
REVDAT   2   02-SEP-15 4R73    1       JRNL                                     
REVDAT   1   12-AUG-15 4R73    0                                                
JRNL        AUTH   B.SIT,S.M.CROWLEY,K.BHULLAR,C.C.LAI,C.TANG,Y.HOODA,          
JRNL        AUTH 2 C.CALMETTES,H.KHAMBATI,C.MA,J.H.BRUMELL,A.B.SCHRYVERS,       
JRNL        AUTH 3 B.A.VALLANCE,T.F.MORAES                                      
JRNL        TITL   ACTIVE TRANSPORT OF PHOSPHORYLATED CARBOHYDRATES PROMOTES    
JRNL        TITL 2 INTESTINAL COLONIZATION AND TRANSMISSION OF A BACTERIAL      
JRNL        TITL 3 PATHOGEN.                                                    
JRNL        REF    PLOS PATHOG.                  V.  11 05107 2015              
JRNL        REFN                   ISSN 1553-7366                               
JRNL        PMID   26295949                                                     
JRNL        DOI    10.1371/JOURNAL.PPAT.1005107                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.60                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 83626                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4182                            
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 39.6086 -  4.9684    0.99     2903   153  0.1635 0.1794        
REMARK   3     2  4.9684 -  3.9447    1.00     2769   146  0.1379 0.1617        
REMARK   3     3  3.9447 -  3.4464    1.00     2744   145  0.1379 0.1534        
REMARK   3     4  3.4464 -  3.1314    1.00     2720   143  0.1560 0.1702        
REMARK   3     5  3.1314 -  2.9071    1.00     2695   141  0.1664 0.2060        
REMARK   3     6  2.9071 -  2.7357    1.00     2713   143  0.1638 0.2183        
REMARK   3     7  2.7357 -  2.5987    1.00     2695   142  0.1702 0.1999        
REMARK   3     8  2.5987 -  2.4856    1.00     2688   142  0.1661 0.2256        
REMARK   3     9  2.4856 -  2.3900    1.00     2664   140  0.1649 0.1971        
REMARK   3    10  2.3900 -  2.3075    1.00     2669   140  0.1608 0.2063        
REMARK   3    11  2.3075 -  2.2354    1.00     2699   142  0.1609 0.1969        
REMARK   3    12  2.2354 -  2.1715    1.00     2632   139  0.1576 0.1955        
REMARK   3    13  2.1715 -  2.1143    1.00     2680   141  0.1591 0.1890        
REMARK   3    14  2.1143 -  2.0627    1.00     2646   139  0.1599 0.1896        
REMARK   3    15  2.0627 -  2.0158    1.00     2666   140  0.1627 0.2130        
REMARK   3    16  2.0158 -  1.9729    1.00     2640   139  0.1640 0.1986        
REMARK   3    17  1.9729 -  1.9335    1.00     2677   141  0.1649 0.1958        
REMARK   3    18  1.9335 -  1.8970    1.00     2645   140  0.1683 0.2479        
REMARK   3    19  1.8970 -  1.8631    1.00     2657   139  0.1600 0.1897        
REMARK   3    20  1.8631 -  1.8315    1.00     2620   138  0.1707 0.2233        
REMARK   3    21  1.8315 -  1.8020    1.00     2672   141  0.1664 0.2115        
REMARK   3    22  1.8020 -  1.7743    1.00     2646   139  0.1703 0.2132        
REMARK   3    23  1.7743 -  1.7482    1.00     2609   138  0.1651 0.2211        
REMARK   3    24  1.7482 -  1.7235    1.00     2675   140  0.1752 0.2282        
REMARK   3    25  1.7235 -  1.7002    0.99     2612   138  0.1717 0.2342        
REMARK   3    26  1.7002 -  1.6782    0.98     2554   134  0.1728 0.2042        
REMARK   3    27  1.6782 -  1.6572    0.97     2580   136  0.1773 0.2513        
REMARK   3    28  1.6572 -  1.6372    0.94     2490   131  0.1818 0.2067        
REMARK   3    29  1.6372 -  1.6182    0.92     2402   126  0.1892 0.1891        
REMARK   3    30  1.6182 -  1.6000    0.89     2382   126  0.2108 0.2454        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.020           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.81                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.014           5310                                  
REMARK   3   ANGLE     :  1.641           7212                                  
REMARK   3   CHIRALITY :  0.377            801                                  
REMARK   3   PLANARITY :  0.007            923                                  
REMARK   3   DIHEDRAL  : 14.374           2007                                  
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 4R73 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-AUG-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB086981.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : ACCEL/BRUKER DOUBLE CRYSTAL        
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83626                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.596                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
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) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M TRIS,    
REMARK 280  PH 6.5, 25% PEG3350, 20% GLYCEROL, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       21.76500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.05000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.66000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       76.05000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.76500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.66000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 B    -1                                                      
REMARK 465     LYS B   319                                                      
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     LYS A 118    CG   CD   CE   NZ                                   
REMARK 470     LYS A 319    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A 166   N     LYS A 166   CA      0.132                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B  27   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
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    MET A  85      120.53    -39.16                                   
REMARK 500    ASP A  90       72.15   -151.77                                   
REMARK 500    LYS A 118        7.19    -67.52                                   
REMARK 500    ASN A 241       66.11   -114.31                                   
REMARK 500    LYS B  29       98.74    -65.31                                   
REMARK 500    ASN B  50       74.30   -152.57                                   
REMARK 500    TYR B  76      116.01   -160.19                                   
REMARK 500    ASP B  90       69.64   -151.66                                   
REMARK 500    LEU B 317     -122.23     53.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS A 166        24.0      L          L   OUTSIDE RANGE           
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 G6P A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M6P A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M6P B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 406                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4R72   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4R74   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4R75   RELATED DB: PDB                                   
DBREF  4R73 A    1   319  UNP    A3N294   A3N294_ACTP2    28    346             
DBREF  4R73 B    1   319  UNP    A3N294   A3N294_ACTP2    28    346             
SEQADV 4R73 GLY A   -1  UNP  A3N294              EXPRESSION TAG                 
SEQADV 4R73 SER A    0  UNP  A3N294              EXPRESSION TAG                 
SEQADV 4R73 GLY B   -1  UNP  A3N294              EXPRESSION TAG                 
SEQADV 4R73 SER B    0  UNP  A3N294              EXPRESSION TAG                 
SEQRES   1 A  321  GLY SER LYS GLY ARG LEU VAL ILE TYR CYS SER ALA THR          
SEQRES   2 A  321  ASN VAL MET CYS GLU ASN ALA ALA LYS THR PHE GLU GLN          
SEQRES   3 A  321  LYS TYR ASP VAL LYS THR SER PHE ILE ARG ASN GLY SER          
SEQRES   4 A  321  GLY SER THR PHE ALA LYS ILE GLU ALA GLU LYS ASN ASN          
SEQRES   5 A  321  PRO GLN ALA ASP VAL TRP TYR GLY GLY THR LEU ASP PRO          
SEQRES   6 A  321  GLN SER GLN ALA GLY GLU LEU GLY LEU LEU GLU ALA TYR          
SEQRES   7 A  321  ARG SER PRO ASN ILE ASP GLN ILE MET PRO LYS PHE GLN          
SEQRES   8 A  321  ASP PRO ALA LYS VAL LYS GLY ASN LEU SER SER ALA VAL          
SEQRES   9 A  321  TYR ILE GLY ILE LEU GLY PHE ALA VAL ASN THR GLU ARG          
SEQRES  10 A  321  LEU LYS LYS LEU GLY ILE GLU LYS ILE PRO GLN CYS TRP          
SEQRES  11 A  321  ASN ASP LEU THR ASP PRO LYS LEU LYS GLY GLU ILE GLN          
SEQRES  12 A  321  ILE ALA ASP PRO GLN SER SER GLY THR ALA TYR THR ALA          
SEQRES  13 A  321  ILE ALA THR PHE ALA GLN LEU TRP GLY GLU ASP LYS ALA          
SEQRES  14 A  321  PHE ASP TYR PHE LYS HIS LEU HIS PRO ASN ILE SER GLN          
SEQRES  15 A  321  TYR THR LYS SER GLY ILE THR PRO ALA ARG ASN ALA ALA          
SEQRES  16 A  321  ARG GLY GLU THR THR VAL GLY ILE GLY PHE LEU HIS ASP          
SEQRES  17 A  321  TYR ALA LEU GLU LYS GLU GLN GLY ALA PRO LEU GLU MET          
SEQRES  18 A  321  VAL VAL PRO CYS GLU GLY THR GLY TYR GLU LEU GLY GLY          
SEQRES  19 A  321  VAL SER ILE LEU LYS GLY ALA ARG ASN LEU ASP ASN ALA          
SEQRES  20 A  321  LYS LEU PHE VAL ASP PHE ALA LEU SER LYS GLU GLY GLN          
SEQRES  21 A  321  GLU THR ALA TRP LYS LYS GLY GLN ALA LEU GLN THR LEU          
SEQRES  22 A  321  THR ASN THR THR ALA GLU GLN SER PRO LEU ALA PHE ASP          
SEQRES  23 A  321  LEU THR LYS LEU LYS LEU ILE ASP TYR ASP PHE GLU LYS          
SEQRES  24 A  321  TYR GLY ALA SER ASP GLU ARG LYS ARG LEU ILE ASN LYS          
SEQRES  25 A  321  TRP VAL ASP GLU ILE LYS LEU ALA LYS                          
SEQRES   1 B  321  GLY SER LYS GLY ARG LEU VAL ILE TYR CYS SER ALA THR          
SEQRES   2 B  321  ASN VAL MET CYS GLU ASN ALA ALA LYS THR PHE GLU GLN          
SEQRES   3 B  321  LYS TYR ASP VAL LYS THR SER PHE ILE ARG ASN GLY SER          
SEQRES   4 B  321  GLY SER THR PHE ALA LYS ILE GLU ALA GLU LYS ASN ASN          
SEQRES   5 B  321  PRO GLN ALA ASP VAL TRP TYR GLY GLY THR LEU ASP PRO          
SEQRES   6 B  321  GLN SER GLN ALA GLY GLU LEU GLY LEU LEU GLU ALA TYR          
SEQRES   7 B  321  ARG SER PRO ASN ILE ASP GLN ILE MET PRO LYS PHE GLN          
SEQRES   8 B  321  ASP PRO ALA LYS VAL LYS GLY ASN LEU SER SER ALA VAL          
SEQRES   9 B  321  TYR ILE GLY ILE LEU GLY PHE ALA VAL ASN THR GLU ARG          
SEQRES  10 B  321  LEU LYS LYS LEU GLY ILE GLU LYS ILE PRO GLN CYS TRP          
SEQRES  11 B  321  ASN ASP LEU THR ASP PRO LYS LEU LYS GLY GLU ILE GLN          
SEQRES  12 B  321  ILE ALA ASP PRO GLN SER SER GLY THR ALA TYR THR ALA          
SEQRES  13 B  321  ILE ALA THR PHE ALA GLN LEU TRP GLY GLU ASP LYS ALA          
SEQRES  14 B  321  PHE ASP TYR PHE LYS HIS LEU HIS PRO ASN ILE SER GLN          
SEQRES  15 B  321  TYR THR LYS SER GLY ILE THR PRO ALA ARG ASN ALA ALA          
SEQRES  16 B  321  ARG GLY GLU THR THR VAL GLY ILE GLY PHE LEU HIS ASP          
SEQRES  17 B  321  TYR ALA LEU GLU LYS GLU GLN GLY ALA PRO LEU GLU MET          
SEQRES  18 B  321  VAL VAL PRO CYS GLU GLY THR GLY TYR GLU LEU GLY GLY          
SEQRES  19 B  321  VAL SER ILE LEU LYS GLY ALA ARG ASN LEU ASP ASN ALA          
SEQRES  20 B  321  LYS LEU PHE VAL ASP PHE ALA LEU SER LYS GLU GLY GLN          
SEQRES  21 B  321  GLU THR ALA TRP LYS LYS GLY GLN ALA LEU GLN THR LEU          
SEQRES  22 B  321  THR ASN THR THR ALA GLU GLN SER PRO LEU ALA PHE ASP          
SEQRES  23 B  321  LEU THR LYS LEU LYS LEU ILE ASP TYR ASP PHE GLU LYS          
SEQRES  24 B  321  TYR GLY ALA SER ASP GLU ARG LYS ARG LEU ILE ASN LYS          
SEQRES  25 B  321  TRP VAL ASP GLU ILE LYS LEU ALA LYS                          
HET    G6P  A 401      16                                                       
HET    M6P  A 402      16                                                       
HET    GOL  A 403       6                                                       
HET    GOL  A 404       6                                                       
HET     CL  A 405       1                                                       
HET     CL  A 406       1                                                       
HET    G6P  B 401      16                                                       
HET    M6P  B 402      16                                                       
HET    GOL  B 403       6                                                       
HET    GOL  B 404       6                                                       
HET     CL  B 405       1                                                       
HET     CL  B 406       1                                                       
HETNAM     G6P ALPHA-D-GLUCOSE-6-PHOSPHATE                                      
HETNAM     M6P ALPHA-D-MANNOSE-6-PHOSPHATE                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  G6P    2(C6 H13 O9 P)                                               
FORMUL   4  M6P    2(C6 H13 O9 P)                                               
FORMUL   5  GOL    4(C3 H8 O3)                                                  
FORMUL   7   CL    4(CL 1-)                                                     
FORMUL  15  HOH   *723(H2 O)                                                    
HELIX    1   1 THR A   11  ASP A   27  1                                  17    
HELIX    2   2 GLY A   36  GLU A   47  1                                  12    
HELIX    3   3 LEU A   61  LEU A   70  1                                  10    
HELIX    4   4 SER A   78  ILE A   84  5                                   7    
HELIX    5   5 MET A   85  GLN A   89  5                                   5    
HELIX    6   6 THR A  113  LYS A  118  1                                   6    
HELIX    7   7 CYS A  127  LYS A  137  5                                  11    
HELIX    8   8 SER A  148  GLY A  163  1                                  16    
HELIX    9   9 GLY A  163  HIS A  175  1                                  13    
HELIX   10  10 ILE A  186  ARG A  194  1                                   9    
HELIX   11  11 LEU A  204  GLN A  213  1                                  10    
HELIX   12  12 ASN A  241  SER A  254  1                                  14    
HELIX   13  13 SER A  254  LYS A  264  1                                  11    
HELIX   14  14 ASP A  284  LEU A  288  5                                   5    
HELIX   15  15 ASP A  294  GLY A  299  1                                   6    
HELIX   16  16 ALA A  300  LYS A  316  1                                  17    
HELIX   17  17 THR B   11  ASP B   27  1                                  17    
HELIX   18  18 GLY B   36  GLU B   47  1                                  12    
HELIX   19  19 LEU B   61  LEU B   70  1                                  10    
HELIX   20  20 SER B   78  ILE B   84  5                                   7    
HELIX   21  21 MET B   85  GLN B   89  5                                   5    
HELIX   22  22 THR B  113  LEU B  119  1                                   7    
HELIX   23  23 CYS B  127  LYS B  137  5                                  11    
HELIX   24  24 SER B  148  GLY B  163  1                                  16    
HELIX   25  25 GLY B  163  HIS B  175  1                                  13    
HELIX   26  26 ILE B  186  ARG B  194  1                                   9    
HELIX   27  27 LEU B  204  GLN B  213  1                                  10    
HELIX   28  28 ASN B  241  LEU B  253  1                                  13    
HELIX   29  29 SER B  254  LYS B  264  1                                  11    
HELIX   30  30 ASP B  284  LEU B  288  5                                   5    
HELIX   31  31 ASP B  294  GLY B  299  1                                   6    
HELIX   32  32 ALA B  300  ILE B  315  1                                  16    
SHEET    1   A 5 LYS A  29  ARG A  34  0                                        
SHEET    2   A 5 ARG A   3  CYS A   8  1  N  ILE A   6   O  SER A  31           
SHEET    3   A 5 VAL A  55  THR A  60  1  O  VAL A  55   N  TYR A   7           
SHEET    4   A 5 TYR A 228  LEU A 236 -1  O  SER A 234   N  TRP A  56           
SHEET    5   A 5 LEU A  73  GLU A  74 -1  N  GLU A  74   O  ILE A 235           
SHEET    1   B 4 LEU A  73  GLU A  74  0                                        
SHEET    2   B 4 TYR A 228  LEU A 236 -1  O  ILE A 235   N  GLU A  74           
SHEET    3   B 4 SER A  99  ASN A 112 -1  N  VAL A 102   O  GLY A 231           
SHEET    4   B 4 THR A 270  LEU A 271 -1  O  THR A 270   N  ILE A 104           
SHEET    1   C 5 THR A 270  LEU A 271  0                                        
SHEET    2   C 5 SER A  99  ASN A 112 -1  N  ILE A 104   O  THR A 270           
SHEET    3   C 5 VAL A 199  PHE A 203 -1  O  GLY A 202   N  GLY A 108           
SHEET    4   C 5 ILE A 140  ALA A 143  1  N  GLN A 141   O  ILE A 201           
SHEET    5   C 5 ILE A 178  THR A 182  1  O  SER A 179   N  ILE A 140           
SHEET    1   D 5 ILE A 178  THR A 182  0                                        
SHEET    2   D 5 ILE A 140  ALA A 143  1  N  ILE A 140   O  SER A 179           
SHEET    3   D 5 VAL A 199  PHE A 203  1  O  ILE A 201   N  GLN A 141           
SHEET    4   D 5 SER A  99  ASN A 112 -1  N  GLY A 108   O  GLY A 202           
SHEET    5   D 5 LEU A 217  VAL A 220 -1  O  VAL A 220   N  PHE A 109           
SHEET    1   E 6 LEU A 217  VAL A 220  0                                        
SHEET    2   E 6 SER A  99  ASN A 112 -1  N  PHE A 109   O  VAL A 220           
SHEET    3   E 6 TYR A 228  LEU A 236 -1  O  GLY A 231   N  VAL A 102           
SHEET    4   E 6 VAL A  55  THR A  60 -1  N  TRP A  56   O  SER A 234           
SHEET    5   E 6 ARG A   3  CYS A   8  1  N  TYR A   7   O  VAL A  55           
SHEET    6   E 6 LYS A  29  ARG A  34  1  O  SER A  31   N  ILE A   6           
SHEET    1   F 5 LYS B  29  ARG B  34  0                                        
SHEET    2   F 5 ARG B   3  CYS B   8  1  N  CYS B   8   O  ILE B  33           
SHEET    3   F 5 VAL B  55  THR B  60  1  O  VAL B  55   N  TYR B   7           
SHEET    4   F 5 TYR B 228  LEU B 236 -1  O  SER B 234   N  TRP B  56           
SHEET    5   F 5 LEU B  73  GLU B  74 -1  N  GLU B  74   O  ILE B 235           
SHEET    1   G 4 LEU B  73  GLU B  74  0                                        
SHEET    2   G 4 TYR B 228  LEU B 236 -1  O  ILE B 235   N  GLU B  74           
SHEET    3   G 4 SER B  99  ASN B 112 -1  N  VAL B 102   O  GLY B 231           
SHEET    4   G 4 THR B 270  LEU B 271 -1  O  THR B 270   N  ILE B 104           
SHEET    1   H 5 THR B 270  LEU B 271  0                                        
SHEET    2   H 5 SER B  99  ASN B 112 -1  N  ILE B 104   O  THR B 270           
SHEET    3   H 5 VAL B 199  PHE B 203 -1  O  GLY B 202   N  GLY B 108           
SHEET    4   H 5 ILE B 140  ALA B 143  1  N  GLN B 141   O  ILE B 201           
SHEET    5   H 5 ILE B 178  THR B 182  1  O  SER B 179   N  ILE B 140           
SHEET    1   I 5 ILE B 178  THR B 182  0                                        
SHEET    2   I 5 ILE B 140  ALA B 143  1  N  ILE B 140   O  SER B 179           
SHEET    3   I 5 VAL B 199  PHE B 203  1  O  ILE B 201   N  GLN B 141           
SHEET    4   I 5 SER B  99  ASN B 112 -1  N  GLY B 108   O  GLY B 202           
SHEET    5   I 5 LEU B 217  VAL B 220 -1  O  VAL B 220   N  PHE B 109           
SHEET    1   J 6 LEU B 217  VAL B 220  0                                        
SHEET    2   J 6 SER B  99  ASN B 112 -1  N  PHE B 109   O  VAL B 220           
SHEET    3   J 6 TYR B 228  LEU B 236 -1  O  GLY B 231   N  VAL B 102           
SHEET    4   J 6 VAL B  55  THR B  60 -1  N  TRP B  56   O  SER B 234           
SHEET    5   J 6 ARG B   3  CYS B   8  1  N  TYR B   7   O  VAL B  55           
SHEET    6   J 6 LYS B  29  ARG B  34  1  O  ILE B  33   N  CYS B   8           
SSBOND   1 CYS A    8    CYS A   15                          1555   1555  2.03  
SSBOND   2 CYS A  127    CYS A  223                          1555   1555  2.06  
SSBOND   3 CYS B    8    CYS B   15                          1555   1555  2.02  
SSBOND   4 CYS B  127    CYS B  223                          1555   1555  2.05  
CISPEP   1 ALA A  318    LYS A  319          0        -6.26                     
SITE     1 AC1 18 SER A   9  ARG A  34  SER A  37  GLY A  59                    
SITE     2 AC1 18 TYR A 103  SER A 148  GLY A 149  THR A 150                    
SITE     3 AC1 18 GLY A 185  ILE A 186  HIS A 205  ASP A 206                    
SITE     4 AC1 18 GLU A 229  GLN A 269  HOH A 504  HOH A 521                    
SITE     5 AC1 18 HOH A 528  HOH A 537                                          
SITE     1 AC2 17 SER A   9  ARG A  34  SER A  37  GLY A  59                    
SITE     2 AC2 17 TYR A 103  SER A 148  GLY A 149  THR A 150                    
SITE     3 AC2 17 GLY A 185  ILE A 186  HIS A 205  ASP A 206                    
SITE     4 AC2 17 GLU A 229  GLN A 269  HOH A 504  HOH A 528                    
SITE     5 AC2 17 HOH A 537                                                     
SITE     1 AC3  7 LYS A  87  PHE A  88  TYR A 228  LEU A 290                    
SITE     2 AC3  7 ILE A 291  ASP A 292  HOH A 645                               
SITE     1 AC4  8 PRO A  91  TYR A 293  ASP A 294  PHE A 295                    
SITE     2 AC4  8 GLU A 296  HOH A 734  HOH A 821  HOH A 863                    
SITE     1 AC5  3 ASN A  12  ARG A 190  HOH A 752                               
SITE     1 AC6  5 ASN A 241  ASP A 243  ASN A 244  HOH B 508                    
SITE     2 AC6  5 HOH B 563                                                     
SITE     1 AC7 18 SER B   9  THR B  11  ARG B  34  SER B  37                    
SITE     2 AC7 18 GLY B  59  TYR B 103  SER B 148  GLY B 149                    
SITE     3 AC7 18 THR B 150  GLY B 185  ILE B 186  HIS B 205                    
SITE     4 AC7 18 ASP B 206  GLU B 229  GLN B 269  HOH B 507                    
SITE     5 AC7 18 HOH B 512  HOH B 522                                          
SITE     1 AC8 17 SER B   9  THR B  11  ARG B  34  SER B  37                    
SITE     2 AC8 17 GLY B  59  TYR B 103  SER B 148  GLY B 149                    
SITE     3 AC8 17 THR B 150  GLY B 185  ILE B 186  HIS B 205                    
SITE     4 AC8 17 ASP B 206  GLU B 229  GLN B 269  HOH B 507                    
SITE     5 AC8 17 HOH B 512                                                     
SITE     1 AC9  8 GLN A 180  HOH A 880  TYR B  76  LYS B 246                    
SITE     2 AC9  8 LEU B 247  ASP B 250  HOH B 502  HOH B 503                    
SITE     1 BC1  8 ASN A 129  HOH A 751  HOH A 836  HOH A 859                    
SITE     2 BC1  8 HIS B 175  ILE B 178  HOH B 615  HOH B 749                    
SITE     1 BC2  4 HOH A 606  ASN B 241  ASP B 243  ASN B 244                    
SITE     1 BC3  3 ASN B  12  ARG B 190  HOH B 539                               
CRYST1   43.530   95.320  152.100  90.00  90.00  90.00 P 21 21 21    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      0.022973  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010491  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006575        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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