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Database: PDB
Entry: 1U60
LinkDB: 1U60
Original site: 1U60 
HEADER    HYDROLASE                               28-JUL-04   1U60              
TITLE     MCSG APC5046 PROBABLE GLUTAMINASE YBAS                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE GLUTAMINASE YBAS;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.5.1.2;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: YBAS;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    STRUCTURAL GENOMICS, APC5046, PSI, PROTEIN STRUCTURE INITIATIVE,      
KEYWDS   2 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, HYDROLASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHANG,M.E.CUFF,A.JOACHIMIAK,A.SAVCHENKO,A.EDWARDS,T.SKARINA,MIDWEST 
AUTHOR   2 CENTER FOR STRUCTURAL GENOMICS (MCSG)                                
REVDAT   8   14-FEB-24 1U60    1       REMARK                                   
REVDAT   7   26-SEP-12 1U60    1       AUTHOR                                   
REVDAT   6   13-JUL-11 1U60    1       VERSN                                    
REVDAT   5   24-FEB-09 1U60    1       VERSN                                    
REVDAT   4   03-JUN-08 1U60    1       JRNL                                     
REVDAT   3   20-MAY-08 1U60    1       JRNL                                     
REVDAT   2   18-JAN-05 1U60    1       AUTHOR KEYWDS REMARK                     
REVDAT   1   07-SEP-04 1U60    0                                                
JRNL        AUTH   G.BROWN,A.SINGER,M.PROUDFOOT,T.SKARINA,Y.KIM,C.CHANG,        
JRNL        AUTH 2 I.DEMENTIEVA,E.KUZNETSOVA,C.F.GONZALEZ,A.JOACHIMIAK,         
JRNL        AUTH 3 A.SAVCHENKO,A.F.YAKUNIN                                      
JRNL        TITL   FUNCTIONAL AND STRUCTURAL CHARACTERIZATION OF FOUR           
JRNL        TITL 2 GLUTAMINASES FROM ESCHERICHIA COLI AND BACILLUS SUBTILIS.    
JRNL        REF    BIOCHEMISTRY                  V.  47  5724 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18459799                                                     
JRNL        DOI    10.1021/BI800097H                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 78.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 125216                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.145                           
REMARK   3   R VALUE            (WORKING SET) : 0.143                           
REMARK   3   FREE R VALUE                     : 0.178                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6641                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.66                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2786                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 160                          
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9216                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 75                                      
REMARK   3   SOLVENT ATOMS            : 1150                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.71000                                             
REMARK   3    B22 (A**2) : -1.68000                                             
REMARK   3    B33 (A**2) : 2.38000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.090         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.091         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.061         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.856         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9490 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  8541 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12897 ; 1.599 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 19874 ; 0.925 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1252 ; 6.010 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1476 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10818 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1766 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2117 ; 0.234 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 10300 ; 0.248 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5389 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   813 ; 0.210 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    35 ; 0.250 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   124 ; 0.314 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.248 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6156 ; 0.877 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9790 ; 1.507 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3334 ; 2.902 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3097 ; 4.556 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.0920  55.4400  50.1810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0359 T22:   0.0502                                     
REMARK   3      T33:   0.0174 T12:   0.0056                                     
REMARK   3      T13:  -0.0016 T23:  -0.0177                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3584 L22:   0.3768                                     
REMARK   3      L33:   0.1469 L12:   0.0532                                     
REMARK   3      L13:   0.1149 L23:   0.0248                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0013 S12:  -0.0056 S13:   0.0006                       
REMARK   3      S21:  -0.0231 S22:  -0.0242 S23:   0.0091                       
REMARK   3      S31:   0.0000 S32:  -0.0076 S33:   0.0229                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3180  60.0600  79.1900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0517 T22:   0.0460                                     
REMARK   3      T33:   0.0085 T12:   0.0011                                     
REMARK   3      T13:  -0.0114 T23:   0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3782 L22:   0.2681                                     
REMARK   3      L33:   0.2313 L12:  -0.1147                                     
REMARK   3      L13:   0.0545 L23:   0.0760                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0329 S12:  -0.0041 S13:   0.0023                       
REMARK   3      S21:   0.0466 S22:   0.0086 S23:   0.0082                       
REMARK   3      S31:   0.0009 S32:   0.0298 S33:   0.0243                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.4930  23.5700   5.2440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0637 T22:   0.0357                                     
REMARK   3      T33:   0.0051 T12:  -0.0056                                     
REMARK   3      T13:  -0.0042 T23:   0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4433 L22:   0.4415                                     
REMARK   3      L33:   0.0791 L12:   0.1407                                     
REMARK   3      L13:  -0.0528 L23:   0.1494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0751 S12:  -0.0361 S13:   0.0074                       
REMARK   3      S21:  -0.1024 S22:   0.0339 S23:   0.0090                       
REMARK   3      S31:  -0.0270 S32:   0.0166 S33:   0.0412                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.4420  24.9010  34.6090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0302 T22:   0.0529                                     
REMARK   3      T33:   0.0241 T12:   0.0031                                     
REMARK   3      T13:  -0.0043 T23:  -0.0291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3206 L22:   0.3790                                     
REMARK   3      L33:   0.1867 L12:  -0.0972                                     
REMARK   3      L13:  -0.1215 L23:   0.0902                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0210 S12:   0.0238 S13:  -0.0071                       
REMARK   3      S21:   0.0283 S22:  -0.0406 S23:   0.0250                       
REMARK   3      S31:   0.0086 S32:  -0.0266 S33:   0.0616                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1U60 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000023288.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97978                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 131904                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.610                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 23.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION SOLUTION: 0.1M HEPES,    
REMARK 280  10% ISOPROPANOL, 20% PEG 4000. CRYOPROTECTANT: CRYSTALLIZATION      
REMARK 280  SOLUTION PLUS 12% ETHYLENE GLYCOL, PH 7.5                           
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       25.25450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.08550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       77.94550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.08550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.25450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       77.94550            
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, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12490 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       50.50900            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       77.94550            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       82.08550            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10220 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -50.50900            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  1284     O    HOH B  1469              1.74            
REMARK 500   O    HOH A  1496     O    HOH A  1519              1.86            
REMARK 500   CB   VAL B   231     O    HOH B  1455              1.86            
REMARK 500   NH1  ARG D    61     O    HOH D  1339              1.90            
REMARK 500   O    HOH C  1253     O    HOH C  1464              1.96            
REMARK 500   O    HOH A  1352     O    HOH B  1353              1.99            
REMARK 500   O    HOH C  1346     O    HOH C  1452              1.99            
REMARK 500   O    HOH D  1467     O    HOH D  1501              2.02            
REMARK 500   O    HOH C  1364     O    HOH C  1453              2.06            
REMARK 500   O    HOH B  1397     O    HOH B  1499              2.08            
REMARK 500   O    HOH D  1319     O    HOH D  1335              2.13            
REMARK 500   O    HOH A  1463     O    HOH A  1471              2.13            
REMARK 500   C    GLY B   310     O    HOH B  1441              2.16            
REMARK 500   N    LEU B     2     O    HOH B  1464              2.16            
REMARK 500   O2   EDO A  1217     O    HOH A  1374              2.17            
REMARK 500   O    HOH A  1407     O    HOH D  1263              2.17            
REMARK 500   O    HOH B  1329     O    HOH B  1469              2.18            
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   O    HOH C  1444     O    HOH C  1466     4455     1.98            
REMARK 500   O    HOH C  1467     O    HOH C  1486     4455     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU C 105   CD    GLU C 105   OE2     0.086                       
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 A  49   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A  61   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG A  61   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ASP B  57   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B  92   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP C  57   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP C 184   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP D 184   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 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    GLU A  65     -128.70     47.86                                   
REMARK 500    ILE A  89      -60.45   -126.11                                   
REMARK 500    LEU A 112      -47.74     67.84                                   
REMARK 500    ASN A 165       36.48    -92.13                                   
REMARK 500    GLU A 241       -1.76   -146.14                                   
REMARK 500    TYR A 244     -133.87     64.03                                   
REMARK 500    VAL A 273      -57.97   -130.25                                   
REMARK 500    GLU B  65     -132.90     52.79                                   
REMARK 500    ILE B  89      -63.14   -123.30                                   
REMARK 500    LEU B 112      -45.97     78.42                                   
REMARK 500    ALA B 129      141.25   -170.40                                   
REMARK 500    ASN B 165       36.61    -94.68                                   
REMARK 500    GLU B 241       -0.26   -143.51                                   
REMARK 500    TYR B 244     -132.67     58.84                                   
REMARK 500    VAL B 273      -53.59   -128.45                                   
REMARK 500    GLU C  65     -134.63     50.04                                   
REMARK 500    ILE C  89      -58.98   -124.75                                   
REMARK 500    LEU C 112      -44.65     77.42                                   
REMARK 500    ASN C 165       35.30    -91.22                                   
REMARK 500    GLU C 241       -1.33   -144.37                                   
REMARK 500    TYR C 244     -133.37     60.51                                   
REMARK 500    VAL C 273      -55.61   -128.05                                   
REMARK 500    GLU D  65     -128.80     49.72                                   
REMARK 500    ILE D  89      -60.92   -123.49                                   
REMARK 500    ILE D  89      -59.50   -124.20                                   
REMARK 500    LEU D 112      -45.37     70.18                                   
REMARK 500    ASN D 165       38.23    -93.56                                   
REMARK 500    TYR D 244     -133.27     64.37                                   
REMARK 500    VAL D 273      -59.38   -132.17                                   
REMARK 500    ASN D 306      122.30   -172.32                                   
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 EDO A 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1217                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1219                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1224                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1214                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1225                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 1222                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 1226                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 1215                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC5046   RELATED DB: TARGETDB                           
DBREF  1U60 A    1   310  UNP    P77454   GLSA1_ECOLI      1    310             
DBREF  1U60 B    1   310  UNP    P77454   GLSA1_ECOLI      1    310             
DBREF  1U60 C    1   310  UNP    P77454   GLSA1_ECOLI      1    310             
DBREF  1U60 D    1   310  UNP    P77454   GLSA1_ECOLI      1    310             
SEQRES   1 A  310  MET LEU ASP ALA ASN LYS LEU GLN GLN ALA VAL ASP GLN          
SEQRES   2 A  310  ALA TYR THR GLN PHE HIS SER LEU ASN GLY GLY GLN ASN          
SEQRES   3 A  310  ALA ASP TYR ILE PRO PHE LEU ALA ASN VAL PRO GLY GLN          
SEQRES   4 A  310  LEU ALA ALA VAL ALA ILE VAL THR CYS ASP GLY ASN VAL          
SEQRES   5 A  310  TYR SER ALA GLY ASP SER ASP TYR ARG PHE ALA LEU GLU          
SEQRES   6 A  310  SER ILE SER LYS VAL CYS THR LEU ALA LEU ALA LEU GLU          
SEQRES   7 A  310  ASP VAL GLY PRO GLN ALA VAL GLN ASP LYS ILE GLY ALA          
SEQRES   8 A  310  ASP PRO THR GLY LEU PRO PHE ASN SER VAL ILE ALA LEU          
SEQRES   9 A  310  GLU LEU HIS GLY GLY LYS PRO LEU SER PRO LEU VAL ASN          
SEQRES  10 A  310  ALA GLY ALA ILE ALA THR THR SER LEU ILE ASN ALA GLU          
SEQRES  11 A  310  ASN VAL GLU GLN ARG TRP GLN ARG ILE LEU HIS ILE GLN          
SEQRES  12 A  310  GLN GLN LEU ALA GLY GLU GLN VAL ALA LEU SER ASP GLU          
SEQRES  13 A  310  VAL ASN GLN SER GLU GLN THR THR ASN PHE HIS ASN ARG          
SEQRES  14 A  310  ALA ILE ALA TRP LEU LEU TYR SER ALA GLY TYR LEU TYR          
SEQRES  15 A  310  CYS ASP ALA MET GLU ALA CYS ASP VAL TYR THR ARG GLN          
SEQRES  16 A  310  CYS SER THR LEU LEU ASN THR ILE GLU LEU ALA THR LEU          
SEQRES  17 A  310  GLY ALA THR LEU ALA ALA GLY GLY VAL ASN PRO LEU THR          
SEQRES  18 A  310  HIS LYS ARG VAL LEU GLN ALA ASP ASN VAL PRO TYR ILE          
SEQRES  19 A  310  LEU ALA GLU MET MET MET GLU GLY LEU TYR GLY ARG SER          
SEQRES  20 A  310  GLY ASP TRP ALA TYR ARG VAL GLY LEU PRO GLY LYS SER          
SEQRES  21 A  310  GLY VAL GLY GLY GLY ILE LEU ALA VAL VAL PRO GLY VAL          
SEQRES  22 A  310  MET GLY ILE ALA ALA PHE SER PRO PRO LEU ASP GLU ASP          
SEQRES  23 A  310  GLY ASN SER VAL ARG GLY GLN LYS MET VAL ALA SER VAL          
SEQRES  24 A  310  ALA LYS GLN LEU GLY TYR ASN VAL PHE LYS GLY                  
SEQRES   1 B  310  MET LEU ASP ALA ASN LYS LEU GLN GLN ALA VAL ASP GLN          
SEQRES   2 B  310  ALA TYR THR GLN PHE HIS SER LEU ASN GLY GLY GLN ASN          
SEQRES   3 B  310  ALA ASP TYR ILE PRO PHE LEU ALA ASN VAL PRO GLY GLN          
SEQRES   4 B  310  LEU ALA ALA VAL ALA ILE VAL THR CYS ASP GLY ASN VAL          
SEQRES   5 B  310  TYR SER ALA GLY ASP SER ASP TYR ARG PHE ALA LEU GLU          
SEQRES   6 B  310  SER ILE SER LYS VAL CYS THR LEU ALA LEU ALA LEU GLU          
SEQRES   7 B  310  ASP VAL GLY PRO GLN ALA VAL GLN ASP LYS ILE GLY ALA          
SEQRES   8 B  310  ASP PRO THR GLY LEU PRO PHE ASN SER VAL ILE ALA LEU          
SEQRES   9 B  310  GLU LEU HIS GLY GLY LYS PRO LEU SER PRO LEU VAL ASN          
SEQRES  10 B  310  ALA GLY ALA ILE ALA THR THR SER LEU ILE ASN ALA GLU          
SEQRES  11 B  310  ASN VAL GLU GLN ARG TRP GLN ARG ILE LEU HIS ILE GLN          
SEQRES  12 B  310  GLN GLN LEU ALA GLY GLU GLN VAL ALA LEU SER ASP GLU          
SEQRES  13 B  310  VAL ASN GLN SER GLU GLN THR THR ASN PHE HIS ASN ARG          
SEQRES  14 B  310  ALA ILE ALA TRP LEU LEU TYR SER ALA GLY TYR LEU TYR          
SEQRES  15 B  310  CYS ASP ALA MET GLU ALA CYS ASP VAL TYR THR ARG GLN          
SEQRES  16 B  310  CYS SER THR LEU LEU ASN THR ILE GLU LEU ALA THR LEU          
SEQRES  17 B  310  GLY ALA THR LEU ALA ALA GLY GLY VAL ASN PRO LEU THR          
SEQRES  18 B  310  HIS LYS ARG VAL LEU GLN ALA ASP ASN VAL PRO TYR ILE          
SEQRES  19 B  310  LEU ALA GLU MET MET MET GLU GLY LEU TYR GLY ARG SER          
SEQRES  20 B  310  GLY ASP TRP ALA TYR ARG VAL GLY LEU PRO GLY LYS SER          
SEQRES  21 B  310  GLY VAL GLY GLY GLY ILE LEU ALA VAL VAL PRO GLY VAL          
SEQRES  22 B  310  MET GLY ILE ALA ALA PHE SER PRO PRO LEU ASP GLU ASP          
SEQRES  23 B  310  GLY ASN SER VAL ARG GLY GLN LYS MET VAL ALA SER VAL          
SEQRES  24 B  310  ALA LYS GLN LEU GLY TYR ASN VAL PHE LYS GLY                  
SEQRES   1 C  310  MET LEU ASP ALA ASN LYS LEU GLN GLN ALA VAL ASP GLN          
SEQRES   2 C  310  ALA TYR THR GLN PHE HIS SER LEU ASN GLY GLY GLN ASN          
SEQRES   3 C  310  ALA ASP TYR ILE PRO PHE LEU ALA ASN VAL PRO GLY GLN          
SEQRES   4 C  310  LEU ALA ALA VAL ALA ILE VAL THR CYS ASP GLY ASN VAL          
SEQRES   5 C  310  TYR SER ALA GLY ASP SER ASP TYR ARG PHE ALA LEU GLU          
SEQRES   6 C  310  SER ILE SER LYS VAL CYS THR LEU ALA LEU ALA LEU GLU          
SEQRES   7 C  310  ASP VAL GLY PRO GLN ALA VAL GLN ASP LYS ILE GLY ALA          
SEQRES   8 C  310  ASP PRO THR GLY LEU PRO PHE ASN SER VAL ILE ALA LEU          
SEQRES   9 C  310  GLU LEU HIS GLY GLY LYS PRO LEU SER PRO LEU VAL ASN          
SEQRES  10 C  310  ALA GLY ALA ILE ALA THR THR SER LEU ILE ASN ALA GLU          
SEQRES  11 C  310  ASN VAL GLU GLN ARG TRP GLN ARG ILE LEU HIS ILE GLN          
SEQRES  12 C  310  GLN GLN LEU ALA GLY GLU GLN VAL ALA LEU SER ASP GLU          
SEQRES  13 C  310  VAL ASN GLN SER GLU GLN THR THR ASN PHE HIS ASN ARG          
SEQRES  14 C  310  ALA ILE ALA TRP LEU LEU TYR SER ALA GLY TYR LEU TYR          
SEQRES  15 C  310  CYS ASP ALA MET GLU ALA CYS ASP VAL TYR THR ARG GLN          
SEQRES  16 C  310  CYS SER THR LEU LEU ASN THR ILE GLU LEU ALA THR LEU          
SEQRES  17 C  310  GLY ALA THR LEU ALA ALA GLY GLY VAL ASN PRO LEU THR          
SEQRES  18 C  310  HIS LYS ARG VAL LEU GLN ALA ASP ASN VAL PRO TYR ILE          
SEQRES  19 C  310  LEU ALA GLU MET MET MET GLU GLY LEU TYR GLY ARG SER          
SEQRES  20 C  310  GLY ASP TRP ALA TYR ARG VAL GLY LEU PRO GLY LYS SER          
SEQRES  21 C  310  GLY VAL GLY GLY GLY ILE LEU ALA VAL VAL PRO GLY VAL          
SEQRES  22 C  310  MET GLY ILE ALA ALA PHE SER PRO PRO LEU ASP GLU ASP          
SEQRES  23 C  310  GLY ASN SER VAL ARG GLY GLN LYS MET VAL ALA SER VAL          
SEQRES  24 C  310  ALA LYS GLN LEU GLY TYR ASN VAL PHE LYS GLY                  
SEQRES   1 D  310  MET LEU ASP ALA ASN LYS LEU GLN GLN ALA VAL ASP GLN          
SEQRES   2 D  310  ALA TYR THR GLN PHE HIS SER LEU ASN GLY GLY GLN ASN          
SEQRES   3 D  310  ALA ASP TYR ILE PRO PHE LEU ALA ASN VAL PRO GLY GLN          
SEQRES   4 D  310  LEU ALA ALA VAL ALA ILE VAL THR CYS ASP GLY ASN VAL          
SEQRES   5 D  310  TYR SER ALA GLY ASP SER ASP TYR ARG PHE ALA LEU GLU          
SEQRES   6 D  310  SER ILE SER LYS VAL CYS THR LEU ALA LEU ALA LEU GLU          
SEQRES   7 D  310  ASP VAL GLY PRO GLN ALA VAL GLN ASP LYS ILE GLY ALA          
SEQRES   8 D  310  ASP PRO THR GLY LEU PRO PHE ASN SER VAL ILE ALA LEU          
SEQRES   9 D  310  GLU LEU HIS GLY GLY LYS PRO LEU SER PRO LEU VAL ASN          
SEQRES  10 D  310  ALA GLY ALA ILE ALA THR THR SER LEU ILE ASN ALA GLU          
SEQRES  11 D  310  ASN VAL GLU GLN ARG TRP GLN ARG ILE LEU HIS ILE GLN          
SEQRES  12 D  310  GLN GLN LEU ALA GLY GLU GLN VAL ALA LEU SER ASP GLU          
SEQRES  13 D  310  VAL ASN GLN SER GLU GLN THR THR ASN PHE HIS ASN ARG          
SEQRES  14 D  310  ALA ILE ALA TRP LEU LEU TYR SER ALA GLY TYR LEU TYR          
SEQRES  15 D  310  CYS ASP ALA MET GLU ALA CYS ASP VAL TYR THR ARG GLN          
SEQRES  16 D  310  CYS SER THR LEU LEU ASN THR ILE GLU LEU ALA THR LEU          
SEQRES  17 D  310  GLY ALA THR LEU ALA ALA GLY GLY VAL ASN PRO LEU THR          
SEQRES  18 D  310  HIS LYS ARG VAL LEU GLN ALA ASP ASN VAL PRO TYR ILE          
SEQRES  19 D  310  LEU ALA GLU MET MET MET GLU GLY LEU TYR GLY ARG SER          
SEQRES  20 D  310  GLY ASP TRP ALA TYR ARG VAL GLY LEU PRO GLY LYS SER          
SEQRES  21 D  310  GLY VAL GLY GLY GLY ILE LEU ALA VAL VAL PRO GLY VAL          
SEQRES  22 D  310  MET GLY ILE ALA ALA PHE SER PRO PRO LEU ASP GLU ASP          
SEQRES  23 D  310  GLY ASN SER VAL ARG GLY GLN LYS MET VAL ALA SER VAL          
SEQRES  24 D  310  ALA LYS GLN LEU GLY TYR ASN VAL PHE LYS GLY                  
HET    EDO  A1203       4                                                       
HET    EDO  A1204       4                                                       
HET    EDO  A1205       4                                                       
HET    EDO  A1211       4                                                       
HET    EDO  A1217       4                                                       
HET    EDO  A1219       4                                                       
HET    FMT  A1212       3                                                       
HET    FMT  A1218       3                                                       
HET    EDO  B1210       4                                                       
HET    EDO  B1224       4                                                       
HET    FMT  B1206       3                                                       
HET    FMT  B1207       3                                                       
HET    FMT  B1209       3                                                       
HET    FMT  B1225       3                                                       
HET    EDO  C1208       4                                                       
HET    FMT  C1222       3                                                       
HET    FMT  C1226       3                                                       
HET    EDO  D1213       4                                                       
HET    EDO  D1214       4                                                       
HET    EDO  D1216       4                                                       
HET    FMT  D1215       3                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     FMT FORMIC ACID                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  EDO    12(C2 H6 O2)                                                 
FORMUL  11  FMT    9(C H2 O2)                                                   
FORMUL  26  HOH   *1150(H2 O)                                                   
HELIX    1   1 ASP A    3  HIS A   19  1                                  17    
HELIX    2   2 ILE A   30  ASN A   35  1                                   6    
HELIX    3   3 ILE A   67  GLY A   81  1                                  15    
HELIX    4   4 GLY A   81  ILE A   89  1                                   9    
HELIX    5   5 SER A  100  HIS A  107  1                                   8    
HELIX    6   6 VAL A  116  ILE A  127  1                                  12    
HELIX    7   7 ASN A  131  GLY A  148  1                                  18    
HELIX    8   8 SER A  154  THR A  163  1                                  10    
HELIX    9   9 ASN A  165  GLY A  179  1                                  15    
HELIX   10  10 ASP A  184  CYS A  196  1                                  13    
HELIX   11  11 ASN A  201  ALA A  214  1                                  14    
HELIX   12  12 GLN A  227  ASP A  229  5                                   3    
HELIX   13  13 ASN A  230  GLY A  242  1                                  13    
HELIX   14  14 LEU A  243  GLY A  245  5                                   3    
HELIX   15  15 ARG A  246  VAL A  254  1                                   9    
HELIX   16  16 SER A  289  GLY A  304  1                                  16    
HELIX   17  17 ASP B    3  HIS B   19  1                                  17    
HELIX   18  18 ILE B   30  ASN B   35  1                                   6    
HELIX   19  19 ILE B   67  GLY B   81  1                                  15    
HELIX   20  20 GLY B   81  ILE B   89  1                                   9    
HELIX   21  21 SER B  100  LEU B  106  1                                   7    
HELIX   22  22 VAL B  116  ILE B  127  1                                  12    
HELIX   23  23 ASN B  131  GLY B  148  1                                  18    
HELIX   24  24 SER B  154  THR B  163  1                                  10    
HELIX   25  25 ASN B  165  GLY B  179  1                                  15    
HELIX   26  26 ASP B  184  CYS B  196  1                                  13    
HELIX   27  27 ASN B  201  ALA B  214  1                                  14    
HELIX   28  28 GLN B  227  ASP B  229  5                                   3    
HELIX   29  29 ASN B  230  GLY B  242  1                                  13    
HELIX   30  30 LEU B  243  GLY B  245  5                                   3    
HELIX   31  31 ARG B  246  VAL B  254  1                                   9    
HELIX   32  32 SER B  289  GLY B  304  1                                  16    
HELIX   33  33 ASP C    3  HIS C   19  1                                  17    
HELIX   34  34 ILE C   30  ASN C   35  1                                   6    
HELIX   35  35 ILE C   67  GLY C   81  1                                  15    
HELIX   36  36 GLY C   81  ILE C   89  1                                   9    
HELIX   37  37 SER C  100  LEU C  106  1                                   7    
HELIX   38  38 VAL C  116  ILE C  127  1                                  12    
HELIX   39  39 ASN C  131  GLY C  148  1                                  18    
HELIX   40  40 SER C  154  THR C  163  1                                  10    
HELIX   41  41 ASN C  165  GLY C  179  1                                  15    
HELIX   42  42 ASP C  184  SER C  197  1                                  14    
HELIX   43  43 ASN C  201  ALA C  214  1                                  14    
HELIX   44  44 GLN C  227  ASP C  229  5                                   3    
HELIX   45  45 ASN C  230  GLY C  242  1                                  13    
HELIX   46  46 LEU C  243  GLY C  245  5                                   3    
HELIX   47  47 ARG C  246  VAL C  254  1                                   9    
HELIX   48  48 SER C  289  GLY C  304  1                                  16    
HELIX   49  49 ASP D    3  HIS D   19  1                                  17    
HELIX   50  50 ILE D   30  ASN D   35  1                                   6    
HELIX   51  51 ILE D   67  GLY D   81  1                                  15    
HELIX   52  52 GLY D   81  ILE D   89  1                                   9    
HELIX   53  53 SER D  100  HIS D  107  1                                   8    
HELIX   54  54 VAL D  116  ILE D  127  1                                  12    
HELIX   55  55 ASN D  131  GLY D  148  1                                  18    
HELIX   56  56 SER D  154  THR D  163  1                                  10    
HELIX   57  57 ASN D  165  GLY D  179  1                                  15    
HELIX   58  58 ASP D  184  SER D  197  1                                  14    
HELIX   59  59 ASN D  201  ALA D  214  1                                  14    
HELIX   60  60 GLN D  227  ASP D  229  5                                   3    
HELIX   61  61 ASN D  230  GLY D  242  1                                  13    
HELIX   62  62 LEU D  243  GLY D  245  5                                   3    
HELIX   63  63 ARG D  246  VAL D  254  1                                   9    
HELIX   64  64 SER D  289  GLY D  304  1                                  16    
SHEET    1   A 5 VAL A  52  GLY A  56  0                                        
SHEET    2   A 5 ALA A  42  THR A  47 -1  N  ILE A  45   O  TYR A  53           
SHEET    3   A 5 MET A 274  PHE A 279 -1  O  ALA A 277   N  ALA A  44           
SHEET    4   A 5 GLY A 265  VAL A 270 -1  N  VAL A 270   O  MET A 274           
SHEET    5   A 5 GLY A 258  SER A 260 -1  N  LYS A 259   O  LEU A 267           
SHEET    1   B 3 PHE A  62  ALA A  63  0                                        
SHEET    2   B 3 THR A 198  LEU A 200 -1  O  LEU A 200   N  PHE A  62           
SHEET    3   B 3 ALA A 152  LEU A 153 -1  N  ALA A 152   O  LEU A 199           
SHEET    1   C 2 VAL A 217  ASN A 218  0                                        
SHEET    2   C 2 LYS A 223  ARG A 224 -1  O  LYS A 223   N  ASN A 218           
SHEET    1   D 5 VAL B  52  GLY B  56  0                                        
SHEET    2   D 5 ALA B  42  THR B  47 -1  N  ILE B  45   O  TYR B  53           
SHEET    3   D 5 MET B 274  PHE B 279 -1  O  ALA B 277   N  ALA B  44           
SHEET    4   D 5 GLY B 265  VAL B 270 -1  N  VAL B 270   O  MET B 274           
SHEET    5   D 5 GLY B 258  SER B 260 -1  N  LYS B 259   O  LEU B 267           
SHEET    1   E 3 PHE B  62  ALA B  63  0                                        
SHEET    2   E 3 THR B 198  LEU B 200 -1  O  LEU B 200   N  PHE B  62           
SHEET    3   E 3 ALA B 152  LEU B 153 -1  N  ALA B 152   O  LEU B 199           
SHEET    1   F 5 VAL C  52  GLY C  56  0                                        
SHEET    2   F 5 ALA C  42  THR C  47 -1  N  ILE C  45   O  TYR C  53           
SHEET    3   F 5 MET C 274  PHE C 279 -1  O  ALA C 277   N  ALA C  44           
SHEET    4   F 5 GLY C 265  VAL C 270 -1  N  VAL C 270   O  MET C 274           
SHEET    5   F 5 GLY C 258  SER C 260 -1  N  LYS C 259   O  LEU C 267           
SHEET    1   G 3 PHE C  62  ALA C  63  0                                        
SHEET    2   G 3 THR C 198  LEU C 200 -1  O  LEU C 200   N  PHE C  62           
SHEET    3   G 3 ALA C 152  LEU C 153 -1  N  ALA C 152   O  LEU C 199           
SHEET    1   H 5 VAL D  52  GLY D  56  0                                        
SHEET    2   H 5 ALA D  42  THR D  47 -1  N  ILE D  45   O  TYR D  53           
SHEET    3   H 5 MET D 274  PHE D 279 -1  O  ALA D 277   N  ALA D  44           
SHEET    4   H 5 GLY D 265  VAL D 270 -1  N  ALA D 268   O  ILE D 276           
SHEET    5   H 5 GLY D 258  SER D 260 -1  N  LYS D 259   O  LEU D 267           
SHEET    1   I 3 PHE D  62  ALA D  63  0                                        
SHEET    2   I 3 THR D 198  LEU D 200 -1  O  LEU D 200   N  PHE D  62           
SHEET    3   I 3 ALA D 152  LEU D 153 -1  N  ALA D 152   O  LEU D 199           
SHEET    1   J 2 VAL D 217  ASN D 218  0                                        
SHEET    2   J 2 LYS D 223  ARG D 224 -1  O  LYS D 223   N  ASN D 218           
SITE     1 AC1  4 LYS A 294  HOH A1377  THR B  16  GLN B  17                    
SITE     1 AC2  5 LYS A  88  GLY A 179  TYR A 180  EDO A1205                    
SITE     2 AC2  5 HOH A1527                                                     
SITE     1 AC3  3 ASP A  87  LYS A  88  EDO A1204                               
SITE     1 AC4  5 PHE A  98  GLY A 287  FMT A1212  HOH A1413                    
SITE     2 AC4  5 HOH A1415                                                     
SITE     1 AC5  5 ASP A  59  ASN A 201  HOH A1229  HOH A1285                    
SITE     2 AC5  5 HOH A1374                                                     
SITE     1 AC6  8 PRO A  37  GLN A  39  LEU A  40  HOH A1380                    
SITE     2 AC6  8 HOH A1462  HOH A1489  HIS D 222  HOH D1312                    
SITE     1 AC7  2 ASN B 128  ARG B 138                                          
SITE     1 AC8  8 GLU B  65  GLU B 161  ASN B 168  TYR B 192                    
SITE     2 AC8  8 THR B 193  HOH B1288  HOH B1404  HOH B1413                    
SITE     1 AC9  7 VAL C  52  ARG C 224  GLN C 227  HOH C1284                    
SITE     2 AC9  7 HOH C1298  HOH C1316  HOH C1382                               
SITE     1 BC1  8 GLU D  65  GLU D 161  ASN D 168  THR D 193                    
SITE     2 BC1  8 CYS D 196  HOH D1249  HOH D1293  HOH D1372                    
SITE     1 BC2  5 GLY D 287  FMT D1215  HOH D1418  HOH D1436                    
SITE     2 BC2  5 HOH D1486                                                     
SITE     1 BC3  2 GLN D  25  ASN D  26                                          
SITE     1 BC4  4 GLN A  25  ASP A 284  EDO A1211  HOH A1433                    
SITE     1 BC5  4 LEU A 199  HOH A1278  HOH A1347  HOH A1372                    
SITE     1 BC6  3 GLN B  39  ALA B 178  FMT B1207                               
SITE     1 BC7  7 GLN B  39  GLY B 179  TYR B 180  TYR B 182                    
SITE     2 BC7  7 FMT B1206  HOH B1410  HOH B1444                               
SITE     1 BC8  6 SER B 100  VAL B 101  ILE B 102  HOH B1460                    
SITE     2 BC8  6 GLU C 105  HOH C1430                                          
SITE     1 BC9  3 ASN B  22  GLY B  23  GLY B  24                               
SITE     1 CC1  4 ASN C  51  VAL C  52  GLU C  78  HOH C1427                    
SITE     1 CC2  3 ASN C  22  GLY C  23  ARG C 291                               
SITE     1 CC3  7 SER D  66  TYR D 244  VAL D 262  EDO D1214                    
SITE     2 CC3  7 HOH D1224  HOH D1242  HOH D1361                               
CRYST1   50.509  155.891  164.171  90.00  90.00  90.00 P 21 21 21   16          
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      0.019798  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006415  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006091        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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