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Database: PDB
Entry: 3FZ7
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Original site: 3FZ7 
HEADER    LYASE                                   23-JAN-09   3FZ7              
TITLE     CRYSTAL STRUCTURE OF APO GLUTAMATE DECARBOXYLASE BETA FROM ESCHERICHIA
TITLE    2 COLI                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE DECARBOXYLASE BETA;                              
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: GAD-BETA;                                                   
COMPND   5 EC: 4.1.1.15;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 GENE: B1493, GADB, JW1488;                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE60                                     
KEYWDS    GLUTAMATE DECARBOXYLASE, APO, DECARBOXYLASE, LYASE, MEMBRANE,         
KEYWDS   2 PYRIDOXAL PHOSPHATE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.N.MALASHKEVICH,D.DE BIASE,F.BOSSA                                   
REVDAT   2   13-JUL-11 3FZ7    1       VERSN                                    
REVDAT   1   03-FEB-09 3FZ7    0                                                
JRNL        AUTH   V.N.MALASHKEVICH,D.DE BIASE,F.BOSSA                          
JRNL        TITL   CRYSTAL STRUCTURE OF APO GLUTAMATE DECARBOXYLASE BETA FROM   
JRNL        TITL 2 ESCHERICHIA COLI                                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0070                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 105257                         
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) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5253                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7211                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.20                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 366                          
REMARK   3   BIN FREE R VALUE                    : 0.2910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 21817                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 998                                     
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) : 15.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.05000                                              
REMARK   3    B22 (A**2) : 0.05000                                              
REMARK   3    B33 (A**2) : -0.08000                                             
REMARK   3    B12 (A**2) : 0.03000                                              
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): 0.627         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.270         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.176         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.245        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 22405 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 30377 ; 1.694 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2739 ; 6.594 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1090 ;34.500 ;23.963       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3714 ;16.829 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   152 ;18.686 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3183 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17394 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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): 13659 ; 1.439 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21934 ; 4.780 ;20.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8746 ; 9.622 ;20.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  8443 ; 5.243 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B C D E F G                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B  -9999       B    9999      1                      
REMARK   3           1     C  -9999       C    9999      1                      
REMARK   3           1     D  -9999       D    9999      1                      
REMARK   3           1     E  -9999       E    9999      1                      
REMARK   3           1     F  -9999       F    9999      1                      
REMARK   3           1     G  -9999       G    9999      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3607 ; 0.340 ; 5.000           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   3607 ; 0.300 ; 5.000           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   3607 ; 0.380 ; 5.000           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   3607 ; 0.320 ; 5.000           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   3607 ; 0.350 ; 5.000           
REMARK   3   TIGHT POSITIONAL   1    F    (A):   3607 ; 0.340 ; 5.000           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3607 ; 3.630 ;10.000           
REMARK   3   TIGHT THERMAL      1    B (A**2):   3607 ; 3.490 ;10.000           
REMARK   3   TIGHT THERMAL      1    C (A**2):   3607 ; 3.670 ;10.000           
REMARK   3   TIGHT THERMAL      1    D (A**2):   3607 ; 3.610 ;10.000           
REMARK   3   TIGHT THERMAL      1    E (A**2):   3607 ; 4.310 ;10.000           
REMARK   3   TIGHT THERMAL      1    F (A**2):   3607 ; 3.030 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    12        B   466                          
REMARK   3    RESIDUE RANGE :   B   467        B   467                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.2262  17.4531  -5.7648              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0060 T22:   0.0254                                     
REMARK   3      T33:   0.0318 T12:  -0.0029                                     
REMARK   3      T13:   0.0106 T23:  -0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3449 L22:   0.2748                                     
REMARK   3      L33:   0.3463 L12:  -0.0514                                     
REMARK   3      L13:  -0.1545 L23:   0.0399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0405 S12:   0.0189 S13:   0.0563                       
REMARK   3      S21:  -0.0208 S22:   0.0270 S23:  -0.0219                       
REMARK   3      S31:  -0.0290 S32:   0.0511 S33:  -0.0675                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     4        C   466                          
REMARK   3    RESIDUE RANGE :   C   467        C   467                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.9117  -4.1016  12.3350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0195 T22:   0.0732                                     
REMARK   3      T33:   0.0140 T12:   0.0244                                     
REMARK   3      T13:  -0.0157 T23:  -0.0268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2455 L22:   0.2310                                     
REMARK   3      L33:   0.3139 L12:   0.1218                                     
REMARK   3      L13:   0.1685 L23:   0.0412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0194 S12:  -0.0259 S13:  -0.0130                       
REMARK   3      S21:   0.0571 S22:   0.0196 S23:  -0.0373                       
REMARK   3      S31:   0.0310 S32:   0.0843 S33:  -0.0391                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    13        D   466                          
REMARK   3    RESIDUE RANGE :   D   467        D   467                          
REMARK   3    RESIDUE RANGE :   D   468        D  1465                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2962 -28.8559 -12.4775              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0226 T22:   0.0036                                     
REMARK   3      T33:   0.0009 T12:  -0.0058                                     
REMARK   3      T13:  -0.0012 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2083 L22:   0.2567                                     
REMARK   3      L33:   0.3607 L12:  -0.0398                                     
REMARK   3      L13:  -0.0486 L23:   0.1793                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0104 S12:  -0.0158 S13:   0.0007                       
REMARK   3      S21:   0.0414 S22:  -0.0071 S23:   0.0093                       
REMARK   3      S31:   0.0797 S32:  -0.0225 S33:  -0.0033                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    12        E   466                          
REMARK   3    RESIDUE RANGE :   E   467        E   467                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.1703 -24.0598   8.2757              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0613 T22:   0.0052                                     
REMARK   3      T33:   0.0286 T12:  -0.0145                                     
REMARK   3      T13:   0.0308 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1782 L22:   0.5002                                     
REMARK   3      L33:   0.3177 L12:  -0.0821                                     
REMARK   3      L13:  -0.1457 L23:  -0.0611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0362 S12:  -0.0029 S13:  -0.0213                       
REMARK   3      S21:   0.0702 S22:   0.0046 S23:   0.0931                       
REMARK   3      S31:   0.1021 S32:  -0.0254 S33:   0.0316                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     3        F   466                          
REMARK   3    RESIDUE RANGE :   F   467        F   467                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.8865  20.3910  -7.7364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0108 T22:   0.0098                                     
REMARK   3      T33:   0.0098 T12:   0.0093                                     
REMARK   3      T13:  -0.0055 T23:  -0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2009 L22:   0.3745                                     
REMARK   3      L33:   0.3127 L12:  -0.0964                                     
REMARK   3      L13:   0.0915 L23:   0.0331                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0316 S12:   0.0285 S13:  -0.0358                       
REMARK   3      S21:  -0.0255 S22:  -0.0296 S23:   0.0209                       
REMARK   3      S31:  -0.0224 S32:  -0.0085 S33:  -0.0021                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    13        A   466                          
REMARK   3    RESIDUE RANGE :   A   467        A   467                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.6422  30.6387  14.7190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0201 T22:   0.0031                                     
REMARK   3      T33:   0.0109 T12:   0.0063                                     
REMARK   3      T13:   0.0070 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3488 L22:   0.2018                                     
REMARK   3      L33:   0.3008 L12:  -0.1125                                     
REMARK   3      L13:  -0.0286 L23:   0.1245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0230 S12:  -0.0117 S13:   0.0334                       
REMARK   3      S21:  -0.0198 S22:   0.0024 S23:  -0.0398                       
REMARK   3      S31:  -0.0702 S32:  -0.0236 S33:  -0.0254                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE       
REMARK   3  RIDING POSITIONS. 2. U VALUES: RESIDUAL ONLY.                       
REMARK   4                                                                      
REMARK   4 3FZ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051221.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-OCT-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 106626                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE, 0.1 M TRIS-      
REMARK 280  HCL, PH 7.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      137.70733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       68.85367            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 46910 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 87280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -217.7 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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     ASP A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     LYS D     4                                                      
REMARK 465     GLN D     5                                                      
REMARK 465     VAL D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     ASP D     8                                                      
REMARK 465     LEU D     9                                                      
REMARK 465     ARG D    10                                                      
REMARK 465     SER D    11                                                      
REMARK 465     GLU D    12                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ASP E     2                                                      
REMARK 465     LYS E     3                                                      
REMARK 465     LYS E     4                                                      
REMARK 465     GLN E     5                                                      
REMARK 465     VAL E     6                                                      
REMARK 465     THR E     7                                                      
REMARK 465     ASP E     8                                                      
REMARK 465     LEU E     9                                                      
REMARK 465     ARG E    10                                                      
REMARK 465     SER E    11                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ASP F     2                                                      
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   OH   TYR E   305     O    HOH D   725              1.51            
REMARK 500   OH   TYR C   352     OE1  GLU C   435              1.96            
REMARK 500   O    GLU B    28     N    LYS B    30              2.03            
REMARK 500   OH   TYR B   352     OE1  GLU B   435              2.06            
REMARK 500   O    ALA C    27     O    HOH D   757              2.08            
REMARK 500   OD2  ASP A   239     O    HOH D  1410              2.12            
REMARK 500   OH   TYR D   305     O    HOH D   731              2.13            
REMARK 500   OH   TYR A   352     OE1  GLU A   435              2.15            
REMARK 500   O    ASN C    59     NH2  ARG C   426              2.16            
REMARK 500   O    HOH D   586     O    HOH D   753              2.17            
REMARK 500   O    ASN B    59     NH2  ARG B   426              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH D   649     O    HOH D   803     1455     1.88            
REMARK 500   O    HOH D   869     O    HOH D   810     2554     2.10            
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 B 157   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    ARG B 290   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG B 398   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B 426   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 426   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG C 426   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    LEU D  34   CB  -  CG  -  CD1 ANGL. DEV. = -13.3 DEGREES          
REMARK 500    ARG D 193   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG D 193   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG D 290   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG D 290   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    LEU D 332   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ARG D 426   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    LEU E 157   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ARG F 398   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 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    ALA A  56       -2.16     58.30                                   
REMARK 500    GLU A 200       -8.58    -59.36                                   
REMARK 500    ALA A 255       69.51   -157.72                                   
REMARK 500    ASP A 261     -149.21   -120.67                                   
REMARK 500    LYS A 276     -115.88   -101.89                                   
REMARK 500    LEU A 282      132.35    -35.75                                   
REMARK 500    PHE A 317      -99.30   -132.51                                   
REMARK 500    GLN A 459       23.66   -153.52                                   
REMARK 500    GLU B  28      -85.70     72.55                                   
REMARK 500    SER B  29      -14.24     28.22                                   
REMARK 500    ALA B  56      -14.38     58.34                                   
REMARK 500    PRO B 161       78.91    -69.15                                   
REMARK 500    GLN B 186       79.94   -151.65                                   
REMARK 500    LEU B 187       41.52    -93.55                                   
REMARK 500    LEU B 250      -71.33   -119.51                                   
REMARK 500    ASP B 261     -148.72   -110.28                                   
REMARK 500    LYS B 276     -117.23    -97.62                                   
REMARK 500    ASP B 291     -175.53   -175.07                                   
REMARK 500    PHE B 317     -104.23   -138.96                                   
REMARK 500    PRO B 376       77.03    -69.78                                   
REMARK 500    GLU B 386       -5.03    -46.11                                   
REMARK 500    ASP B 387       90.97     17.95                                   
REMARK 500    GLN B 459       27.03   -148.81                                   
REMARK 500    PHE B 463      121.94    -34.94                                   
REMARK 500    SER C  11       35.32    -96.95                                   
REMARK 500    LYS C 154       54.28   -117.32                                   
REMARK 500    PRO C 161       70.96    -68.44                                   
REMARK 500    THR C 214      -35.42   -130.75                                   
REMARK 500    ALA C 245      -63.54    -26.65                                   
REMARK 500    LEU C 250      -71.53   -114.03                                   
REMARK 500    ALA C 255       59.95   -145.46                                   
REMARK 500    ASP C 261     -150.90   -116.17                                   
REMARK 500    PHE C 262        1.35    -64.43                                   
REMARK 500    LYS C 276     -114.48   -103.59                                   
REMARK 500    LEU C 279       -1.68     83.02                                   
REMARK 500    PHE C 317      -94.31   -133.52                                   
REMARK 500    LEU C 411     -177.98    -68.32                                   
REMARK 500    GLN C 459       41.74   -152.73                                   
REMARK 500    ALA D  27      -92.93    -49.76                                   
REMARK 500    GLU D  28       33.10    -75.80                                   
REMARK 500    ALA D  56       -4.83     71.16                                   
REMARK 500    TYR D  90       67.55   -119.74                                   
REMARK 500    GLN D 186       83.65   -157.82                                   
REMARK 500    ALA D 245      -55.92    -28.29                                   
REMARK 500    LEU D 250      -65.97   -108.73                                   
REMARK 500    ALA D 255       55.99   -141.03                                   
REMARK 500    ASP D 261     -141.51   -114.23                                   
REMARK 500    LYS D 276     -107.53   -101.20                                   
REMARK 500    LEU D 282      128.19    -34.18                                   
REMARK 500    ASP D 291     -174.11   -170.16                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      78 RAMACHANDRAN OUTLIERS.                        
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 SER F   11     GLU F   12                 -131.46                    
REMARK 500 GLU F   12     LEU F   13                  145.10                    
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    GLU A  49        24.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU B  49        22.4      L          L   OUTSIDE RANGE           
REMARK 500    GLU B 386        24.2      L          L   OUTSIDE RANGE           
REMARK 500    GLU C  49        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ILE D 310        23.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 538        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH D1083        DISTANCE =  7.81 ANGSTROMS                       
REMARK 525    HOH D1132        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH D1135        DISTANCE =  5.52 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 467                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 467                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 467                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 467                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 467                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 467                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FZ6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM               
REMARK 900 ESCHERICHIA COLI: COMPLEX WITH XENON                                 
REMARK 900 RELATED ID: 3FZ8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GLUTAMATE DECARBOXYLASE BETA FROM               
REMARK 900 ESCHERICHIA COLI: REDUCED SCHIFF BASE WITH PLP                       
DBREF  3FZ7 A    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  3FZ7 B    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  3FZ7 C    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  3FZ7 D    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  3FZ7 E    1   466  UNP    P69910   DCEB_ECOLI       1    466             
DBREF  3FZ7 F    1   466  UNP    P69910   DCEB_ECOLI       1    466             
SEQRES   1 A  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 A  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE          
SEQRES   3 A  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 A  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 A  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 A  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 A  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 A  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 A  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 A  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 A  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 A  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 A  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 A  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 A  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 A  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 A  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 A  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 A  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 A  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 A  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 A  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 A  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 A  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 A  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 A  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 A  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 A  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 A  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 A  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 A  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 A  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 A  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 A  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 A  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 A  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
SEQRES   1 B  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 B  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE          
SEQRES   3 B  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 B  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 B  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 B  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 B  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 B  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 B  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 B  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 B  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 B  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 B  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 B  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 B  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 B  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 B  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 B  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 B  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 B  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 B  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 B  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 B  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 B  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 B  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 B  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 B  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 B  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 B  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 B  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 B  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 B  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 B  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 B  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 B  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 B  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
SEQRES   1 C  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 C  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE          
SEQRES   3 C  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 C  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 C  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 C  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 C  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 C  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 C  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 C  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 C  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 C  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 C  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 C  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 C  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 C  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 C  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 C  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 C  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 C  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 C  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 C  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 C  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 C  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 C  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 C  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 C  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 C  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 C  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 C  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 C  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 C  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 C  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 C  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 C  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 C  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
SEQRES   1 D  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 D  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE          
SEQRES   3 D  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 D  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 D  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 D  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 D  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 D  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 D  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 D  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 D  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 D  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 D  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 D  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 D  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 D  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 D  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 D  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 D  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 D  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 D  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 D  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 D  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 D  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 D  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 D  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 D  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 D  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 D  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 D  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 D  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 D  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 D  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 D  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 D  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 D  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
SEQRES   1 E  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 E  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE          
SEQRES   3 E  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 E  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 E  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 E  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 E  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 E  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 E  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 E  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 E  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 E  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 E  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 E  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 E  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 E  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 E  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 E  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 E  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 E  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 E  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 E  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 E  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 E  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 E  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 E  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 E  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 E  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 E  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 E  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 E  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 E  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 E  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 E  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 E  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 E  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
SEQRES   1 F  466  MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU          
SEQRES   2 F  466  LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE          
SEQRES   3 F  466  ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP          
SEQRES   4 F  466  ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU          
SEQRES   5 F  466  ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN          
SEQRES   6 F  466  THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU          
SEQRES   7 F  466  SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO          
SEQRES   8 F  466  GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL          
SEQRES   9 F  466  ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN          
SEQRES  10 F  466  ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS          
SEQRES  11 F  466  MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS          
SEQRES  12 F  466  ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN          
SEQRES  13 F  466  LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE          
SEQRES  14 F  466  ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET          
SEQRES  15 F  466  ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE          
SEQRES  16 F  466  GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR          
SEQRES  17 F  466  PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN          
SEQRES  18 F  466  PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR          
SEQRES  19 F  466  GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY          
SEQRES  20 F  466  GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP          
SEQRES  21 F  466  ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER          
SEQRES  22 F  466  GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP          
SEQRES  23 F  466  VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU          
SEQRES  24 F  466  VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR          
SEQRES  25 F  466  PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE          
SEQRES  26 F  466  ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY          
SEQRES  27 F  466  TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA          
SEQRES  28 F  466  TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU          
SEQRES  29 F  466  PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA          
SEQRES  30 F  466  VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR          
SEQRES  31 F  466  THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY          
SEQRES  32 F  466  TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR          
SEQRES  33 F  466  ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE          
SEQRES  34 F  466  GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS          
SEQRES  35 F  466  ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN          
SEQRES  36 F  466  GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR                  
HET    PO4  A 467       5                                                       
HET    PO4  F 467       5                                                       
HET    PO4  D 467       5                                                       
HET    PO4  B 467       5                                                       
HET    PO4  E 467       5                                                       
HET    PO4  C 467       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   7  PO4    6(O4 P 3-)                                                   
FORMUL  13  HOH   *998(H2 O)                                                    
HELIX    1   1 ARG A   38  TYR A   51  1                                  14    
HELIX    2   2 ASP A   69  SER A   79  1                                  11    
HELIX    3   3 TYR A   90  TRP A  108  1                                  19    
HELIX    4   4 GLY A  125  ALA A  148  1                                  24    
HELIX    5   5 GLN A  163  TRP A  173  1                                  11    
HELIX    6   6 ASP A  190  CYS A  198  1                                   9    
HELIX    7   7 PHE A  219  GLY A  235  1                                  17    
HELIX    8   8 SER A  246  PHE A  249  5                                   4    
HELIX    9   9 LEU A  250  ALA A  255  1                                   6    
HELIX   10  10 ASP A  291  LEU A  295  5                                   5    
HELIX   11  11 PRO A  296  VAL A  300  5                                   5    
HELIX   12  12 ALA A  321  ALA A  358  1                                  38    
HELIX   13  13 THR A  391  LEU A  401  1                                  11    
HELIX   14  14 GLU A  430  HIS A  451  1                                  22    
HELIX   15  15 PRO A  452  GLN A  455  5                                   4    
HELIX   16  16 ARG B   38  TYR B   51  1                                  14    
HELIX   17  17 ASP B   69  SER B   79  1                                  11    
HELIX   18  18 TYR B   90  TRP B  108  1                                  19    
HELIX   19  19 GLY B  125  ALA B  148  1                                  24    
HELIX   20  20 GLN B  163  ASP B  174  1                                  12    
HELIX   21  21 ASP B  190  CYS B  198  1                                   9    
HELIX   22  22 PHE B  219  GLY B  235  1                                  17    
HELIX   23  23 SER B  246  PHE B  249  5                                   4    
HELIX   24  24 LEU B  250  ALA B  255  1                                   6    
HELIX   25  25 ASP B  291  LEU B  295  5                                   5    
HELIX   26  26 PRO B  296  VAL B  300  5                                   5    
HELIX   27  27 ALA B  321  LYS B  359  1                                  39    
HELIX   28  28 THR B  391  LEU B  401  1                                  11    
HELIX   29  29 GLU B  430  HIS B  451  1                                  22    
HELIX   30  30 PRO B  452  GLN B  455  5                                   4    
HELIX   31  31 ARG C   38  TYR C   51  1                                  14    
HELIX   32  32 ASP C   69  SER C   79  1                                  11    
HELIX   33  33 TYR C   90  TRP C  108  1                                  19    
HELIX   34  34 GLY C  125  ALA C  148  1                                  24    
HELIX   35  35 GLN C  163  TRP C  173  1                                  11    
HELIX   36  36 ASP C  190  CYS C  198  1                                   9    
HELIX   37  37 PHE C  219  GLY C  235  1                                  17    
HELIX   38  38 SER C  246  PHE C  249  5                                   4    
HELIX   39  39 LEU C  250  ALA C  255  1                                   6    
HELIX   40  40 ASP C  291  LEU C  295  5                                   5    
HELIX   41  41 PRO C  296  VAL C  300  5                                   5    
HELIX   42  42 ALA C  321  LYS C  359  1                                  39    
HELIX   43  43 THR C  391  ARG C  402  1                                  12    
HELIX   44  44 GLY C  412  THR C  416  5                                   5    
HELIX   45  45 GLU C  430  HIS C  451  1                                  22    
HELIX   46  46 PRO C  452  GLN C  455  5                                   4    
HELIX   47  47 ARG D   38  TYR D   51  1                                  14    
HELIX   48  48 ASP D   69  SER D   79  1                                  11    
HELIX   49  49 TYR D   90  TRP D  108  1                                  19    
HELIX   50  50 GLY D  125  ALA D  147  1                                  23    
HELIX   51  51 GLN D  163  TRP D  173  1                                  11    
HELIX   52  52 ASP D  190  ALA D  197  1                                   8    
HELIX   53  53 PHE D  219  GLY D  235  1                                  17    
HELIX   54  54 SER D  246  PHE D  249  5                                   4    
HELIX   55  55 LEU D  250  ALA D  255  1                                   6    
HELIX   56  56 ASP D  291  LEU D  295  5                                   5    
HELIX   57  57 PRO D  296  VAL D  300  5                                   5    
HELIX   58  58 ALA D  321  LYS D  359  1                                  39    
HELIX   59  59 THR D  391  LEU D  401  1                                  11    
HELIX   60  60 GLU D  430  HIS D  451  1                                  22    
HELIX   61  61 PRO D  452  GLN D  455  5                                   4    
HELIX   62  62 ARG E   38  TYR E   51  1                                  14    
HELIX   63  63 ASP E   69  SER E   79  1                                  11    
HELIX   64  64 TYR E   90  TRP E  108  1                                  19    
HELIX   65  65 GLY E  125  ALA E  148  1                                  24    
HELIX   66  66 GLN E  163  TRP E  173  1                                  11    
HELIX   67  67 ASP E  190  CYS E  198  1                                   9    
HELIX   68  68 PHE E  219  GLY E  235  1                                  17    
HELIX   69  69 SER E  246  PHE E  249  5                                   4    
HELIX   70  70 LEU E  250  ALA E  255  1                                   6    
HELIX   71  71 ASP E  291  LEU E  295  5                                   5    
HELIX   72  72 PRO E  296  VAL E  300  5                                   5    
HELIX   73  73 ALA E  321  ALA E  358  1                                  38    
HELIX   74  74 THR E  391  ARG E  402  1                                  12    
HELIX   75  75 GLY E  412  THR E  416  5                                   5    
HELIX   76  76 GLU E  430  HIS E  451  1                                  22    
HELIX   77  77 PRO E  452  GLN E  455  5                                   4    
HELIX   78  78 VAL F    6  ARG F   10  5                                   5    
HELIX   79  79 ARG F   38  LEU F   50  1                                  13    
HELIX   80  80 TYR F   51  ASP F   53  5                                   3    
HELIX   81  81 ASP F   69  SER F   79  1                                  11    
HELIX   82  82 TYR F   90  TRP F  108  1                                  19    
HELIX   83  83 GLY F  125  GLY F  149  1                                  25    
HELIX   84  84 GLN F  163  TRP F  173  1                                  11    
HELIX   85  85 ASP F  190  ALA F  197  1                                   8    
HELIX   86  86 PHE F  219  GLY F  235  1                                  17    
HELIX   87  87 SER F  246  PHE F  249  5                                   4    
HELIX   88  88 LEU F  250  ALA F  255  1                                   6    
HELIX   89  89 ASP F  291  LEU F  295  5                                   5    
HELIX   90  90 PRO F  296  VAL F  300  5                                   5    
HELIX   91  91 ALA F  321  LYS F  359  1                                  39    
HELIX   92  92 THR F  391  ARG F  402  1                                  12    
HELIX   93  93 GLY F  412  THR F  416  5                                   5    
HELIX   94  94 GLU F  430  HIS F  451  1                                  22    
HELIX   95  95 PRO F  452  GLN F  455  5                                   4    
SHEET    1   A 2 LEU A  14  ASP A  15  0                                        
SHEET    2   A 2 ALA A  20  LYS A  21 -1  O  ALA A  20   N  ASP A  15           
SHEET    1   B 4 VAL A 119  THR A 123  0                                        
SHEET    2   B 4 GLY A 285  TRP A 289 -1  O  GLY A 285   N  THR A 123           
SHEET    3   B 4 VAL A 267  SER A 273 -1  N  ALA A 272   O  TRP A 286           
SHEET    4   B 4 MET A 240  ASP A 243  1  N  MET A 240   O  LYS A 268           
SHEET    1   C 3 GLU A 176  GLU A 179  0                                        
SHEET    2   C 3 ASN A 156  CYS A 159  1  N  LEU A 157   O  ARG A 178           
SHEET    3   C 3 THR A 202  VAL A 206  1  O  ILE A 203   N  ASN A 156           
SHEET    1   D 2 PHE A 301  TYR A 305  0                                        
SHEET    2   D 2 GLY A 308  THR A 312 -1  O  THR A 312   N  PHE A 301           
SHEET    1   E 4 TYR A 363  THR A 368  0                                        
SHEET    2   E 4 ALA A 377  LEU A 382 -1  O  LYS A 381   N  GLU A 364           
SHEET    3   E 4 VAL A 419  MET A 424 -1  O  MET A 421   N  PHE A 380           
SHEET    4   E 4 ALA A 408  THR A 410 -1  N  PHE A 409   O  VAL A 420           
SHEET    1   F 2 LEU B  14  ASP B  15  0                                        
SHEET    2   F 2 ALA B  20  LYS B  21 -1  O  ALA B  20   N  ASP B  15           
SHEET    1   G 4 VAL B 119  THR B 123  0                                        
SHEET    2   G 4 GLY B 285  TRP B 289 -1  O  GLY B 285   N  THR B 123           
SHEET    3   G 4 VAL B 267  SER B 273 -1  N  ILE B 270   O  ILE B 288           
SHEET    4   G 4 MET B 240  ASP B 243  1  N  MET B 240   O  LYS B 268           
SHEET    1   H 3 GLU B 176  GLU B 179  0                                        
SHEET    2   H 3 ASN B 156  CYS B 159  1  N  LEU B 157   O  ARG B 178           
SHEET    3   H 3 THR B 202  VAL B 206  1  O  ILE B 203   N  ASN B 156           
SHEET    1   I 2 PHE B 301  TYR B 305  0                                        
SHEET    2   I 2 GLY B 308  THR B 312 -1  O  THR B 312   N  PHE B 301           
SHEET    1   J 4 TYR B 363  THR B 368  0                                        
SHEET    2   J 4 ALA B 377  LEU B 382 -1  O  LYS B 381   N  GLU B 364           
SHEET    3   J 4 VAL B 419  MET B 424 -1  O  ILE B 423   N  VAL B 378           
SHEET    4   J 4 ALA B 408  THR B 410 -1  N  PHE B 409   O  VAL B 420           
SHEET    1   K 2 LEU C  14  ASP C  15  0                                        
SHEET    2   K 2 ALA C  20  LYS C  21 -1  O  ALA C  20   N  ASP C  15           
SHEET    1   L 4 GLY C 120  THR C 123  0                                        
SHEET    2   L 4 GLY C 285  TRP C 289 -1  O  GLY C 285   N  THR C 123           
SHEET    3   L 4 VAL C 267  SER C 273 -1  N  ILE C 270   O  ILE C 288           
SHEET    4   L 4 MET C 240  ASP C 243  1  N  ILE C 242   O  SER C 271           
SHEET    1   M 3 GLU C 176  GLU C 179  0                                        
SHEET    2   M 3 ASN C 156  CYS C 159  1  N  LEU C 157   O  ARG C 178           
SHEET    3   M 3 THR C 202  VAL C 206  1  O  ILE C 203   N  ASN C 156           
SHEET    1   N 2 PHE C 301  TYR C 305  0                                        
SHEET    2   N 2 GLY C 308  THR C 312 -1  O  THR C 312   N  PHE C 301           
SHEET    1   O 4 TYR C 363  THR C 368  0                                        
SHEET    2   O 4 ALA C 377  LEU C 382 -1  O  CYS C 379   N  ILE C 366           
SHEET    3   O 4 VAL C 419  MET C 424 -1  O  MET C 421   N  PHE C 380           
SHEET    4   O 4 ALA C 408  THR C 410 -1  N  PHE C 409   O  VAL C 420           
SHEET    1   P 2 LEU D  14  ASP D  15  0                                        
SHEET    2   P 2 ALA D  20  LYS D  21 -1  O  ALA D  20   N  ASP D  15           
SHEET    1   Q 4 VAL D 119  THR D 123  0                                        
SHEET    2   Q 4 GLY D 285  TRP D 289 -1  O  GLY D 285   N  THR D 123           
SHEET    3   Q 4 VAL D 267  SER D 273 -1  N  ALA D 272   O  TRP D 286           
SHEET    4   Q 4 MET D 240  ASP D 243  1  N  MET D 240   O  LYS D 268           
SHEET    1   R 3 GLU D 176  GLU D 179  0                                        
SHEET    2   R 3 ASN D 156  CYS D 159  1  N  LEU D 157   O  ARG D 178           
SHEET    3   R 3 THR D 202  VAL D 206  1  O  ILE D 203   N  ASN D 156           
SHEET    1   S 2 PHE D 301  TYR D 305  0                                        
SHEET    2   S 2 GLY D 308  THR D 312 -1  O  GLY D 308   N  TYR D 305           
SHEET    1   T 4 TYR D 363  THR D 368  0                                        
SHEET    2   T 4 ALA D 377  LEU D 382 -1  O  LYS D 381   N  GLU D 364           
SHEET    3   T 4 VAL D 419  MET D 424 -1  O  ILE D 423   N  VAL D 378           
SHEET    4   T 4 ALA D 408  THR D 410 -1  N  PHE D 409   O  VAL D 420           
SHEET    1   U 2 LEU E  14  ASP E  15  0                                        
SHEET    2   U 2 ALA E  20  LYS E  21 -1  O  ALA E  20   N  ASP E  15           
SHEET    1   V 4 GLY E 120  THR E 123  0                                        
SHEET    2   V 4 GLY E 285  TRP E 289 -1  O  GLY E 285   N  THR E 123           
SHEET    3   V 4 VAL E 267  SER E 273 -1  N  ILE E 270   O  ILE E 288           
SHEET    4   V 4 MET E 240  ASP E 243  1  N  MET E 240   O  LYS E 268           
SHEET    1   W 3 GLU E 176  GLU E 179  0                                        
SHEET    2   W 3 ASN E 156  CYS E 159  1  N  LEU E 157   O  ARG E 178           
SHEET    3   W 3 THR E 202  VAL E 206  1  O  ILE E 203   N  ASN E 156           
SHEET    1   X 2 PHE E 301  TYR E 305  0                                        
SHEET    2   X 2 GLY E 308  THR E 312 -1  O  THR E 312   N  PHE E 301           
SHEET    1   Y 4 TYR E 363  THR E 368  0                                        
SHEET    2   Y 4 ALA E 377  LEU E 382 -1  O  LYS E 381   N  GLU E 364           
SHEET    3   Y 4 VAL E 419  MET E 424 -1  O  MET E 421   N  PHE E 380           
SHEET    4   Y 4 ALA E 408  THR E 410 -1  N  PHE E 409   O  VAL E 420           
SHEET    1   Z 2 LEU F  14  ASP F  15  0                                        
SHEET    2   Z 2 ALA F  20  LYS F  21 -1  O  ALA F  20   N  ASP F  15           
SHEET    1  AA 4 GLY F 120  THR F 123  0                                        
SHEET    2  AA 4 GLY F 285  TRP F 289 -1  O  GLY F 285   N  THR F 123           
SHEET    3  AA 4 VAL F 267  SER F 273 -1  N  ALA F 272   O  TRP F 286           
SHEET    4  AA 4 MET F 240  ASP F 243  1  N  MET F 240   O  LYS F 268           
SHEET    1  AB 3 GLU F 176  GLU F 179  0                                        
SHEET    2  AB 3 ASN F 156  CYS F 159  1  N  LEU F 157   O  ARG F 178           
SHEET    3  AB 3 THR F 202  VAL F 206  1  O  ILE F 203   N  ASN F 156           
SHEET    1  AC 2 PHE F 301  TYR F 305  0                                        
SHEET    2  AC 2 GLY F 308  THR F 312 -1  O  THR F 312   N  PHE F 301           
SHEET    1  AD 4 TYR F 363  THR F 368  0                                        
SHEET    2  AD 4 ALA F 377  LEU F 382 -1  O  CYS F 379   N  ILE F 366           
SHEET    3  AD 4 VAL F 419  MET F 424 -1  O  ILE F 423   N  VAL F 378           
SHEET    4  AD 4 ALA F 408  THR F 410 -1  N  PHE F 409   O  VAL F 420           
SSBOND   1 CYS A  130    CYS A  165                          1555   1555  2.86  
SSBOND   2 CYS B  130    CYS B  165                          1555   1555  3.00  
SSBOND   3 CYS E  130    CYS E  165                          1555   1555  2.79  
SITE     1 AC1 10 GLY A 125  SER A 126  SER A 127  SER A 273                    
SITE     2 AC1 10 HIS A 275  LYS A 276  HOH D1316  HOH D1437                    
SITE     3 AC1 10 PHE F 317  SER F 318                                          
SITE     1 AC2 11 PHE A 317  SER A 318  HOH D 813  HOH D1058                    
SITE     2 AC2 11 HOH D1193  HOH D1288  SER F 126  SER F 127                    
SITE     3 AC2 11 SER F 273  HIS F 275  LYS F 276                               
SITE     1 AC3 10 GLY D 125  SER D 126  SER D 127  SER D 273                    
SITE     2 AC3 10 HIS D 275  LYS D 276  HOH D1352  HOH D1396                    
SITE     3 AC3 10 PHE E 317  SER E 318                                          
SITE     1 AC4  9 SER B 126  SER B 127  SER B 273  HIS B 275                    
SITE     2 AC4  9 LYS B 276  PHE C 317  SER C 318  HOH D1002                    
SITE     3 AC4  9 HOH D1098                                                     
SITE     1 AC5  9 PHE D 317  SER D 318  HOH D1256  GLY E 125                    
SITE     2 AC5  9 SER E 126  SER E 127  SER E 273  HIS E 275                    
SITE     3 AC5  9 LYS E 276                                                     
SITE     1 AC6  9 PHE B 317  SER B 318  GLY C 125  SER C 126                    
SITE     2 AC6  9 SER C 127  SER C 273  HIS C 275  LYS C 276                    
SITE     3 AC6  9 HOH D1169                                                     
CRYST1  115.564  115.564  206.561  90.00  90.00 120.00 P 32         18          
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      0.008653  0.004996  0.000000        0.00000                         
SCALE2      0.000000  0.009992  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004841        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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