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Database: PDB
Entry: 1YJ8
LinkDB: 1YJ8
Original site: 1YJ8 
HEADER    OXIDOREDUCTASE                          13-JAN-05   1YJ8              
TITLE     INITIAL STRUCTURAL ANALYSIS OF PLASMODIUM FALCIPARUM GLYCEROL-3-      
TITLE    2 PHOSPHATE DEHYDROGENASE                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCEROL-3-PHOSPHATE DEHYDROGENASE;                        
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 EC: 1.1.1.8;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;                          
SOURCE   3 ORGANISM_TAXID: 36329;                                               
SOURCE   4 STRAIN: 3D7;                                                         
SOURCE   5 GENE: PFL0780W;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21STAR/DE3;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 SYSTEM;                            
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET14B                                    
KEYWDS    SGPP, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE,         
KEYWDS   2 STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA CONSORTIUM,               
KEYWDS   3 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.ROBIEN,W.G.J.HOL,STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA       
AUTHOR   2 CONSORTIUM (SGPP)                                                    
REVDAT   3   13-JUL-11 1YJ8    1       VERSN                                    
REVDAT   2   24-FEB-09 1YJ8    1       VERSN                                    
REVDAT   1   01-FEB-05 1YJ8    0                                                
JRNL        AUTH   M.A.ROBIEN,W.G.J.HOL,                                        
JRNL        AUTH 2 STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA (SGPP)            
JRNL        TITL   INITIAL STRUCTURAL ANALYSIS OF PLASMODIUM FALCIPARUM         
JRNL        TITL 2 GLYCEROL-3-PHOSPHATE DEHYDROGENASE                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 47958                          
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) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2557                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6604                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 364                          
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8415                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 69.78                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.03000                                              
REMARK   3    B12 (A**2) : -0.01000                                             
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): 0.528         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.312         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.246         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.568        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
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):  8565 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7825 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11560 ; 0.944 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18299 ; 0.730 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1062 ; 4.761 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   374 ;39.426 ;25.749       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1578 ;14.926 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;14.453 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1331 ; 0.056 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9374 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1623 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1790 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7865 ; 0.158 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4203 ; 0.171 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4739 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   182 ; 0.127 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    30 ; 0.188 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   107 ; 0.221 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.090 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5720 ; 1.011 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2172 ; 0.113 ; 4.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8606 ; 1.694 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3541 ; 1.406 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2954 ; 2.229 ;10.000       
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 : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     10       A      28      3                      
REMARK   3           1     B     10       B      28      3                      
REMARK   3           1     C     10       C      28      3                      
REMARK   3           2     A     31       A      62      3                      
REMARK   3           2     B     31       B      62      3                      
REMARK   3           2     C     31       C      62      3                      
REMARK   3           3     A     66       A      88      3                      
REMARK   3           3     B     66       B      88      3                      
REMARK   3           3     C     66       C      88      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    436 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    436 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):    436 ;  0.02 ;  0.05           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    746 ;  0.59 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):    746 ;  0.62 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):    746 ;  0.63 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):    436 ;  0.03 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    436 ;  0.03 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):    436 ;  0.04 ;  0.50           
REMARK   3   LOOSE THERMAL      1    A (A**2):    746 ;  0.82 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):    746 ;  1.03 ; 10.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):    746 ;  1.18 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    113       A     124      3                      
REMARK   3           1     B    113       B     124      3                      
REMARK   3           1     C    113       C     124      3                      
REMARK   3           2     A    129       A     210      3                      
REMARK   3           2     B    129       B     210      3                      
REMARK   3           2     C    129       C     210      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    558 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    B    (A):    558 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    C    (A):    558 ;  0.02 ;  0.05           
REMARK   3   LOOSE POSITIONAL   2    A    (A):    822 ;  0.50 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    B    (A):    822 ;  0.46 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    C    (A):    822 ;  0.46 ;  5.00           
REMARK   3   TIGHT THERMAL      2    A (A**2):    558 ;  0.03 ;  0.50           
REMARK   3   TIGHT THERMAL      2    B (A**2):    558 ;  0.03 ;  0.50           
REMARK   3   TIGHT THERMAL      2    C (A**2):    558 ;  0.03 ;  0.50           
REMARK   3   LOOSE THERMAL      2    A (A**2):    822 ;  1.18 ; 10.00           
REMARK   3   LOOSE THERMAL      2    B (A**2):    822 ;  1.14 ; 10.00           
REMARK   3   LOOSE THERMAL      2    C (A**2):    822 ;  1.22 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    216       A     285      3                      
REMARK   3           1     B    216       B     285      3                      
REMARK   3           1     C    216       C     285      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):    413 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    B    (A):    413 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    C    (A):    413 ;  0.02 ;  0.05           
REMARK   3   LOOSE POSITIONAL   3    A    (A):    624 ;  0.58 ;  5.00           
REMARK   3   LOOSE POSITIONAL   3    B    (A):    624 ;  0.60 ;  5.00           
REMARK   3   LOOSE POSITIONAL   3    C    (A):    624 ;  0.50 ;  5.00           
REMARK   3   TIGHT THERMAL      3    A (A**2):    413 ;  0.05 ;  0.50           
REMARK   3   TIGHT THERMAL      3    B (A**2):    413 ;  0.03 ;  0.50           
REMARK   3   TIGHT THERMAL      3    C (A**2):    413 ;  0.04 ;  0.50           
REMARK   3   LOOSE THERMAL      3    A (A**2):    624 ;  1.53 ; 10.00           
REMARK   3   LOOSE THERMAL      3    B (A**2):    624 ;  0.89 ; 10.00           
REMARK   3   LOOSE THERMAL      3    C (A**2):    624 ;  1.41 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    312       A     320      3                      
REMARK   3           1     B    312       B     320      3                      
REMARK   3           1     C    312       C     320      3                      
REMARK   3           2     A    323       A     372      3                      
REMARK   3           2     B    323       B     372      3                      
REMARK   3           2     C    323       C     372      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    A    (A):    351 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    B    (A):    351 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    C    (A):    351 ;  0.02 ;  0.05           
REMARK   3   LOOSE POSITIONAL   4    A    (A):    576 ;  0.72 ;  5.00           
REMARK   3   LOOSE POSITIONAL   4    B    (A):    576 ;  0.61 ;  5.00           
REMARK   3   LOOSE POSITIONAL   4    C    (A):    576 ;  0.69 ;  5.00           
REMARK   3   TIGHT THERMAL      4    A (A**2):    351 ;  0.05 ;  0.50           
REMARK   3   TIGHT THERMAL      4    B (A**2):    351 ;  0.03 ;  0.50           
REMARK   3   TIGHT THERMAL      4    C (A**2):    351 ;  0.05 ;  0.50           
REMARK   3   LOOSE THERMAL      4    A (A**2):    576 ;  1.42 ; 10.00           
REMARK   3   LOOSE THERMAL      4    B (A**2):    576 ;  0.96 ; 10.00           
REMARK   3   LOOSE THERMAL      4    C (A**2):    576 ;  1.56 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE AUTHORS      
REMARK   3  STATE THAT THE ELECTRON DENSITY OF RESIDUES IN THE REGION OF        
REMARK   3  APPROXIMATELY                                                       
REMARK   3  RESIDUES 285-313 IS QUITE WEAK, AND HENCE SOMEWHAT UNCERTAIN,       
REMARK   3  ESPECIALLY IN CHAINS B AND C.                                       
REMARK   4                                                                      
REMARK   4 1YJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB031576.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-04; 20-JUN-04               
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL                          
REMARK 200  PH                             : 10                                 
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SSRL; ALS                          
REMARK 200  BEAMLINE                       : BL11-3; 8.2.1                      
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976; 0.9794, 0.91840, 0.97950    
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(111) BENT        
REMARK 200                                   MONOCHROMATOR; NULL                
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210; ADSC QUANTUM     
REMARK 200                                   210                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50574                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.70800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, POTASSIUM PHOSPHATE             
REMARK 280  MONOBASIC, CAPS, DTT, PH 10, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      116.34950            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      116.34950            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      116.34950            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      116.34950            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      116.34950            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      116.34950            
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.500000 -0.866025  0.000000       88.72750            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000      153.68054            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      116.34950            
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: 4410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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     ALA A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     MET A     9                                                      
REMARK 465     VAL A    63                                                      
REMARK 465     ASN A    64                                                      
REMARK 465     GLY A    65                                                      
REMARK 465     SER A   126                                                      
REMARK 465     GLU A   127                                                      
REMARK 465     SER A   128                                                      
REMARK 465     LEU A   373                                                      
REMARK 465     ASN A   374                                                      
REMARK 465     LEU A   375                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     MET B     9                                                      
REMARK 465     VAL B    63                                                      
REMARK 465     ASN B    64                                                      
REMARK 465     GLY B    65                                                      
REMARK 465     SER B   126                                                      
REMARK 465     GLU B   127                                                      
REMARK 465     SER B   128                                                      
REMARK 465     LEU B   373                                                      
REMARK 465     ASN B   374                                                      
REMARK 465     LEU B   375                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     MET C     9                                                      
REMARK 465     VAL C    63                                                      
REMARK 465     ASN C    64                                                      
REMARK 465     GLY C    65                                                      
REMARK 465     SER C   126                                                      
REMARK 465     GLU C   127                                                      
REMARK 465     SER C   128                                                      
REMARK 465     LEU C   373                                                      
REMARK 465     ASN C   374                                                      
REMARK 465     LEU C   375                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 304    CE   NZ                                             
REMARK 470     GLU A 313    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 316    CG   CD   CE   NZ                                   
REMARK 470     LYS B 130    CD   CE   NZ                                        
REMARK 470     LYS B 148    CD   CE   NZ                                        
REMARK 470     LYS B 304    CE   NZ                                             
REMARK 470     GLU B 313    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 316    CG   CD   CE   NZ                                   
REMARK 470     LYS C 124    CD   CE   NZ                                        
REMARK 470     LYS C 147    CD   CE   NZ                                        
REMARK 470     LYS C 148    CG   CD   CE   NZ                                   
REMARK 470     LYS C 304    CE   NZ                                             
REMARK 470     GLU C 313    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 316    CG   CD   CE   NZ                                   
REMARK 470     GLN C 321    CB   CG   CD   OE1  NE2                             
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    ASN A 149       14.94     56.91                                   
REMARK 500    GLN A 266      -12.83     69.74                                   
REMARK 500    THR A 302     -100.91     65.74                                   
REMARK 500    SER B  29       17.89   -143.90                                   
REMARK 500    ASN B 149       15.89     56.09                                   
REMARK 500    GLN B 266       -9.96     67.48                                   
REMARK 500    ASN B 291      -55.45   -176.04                                   
REMARK 500    LYS B 300      -56.62   -148.79                                   
REMARK 500    ASN C 149       15.86     55.61                                   
REMARK 500    GLN C 266      -11.51     69.33                                   
REMARK 500    ARG C 290       39.90   -160.30                                   
REMARK 500    SER C 301       85.28   -159.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: PFAL009132AAA   RELATED DB: TARGETDB                     
DBREF  1YJ8 A    9   375  UNP    Q8I5P5   Q8I5P5_PLAF7     1    367             
DBREF  1YJ8 B    9   375  UNP    Q8I5P5   Q8I5P5_PLAF7     1    367             
DBREF  1YJ8 C    9   375  UNP    Q8I5P5   Q8I5P5_PLAF7     1    367             
SEQADV 1YJ8 MET A    1  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 ALA A    2  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS A    3  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS A    4  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS A    5  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS A    6  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS A    7  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS A    8  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 MET B    1  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 ALA B    2  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS B    3  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS B    4  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS B    5  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS B    6  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS B    7  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS B    8  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 MET C    1  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 ALA C    2  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS C    3  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS C    4  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS C    5  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS C    6  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS C    7  UNP  Q8I5P5              CLONING ARTIFACT               
SEQADV 1YJ8 HIS C    8  UNP  Q8I5P5              CLONING ARTIFACT               
SEQRES   1 A  375  MET ALA HIS HIS HIS HIS HIS HIS MET TYR ARG ASN LEU          
SEQRES   2 A  375  PHE ASP LYS LEU LYS ASP GLY PRO LEU LYS ILE SER ILE          
SEQRES   3 A  375  LEU GLY SER GLY ASN TRP ALA SER ALA ILE SER LYS VAL          
SEQRES   4 A  375  VAL GLY THR ASN ALA LYS ASN ASN TYR LEU PHE GLU ASN          
SEQRES   5 A  375  GLU VAL ARG MET TRP ILE ARG ASP GLU PHE VAL ASN GLY          
SEQRES   6 A  375  GLU ARG MET VAL ASP ILE ILE ASN ASN LYS HIS GLU ASN          
SEQRES   7 A  375  THR LYS TYR LEU LYS GLY VAL PRO LEU PRO HIS ASN ILE          
SEQRES   8 A  375  VAL ALA HIS SER ASP LEU ALA SER VAL ILE ASN ASP ALA          
SEQRES   9 A  375  ASP LEU LEU ILE PHE ILE VAL PRO CYS GLN TYR LEU GLU          
SEQRES  10 A  375  SER VAL LEU ALA SER ILE LYS GLU SER GLU SER ILE LYS          
SEQRES  11 A  375  ILE ALA SER HIS ALA LYS ALA ILE SER LEU THR LYS GLY          
SEQRES  12 A  375  PHE ILE VAL LYS LYS ASN GLN MET LYS LEU CYS SER ASN          
SEQRES  13 A  375  TYR ILE SER ASP PHE LEU ASN ILE PRO CYS SER ALA LEU          
SEQRES  14 A  375  SER GLY ALA ASN ILE ALA MET ASP VAL ALA MET GLU ASN          
SEQRES  15 A  375  PHE SER GLU ALA THR ILE GLY GLY ASN ASP LYS ASP SER          
SEQRES  16 A  375  LEU VAL ILE TRP GLN ARG VAL PHE ASP LEU PRO TYR PHE          
SEQRES  17 A  375  LYS ILE ASN CYS VAL ASN GLU THR ILE GLU VAL GLU ILE          
SEQRES  18 A  375  CYS GLY ALA LEU LYS ASN ILE ILE THR LEU ALA CYS GLY          
SEQRES  19 A  375  PHE CYS ASP GLY LEU ASN LEU PRO THR ASN SER LYS SER          
SEQRES  20 A  375  ALA ILE ILE ARG ASN GLY ILE ASN GLU MET ILE LEU PHE          
SEQRES  21 A  375  GLY LYS VAL PHE PHE GLN LYS PHE ASN GLU ASN ILE LEU          
SEQRES  22 A  375  LEU GLU SER CYS GLY PHE ALA ASP ILE ILE THR SER PHE          
SEQRES  23 A  375  LEU ALA GLY ARG ASN ALA LYS CYS SER ALA GLU PHE ILE          
SEQRES  24 A  375  LYS SER THR PRO LYS LYS THR TRP GLU GLU LEU GLU ASN          
SEQRES  25 A  375  GLU ILE LEU LYS GLY GLN LYS LEU GLN GLY THR VAL THR          
SEQRES  26 A  375  LEU LYS TYR VAL TYR HIS MET ILE LYS GLU LYS ASN MET          
SEQRES  27 A  375  THR ASN GLU PHE PRO LEU PHE THR VAL LEU HIS LYS ILE          
SEQRES  28 A  375  SER PHE GLU ASN GLU ASP PRO SER SER LEU LEU LYS THR          
SEQRES  29 A  375  PHE MET ASN ASN LYS ILE ASN GLN LEU ASN LEU                  
SEQRES   1 B  375  MET ALA HIS HIS HIS HIS HIS HIS MET TYR ARG ASN LEU          
SEQRES   2 B  375  PHE ASP LYS LEU LYS ASP GLY PRO LEU LYS ILE SER ILE          
SEQRES   3 B  375  LEU GLY SER GLY ASN TRP ALA SER ALA ILE SER LYS VAL          
SEQRES   4 B  375  VAL GLY THR ASN ALA LYS ASN ASN TYR LEU PHE GLU ASN          
SEQRES   5 B  375  GLU VAL ARG MET TRP ILE ARG ASP GLU PHE VAL ASN GLY          
SEQRES   6 B  375  GLU ARG MET VAL ASP ILE ILE ASN ASN LYS HIS GLU ASN          
SEQRES   7 B  375  THR LYS TYR LEU LYS GLY VAL PRO LEU PRO HIS ASN ILE          
SEQRES   8 B  375  VAL ALA HIS SER ASP LEU ALA SER VAL ILE ASN ASP ALA          
SEQRES   9 B  375  ASP LEU LEU ILE PHE ILE VAL PRO CYS GLN TYR LEU GLU          
SEQRES  10 B  375  SER VAL LEU ALA SER ILE LYS GLU SER GLU SER ILE LYS          
SEQRES  11 B  375  ILE ALA SER HIS ALA LYS ALA ILE SER LEU THR LYS GLY          
SEQRES  12 B  375  PHE ILE VAL LYS LYS ASN GLN MET LYS LEU CYS SER ASN          
SEQRES  13 B  375  TYR ILE SER ASP PHE LEU ASN ILE PRO CYS SER ALA LEU          
SEQRES  14 B  375  SER GLY ALA ASN ILE ALA MET ASP VAL ALA MET GLU ASN          
SEQRES  15 B  375  PHE SER GLU ALA THR ILE GLY GLY ASN ASP LYS ASP SER          
SEQRES  16 B  375  LEU VAL ILE TRP GLN ARG VAL PHE ASP LEU PRO TYR PHE          
SEQRES  17 B  375  LYS ILE ASN CYS VAL ASN GLU THR ILE GLU VAL GLU ILE          
SEQRES  18 B  375  CYS GLY ALA LEU LYS ASN ILE ILE THR LEU ALA CYS GLY          
SEQRES  19 B  375  PHE CYS ASP GLY LEU ASN LEU PRO THR ASN SER LYS SER          
SEQRES  20 B  375  ALA ILE ILE ARG ASN GLY ILE ASN GLU MET ILE LEU PHE          
SEQRES  21 B  375  GLY LYS VAL PHE PHE GLN LYS PHE ASN GLU ASN ILE LEU          
SEQRES  22 B  375  LEU GLU SER CYS GLY PHE ALA ASP ILE ILE THR SER PHE          
SEQRES  23 B  375  LEU ALA GLY ARG ASN ALA LYS CYS SER ALA GLU PHE ILE          
SEQRES  24 B  375  LYS SER THR PRO LYS LYS THR TRP GLU GLU LEU GLU ASN          
SEQRES  25 B  375  GLU ILE LEU LYS GLY GLN LYS LEU GLN GLY THR VAL THR          
SEQRES  26 B  375  LEU LYS TYR VAL TYR HIS MET ILE LYS GLU LYS ASN MET          
SEQRES  27 B  375  THR ASN GLU PHE PRO LEU PHE THR VAL LEU HIS LYS ILE          
SEQRES  28 B  375  SER PHE GLU ASN GLU ASP PRO SER SER LEU LEU LYS THR          
SEQRES  29 B  375  PHE MET ASN ASN LYS ILE ASN GLN LEU ASN LEU                  
SEQRES   1 C  375  MET ALA HIS HIS HIS HIS HIS HIS MET TYR ARG ASN LEU          
SEQRES   2 C  375  PHE ASP LYS LEU LYS ASP GLY PRO LEU LYS ILE SER ILE          
SEQRES   3 C  375  LEU GLY SER GLY ASN TRP ALA SER ALA ILE SER LYS VAL          
SEQRES   4 C  375  VAL GLY THR ASN ALA LYS ASN ASN TYR LEU PHE GLU ASN          
SEQRES   5 C  375  GLU VAL ARG MET TRP ILE ARG ASP GLU PHE VAL ASN GLY          
SEQRES   6 C  375  GLU ARG MET VAL ASP ILE ILE ASN ASN LYS HIS GLU ASN          
SEQRES   7 C  375  THR LYS TYR LEU LYS GLY VAL PRO LEU PRO HIS ASN ILE          
SEQRES   8 C  375  VAL ALA HIS SER ASP LEU ALA SER VAL ILE ASN ASP ALA          
SEQRES   9 C  375  ASP LEU LEU ILE PHE ILE VAL PRO CYS GLN TYR LEU GLU          
SEQRES  10 C  375  SER VAL LEU ALA SER ILE LYS GLU SER GLU SER ILE LYS          
SEQRES  11 C  375  ILE ALA SER HIS ALA LYS ALA ILE SER LEU THR LYS GLY          
SEQRES  12 C  375  PHE ILE VAL LYS LYS ASN GLN MET LYS LEU CYS SER ASN          
SEQRES  13 C  375  TYR ILE SER ASP PHE LEU ASN ILE PRO CYS SER ALA LEU          
SEQRES  14 C  375  SER GLY ALA ASN ILE ALA MET ASP VAL ALA MET GLU ASN          
SEQRES  15 C  375  PHE SER GLU ALA THR ILE GLY GLY ASN ASP LYS ASP SER          
SEQRES  16 C  375  LEU VAL ILE TRP GLN ARG VAL PHE ASP LEU PRO TYR PHE          
SEQRES  17 C  375  LYS ILE ASN CYS VAL ASN GLU THR ILE GLU VAL GLU ILE          
SEQRES  18 C  375  CYS GLY ALA LEU LYS ASN ILE ILE THR LEU ALA CYS GLY          
SEQRES  19 C  375  PHE CYS ASP GLY LEU ASN LEU PRO THR ASN SER LYS SER          
SEQRES  20 C  375  ALA ILE ILE ARG ASN GLY ILE ASN GLU MET ILE LEU PHE          
SEQRES  21 C  375  GLY LYS VAL PHE PHE GLN LYS PHE ASN GLU ASN ILE LEU          
SEQRES  22 C  375  LEU GLU SER CYS GLY PHE ALA ASP ILE ILE THR SER PHE          
SEQRES  23 C  375  LEU ALA GLY ARG ASN ALA LYS CYS SER ALA GLU PHE ILE          
SEQRES  24 C  375  LYS SER THR PRO LYS LYS THR TRP GLU GLU LEU GLU ASN          
SEQRES  25 C  375  GLU ILE LEU LYS GLY GLN LYS LEU GLN GLY THR VAL THR          
SEQRES  26 C  375  LEU LYS TYR VAL TYR HIS MET ILE LYS GLU LYS ASN MET          
SEQRES  27 C  375  THR ASN GLU PHE PRO LEU PHE THR VAL LEU HIS LYS ILE          
SEQRES  28 C  375  SER PHE GLU ASN GLU ASP PRO SER SER LEU LEU LYS THR          
SEQRES  29 C  375  PHE MET ASN ASN LYS ILE ASN GLN LEU ASN LEU                  
FORMUL   4  HOH   *10(H2 O)                                                     
HELIX    1   1 ASN A   12  GLY A   20  1                                   9    
HELIX    2   2 GLY A   30  ASN A   47  1                                  18    
HELIX    3   3 ARG A   67  HIS A   76  1                                  10    
HELIX    4   4 LEU A   97  ASN A  102  1                                   6    
HELIX    5   5 PRO A  112  LYS A  124  1                                  13    
HELIX    6   6 LEU A  153  LEU A  162  1                                  10    
HELIX    7   7 ILE A  174  MET A  180  1                                   7    
HELIX    8   8 ASP A  192  ASP A  204  1                                  13    
HELIX    9   9 THR A  216  LEU A  239  1                                  24    
HELIX   10  10 PRO A  242  PHE A  265  1                                  24    
HELIX   11  11 ASN A  269  GLU A  275  5                                   7    
HELIX   12  12 GLY A  278  LEU A  287  1                                  10    
HELIX   13  13 ARG A  290  THR A  302  1                                  13    
HELIX   14  14 THR A  306  LYS A  316  1                                  11    
HELIX   15  15 LEU A  320  LYS A  336  1                                  17    
HELIX   16  16 MET A  338  GLU A  341  5                                   4    
HELIX   17  17 PHE A  342  GLU A  354  1                                  13    
HELIX   18  18 SER A  359  MET A  366  1                                   8    
HELIX   19  19 ASN B   12  GLY B   20  1                                   9    
HELIX   20  20 GLY B   30  ASN B   47  1                                  18    
HELIX   21  21 ARG B   67  HIS B   76  1                                  10    
HELIX   22  22 LEU B   97  ASN B  102  1                                   6    
HELIX   23  23 PRO B  112  LYS B  124  1                                  13    
HELIX   24  24 LEU B  153  LEU B  162  1                                  10    
HELIX   25  25 ILE B  174  MET B  180  1                                   7    
HELIX   26  26 ASP B  192  ASP B  204  1                                  13    
HELIX   27  27 THR B  216  LEU B  239  1                                  24    
HELIX   28  28 PRO B  242  PHE B  265  1                                  24    
HELIX   29  29 ASN B  269  GLU B  275  5                                   7    
HELIX   30  30 GLY B  278  ALA B  288  1                                  11    
HELIX   31  31 ALA B  288  ILE B  299  1                                  12    
HELIX   32  32 THR B  306  ILE B  314  1                                   9    
HELIX   33  33 LEU B  320  LYS B  336  1                                  17    
HELIX   34  34 MET B  338  GLU B  341  5                                   4    
HELIX   35  35 PHE B  342  GLU B  354  1                                  13    
HELIX   36  36 SER B  359  MET B  366  1                                   8    
HELIX   37  37 ASN C   12  GLY C   20  1                                   9    
HELIX   38  38 GLY C   30  ASN C   47  1                                  18    
HELIX   39  39 ARG C   67  HIS C   76  1                                  10    
HELIX   40  40 LEU C   97  ASN C  102  1                                   6    
HELIX   41  41 PRO C  112  LYS C  124  1                                  13    
HELIX   42  42 LEU C  153  LEU C  162  1                                  10    
HELIX   43  43 ILE C  174  MET C  180  1                                   7    
HELIX   44  44 ASP C  192  ASP C  204  1                                  13    
HELIX   45  45 THR C  216  LEU C  239  1                                  24    
HELIX   46  46 PRO C  242  PHE C  265  1                                  24    
HELIX   47  47 ASN C  269  GLU C  275  5                                   7    
HELIX   48  48 GLY C  278  ALA C  288  1                                  11    
HELIX   49  49 ASN C  291  SER C  301  1                                  11    
HELIX   50  50 THR C  306  ILE C  314  1                                   9    
HELIX   51  51 LEU C  320  LYS C  336  1                                  17    
HELIX   52  52 PHE C  342  GLU C  354  1                                  13    
HELIX   53  53 SER C  359  MET C  366  1                                   8    
SHEET    1   A 8 ILE A  91  HIS A  94  0                                        
SHEET    2   A 8 VAL A  54  TRP A  57  1  N  MET A  56   O  VAL A  92           
SHEET    3   A 8 ILE A  24  LEU A  27  1  N  ILE A  26   O  TRP A  57           
SHEET    4   A 8 LEU A 106  PHE A 109  1  O  ILE A 108   N  SER A  25           
SHEET    5   A 8 LYS A 136  SER A 139  1  O  ILE A 138   N  PHE A 109           
SHEET    6   A 8 CYS A 166  SER A 170  1  O  LEU A 169   N  SER A 139           
SHEET    7   A 8 SER A 184  GLY A 189 -1  O  THR A 187   N  SER A 170           
SHEET    8   A 8 PHE A 208  VAL A 213  1  O  ASN A 211   N  ILE A 188           
SHEET    1   B 2 ILE A 145  LYS A 147  0                                        
SHEET    2   B 2 GLN A 150  LYS A 152 -1  O  LYS A 152   N  ILE A 145           
SHEET    1   C 8 ILE B  91  HIS B  94  0                                        
SHEET    2   C 8 VAL B  54  TRP B  57  1  N  MET B  56   O  VAL B  92           
SHEET    3   C 8 ILE B  24  LEU B  27  1  N  ILE B  26   O  TRP B  57           
SHEET    4   C 8 LEU B 106  PHE B 109  1  O  ILE B 108   N  SER B  25           
SHEET    5   C 8 LYS B 136  SER B 139  1  O  ILE B 138   N  PHE B 109           
SHEET    6   C 8 CYS B 166  SER B 170  1  O  LEU B 169   N  SER B 139           
SHEET    7   C 8 SER B 184  GLY B 189 -1  O  THR B 187   N  SER B 170           
SHEET    8   C 8 PHE B 208  VAL B 213  1  O  ASN B 211   N  ILE B 188           
SHEET    1   D 2 ILE B 145  LYS B 147  0                                        
SHEET    2   D 2 GLN B 150  LYS B 152 -1  O  LYS B 152   N  ILE B 145           
SHEET    1   E 8 ILE C  91  HIS C  94  0                                        
SHEET    2   E 8 VAL C  54  TRP C  57  1  N  MET C  56   O  VAL C  92           
SHEET    3   E 8 ILE C  24  LEU C  27  1  N  ILE C  26   O  TRP C  57           
SHEET    4   E 8 LEU C 106  PHE C 109  1  O  ILE C 108   N  SER C  25           
SHEET    5   E 8 LYS C 136  SER C 139  1  O  ILE C 138   N  PHE C 109           
SHEET    6   E 8 CYS C 166  SER C 170  1  O  LEU C 169   N  SER C 139           
SHEET    7   E 8 SER C 184  GLY C 189 -1  O  THR C 187   N  SER C 170           
SHEET    8   E 8 PHE C 208  VAL C 213  1  O  ASN C 211   N  ILE C 188           
SHEET    1   F 2 ILE C 145  LYS C 147  0                                        
SHEET    2   F 2 GLN C 150  LYS C 152 -1  O  LYS C 152   N  ILE C 145           
CRYST1  177.455  177.455  232.699  90.00  90.00 120.00 P 63 2 2     36          
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      0.005635  0.003254  0.000000        0.00000                         
SCALE2      0.000000  0.006507  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004297        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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