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Database: PDB
Entry: 3Q8N
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Original site: 3Q8N 
HEADER    TRANSFERASE                             06-JAN-11   3Q8N              
TITLE     CRYSTAL STRUCTURE OF 4-AMINOBUTYRATE TRANSAMINASE FROM MYCOBACTERIUM  
TITLE    2 SMEGMATIS                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 4-AMINOBUTYRATE TRANSAMINASE;                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 2.6.1.19;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;                        
SOURCE   3 ORGANISM_TAXID: 246196;                                              
SOURCE   4 STRAIN: ATCC 700084 / MC(2)155;                                      
SOURCE   5 GENE: GABT, MSMEG_0581;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: AVA0421                                   
KEYWDS    SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR   
KEYWDS   2 INFECTIOUS DISEASE, TRANSFERASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   1   09-FEB-11 3Q8N    0                                                
JRNL        AUTH   SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE    
JRNL        AUTH 2 (SSGCID),A.GARDBERG,T.EDWARDS,B.STAKER,L.STEWART             
JRNL        TITL   CRYSTAL STRUCTURE OF 4-AMINOBUTYRATE TRANSAMINASE FROM       
JRNL        TITL 2 MYCOBACTERIUM SMEGMATIS                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 100170                         
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) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5025                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6109                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.36                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 297                          
REMARK   3   BIN FREE R VALUE                    : 0.3720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12772                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 733                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.79                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.13000                                              
REMARK   3    B22 (A**2) : -0.51000                                             
REMARK   3    B33 (A**2) : 0.65000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.37000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.191         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.135         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.402        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13087 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  8432 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17859 ; 1.476 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20624 ; 0.952 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1766 ; 6.257 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   529 ;37.959 ;23.856       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1910 ;13.753 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    88 ;18.045 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2096 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15072 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2588 ; 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):  8690 ; 0.647 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3612 ; 0.179 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13859 ; 1.160 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4397 ; 2.151 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3992 ; 3.504 ; 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 : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   450                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3720  60.4700 -25.4730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0124 T22:   0.0150                                     
REMARK   3      T33:   0.0176 T12:  -0.0040                                     
REMARK   3      T13:  -0.0007 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2915 L22:   0.2301                                     
REMARK   3      L33:   0.2602 L12:   0.1134                                     
REMARK   3      L13:  -0.0642 L23:  -0.0499                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0150 S12:   0.0407 S13:   0.0503                       
REMARK   3      S21:  -0.0324 S22:   0.0191 S23:   0.0288                       
REMARK   3      S31:  -0.0089 S32:  -0.0471 S33:  -0.0040                       
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     1        B   450                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2650  61.0040  19.2970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0214 T22:   0.0195                                     
REMARK   3      T33:   0.0185 T12:   0.0172                                     
REMARK   3      T13:   0.0182 T23:   0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2957 L22:   0.2629                                     
REMARK   3      L33:   0.3017 L12:  -0.0664                                     
REMARK   3      L13:  -0.0190 L23:   0.0969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0529 S12:  -0.0450 S13:  -0.0519                       
REMARK   3      S21:   0.0610 S22:   0.0384 S23:   0.0409                       
REMARK   3      S31:   0.0097 S32:  -0.0328 S33:   0.0146                       
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     1        C   450                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9070  59.4890 -35.2170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0313 T22:   0.0227                                     
REMARK   3      T33:   0.0103 T12:  -0.0055                                     
REMARK   3      T13:   0.0170 T23:  -0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4060 L22:   0.2012                                     
REMARK   3      L33:   0.3491 L12:   0.0668                                     
REMARK   3      L13:   0.0374 L23:  -0.0516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0203 S12:   0.0761 S13:  -0.0169                       
REMARK   3      S21:  -0.0479 S22:   0.0164 S23:  -0.0369                       
REMARK   3      S31:   0.0127 S32:   0.0582 S33:   0.0039                       
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     1        D   450                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.7420  61.3700   9.3440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0067 T22:   0.0242                                     
REMARK   3      T33:   0.0343 T12:   0.0030                                     
REMARK   3      T13:  -0.0068 T23:  -0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3470 L22:   0.1612                                     
REMARK   3      L33:   0.2234 L12:  -0.1073                                     
REMARK   3      L13:  -0.0692 L23:   0.0492                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0333 S12:  -0.0333 S13:   0.0191                       
REMARK   3      S21:   0.0268 S22:   0.0419 S23:  -0.0346                       
REMARK   3      S31:  -0.0062 S32:   0.0652 S33:  -0.0086                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 3Q8N COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063332.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9765                             
REMARK 200  MONOCHROMATOR                  : ASYMMETRIC CUT SINGLE CRYSTAL      
REMARK 200                                   SI(220)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 100299                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.760                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 3.270                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3OKS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: INTERNAL TRACKING NUMBER 216475B10.      
REMARK 280  PACT SCREEN CONDITION B10: 0.2 M MGCL2, 0.1 M MES PH 6.0, 20%       
REMARK 280  PEG6000, MSSMA.01026.B.A1 PW28765 AT 25.2 MG/ML, VAPOR DIFFUSION,   
REMARK 280  SITTING DROP, TEMPERATURE 290K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       49.20500            
REMARK 290   SMTRY3   2  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: 9490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: 9540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     ILE A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     LYS A   449                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     ILE B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     LYS B   449                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     PRO C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     ILE C     7                                                      
REMARK 465     ALA C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     ARG C    10                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     PRO D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     ILE D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     ILE D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     GLY D     9                                                      
REMARK 465     ARG D    10                                                      
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     THR A  11    OG1  CG2                                            
REMARK 470     THR A 203    OG1  CG2                                            
REMARK 470     THR B  11    OG1  CG2                                            
REMARK 470     GLU B  29    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 223    CG   OD1  OD2                                       
REMARK 470     GLU B 354    CG   CD   OE1  OE2                                  
REMARK 470     THR C  11    OG1  CG2                                            
REMARK 470     SER C  36    OG                                                  
REMARK 470     THR D  11    OG1  CG2                                            
REMARK 470     GLU D 354    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 449    CG   CD   CE   NZ                                   
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 A   494     O    HOH B   490              2.02            
REMARK 500   O    HOH A   456     O    HOH A   706              2.04            
REMARK 500   O    HOH C   466     O    HOH C   591              2.07            
REMARK 500   OE2  GLU B   309     O    HOH B   576              2.10            
REMARK 500   O    HOH D   557     O    HOH D   594              2.11            
REMARK 500   O    HOH A   570     O    HOH B   469              2.14            
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    ALA A  74       33.79     71.46                                   
REMARK 500    HIS A  98      138.24   -173.85                                   
REMARK 500    CYS A 100      105.86     62.12                                   
REMARK 500    VAL A 103      -65.91    -93.62                                   
REMARK 500    ALA A 186      130.33    -35.71                                   
REMARK 500    ALA A 271       -8.69     79.11                                   
REMARK 500    ALA A 292     -149.98   -178.54                                   
REMARK 500    LYS A 293      -92.40     39.36                                   
REMARK 500    ASN A 344       66.07     37.30                                   
REMARK 500    CYS A 414     -166.23   -164.28                                   
REMARK 500    ILE B  73       51.59     70.95                                   
REMARK 500    ALA B  74       30.56     72.33                                   
REMARK 500    THR B  76       49.33    -91.42                                   
REMARK 500    HIS B  98      129.92   -172.36                                   
REMARK 500    CYS B 100      106.95     65.43                                   
REMARK 500    VAL B 103      -75.44    -91.18                                   
REMARK 500    ALA B 271       -2.85     76.30                                   
REMARK 500    ALA B 292     -158.86   -171.04                                   
REMARK 500    LYS B 293      -98.56     59.62                                   
REMARK 500    ASN B 344       65.54     31.93                                   
REMARK 500    ALA B 378       30.46    -98.32                                   
REMARK 500    CYS B 414     -166.18   -163.09                                   
REMARK 500    HIS C  98      134.65   -171.71                                   
REMARK 500    CYS C 100      107.40     69.50                                   
REMARK 500    VAL C 103      -68.48    -90.55                                   
REMARK 500    THR C 194     -163.94   -104.39                                   
REMARK 500    ALA C 271      -17.24     79.73                                   
REMARK 500    ALA C 292     -158.47   -175.82                                   
REMARK 500    LYS C 293      -91.27     53.60                                   
REMARK 500    ASP C 393       79.99   -118.05                                   
REMARK 500    ILE D  73       62.06     63.09                                   
REMARK 500    THR D  76       46.54    -86.98                                   
REMARK 500    PHE D  96      146.81   -170.69                                   
REMARK 500    HIS D  98      132.88   -172.23                                   
REMARK 500    CYS D 100      102.36     77.41                                   
REMARK 500    VAL D 103      -74.46    -97.23                                   
REMARK 500    ALA D 186      129.19    -34.28                                   
REMARK 500    PHE D 270       64.62     60.46                                   
REMARK 500    ALA D 271       -9.00     78.06                                   
REMARK 500    ALA D 292     -149.32   -169.48                                   
REMARK 500    LYS D 293      -98.54     48.49                                   
REMARK 500    ALA D 378       34.53    -97.34                                   
REMARK 500    CYS D 414     -167.52   -168.09                                   
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 SSN A 461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SSN B 461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SSN C 461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SSN D 461                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MYSMA.01026.B   RELATED DB: TARGETDB                     
DBREF  3Q8N A    3   449  UNP    A0QQ04   A0QQ04_MYCS2     2    448             
DBREF  3Q8N B    3   449  UNP    A0QQ04   A0QQ04_MYCS2     2    448             
DBREF  3Q8N C    3   449  UNP    A0QQ04   A0QQ04_MYCS2     2    448             
DBREF  3Q8N D    3   449  UNP    A0QQ04   A0QQ04_MYCS2     2    448             
SEQADV 3Q8N GLY A   -3  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N PRO A   -2  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N GLY A   -1  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N SER A    0  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N MET A    1  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N VAL A    2  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N GLY B   -3  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N PRO B   -2  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N GLY B   -1  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N SER B    0  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N MET B    1  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N VAL B    2  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N GLY C   -3  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N PRO C   -2  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N GLY C   -1  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N SER C    0  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N MET C    1  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N VAL C    2  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N GLY D   -3  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N PRO D   -2  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N GLY D   -1  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N SER D    0  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N MET D    1  UNP  A0QQ04              EXPRESSION TAG                 
SEQADV 3Q8N VAL D    2  UNP  A0QQ04              EXPRESSION TAG                 
SEQRES   1 A  453  GLY PRO GLY SER MET VAL THR ILE ALA GLU ILE ALA GLY          
SEQRES   2 A  453  ARG THR LEU THR GLN GLU ARG ARG LEU VAL THR ALA ILE          
SEQRES   3 A  453  PRO GLY PRO ILE SER GLN GLU LEU GLN ALA ARG LYS GLN          
SEQRES   4 A  453  SER ALA VAL ALA ALA GLY VAL GLY VAL THR LEU PRO VAL          
SEQRES   5 A  453  TYR VAL VAL ALA ALA GLY GLY GLY VAL LEU ALA ASP ALA          
SEQRES   6 A  453  ASP GLY ASN GLN LEU ILE ASP PHE GLY SER GLY ILE ALA          
SEQRES   7 A  453  VAL THR THR VAL GLY ASN SER ALA PRO ALA VAL VAL ASP          
SEQRES   8 A  453  ALA VAL THR GLN GLN VAL ALA ALA PHE THR HIS THR CYS          
SEQRES   9 A  453  PHE MET VAL THR PRO TYR GLU GLY TYR VAL LYS VAL ALA          
SEQRES  10 A  453  GLU HIS LEU ASN ARG LEU THR PRO GLY ASP HIS GLU LYS          
SEQRES  11 A  453  ARG THR ALA LEU PHE ASN SER GLY ALA GLU ALA VAL GLU          
SEQRES  12 A  453  ASN ALA VAL LYS ILE ALA ARG ALA TYR THR ARG ARG GLN          
SEQRES  13 A  453  ALA VAL VAL VAL PHE ASP HIS ALA TYR HIS GLY ARG THR          
SEQRES  14 A  453  ASN LEU THR MET ALA MET THR ALA LYS ASN GLN PRO TYR          
SEQRES  15 A  453  LYS HIS GLY PHE GLY PRO PHE ALA ASN GLU VAL TYR ARG          
SEQRES  16 A  453  VAL PRO THR SER TYR PRO PHE ARG ASP GLY GLU THR ASP          
SEQRES  17 A  453  GLY ALA ALA ALA ALA ALA HIS ALA LEU ASP LEU ILE ASN          
SEQRES  18 A  453  LYS GLN VAL GLY ALA ASP ASN VAL ALA ALA VAL VAL ILE          
SEQRES  19 A  453  GLU PRO VAL HIS GLY GLU GLY GLY PHE VAL VAL PRO ALA          
SEQRES  20 A  453  PRO GLY PHE LEU GLY ALA LEU GLN LYS TRP CYS THR ASP          
SEQRES  21 A  453  ASN GLY ALA VAL PHE VAL ALA ASP GLU VAL GLN THR GLY          
SEQRES  22 A  453  PHE ALA ARG THR GLY ALA LEU PHE ALA CYS GLU HIS GLU          
SEQRES  23 A  453  ASN VAL VAL PRO ASP LEU ILE VAL THR ALA LYS GLY ILE          
SEQRES  24 A  453  ALA GLY GLY LEU PRO LEU SER ALA VAL THR GLY ARG ALA          
SEQRES  25 A  453  GLU ILE MET ASP GLY PRO GLN SER GLY GLY LEU GLY GLY          
SEQRES  26 A  453  THR TYR GLY GLY ASN PRO LEU ALA CYS ALA ALA ALA LEU          
SEQRES  27 A  453  ALA VAL ILE ASP THR ILE GLU ARG GLU ASN LEU VAL ALA          
SEQRES  28 A  453  ARG ALA ARG ALA ILE GLY GLU THR MET LEU SER ARG LEU          
SEQRES  29 A  453  GLY ALA LEU ALA ALA ALA ASP PRO ARG ILE GLY GLU VAL          
SEQRES  30 A  453  ARG GLY ARG GLY ALA MET ILE ALA VAL GLU LEU VAL LYS          
SEQRES  31 A  453  PRO GLY THR THR GLU PRO ASP ALA ASP LEU THR LYS ARG          
SEQRES  32 A  453  VAL ALA ALA ALA ALA HIS ALA GLN GLY LEU VAL VAL LEU          
SEQRES  33 A  453  THR CYS GLY THR TYR GLY ASN VAL LEU ARG PHE LEU PRO          
SEQRES  34 A  453  PRO LEU SER MET PRO ASP HIS LEU LEU ASP GLU GLY LEU          
SEQRES  35 A  453  ASP ILE LEU ALA ALA VAL PHE ALA GLU VAL LYS                  
SEQRES   1 B  453  GLY PRO GLY SER MET VAL THR ILE ALA GLU ILE ALA GLY          
SEQRES   2 B  453  ARG THR LEU THR GLN GLU ARG ARG LEU VAL THR ALA ILE          
SEQRES   3 B  453  PRO GLY PRO ILE SER GLN GLU LEU GLN ALA ARG LYS GLN          
SEQRES   4 B  453  SER ALA VAL ALA ALA GLY VAL GLY VAL THR LEU PRO VAL          
SEQRES   5 B  453  TYR VAL VAL ALA ALA GLY GLY GLY VAL LEU ALA ASP ALA          
SEQRES   6 B  453  ASP GLY ASN GLN LEU ILE ASP PHE GLY SER GLY ILE ALA          
SEQRES   7 B  453  VAL THR THR VAL GLY ASN SER ALA PRO ALA VAL VAL ASP          
SEQRES   8 B  453  ALA VAL THR GLN GLN VAL ALA ALA PHE THR HIS THR CYS          
SEQRES   9 B  453  PHE MET VAL THR PRO TYR GLU GLY TYR VAL LYS VAL ALA          
SEQRES  10 B  453  GLU HIS LEU ASN ARG LEU THR PRO GLY ASP HIS GLU LYS          
SEQRES  11 B  453  ARG THR ALA LEU PHE ASN SER GLY ALA GLU ALA VAL GLU          
SEQRES  12 B  453  ASN ALA VAL LYS ILE ALA ARG ALA TYR THR ARG ARG GLN          
SEQRES  13 B  453  ALA VAL VAL VAL PHE ASP HIS ALA TYR HIS GLY ARG THR          
SEQRES  14 B  453  ASN LEU THR MET ALA MET THR ALA LYS ASN GLN PRO TYR          
SEQRES  15 B  453  LYS HIS GLY PHE GLY PRO PHE ALA ASN GLU VAL TYR ARG          
SEQRES  16 B  453  VAL PRO THR SER TYR PRO PHE ARG ASP GLY GLU THR ASP          
SEQRES  17 B  453  GLY ALA ALA ALA ALA ALA HIS ALA LEU ASP LEU ILE ASN          
SEQRES  18 B  453  LYS GLN VAL GLY ALA ASP ASN VAL ALA ALA VAL VAL ILE          
SEQRES  19 B  453  GLU PRO VAL HIS GLY GLU GLY GLY PHE VAL VAL PRO ALA          
SEQRES  20 B  453  PRO GLY PHE LEU GLY ALA LEU GLN LYS TRP CYS THR ASP          
SEQRES  21 B  453  ASN GLY ALA VAL PHE VAL ALA ASP GLU VAL GLN THR GLY          
SEQRES  22 B  453  PHE ALA ARG THR GLY ALA LEU PHE ALA CYS GLU HIS GLU          
SEQRES  23 B  453  ASN VAL VAL PRO ASP LEU ILE VAL THR ALA LYS GLY ILE          
SEQRES  24 B  453  ALA GLY GLY LEU PRO LEU SER ALA VAL THR GLY ARG ALA          
SEQRES  25 B  453  GLU ILE MET ASP GLY PRO GLN SER GLY GLY LEU GLY GLY          
SEQRES  26 B  453  THR TYR GLY GLY ASN PRO LEU ALA CYS ALA ALA ALA LEU          
SEQRES  27 B  453  ALA VAL ILE ASP THR ILE GLU ARG GLU ASN LEU VAL ALA          
SEQRES  28 B  453  ARG ALA ARG ALA ILE GLY GLU THR MET LEU SER ARG LEU          
SEQRES  29 B  453  GLY ALA LEU ALA ALA ALA ASP PRO ARG ILE GLY GLU VAL          
SEQRES  30 B  453  ARG GLY ARG GLY ALA MET ILE ALA VAL GLU LEU VAL LYS          
SEQRES  31 B  453  PRO GLY THR THR GLU PRO ASP ALA ASP LEU THR LYS ARG          
SEQRES  32 B  453  VAL ALA ALA ALA ALA HIS ALA GLN GLY LEU VAL VAL LEU          
SEQRES  33 B  453  THR CYS GLY THR TYR GLY ASN VAL LEU ARG PHE LEU PRO          
SEQRES  34 B  453  PRO LEU SER MET PRO ASP HIS LEU LEU ASP GLU GLY LEU          
SEQRES  35 B  453  ASP ILE LEU ALA ALA VAL PHE ALA GLU VAL LYS                  
SEQRES   1 C  453  GLY PRO GLY SER MET VAL THR ILE ALA GLU ILE ALA GLY          
SEQRES   2 C  453  ARG THR LEU THR GLN GLU ARG ARG LEU VAL THR ALA ILE          
SEQRES   3 C  453  PRO GLY PRO ILE SER GLN GLU LEU GLN ALA ARG LYS GLN          
SEQRES   4 C  453  SER ALA VAL ALA ALA GLY VAL GLY VAL THR LEU PRO VAL          
SEQRES   5 C  453  TYR VAL VAL ALA ALA GLY GLY GLY VAL LEU ALA ASP ALA          
SEQRES   6 C  453  ASP GLY ASN GLN LEU ILE ASP PHE GLY SER GLY ILE ALA          
SEQRES   7 C  453  VAL THR THR VAL GLY ASN SER ALA PRO ALA VAL VAL ASP          
SEQRES   8 C  453  ALA VAL THR GLN GLN VAL ALA ALA PHE THR HIS THR CYS          
SEQRES   9 C  453  PHE MET VAL THR PRO TYR GLU GLY TYR VAL LYS VAL ALA          
SEQRES  10 C  453  GLU HIS LEU ASN ARG LEU THR PRO GLY ASP HIS GLU LYS          
SEQRES  11 C  453  ARG THR ALA LEU PHE ASN SER GLY ALA GLU ALA VAL GLU          
SEQRES  12 C  453  ASN ALA VAL LYS ILE ALA ARG ALA TYR THR ARG ARG GLN          
SEQRES  13 C  453  ALA VAL VAL VAL PHE ASP HIS ALA TYR HIS GLY ARG THR          
SEQRES  14 C  453  ASN LEU THR MET ALA MET THR ALA LYS ASN GLN PRO TYR          
SEQRES  15 C  453  LYS HIS GLY PHE GLY PRO PHE ALA ASN GLU VAL TYR ARG          
SEQRES  16 C  453  VAL PRO THR SER TYR PRO PHE ARG ASP GLY GLU THR ASP          
SEQRES  17 C  453  GLY ALA ALA ALA ALA ALA HIS ALA LEU ASP LEU ILE ASN          
SEQRES  18 C  453  LYS GLN VAL GLY ALA ASP ASN VAL ALA ALA VAL VAL ILE          
SEQRES  19 C  453  GLU PRO VAL HIS GLY GLU GLY GLY PHE VAL VAL PRO ALA          
SEQRES  20 C  453  PRO GLY PHE LEU GLY ALA LEU GLN LYS TRP CYS THR ASP          
SEQRES  21 C  453  ASN GLY ALA VAL PHE VAL ALA ASP GLU VAL GLN THR GLY          
SEQRES  22 C  453  PHE ALA ARG THR GLY ALA LEU PHE ALA CYS GLU HIS GLU          
SEQRES  23 C  453  ASN VAL VAL PRO ASP LEU ILE VAL THR ALA LYS GLY ILE          
SEQRES  24 C  453  ALA GLY GLY LEU PRO LEU SER ALA VAL THR GLY ARG ALA          
SEQRES  25 C  453  GLU ILE MET ASP GLY PRO GLN SER GLY GLY LEU GLY GLY          
SEQRES  26 C  453  THR TYR GLY GLY ASN PRO LEU ALA CYS ALA ALA ALA LEU          
SEQRES  27 C  453  ALA VAL ILE ASP THR ILE GLU ARG GLU ASN LEU VAL ALA          
SEQRES  28 C  453  ARG ALA ARG ALA ILE GLY GLU THR MET LEU SER ARG LEU          
SEQRES  29 C  453  GLY ALA LEU ALA ALA ALA ASP PRO ARG ILE GLY GLU VAL          
SEQRES  30 C  453  ARG GLY ARG GLY ALA MET ILE ALA VAL GLU LEU VAL LYS          
SEQRES  31 C  453  PRO GLY THR THR GLU PRO ASP ALA ASP LEU THR LYS ARG          
SEQRES  32 C  453  VAL ALA ALA ALA ALA HIS ALA GLN GLY LEU VAL VAL LEU          
SEQRES  33 C  453  THR CYS GLY THR TYR GLY ASN VAL LEU ARG PHE LEU PRO          
SEQRES  34 C  453  PRO LEU SER MET PRO ASP HIS LEU LEU ASP GLU GLY LEU          
SEQRES  35 C  453  ASP ILE LEU ALA ALA VAL PHE ALA GLU VAL LYS                  
SEQRES   1 D  453  GLY PRO GLY SER MET VAL THR ILE ALA GLU ILE ALA GLY          
SEQRES   2 D  453  ARG THR LEU THR GLN GLU ARG ARG LEU VAL THR ALA ILE          
SEQRES   3 D  453  PRO GLY PRO ILE SER GLN GLU LEU GLN ALA ARG LYS GLN          
SEQRES   4 D  453  SER ALA VAL ALA ALA GLY VAL GLY VAL THR LEU PRO VAL          
SEQRES   5 D  453  TYR VAL VAL ALA ALA GLY GLY GLY VAL LEU ALA ASP ALA          
SEQRES   6 D  453  ASP GLY ASN GLN LEU ILE ASP PHE GLY SER GLY ILE ALA          
SEQRES   7 D  453  VAL THR THR VAL GLY ASN SER ALA PRO ALA VAL VAL ASP          
SEQRES   8 D  453  ALA VAL THR GLN GLN VAL ALA ALA PHE THR HIS THR CYS          
SEQRES   9 D  453  PHE MET VAL THR PRO TYR GLU GLY TYR VAL LYS VAL ALA          
SEQRES  10 D  453  GLU HIS LEU ASN ARG LEU THR PRO GLY ASP HIS GLU LYS          
SEQRES  11 D  453  ARG THR ALA LEU PHE ASN SER GLY ALA GLU ALA VAL GLU          
SEQRES  12 D  453  ASN ALA VAL LYS ILE ALA ARG ALA TYR THR ARG ARG GLN          
SEQRES  13 D  453  ALA VAL VAL VAL PHE ASP HIS ALA TYR HIS GLY ARG THR          
SEQRES  14 D  453  ASN LEU THR MET ALA MET THR ALA LYS ASN GLN PRO TYR          
SEQRES  15 D  453  LYS HIS GLY PHE GLY PRO PHE ALA ASN GLU VAL TYR ARG          
SEQRES  16 D  453  VAL PRO THR SER TYR PRO PHE ARG ASP GLY GLU THR ASP          
SEQRES  17 D  453  GLY ALA ALA ALA ALA ALA HIS ALA LEU ASP LEU ILE ASN          
SEQRES  18 D  453  LYS GLN VAL GLY ALA ASP ASN VAL ALA ALA VAL VAL ILE          
SEQRES  19 D  453  GLU PRO VAL HIS GLY GLU GLY GLY PHE VAL VAL PRO ALA          
SEQRES  20 D  453  PRO GLY PHE LEU GLY ALA LEU GLN LYS TRP CYS THR ASP          
SEQRES  21 D  453  ASN GLY ALA VAL PHE VAL ALA ASP GLU VAL GLN THR GLY          
SEQRES  22 D  453  PHE ALA ARG THR GLY ALA LEU PHE ALA CYS GLU HIS GLU          
SEQRES  23 D  453  ASN VAL VAL PRO ASP LEU ILE VAL THR ALA LYS GLY ILE          
SEQRES  24 D  453  ALA GLY GLY LEU PRO LEU SER ALA VAL THR GLY ARG ALA          
SEQRES  25 D  453  GLU ILE MET ASP GLY PRO GLN SER GLY GLY LEU GLY GLY          
SEQRES  26 D  453  THR TYR GLY GLY ASN PRO LEU ALA CYS ALA ALA ALA LEU          
SEQRES  27 D  453  ALA VAL ILE ASP THR ILE GLU ARG GLU ASN LEU VAL ALA          
SEQRES  28 D  453  ARG ALA ARG ALA ILE GLY GLU THR MET LEU SER ARG LEU          
SEQRES  29 D  453  GLY ALA LEU ALA ALA ALA ASP PRO ARG ILE GLY GLU VAL          
SEQRES  30 D  453  ARG GLY ARG GLY ALA MET ILE ALA VAL GLU LEU VAL LYS          
SEQRES  31 D  453  PRO GLY THR THR GLU PRO ASP ALA ASP LEU THR LYS ARG          
SEQRES  32 D  453  VAL ALA ALA ALA ALA HIS ALA GLN GLY LEU VAL VAL LEU          
SEQRES  33 D  453  THR CYS GLY THR TYR GLY ASN VAL LEU ARG PHE LEU PRO          
SEQRES  34 D  453  PRO LEU SER MET PRO ASP HIS LEU LEU ASP GLU GLY LEU          
SEQRES  35 D  453  ASP ILE LEU ALA ALA VAL PHE ALA GLU VAL LYS                  
HET    SSN  A 461       7                                                       
HET    SSN  B 461       7                                                       
HET    SSN  C 461       7                                                       
HET    SSN  D 461       7                                                       
HETNAM     SSN 4-OXOBUTANOIC ACID                                               
HETSYN     SSN SUCCINIC SEMIALDEHYDE                                            
FORMUL   5  SSN    4(C4 H6 O3)                                                  
FORMUL   9  HOH   *733(H2 O)                                                    
HELIX    1   1 GLY A   24  VAL A   38  1                                  15    
HELIX    2   2 GLY A   70  VAL A   75  1                                   6    
HELIX    3   3 ALA A   82  PHE A   96  1                                  15    
HELIX    4   4 TYR A  106  THR A  120  1                                  15    
HELIX    5   5 SER A  133  ARG A  150  1                                  18    
HELIX    6   6 THR A  165  THR A  172  1                                   8    
HELIX    7   7 TYR A  196  GLY A  201  1                                   6    
HELIX    8   8 ASP A  204  VAL A  220  1                                  17    
HELIX    9   9 GLY A  221  ASP A  223  5                                   3    
HELIX   10  10 GLY A  245  GLY A  258  1                                  14    
HELIX   11  11 PHE A  277  ASN A  283  5                                   7    
HELIX   12  12 ALA A  292  GLY A  297  5                                   6    
HELIX   13  13 ALA A  308  ASP A  312  1                                   5    
HELIX   14  14 ASN A  326  GLU A  343  1                                  18    
HELIX   15  15 ASN A  344  ASP A  367  1                                  24    
HELIX   16  16 ASP A  393  GLN A  407  1                                  15    
HELIX   17  17 PRO A  430  VAL A  448  1                                  19    
HELIX   18  18 GLY B   24  VAL B   38  1                                  15    
HELIX   19  19 GLY B   70  VAL B   75  1                                   6    
HELIX   20  20 ALA B   82  PHE B   96  1                                  15    
HELIX   21  21 TYR B  106  THR B  120  1                                  15    
HELIX   22  22 SER B  133  ARG B  150  1                                  18    
HELIX   23  23 THR B  165  THR B  172  1                                   8    
HELIX   24  24 TYR B  196  GLY B  201  1                                   6    
HELIX   25  25 ASP B  204  VAL B  220  1                                  17    
HELIX   26  26 GLY B  221  ASP B  223  5                                   3    
HELIX   27  27 GLY B  245  GLY B  258  1                                  14    
HELIX   28  28 PHE B  277  ASN B  283  5                                   7    
HELIX   29  29 ALA B  292  GLY B  297  5                                   6    
HELIX   30  30 ALA B  308  ASP B  312  1                                   5    
HELIX   31  31 ASN B  326  GLU B  343  1                                  18    
HELIX   32  32 ASN B  344  ASP B  367  1                                  24    
HELIX   33  33 ASP B  393  GLN B  407  1                                  15    
HELIX   34  34 PRO B  430  VAL B  448  1                                  19    
HELIX   35  35 GLY C   24  VAL C   38  1                                  15    
HELIX   36  36 GLY C   70  VAL C   75  1                                   6    
HELIX   37  37 ALA C   82  PHE C   96  1                                  15    
HELIX   38  38 TYR C  106  THR C  120  1                                  15    
HELIX   39  39 SER C  133  ARG C  150  1                                  18    
HELIX   40  40 THR C  165  THR C  172  1                                   8    
HELIX   41  41 TYR C  196  GLY C  201  1                                   6    
HELIX   42  42 ASP C  204  VAL C  220  1                                  17    
HELIX   43  43 GLY C  221  ASP C  223  5                                   3    
HELIX   44  44 GLY C  245  GLY C  258  1                                  14    
HELIX   45  45 PHE C  277  ASN C  283  5                                   7    
HELIX   46  46 ALA C  292  GLY C  297  5                                   6    
HELIX   47  47 ALA C  308  ASP C  312  1                                   5    
HELIX   48  48 ASN C  326  GLU C  343  1                                  18    
HELIX   49  49 ASN C  344  ASP C  367  1                                  24    
HELIX   50  50 ASP C  393  GLN C  407  1                                  15    
HELIX   51  51 PRO C  430  VAL C  448  1                                  19    
HELIX   52  52 GLY D   24  VAL D   38  1                                  15    
HELIX   53  53 GLY D   70  VAL D   75  1                                   6    
HELIX   54  54 ALA D   82  PHE D   96  1                                  15    
HELIX   55  55 TYR D  106  THR D  120  1                                  15    
HELIX   56  56 SER D  133  ARG D  150  1                                  18    
HELIX   57  57 THR D  165  THR D  172  1                                   8    
HELIX   58  58 TYR D  196  GLY D  201  1                                   6    
HELIX   59  59 ASP D  204  VAL D  220  1                                  17    
HELIX   60  60 GLY D  221  ASP D  223  5                                   3    
HELIX   61  61 GLY D  245  GLY D  258  1                                  14    
HELIX   62  62 PHE D  277  ASN D  283  5                                   7    
HELIX   63  63 ALA D  292  GLY D  297  5                                   6    
HELIX   64  64 ALA D  308  ASP D  312  1                                   5    
HELIX   65  65 ASN D  326  GLU D  343  1                                  18    
HELIX   66  66 ASN D  344  ASP D  367  1                                  24    
HELIX   67  67 ASP D  393  GLN D  407  1                                  15    
HELIX   68  68 PRO D  430  VAL D  448  1                                  19    
SHEET    1   A 4 VAL A  50  GLY A  54  0                                        
SHEET    2   A 4 VAL A  57  ASP A  60 -1  O  VAL A  57   N  GLY A  54           
SHEET    3   A 4 GLN A  65  ASP A  68 -1  O  LEU A  66   N  LEU A  58           
SHEET    4   A 4 LEU A 409  VAL A 410  1  O  VAL A 410   N  ILE A  67           
SHEET    1   B 7 LYS A 126  PHE A 131  0                                        
SHEET    2   B 7 SER A 302  ARG A 307 -1  O  SER A 302   N  PHE A 131           
SHEET    3   B 7 LEU A 288  THR A 291 -1  N  ILE A 289   O  THR A 305           
SHEET    4   B 7 VAL A 260  ASP A 264  1  N  ALA A 263   O  LEU A 288           
SHEET    5   B 7 VAL A 225  ILE A 230  1  N  ALA A 226   O  VAL A 260           
SHEET    6   B 7 ALA A 153  PHE A 157  1  N  VAL A 155   O  VAL A 229           
SHEET    7   B 7 VAL A 189  VAL A 192  1  O  TYR A 190   N  VAL A 154           
SHEET    1   C 4 ILE A 370  ARG A 376  0                                        
SHEET    2   C 4 MET A 379  LEU A 384 -1  O  GLU A 383   N  GLY A 371           
SHEET    3   C 4 VAL A 420  PHE A 423 -1  O  PHE A 423   N  ILE A 380           
SHEET    4   C 4 LEU A 412  CYS A 414 -1  N  LEU A 412   O  ARG A 422           
SHEET    1   D 4 VAL B  50  GLY B  54  0                                        
SHEET    2   D 4 VAL B  57  ASP B  60 -1  O  ALA B  59   N  ALA B  52           
SHEET    3   D 4 GLN B  65  ASP B  68 -1  O  LEU B  66   N  LEU B  58           
SHEET    4   D 4 LEU B 409  VAL B 410  1  O  VAL B 410   N  ILE B  67           
SHEET    1   E 7 LYS B 126  PHE B 131  0                                        
SHEET    2   E 7 SER B 302  ARG B 307 -1  O  GLY B 306   N  ARG B 127           
SHEET    3   E 7 LEU B 288  THR B 291 -1  N  ILE B 289   O  THR B 305           
SHEET    4   E 7 VAL B 260  ASP B 264  1  N  ALA B 263   O  VAL B 290           
SHEET    5   E 7 VAL B 225  ILE B 230  1  N  VAL B 228   O  VAL B 262           
SHEET    6   E 7 ALA B 153  PHE B 157  1  N  VAL B 155   O  ALA B 227           
SHEET    7   E 7 VAL B 189  VAL B 192  1  O  TYR B 190   N  VAL B 156           
SHEET    1   F 4 ILE B 370  ARG B 376  0                                        
SHEET    2   F 4 MET B 379  LEU B 384 -1  O  ALA B 381   N  ARG B 374           
SHEET    3   F 4 VAL B 420  PHE B 423 -1  O  PHE B 423   N  ILE B 380           
SHEET    4   F 4 LEU B 412  CYS B 414 -1  N  LEU B 412   O  ARG B 422           
SHEET    1   G 4 VAL C  50  GLY C  54  0                                        
SHEET    2   G 4 VAL C  57  ASP C  60 -1  O  ALA C  59   N  ALA C  52           
SHEET    3   G 4 GLN C  65  ASP C  68 -1  O  LEU C  66   N  LEU C  58           
SHEET    4   G 4 LEU C 409  VAL C 410  1  O  VAL C 410   N  ILE C  67           
SHEET    1   H 7 LYS C 126  PHE C 131  0                                        
SHEET    2   H 7 SER C 302  ARG C 307 -1  O  SER C 302   N  PHE C 131           
SHEET    3   H 7 LEU C 288  THR C 291 -1  N  ILE C 289   O  THR C 305           
SHEET    4   H 7 VAL C 260  ASP C 264  1  N  ALA C 263   O  VAL C 290           
SHEET    5   H 7 VAL C 225  ILE C 230  1  N  VAL C 228   O  VAL C 262           
SHEET    6   H 7 ALA C 153  PHE C 157  1  N  VAL C 155   O  ALA C 227           
SHEET    7   H 7 VAL C 189  VAL C 192  1  O  TYR C 190   N  VAL C 156           
SHEET    1   I 4 ILE C 370  ARG C 376  0                                        
SHEET    2   I 4 MET C 379  LEU C 384 -1  O  ALA C 381   N  ARG C 374           
SHEET    3   I 4 VAL C 420  PHE C 423 -1  O  PHE C 423   N  ILE C 380           
SHEET    4   I 4 LEU C 412  CYS C 414 -1  N  CYS C 414   O  VAL C 420           
SHEET    1   J 4 VAL D  50  GLY D  54  0                                        
SHEET    2   J 4 VAL D  57  ASP D  60 -1  O  ALA D  59   N  VAL D  51           
SHEET    3   J 4 GLN D  65  ASP D  68 -1  O  LEU D  66   N  LEU D  58           
SHEET    4   J 4 LEU D 409  VAL D 410  1  O  VAL D 410   N  ILE D  67           
SHEET    1   K 7 LYS D 126  PHE D 131  0                                        
SHEET    2   K 7 SER D 302  ARG D 307 -1  O  SER D 302   N  PHE D 131           
SHEET    3   K 7 LEU D 288  THR D 291 -1  N  ILE D 289   O  THR D 305           
SHEET    4   K 7 VAL D 260  ASP D 264  1  N  ALA D 263   O  VAL D 290           
SHEET    5   K 7 VAL D 225  ILE D 230  1  N  VAL D 228   O  VAL D 262           
SHEET    6   K 7 ALA D 153  PHE D 157  1  N  ALA D 153   O  ALA D 226           
SHEET    7   K 7 VAL D 189  VAL D 192  1  O  TYR D 190   N  VAL D 154           
SHEET    1   L 4 ILE D 370  ARG D 376  0                                        
SHEET    2   L 4 MET D 379  LEU D 384 -1  O  GLU D 383   N  GLY D 371           
SHEET    3   L 4 VAL D 420  PHE D 423 -1  O  PHE D 423   N  ILE D 380           
SHEET    4   L 4 LEU D 412  CYS D 414 -1  N  CYS D 414   O  VAL D 420           
CISPEP   1 ILE A   22    PRO A   23          0        -3.01                     
CISPEP   2 GLN A  176    PRO A  177          0        -7.15                     
CISPEP   3 GLY A  183    PRO A  184          0         2.67                     
CISPEP   4 ILE B   22    PRO B   23          0        -8.33                     
CISPEP   5 GLN B  176    PRO B  177          0        -2.22                     
CISPEP   6 GLY B  183    PRO B  184          0         3.66                     
CISPEP   7 ILE C   22    PRO C   23          0        -0.48                     
CISPEP   8 GLN C  176    PRO C  177          0        -4.67                     
CISPEP   9 GLY C  183    PRO C  184          0         2.17                     
CISPEP  10 ILE D   22    PRO D   23          0        -1.71                     
CISPEP  11 GLN D  176    PRO D  177          0        -4.56                     
CISPEP  12 GLY D  183    PRO D  184          0         4.71                     
SITE     1 AC1  9 SER A 133  GLY A 134  ALA A 135  TYR A 161                    
SITE     2 AC1  9 VAL A 266  LYS A 293  HOH A 489  HOH A 496                    
SITE     3 AC1  9 THR C 322                                                     
SITE     1 AC2  7 GLY B 134  ALA B 135  VAL B 266  LYS B 293                    
SITE     2 AC2  7 HOH B 460  HOH B 546  HOH B 733                               
SITE     1 AC3 10 THR A 322  SER C 133  GLY C 134  ALA C 135                    
SITE     2 AC3 10 VAL C 266  LYS C 293  HOH C 472  HOH C 476                    
SITE     3 AC3 10 HOH C 513  HOH C 642                                          
SITE     1 AC4  8 THR B 322  HOH B 522  GLY D 134  ALA D 135                    
SITE     2 AC4  8 HIS D 162  ASP D 264  VAL D 266  HOH D 459                    
CRYST1   86.220   98.410  109.610  90.00 111.49  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011598  0.000000  0.004566        0.00000                         
SCALE2      0.000000  0.010162  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009805        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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