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Database: PDB
Entry: 3I12
LinkDB: 3I12
Original site: 3I12 
HEADER    LIGASE                                  25-JUN-09   3I12              
TITLE     THE CRYSTAL STRUCTURE OF THE D-ALANYL-ALANINE SYNTHETASE A FROM       
TITLE    2 SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM STR. LT2     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE-D-ALANINE LIGASE A;                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: D-ALANYLALANINE SYNTHETASE A, D-ALA-D-ALA LIGASE A;         
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;                         
SOURCE   3 ORGANISM_TAXID: 90371;                                               
SOURCE   4 STRAIN: LT2';                                                        
SOURCE   5 GENE: DDLA, STM0380;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG19C                                  
KEYWDS    D-ALANYL-ALANINE SYNTHETASE A, ADP BINDING PROTEIN, CSGID, ATP-       
KEYWDS   2 BINDING, CELL SHAPE, CELL WALL BIOGENESIS/DEGRADATION, LIGASE,       
KEYWDS   3 MAGNESIUM, MANGANESE, METAL-BINDING, NUCLEOTIDE-BINDING,             
KEYWDS   4 PEPTIDOGLYCAN SYNTHESIS, STRUCTURAL GENOMICS, NIAID STRUCTURAL       
KEYWDS   5 GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.ZHANG,N.MALTSEVA,L.PAPAZISI,W.ANDERSON,A.JOACHIMIAK                 
REVDAT   2   13-JUL-11 3I12    1       VERSN                                    
REVDAT   1   18-AUG-09 3I12    0                                                
JRNL        AUTH   R.ZHANG,N.MALTSEVA,L.PAPAZISI,W.ANDERSON,A.JOACHIMIAK        
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE D-ALANYL-ALANINE SYNTHETASE A   
JRNL        TITL 2 FROM SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM 
JRNL        TITL 3 STR. LT2                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0054                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 82073                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4332                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5909                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 323                          
REMARK   3   BIN FREE R VALUE                    : 0.2890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10681                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 108                                     
REMARK   3   SOLVENT ATOMS            : 315                                     
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) : 28.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.82000                                             
REMARK   3    B22 (A**2) : -0.16000                                             
REMARK   3    B33 (A**2) : 0.98000                                              
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): 0.241         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.206         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.138         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.774        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11020 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7161 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15000 ; 1.976 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17605 ; 1.097 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1407 ; 7.250 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   491 ;39.509 ;25.316       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1806 ;18.166 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;23.242 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1755 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12347 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2053 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7020 ; 1.052 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2867 ; 0.247 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11295 ; 1.927 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4000 ; 3.101 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3705 ; 4.911 ; 4.500       
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 : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   100                          
REMARK   3    RESIDUE RANGE :   A   101        A   200                          
REMARK   3    RESIDUE RANGE :   A   201        A   300                          
REMARK   3    RESIDUE RANGE :   A   301        A   363                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.0560  26.3660  49.0370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1059 T22:   0.0156                                     
REMARK   3      T33:   0.0535 T12:  -0.0064                                     
REMARK   3      T13:   0.0527 T23:  -0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4112 L22:   0.7188                                     
REMARK   3      L33:   0.8869 L12:   0.1618                                     
REMARK   3      L13:  -0.1329 L23:  -0.6823                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0270 S12:   0.0204 S13:  -0.0227                       
REMARK   3      S21:  -0.0349 S22:   0.0664 S23:   0.0523                       
REMARK   3      S31:   0.1236 S32:  -0.0519 S33:  -0.0394                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   100                          
REMARK   3    RESIDUE RANGE :   B   101        B   200                          
REMARK   3    RESIDUE RANGE :   B   201        B   300                          
REMARK   3    RESIDUE RANGE :   B   301        B   363                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.9590  43.5170  36.6810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0653 T22:   0.0749                                     
REMARK   3      T33:   0.0644 T12:  -0.0139                                     
REMARK   3      T13:   0.0422 T23:   0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2044 L22:   0.2018                                     
REMARK   3      L33:   0.4110 L12:   0.0241                                     
REMARK   3      L13:   0.1340 L23:  -0.2137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0563 S12:   0.1117 S13:   0.1559                       
REMARK   3      S21:   0.0059 S22:   0.0455 S23:   0.0156                       
REMARK   3      S31:   0.0087 S32:   0.0557 S33:   0.0109                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C   100                          
REMARK   3    RESIDUE RANGE :   C   101        C   200                          
REMARK   3    RESIDUE RANGE :   C   201        C   300                          
REMARK   3    RESIDUE RANGE :   C   301        C   364                          
REMARK   3    ORIGIN FOR THE GROUP (A):  92.2480  34.4490   2.5640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0378 T22:   0.0469                                     
REMARK   3      T33:   0.0787 T12:   0.0107                                     
REMARK   3      T13:   0.0267 T23:  -0.0239                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5407 L22:   0.3529                                     
REMARK   3      L33:   0.8511 L12:   0.1603                                     
REMARK   3      L13:  -0.2339 L23:  -0.0748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0392 S12:   0.0313 S13:  -0.0761                       
REMARK   3      S21:  -0.0399 S22:  -0.0764 S23:   0.0717                       
REMARK   3      S31:   0.1385 S32:  -0.0386 S33:   0.1155                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     3        D   100                          
REMARK   3    RESIDUE RANGE :   D   101        D   200                          
REMARK   3    RESIDUE RANGE :   D   201        D   300                          
REMARK   3    RESIDUE RANGE :   D   301        D   363                          
REMARK   3    ORIGIN FOR THE GROUP (A): 108.5330  57.3570   5.6250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0066 T22:   0.0845                                     
REMARK   3      T33:   0.1119 T12:   0.0138                                     
REMARK   3      T13:   0.0135 T23:   0.0523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8494 L22:   0.5663                                     
REMARK   3      L33:   0.4012 L12:   0.4847                                     
REMARK   3      L13:  -0.2587 L23:  -0.1912                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0276 S12:   0.0161 S13:   0.1346                       
REMARK   3      S21:   0.0266 S22:  -0.0726 S23:   0.0344                       
REMARK   3      S31:   0.0186 S32:   0.0579 S33:   0.0450                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3I12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053830.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-08                          
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) : 0.9794, 0.9796                     
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL3000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL3000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82073                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 115.470                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.800                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.5600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.340                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: HKL3000_SOLVE                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 25% PEG3350, PH 7.5, VAPOR   
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 289K                           
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       42.57650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      115.44650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.90650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      115.44650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.57650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.90650            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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: 5790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 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     TYR A   254                                                      
REMARK 465     ALA A   255                                                      
REMARK 465     MET A   364                                                      
REMARK 465     ASN B   250                                                      
REMARK 465     SER B   251                                                      
REMARK 465     GLU B   252                                                      
REMARK 465     PHE B   253                                                      
REMARK 465     TYR B   254                                                      
REMARK 465     ALA B   255                                                      
REMARK 465     TYR B   256                                                      
REMARK 465     ASP B   257                                                      
REMARK 465     THR B   258                                                      
REMARK 465     LYS B   259                                                      
REMARK 465     TYR B   260                                                      
REMARK 465     ILE B   261                                                      
REMARK 465     ASP B   262                                                      
REMARK 465     ASP B   263                                                      
REMARK 465     ASN B   264                                                      
REMARK 465     GLY B   265                                                      
REMARK 465     ALA B   266                                                      
REMARK 465     MET B   364                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASN C   250                                                      
REMARK 465     SER C   251                                                      
REMARK 465     GLU C   252                                                      
REMARK 465     PHE C   253                                                      
REMARK 465     TYR C   254                                                      
REMARK 465     ALA C   255                                                      
REMARK 465     TYR C   256                                                      
REMARK 465     ASP C   257                                                      
REMARK 465     THR C   258                                                      
REMARK 465     LYS C   259                                                      
REMARK 465     TYR C   260                                                      
REMARK 465     ILE C   261                                                      
REMARK 465     ASP C   262                                                      
REMARK 465     ASP C   263                                                      
REMARK 465     ASN C   264                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     TYR D   254                                                      
REMARK 465     ALA D   255                                                      
REMARK 465     TYR D   256                                                      
REMARK 465     ASP D   257                                                      
REMARK 465     THR D   258                                                      
REMARK 465     LYS D   259                                                      
REMARK 465     MET D   364                                                      
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     SER A  72    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU D   315     O1A  ADP D   365              2.02            
REMARK 500   NE2  GLN C   273     O    HOH C   381              2.09            
REMARK 500   OG1  THR D   306     OD1  ASP D   308              2.15            
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    ASP A  44   CB    ASP A  44   CG     -0.151                       
REMARK 500    GLU B 221   CB    GLU B 221   CG     -0.130                       
REMARK 500    GLU B 348   CB    GLU B 348   CG     -0.145                       
REMARK 500    ASP C  44   CB    ASP C  44   CG     -0.194                       
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    LEU A  41   CB  -  CG  -  CD1 ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ASP A  44   CB  -  CA  -  C   ANGL. DEV. = -17.0 DEGREES          
REMARK 500    ASP A  44   CB  -  CG  -  OD1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A 353   CG  -  CD  -  NE  ANGL. DEV. = -16.8 DEGREES          
REMARK 500    ARG A 353   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A 353   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    VAL B 101   CB  -  CA  -  C   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    MET B 139   CG  -  SD  -  CE  ANGL. DEV. = -15.8 DEGREES          
REMARK 500    ARG B 163   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG B 163   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG B 283   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    LEU B 293   CA  -  CB  -  CG  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ASP C  44   CB  -  CG  -  OD1 ANGL. DEV. = -16.2 DEGREES          
REMARK 500    ASP C  44   CB  -  CG  -  OD2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ALA C  54   N   -  CA  -  C   ANGL. DEV. =  21.4 DEGREES          
REMARK 500    GLU C  55   N   -  CA  -  CB  ANGL. DEV. = -25.8 DEGREES          
REMARK 500    VAL C 101   CB  -  CA  -  C   ANGL. DEV. = -12.0 DEGREES          
REMARK 500    ARG C 146   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG C 163   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG C 353   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG C 353   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    VAL D 101   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    ARG D 146   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    MET D 298   CG  -  SD  -  CE  ANGL. DEV. = -15.2 DEGREES          
REMARK 500    LEU D 319   CB  -  CG  -  CD1 ANGL. DEV. =  10.2 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    ASP A  32       91.81    -58.02                                   
REMARK 500    ASP A  44      161.42    -46.98                                   
REMARK 500    ILE A 105       32.87   -140.60                                   
REMARK 500    GLN A 189     -128.37   -120.89                                   
REMARK 500    SER A 192       -7.97     56.23                                   
REMARK 500    ASN A 236      -82.50   -115.04                                   
REMARK 500    THR A 258       43.57   -146.87                                   
REMARK 500    ALA B   2      135.75    178.65                                   
REMARK 500    ASP B  32       98.04    -66.30                                   
REMARK 500    ASN B  56       67.58   -162.09                                   
REMARK 500    HIS B  66      -15.82     83.84                                   
REMARK 500    GLN B 189      154.96    176.27                                   
REMARK 500    SER B 191       80.57    -11.26                                   
REMARK 500    ASN B 236     -101.21   -110.23                                   
REMARK 500    ASN B 238       76.20   -117.48                                   
REMARK 500    ASP C  32       97.92    -64.96                                   
REMARK 500    ASP C  44      157.66    -45.77                                   
REMARK 500    ALA C  54      -35.78    -38.80                                   
REMARK 500    ASN C  56       76.97   -159.49                                   
REMARK 500    ASP C  63       95.97    -60.48                                   
REMARK 500    HIS C  66       -7.11     99.64                                   
REMARK 500    ASN C  92       -1.04   -142.99                                   
REMARK 500    GLN C 189     -113.04   -136.41                                   
REMARK 500    SER C 192       -7.45     43.72                                   
REMARK 500    ASN C 236     -102.80   -110.54                                   
REMARK 500    ASN C 238       70.28   -113.01                                   
REMARK 500    SER D  14      146.94    -35.88                                   
REMARK 500    LEU D  41       76.97   -109.24                                   
REMARK 500    ASN D  56       78.65   -159.57                                   
REMARK 500    ILE D 105       32.94   -141.01                                   
REMARK 500    GLN D 189      -81.89   -142.55                                   
REMARK 500    SER D 192       10.08     41.63                                   
REMARK 500    ASN D 236      -81.99   -115.24                                   
REMARK 500    ASN D 264       16.30     86.59                                   
REMARK 500    ALA D 266      166.22    -48.29                                   
REMARK 500    THR D 362      -61.20   -130.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN C  188     GLN C  189                   64.25                    
REMARK 500 SER D  191     SER D  192                 -145.68                    
REMARK 500 VAL D  193     GLY D  194                  -64.25                    
REMARK 500 ASN D  264     GLY D  265                  -43.46                    
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    THR A 109        22.6      L          L   OUTSIDE RANGE           
REMARK 500    THR B 109        23.9      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 128        22.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 143        20.7      L          L   OUTSIDE RANGE           
REMARK 500    THR B 160        24.4      L          L   OUTSIDE RANGE           
REMARK 500    SER B 191        24.3      L          L   OUTSIDE RANGE           
REMARK 500    ALA C  54        14.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU C  55        54.3      L          L   OUTSIDE RANGE           
REMARK 500    THR D 109        25.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL D 128        23.6      L          L   OUTSIDE RANGE           
REMARK 500    VAL D 143        22.8      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 ADP A 365                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 365                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 365                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 365                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP00919   RELATED DB: TARGETDB                          
DBREF  3I12 A    1   364  UNP    P0A1F0   DDLA_SALTY       1    364             
DBREF  3I12 B    1   364  UNP    P0A1F0   DDLA_SALTY       1    364             
DBREF  3I12 C    1   364  UNP    P0A1F0   DDLA_SALTY       1    364             
DBREF  3I12 D    1   364  UNP    P0A1F0   DDLA_SALTY       1    364             
SEQRES   1 A  364  MET ALA LYS LEU ARG VAL GLY ILE VAL PHE GLY GLY LYS          
SEQRES   2 A  364  SER ALA GLU HIS GLU VAL SER LEU GLN SER ALA LYS ASN          
SEQRES   3 A  364  ILE VAL ASP ALA ILE ASP LYS THR ARG PHE ASP VAL VAL          
SEQRES   4 A  364  LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP HIS VAL ASN          
SEQRES   5 A  364  ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP ASP PRO ALA          
SEQRES   6 A  364  HIS ILE ALA LEU ARG PRO SER ALA ILE SER LEU ALA GLN          
SEQRES   7 A  364  VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE ASN ALA GLN          
SEQRES   8 A  364  ASN GLY GLN PRO LEU PRO THR VAL ASP VAL ILE PHE PRO          
SEQRES   9 A  364  ILE VAL HIS GLY THR LEU GLY GLU ASP GLY SER LEU GLN          
SEQRES  10 A  364  GLY MET LEU ARG VAL ALA ASN LEU PRO PHE VAL GLY SER          
SEQRES  11 A  364  ASP VAL LEU SER SER ALA ALA CYS MET ASP LYS ASP VAL          
SEQRES  12 A  364  ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU ASN ILE ALA          
SEQRES  13 A  364  PRO PHE ILE THR LEU THR ARG THR ASN ARG HIS ALA PHE          
SEQRES  14 A  364  SER PHE ALA GLU VAL GLU SER ARG LEU GLY LEU PRO LEU          
SEQRES  15 A  364  PHE VAL LYS PRO ALA ASN GLN GLY SER SER VAL GLY VAL          
SEQRES  16 A  364  SER LYS VAL ALA ASN GLU ALA GLN TYR GLN GLN ALA VAL          
SEQRES  17 A  364  ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL VAL VAL GLU          
SEQRES  18 A  364  GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS ALA VAL LEU          
SEQRES  19 A  364  GLY ASN ASP ASN PRO GLN ALA SER THR CYS GLY GLU ILE          
SEQRES  20 A  364  VAL LEU ASN SER GLU PHE TYR ALA TYR ASP THR LYS TYR          
SEQRES  21 A  364  ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL PRO ALA GLN          
SEQRES  22 A  364  ILE PRO SER GLU VAL ASN ASP LYS ILE ARG ALA ILE ALA          
SEQRES  23 A  364  ILE GLN ALA TYR GLN THR LEU GLY CYS ALA GLY MET ALA          
SEQRES  24 A  364  ARG VAL ASP VAL PHE LEU THR ALA ASP ASN GLU VAL VAL          
SEQRES  25 A  364  ILE ASN GLU ILE ASN THR LEU PRO GLY PHE THR ASN ILE          
SEQRES  26 A  364  SER MET TYR PRO LYS LEU TRP GLN ALA SER GLY LEU GLY          
SEQRES  27 A  364  TYR THR ASP LEU ILE SER ARG LEU ILE GLU LEU ALA LEU          
SEQRES  28 A  364  GLU ARG HIS THR ALA ASN ASN ALA LEU LYS THR THR MET          
SEQRES   1 B  364  MET ALA LYS LEU ARG VAL GLY ILE VAL PHE GLY GLY LYS          
SEQRES   2 B  364  SER ALA GLU HIS GLU VAL SER LEU GLN SER ALA LYS ASN          
SEQRES   3 B  364  ILE VAL ASP ALA ILE ASP LYS THR ARG PHE ASP VAL VAL          
SEQRES   4 B  364  LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP HIS VAL ASN          
SEQRES   5 B  364  ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP ASP PRO ALA          
SEQRES   6 B  364  HIS ILE ALA LEU ARG PRO SER ALA ILE SER LEU ALA GLN          
SEQRES   7 B  364  VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE ASN ALA GLN          
SEQRES   8 B  364  ASN GLY GLN PRO LEU PRO THR VAL ASP VAL ILE PHE PRO          
SEQRES   9 B  364  ILE VAL HIS GLY THR LEU GLY GLU ASP GLY SER LEU GLN          
SEQRES  10 B  364  GLY MET LEU ARG VAL ALA ASN LEU PRO PHE VAL GLY SER          
SEQRES  11 B  364  ASP VAL LEU SER SER ALA ALA CYS MET ASP LYS ASP VAL          
SEQRES  12 B  364  ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU ASN ILE ALA          
SEQRES  13 B  364  PRO PHE ILE THR LEU THR ARG THR ASN ARG HIS ALA PHE          
SEQRES  14 B  364  SER PHE ALA GLU VAL GLU SER ARG LEU GLY LEU PRO LEU          
SEQRES  15 B  364  PHE VAL LYS PRO ALA ASN GLN GLY SER SER VAL GLY VAL          
SEQRES  16 B  364  SER LYS VAL ALA ASN GLU ALA GLN TYR GLN GLN ALA VAL          
SEQRES  17 B  364  ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL VAL VAL GLU          
SEQRES  18 B  364  GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS ALA VAL LEU          
SEQRES  19 B  364  GLY ASN ASP ASN PRO GLN ALA SER THR CYS GLY GLU ILE          
SEQRES  20 B  364  VAL LEU ASN SER GLU PHE TYR ALA TYR ASP THR LYS TYR          
SEQRES  21 B  364  ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL PRO ALA GLN          
SEQRES  22 B  364  ILE PRO SER GLU VAL ASN ASP LYS ILE ARG ALA ILE ALA          
SEQRES  23 B  364  ILE GLN ALA TYR GLN THR LEU GLY CYS ALA GLY MET ALA          
SEQRES  24 B  364  ARG VAL ASP VAL PHE LEU THR ALA ASP ASN GLU VAL VAL          
SEQRES  25 B  364  ILE ASN GLU ILE ASN THR LEU PRO GLY PHE THR ASN ILE          
SEQRES  26 B  364  SER MET TYR PRO LYS LEU TRP GLN ALA SER GLY LEU GLY          
SEQRES  27 B  364  TYR THR ASP LEU ILE SER ARG LEU ILE GLU LEU ALA LEU          
SEQRES  28 B  364  GLU ARG HIS THR ALA ASN ASN ALA LEU LYS THR THR MET          
SEQRES   1 C  364  MET ALA LYS LEU ARG VAL GLY ILE VAL PHE GLY GLY LYS          
SEQRES   2 C  364  SER ALA GLU HIS GLU VAL SER LEU GLN SER ALA LYS ASN          
SEQRES   3 C  364  ILE VAL ASP ALA ILE ASP LYS THR ARG PHE ASP VAL VAL          
SEQRES   4 C  364  LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP HIS VAL ASN          
SEQRES   5 C  364  ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP ASP PRO ALA          
SEQRES   6 C  364  HIS ILE ALA LEU ARG PRO SER ALA ILE SER LEU ALA GLN          
SEQRES   7 C  364  VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE ASN ALA GLN          
SEQRES   8 C  364  ASN GLY GLN PRO LEU PRO THR VAL ASP VAL ILE PHE PRO          
SEQRES   9 C  364  ILE VAL HIS GLY THR LEU GLY GLU ASP GLY SER LEU GLN          
SEQRES  10 C  364  GLY MET LEU ARG VAL ALA ASN LEU PRO PHE VAL GLY SER          
SEQRES  11 C  364  ASP VAL LEU SER SER ALA ALA CYS MET ASP LYS ASP VAL          
SEQRES  12 C  364  ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU ASN ILE ALA          
SEQRES  13 C  364  PRO PHE ILE THR LEU THR ARG THR ASN ARG HIS ALA PHE          
SEQRES  14 C  364  SER PHE ALA GLU VAL GLU SER ARG LEU GLY LEU PRO LEU          
SEQRES  15 C  364  PHE VAL LYS PRO ALA ASN GLN GLY SER SER VAL GLY VAL          
SEQRES  16 C  364  SER LYS VAL ALA ASN GLU ALA GLN TYR GLN GLN ALA VAL          
SEQRES  17 C  364  ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL VAL VAL GLU          
SEQRES  18 C  364  GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS ALA VAL LEU          
SEQRES  19 C  364  GLY ASN ASP ASN PRO GLN ALA SER THR CYS GLY GLU ILE          
SEQRES  20 C  364  VAL LEU ASN SER GLU PHE TYR ALA TYR ASP THR LYS TYR          
SEQRES  21 C  364  ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL PRO ALA GLN          
SEQRES  22 C  364  ILE PRO SER GLU VAL ASN ASP LYS ILE ARG ALA ILE ALA          
SEQRES  23 C  364  ILE GLN ALA TYR GLN THR LEU GLY CYS ALA GLY MET ALA          
SEQRES  24 C  364  ARG VAL ASP VAL PHE LEU THR ALA ASP ASN GLU VAL VAL          
SEQRES  25 C  364  ILE ASN GLU ILE ASN THR LEU PRO GLY PHE THR ASN ILE          
SEQRES  26 C  364  SER MET TYR PRO LYS LEU TRP GLN ALA SER GLY LEU GLY          
SEQRES  27 C  364  TYR THR ASP LEU ILE SER ARG LEU ILE GLU LEU ALA LEU          
SEQRES  28 C  364  GLU ARG HIS THR ALA ASN ASN ALA LEU LYS THR THR MET          
SEQRES   1 D  364  MET ALA LYS LEU ARG VAL GLY ILE VAL PHE GLY GLY LYS          
SEQRES   2 D  364  SER ALA GLU HIS GLU VAL SER LEU GLN SER ALA LYS ASN          
SEQRES   3 D  364  ILE VAL ASP ALA ILE ASP LYS THR ARG PHE ASP VAL VAL          
SEQRES   4 D  364  LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP HIS VAL ASN          
SEQRES   5 D  364  ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP ASP PRO ALA          
SEQRES   6 D  364  HIS ILE ALA LEU ARG PRO SER ALA ILE SER LEU ALA GLN          
SEQRES   7 D  364  VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE ASN ALA GLN          
SEQRES   8 D  364  ASN GLY GLN PRO LEU PRO THR VAL ASP VAL ILE PHE PRO          
SEQRES   9 D  364  ILE VAL HIS GLY THR LEU GLY GLU ASP GLY SER LEU GLN          
SEQRES  10 D  364  GLY MET LEU ARG VAL ALA ASN LEU PRO PHE VAL GLY SER          
SEQRES  11 D  364  ASP VAL LEU SER SER ALA ALA CYS MET ASP LYS ASP VAL          
SEQRES  12 D  364  ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU ASN ILE ALA          
SEQRES  13 D  364  PRO PHE ILE THR LEU THR ARG THR ASN ARG HIS ALA PHE          
SEQRES  14 D  364  SER PHE ALA GLU VAL GLU SER ARG LEU GLY LEU PRO LEU          
SEQRES  15 D  364  PHE VAL LYS PRO ALA ASN GLN GLY SER SER VAL GLY VAL          
SEQRES  16 D  364  SER LYS VAL ALA ASN GLU ALA GLN TYR GLN GLN ALA VAL          
SEQRES  17 D  364  ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL VAL VAL GLU          
SEQRES  18 D  364  GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS ALA VAL LEU          
SEQRES  19 D  364  GLY ASN ASP ASN PRO GLN ALA SER THR CYS GLY GLU ILE          
SEQRES  20 D  364  VAL LEU ASN SER GLU PHE TYR ALA TYR ASP THR LYS TYR          
SEQRES  21 D  364  ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL PRO ALA GLN          
SEQRES  22 D  364  ILE PRO SER GLU VAL ASN ASP LYS ILE ARG ALA ILE ALA          
SEQRES  23 D  364  ILE GLN ALA TYR GLN THR LEU GLY CYS ALA GLY MET ALA          
SEQRES  24 D  364  ARG VAL ASP VAL PHE LEU THR ALA ASP ASN GLU VAL VAL          
SEQRES  25 D  364  ILE ASN GLU ILE ASN THR LEU PRO GLY PHE THR ASN ILE          
SEQRES  26 D  364  SER MET TYR PRO LYS LEU TRP GLN ALA SER GLY LEU GLY          
SEQRES  27 D  364  TYR THR ASP LEU ILE SER ARG LEU ILE GLU LEU ALA LEU          
SEQRES  28 D  364  GLU ARG HIS THR ALA ASN ASN ALA LEU LYS THR THR MET          
HET    ADP  A 365      27                                                       
HET    ADP  B 365      27                                                       
HET    ADP  C 365      27                                                       
HET    ADP  D 365      27                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   5  ADP    4(C10 H15 N5 O10 P2)                                         
FORMUL   9  HOH   *315(H2 O)                                                    
HELIX    1   1 GLU A   16  ILE A   31  1                                  16    
HELIX    2   2 GLY A  114  ALA A  123  1                                  10    
HELIX    3   3 ASP A  131  ASP A  140  1                                  10    
HELIX    4   4 ASP A  140  ALA A  151  1                                  12    
HELIX    5   5 ASN A  165  PHE A  169  5                                   5    
HELIX    6   6 SER A  170  GLY A  179  1                                  10    
HELIX    7   7 ASN A  200  ASP A  215  1                                  16    
HELIX    8   8 ILE A  261  ALA A  266  5                                   6    
HELIX    9   9 PRO A  275  LEU A  293  1                                  19    
HELIX   10  10 SER A  326  ALA A  334  1                                   9    
HELIX   11  11 GLY A  338  LEU A  360  1                                  23    
HELIX   12  12 GLU B   16  ILE B   31  1                                  16    
HELIX   13  13 GLY B  114  ALA B  123  1                                  10    
HELIX   14  14 ASP B  131  ASP B  140  1                                  10    
HELIX   15  15 ASP B  140  ALA B  151  1                                  12    
HELIX   16  16 SER B  170  GLY B  179  1                                  10    
HELIX   17  17 ASN B  200  PHE B  212  1                                  13    
HELIX   18  18 PRO B  275  LEU B  293  1                                  19    
HELIX   19  19 SER B  326  ALA B  334  1                                   9    
HELIX   20  20 GLY B  338  ALA B  359  1                                  22    
HELIX   21  21 GLU C   16  ILE C   31  1                                  16    
HELIX   22  22 GLY C  108  ASP C  113  1                                   6    
HELIX   23  23 GLY C  114  ALA C  123  1                                  10    
HELIX   24  24 ASP C  131  ASP C  140  1                                  10    
HELIX   25  25 ASP C  140  ALA C  151  1                                  12    
HELIX   26  26 SER C  170  GLY C  179  1                                  10    
HELIX   27  27 ASN C  200  PHE C  212  1                                  13    
HELIX   28  28 PRO C  275  LEU C  293  1                                  19    
HELIX   29  29 SER C  326  ALA C  334  1                                   9    
HELIX   30  30 GLY C  338  LEU C  360  1                                  23    
HELIX   31  31 GLU D   16  ILE D   31  1                                  16    
HELIX   32  32 GLY D  114  ALA D  123  1                                  10    
HELIX   33  33 ASP D  131  ASP D  140  1                                  10    
HELIX   34  34 ASP D  140  ALA D  151  1                                  12    
HELIX   35  35 ASN D  165  PHE D  169  5                                   5    
HELIX   36  36 SER D  170  GLY D  179  1                                  10    
HELIX   37  37 ASN D  200  ASP D  215  1                                  16    
HELIX   38  38 ILE D  261  ALA D  266  5                                   6    
HELIX   39  39 PRO D  275  LEU D  293  1                                  19    
HELIX   40  40 SER D  326  ALA D  334  1                                   9    
HELIX   41  41 GLY D  338  LEU D  360  1                                  23    
SHEET    1   A 4 TRP A  49  ASN A  52  0                                        
SHEET    2   A 4 PHE A  36  ILE A  43 -1  N  LEU A  40   O  ASN A  52           
SHEET    3   A 4 LEU A   4  GLY A  11  1  N  VAL A   6   O  ASP A  37           
SHEET    4   A 4 VAL A 101  PRO A 104  1  O  PHE A 103   N  GLY A   7           
SHEET    1   B 2 LEU A  76  GLN A  78  0                                        
SHEET    2   B 2 LEU A  87  ASN A  89 -1  O  ILE A  88   N  ALA A  77           
SHEET    1   C 4 PHE A 158  THR A 162  0                                        
SHEET    2   C 4 LYS A 217  GLN A 222 -1  O  VAL A 218   N  LEU A 161           
SHEET    3   C 4 LEU A 182  PRO A 186 -1  N  LYS A 185   O  VAL A 219           
SHEET    4   C 4 SER A 196  VAL A 198 -1  O  VAL A 198   N  LEU A 182           
SHEET    1   D 5 GLN A 267  VAL A 269  0                                        
SHEET    2   D 5 GLN A 240  VAL A 248 -1  N  GLU A 246   O  VAL A 269           
SHEET    3   D 5 ARG A 227  GLY A 235 -1  N  LEU A 234   O  GLN A 240           
SHEET    4   D 5 GLY A 297  LEU A 305 -1  O  VAL A 303   N  ILE A 229           
SHEET    5   D 5 VAL A 311  ASN A 317 -1  O  VAL A 312   N  PHE A 304           
SHEET    1   E 4 TRP B  49  ASN B  52  0                                        
SHEET    2   E 4 PHE B  36  ILE B  43 -1  N  LEU B  40   O  ASN B  52           
SHEET    3   E 4 LEU B   4  GLY B  11  1  N  PHE B  10   O  ILE B  43           
SHEET    4   E 4 VAL B 101  PRO B 104  1  O  PHE B 103   N  GLY B   7           
SHEET    1   F 2 LEU B  58  GLN B  59  0                                        
SHEET    2   F 2 ALA B  68  LEU B  69 -1  O  ALA B  68   N  GLN B  59           
SHEET    1   G 2 LEU B  76  GLN B  78  0                                        
SHEET    2   G 2 LEU B  87  ASN B  89 -1  O  ILE B  88   N  ALA B  77           
SHEET    1   H 4 PHE B 158  THR B 162  0                                        
SHEET    2   H 4 LYS B 217  GLN B 222 -1  O  VAL B 218   N  LEU B 161           
SHEET    3   H 4 LEU B 182  PRO B 186 -1  N  LYS B 185   O  VAL B 219           
SHEET    4   H 4 SER B 196  VAL B 198 -1  O  VAL B 198   N  LEU B 182           
SHEET    1   I 5 VAL B 268  VAL B 269  0                                        
SHEET    2   I 5 GLN B 240  ILE B 247 -1  N  GLU B 246   O  VAL B 269           
SHEET    3   I 5 ARG B 227  GLY B 235 -1  N  ALA B 232   O  SER B 242           
SHEET    4   I 5 GLY B 297  LEU B 305 -1  O  ALA B 299   N  VAL B 233           
SHEET    5   I 5 VAL B 311  ASN B 317 -1  O  VAL B 312   N  PHE B 304           
SHEET    1   J 4 TRP C  49  ASN C  52  0                                        
SHEET    2   J 4 PHE C  36  ILE C  43 -1  N  LEU C  40   O  ASN C  52           
SHEET    3   J 4 LEU C   4  GLY C  11  1  N  PHE C  10   O  ILE C  43           
SHEET    4   J 4 VAL C 101  PRO C 104  1  O  VAL C 101   N  GLY C   7           
SHEET    1   K 2 LEU C  58  GLN C  59  0                                        
SHEET    2   K 2 ALA C  68  LEU C  69 -1  O  ALA C  68   N  GLN C  59           
SHEET    1   L 2 LEU C  76  GLN C  78  0                                        
SHEET    2   L 2 LEU C  87  ASN C  89 -1  O  ILE C  88   N  ALA C  77           
SHEET    1   M 4 PHE C 158  THR C 162  0                                        
SHEET    2   M 4 LYS C 217  GLN C 222 -1  O  VAL C 218   N  LEU C 161           
SHEET    3   M 4 LEU C 182  PRO C 186 -1  N  LYS C 185   O  VAL C 219           
SHEET    4   M 4 SER C 196  VAL C 198 -1  O  VAL C 198   N  LEU C 182           
SHEET    1   N 4 GLN C 240  ALA C 241  0                                        
SHEET    2   N 4 ARG C 227  GLY C 235 -1  N  LEU C 234   O  GLN C 240           
SHEET    3   N 4 GLY C 245  VAL C 248 -1  O  GLY C 245   N  GLU C 230           
SHEET    4   N 4 GLN C 267  VAL C 269 -1  O  VAL C 269   N  GLU C 246           
SHEET    1   O 4 GLN C 240  ALA C 241  0                                        
SHEET    2   O 4 ARG C 227  GLY C 235 -1  N  LEU C 234   O  GLN C 240           
SHEET    3   O 4 GLY C 297  LEU C 305 -1  O  VAL C 301   N  CYS C 231           
SHEET    4   O 4 VAL C 311  ASN C 317 -1  O  VAL C 312   N  PHE C 304           
SHEET    1   P 4 TRP D  49  ASN D  52  0                                        
SHEET    2   P 4 PHE D  36  ILE D  43 -1  N  LEU D  40   O  ASN D  52           
SHEET    3   P 4 LEU D   4  GLY D  11  1  N  ILE D   8   O  LEU D  41           
SHEET    4   P 4 VAL D 101  PRO D 104  1  O  VAL D 101   N  GLY D   7           
SHEET    1   Q 2 LEU D  58  GLN D  59  0                                        
SHEET    2   Q 2 ALA D  68  LEU D  69 -1  O  ALA D  68   N  GLN D  59           
SHEET    1   R 2 LEU D  76  GLN D  78  0                                        
SHEET    2   R 2 LEU D  87  ASN D  89 -1  O  ILE D  88   N  ALA D  77           
SHEET    1   S 4 PHE D 158  THR D 162  0                                        
SHEET    2   S 4 LYS D 217  GLN D 222 -1  O  VAL D 218   N  LEU D 161           
SHEET    3   S 4 LEU D 182  PRO D 186 -1  N  LYS D 185   O  VAL D 219           
SHEET    4   S 4 SER D 196  VAL D 198 -1  O  VAL D 198   N  LEU D 182           
SHEET    1   T 5 GLN D 267  VAL D 269  0                                        
SHEET    2   T 5 GLN D 240  VAL D 248 -1  N  GLU D 246   O  VAL D 269           
SHEET    3   T 5 ARG D 227  GLY D 235 -1  N  ALA D 232   O  SER D 242           
SHEET    4   T 5 GLY D 297  LEU D 305 -1  O  ALA D 299   N  VAL D 233           
SHEET    5   T 5 VAL D 311  ASN D 317 -1  O  VAL D 312   N  PHE D 304           
CISPEP   1 LEU A  180    PRO A  181          0         3.06                     
CISPEP   2 VAL A  270    PRO A  271          0         1.74                     
CISPEP   3 LEU B  180    PRO B  181          0        -6.03                     
CISPEP   4 VAL B  270    PRO B  271          0        -0.19                     
CISPEP   5 LEU C  180    PRO C  181          0       -11.97                     
CISPEP   6 VAL C  270    PRO C  271          0       -10.32                     
CISPEP   7 LEU D  180    PRO D  181          0        -7.94                     
CISPEP   8 GLY D  190    SER D  191          0        19.41                     
CISPEP   9 VAL D  270    PRO D  271          0        -1.83                     
SITE     1 AC1 17 LYS A 141  PHE A 183  LYS A 185  GLY A 190                    
SITE     2 AC1 17 SER A 191  SER A 192  GLU A 221  GLN A 222                    
SITE     3 AC1 17 GLY A 223  ILE A 224  GLU A 228  LEU A 249                    
SITE     4 AC1 17 PHE A 304  ASN A 314  GLU A 315  HOH A 371                    
SITE     5 AC1 17 HOH A 374                                                     
SITE     1 AC2 14 LYS B 141  PHE B 183  LYS B 185  GLY B 190                    
SITE     2 AC2 14 SER B 191  SER B 192  GLU B 221  GLN B 222                    
SITE     3 AC2 14 GLY B 223  ILE B 224  GLU B 228  PHE B 304                    
SITE     4 AC2 14 ASN B 314  GLU B 315                                          
SITE     1 AC3 13 PHE C 183  LYS C 185  GLY C 190  SER C 191                    
SITE     2 AC3 13 SER C 192  GLU C 221  GLN C 222  GLY C 223                    
SITE     3 AC3 13 ILE C 224  GLU C 228  PHE C 304  ASN C 314                    
SITE     4 AC3 13 GLU C 315                                                     
SITE     1 AC4 16 LYS D 141  PHE D 183  LYS D 185  SER D 191                    
SITE     2 AC4 16 SER D 192  GLU D 221  GLN D 222  GLY D 223                    
SITE     3 AC4 16 ILE D 224  GLU D 228  LEU D 249  PHE D 304                    
SITE     4 AC4 16 ASN D 314  GLU D 315  HOH D 415  HOH D 443                    
CRYST1   85.153   85.813  230.893  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      0.011744  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011653  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004331        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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