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Database: PDB
Entry: 3WBK
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HEADER    BIOSYNTHETIC PROTEIN                    20-MAY-13   3WBK              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF EUKARYOTIC TRANSLATION INITIATION FACTOR
TITLE    2 5B AND 1A COMPLEX                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 5B;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 401-1002;                                     
COMPND   5 SYNONYM: EIF-5B, TRANSLATION INITIATION FACTOR IF-2;                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 1A;               
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 27-153;                                       
COMPND  11 SYNONYM: EIF-1A, EUKARYOTIC TRANSLATION INITIATION FACTOR 4C, EIF-4C;
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   6 GENE: FUN12, YAL035W;                                                
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: B834-CODONPLUS(DE3)-RIL;                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  12 ORGANISM_COMMON: YEAST;                                              
SOURCE  13 ORGANISM_TAXID: 559292;                                              
SOURCE  14 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  15 GENE: TIF11, YMR260C, YM8156.02C;                                    
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: B834-CODONPLUS(DE3)-RIL                    
KEYWDS    FLEXIBLE, EUKARYOTIC TRANSLATION INITIATION, BIOSYNTHETIC PROTEIN     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ZHENG,R.YAMAMOTO,T.OSE,J.YU,I.TANAKA,M.YAO                          
REVDAT   3   22-NOV-17 3WBK    1       REMARK                                   
REVDAT   2   04-FEB-15 3WBK    1       JRNL                                     
REVDAT   1   19-NOV-14 3WBK    0                                                
JRNL        AUTH   A.ZHENG,J.YU,R.YAMAMOTO,T.OSE,I.TANAKA,M.YAO                 
JRNL        TITL   X-RAY STRUCTURES OF EIF5B AND THE EIF5B-EIF1A COMPLEX: THE   
JRNL        TITL 2 CONFORMATIONAL FLEXIBILITY OF EIF5B IS RESTRICTED ON THE     
JRNL        TITL 3 RIBOSOME BY INTERACTION WITH EIF1A                           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  70  3090 2014              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   25478828                                                     
JRNL        DOI    10.1107/S1399004714021476                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 24828                          
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) : 0.261                           
REMARK   3   R VALUE            (WORKING SET) : 0.257                           
REMARK   3   FREE R VALUE                     : 0.317                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1769                            
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) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1504                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.77                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 146                          
REMARK   3   BIN FREE R VALUE                    : 0.4150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9309                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 159.3                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -12.35000                                            
REMARK   3    B22 (A**2) : 1.66000                                              
REMARK   3    B33 (A**2) : 10.70000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.687         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.608         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.687        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.926                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9448 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12772 ; 1.306 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1184 ; 6.026 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   401 ;33.689 ;24.988       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1780 ;18.218 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    55 ;19.763 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1510 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6882 ; 0.005 ; 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):  4757 ;10.383 ;15.672       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5934 ;16.555 ;23.490       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4691 ;11.418 ;16.085       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     2    602       B     2    602     626 0.230 0.050     
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: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 3WBK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000096128.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.980                              
REMARK 200  MONOCHROMATOR                  : ROTATED-INCLINED DOUBLE-CRYSTAL    
REMARK 200                                   MONOCHROMATOR , SI (111)           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24875                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.150                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 9.400                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49200                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3WBI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL PH 8.2, 12.5%(W/V) PEG    
REMARK 280  3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       50.96950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.37500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.47100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.37500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.96950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.47100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 680 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 31350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     LYS A     1                                                      
REMARK 465     VAL A    30                                                      
REMARK 465     GLN A    31                                                      
REMARK 465     GLY A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     GLU A    34                                                      
REMARK 465     SER A   221                                                      
REMARK 465     LYS A   222                                                      
REMARK 465     GLN A   223                                                      
REMARK 465     LEU A   224                                                      
REMARK 465     MET A   225                                                      
REMARK 465     TYR A   226                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     LYS B     1                                                      
REMARK 465     ASN B    29                                                      
REMARK 465     VAL B    30                                                      
REMARK 465     GLN B    31                                                      
REMARK 465     GLY B    32                                                      
REMARK 465     GLY B    33                                                      
REMARK 465     GLU B    34                                                      
REMARK 465     ALA B    35                                                      
REMARK 465     GLY B    36                                                      
REMARK 465     GLU B   286                                                      
REMARK 465     LEU B   287                                                      
REMARK 465     ARG B   288                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ILE C     1                                                      
REMARK 465     TYR C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     GLU C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     GLN C     7                                                      
REMARK 465     GLU C     8                                                      
REMARK 465     TYR C     9                                                      
REMARK 465     ALA C    10                                                      
REMARK 465     GLN C    11                                                      
REMARK 465     ILE C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     LYS C    14                                                      
REMARK 465     MET C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     GLY C    17                                                      
REMARK 465     ASN C    18                                                      
REMARK 465     GLY C    19                                                      
REMARK 465     ARG C    20                                                      
REMARK 465     VAL C    21                                                      
REMARK 465     GLU C    22                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     SER C    24                                                      
REMARK 465     CYS C    25                                                      
REMARK 465     PHE C    26                                                      
REMARK 465     ASP C    27                                                      
REMARK 465     GLY C    28                                                      
REMARK 465     ASN C    29                                                      
REMARK 465     LYS C    30                                                      
REMARK 465     ARG C    31                                                      
REMARK 465     MET C    32                                                      
REMARK 465     ALA C    33                                                      
REMARK 465     HIS C    34                                                      
REMARK 465     ILE C    35                                                      
REMARK 465     ARG C    36                                                      
REMARK 465     GLY C    37                                                      
REMARK 465     LYS C    38                                                      
REMARK 465     LEU C    39                                                      
REMARK 465     ARG C    40                                                      
REMARK 465     LYS C    41                                                      
REMARK 465     LYS C    42                                                      
REMARK 465     VAL C    43                                                      
REMARK 465     TRP C    44                                                      
REMARK 465     MET C    45                                                      
REMARK 465     GLY C    46                                                      
REMARK 465     GLN C    47                                                      
REMARK 465     GLY C    48                                                      
REMARK 465     ASP C    49                                                      
REMARK 465     ILE C    50                                                      
REMARK 465     ILE C    51                                                      
REMARK 465     LEU C    52                                                      
REMARK 465     VAL C    53                                                      
REMARK 465     SER C    54                                                      
REMARK 465     LEU C    55                                                      
REMARK 465     ARG C    56                                                      
REMARK 465     ASP C    57                                                      
REMARK 465     PHE C    58                                                      
REMARK 465     GLN C    59                                                      
REMARK 465     ASP C    60                                                      
REMARK 465     ASP C    61                                                      
REMARK 465     GLN C    62                                                      
REMARK 465     CYS C    63                                                      
REMARK 465     ASP C    64                                                      
REMARK 465     VAL C    65                                                      
REMARK 465     VAL C    66                                                      
REMARK 465     HIS C    67                                                      
REMARK 465     LYS C    68                                                      
REMARK 465     TYR C    69                                                      
REMARK 465     ASN C    70                                                      
REMARK 465     LEU C    71                                                      
REMARK 465     ASP C    72                                                      
REMARK 465     GLU C    73                                                      
REMARK 465     ALA C    74                                                      
REMARK 465     ARG C    75                                                      
REMARK 465     THR C    76                                                      
REMARK 465     LEU C    77                                                      
REMARK 465     LYS C    78                                                      
REMARK 465     ASN C    79                                                      
REMARK 465     GLN C    80                                                      
REMARK 465     GLY C    81                                                      
REMARK 465     GLU C    82                                                      
REMARK 465     LEU C    83                                                      
REMARK 465     PRO C    84                                                      
REMARK 465     GLU C    85                                                      
REMARK 465     ASN C    86                                                      
REMARK 465     ALA C    87                                                      
REMARK 465     LYS C    88                                                      
REMARK 465     ILE C    89                                                      
REMARK 465     ASN C    90                                                      
REMARK 465     GLU C    91                                                      
REMARK 465     THR C    92                                                      
REMARK 465     ASP C    93                                                      
REMARK 465     ASN C    94                                                      
REMARK 465     PHE C    95                                                      
REMARK 465     GLY C    96                                                      
REMARK 465     PHE C    97                                                      
REMARK 465     GLU C    98                                                      
REMARK 465     SER C    99                                                      
REMARK 465     ASP C   100                                                      
REMARK 465     GLU C   101                                                      
REMARK 465     ASP C   102                                                      
REMARK 465     VAL C   103                                                      
REMARK 465     ASN C   104                                                      
REMARK 465     PHE C   105                                                      
REMARK 465     GLU C   106                                                      
REMARK 465     PHE C   107                                                      
REMARK 465     GLY C   108                                                      
REMARK 465     ASN C   109                                                      
REMARK 465     ALA C   110                                                      
REMARK 465     ASP C   111                                                      
REMARK 465     GLU C   112                                                      
REMARK 465     ASP C   113                                                      
REMARK 465     ASP C   114                                                      
REMARK 465     GLU C   115                                                      
REMARK 465     GLU C   116                                                      
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     HIS A  80    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A  81    CG   CD   OE1  OE2                                  
REMARK 470     PHE A  83    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER A  84    OG                                                  
REMARK 470     ASN A  85    CG   OD1  ND2                                       
REMARK 470     LEU A  86    CG   CD1  CD2                                       
REMARK 470     ARG A  87    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  89    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  91    OG                                                  
REMARK 470     GLU A 292    CG   CD   OE1  OE2                                  
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    SER A  88     -131.92     60.41                                   
REMARK 500    LYS A 131       16.45     81.41                                   
REMARK 500    LYS A 190       13.49     58.62                                   
REMARK 500    LEU A 289      -51.95   -125.39                                   
REMARK 500    GLU A 292     -129.12     57.15                                   
REMARK 500    ALA A 302       40.02     74.20                                   
REMARK 500    THR A 350     -117.41     61.57                                   
REMARK 500    THR A 397        6.80    -67.58                                   
REMARK 500    ALA A 402       76.62   -151.34                                   
REMARK 500    ALA A 406       43.74    -91.40                                   
REMARK 500    ILE A 463      116.59   -167.66                                   
REMARK 500    THR A 505      -60.42   -122.63                                   
REMARK 500    GLU A 508       -6.36     70.58                                   
REMARK 500    PRO A 551      152.12    -49.31                                   
REMARK 500    LYS A 578      -55.54     71.62                                   
REMARK 500    THR B  77       70.22   -157.02                                   
REMARK 500    ASN B 143        8.95     58.54                                   
REMARK 500    PHE B 243       34.72   -142.98                                   
REMARK 500    ALA B 302       14.52     85.46                                   
REMARK 500    LEU B 312     -126.20     47.73                                   
REMARK 500    GLU B 313       -0.50     77.65                                   
REMARK 500    ALA B 406       45.39    -90.00                                   
REMARK 500    ASP B 412      -58.40     72.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WBI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WBJ   RELATED DB: PDB                                   
DBREF  3WBK A    1   602  UNP    P39730   IF2P_YEAST     401   1002             
DBREF  3WBK B    1   602  UNP    P39730   IF2P_YEAST     401   1002             
DBREF  3WBK C    1   127  UNP    P38912   IF1A_YEAST      27    153             
SEQADV 3WBK GLY A   -3  UNP  P39730              EXPRESSION TAG                 
SEQADV 3WBK SER A   -2  UNP  P39730              EXPRESSION TAG                 
SEQADV 3WBK HIS A   -1  UNP  P39730              EXPRESSION TAG                 
SEQADV 3WBK MET A    0  UNP  P39730              EXPRESSION TAG                 
SEQADV 3WBK GLY B   -3  UNP  P39730              EXPRESSION TAG                 
SEQADV 3WBK SER B   -2  UNP  P39730              EXPRESSION TAG                 
SEQADV 3WBK HIS B   -1  UNP  P39730              EXPRESSION TAG                 
SEQADV 3WBK MET B    0  UNP  P39730              EXPRESSION TAG                 
SEQADV 3WBK GLY C   -3  UNP  P38912              EXPRESSION TAG                 
SEQADV 3WBK SER C   -2  UNP  P38912              EXPRESSION TAG                 
SEQADV 3WBK HIS C   -1  UNP  P38912              EXPRESSION TAG                 
SEQADV 3WBK MET C    0  UNP  P38912              EXPRESSION TAG                 
SEQRES   1 A  606  GLY SER HIS MET LYS ASP LEU ARG SER PRO ILE CYS CYS          
SEQRES   2 A  606  ILE LEU GLY HIS VAL ASP THR GLY LYS THR LYS LEU LEU          
SEQRES   3 A  606  ASP LYS ILE ARG GLN THR ASN VAL GLN GLY GLY GLU ALA          
SEQRES   4 A  606  GLY GLY ILE THR GLN GLN ILE GLY ALA THR TYR PHE PRO          
SEQRES   5 A  606  ILE ASP ALA ILE LYS ALA LYS THR LYS VAL MET ALA GLU          
SEQRES   6 A  606  TYR GLU LYS GLN THR PHE ASP VAL PRO GLY LEU LEU VAL          
SEQRES   7 A  606  ILE ASP THR PRO GLY HIS GLU SER PHE SER ASN LEU ARG          
SEQRES   8 A  606  SER ARG GLY SER SER LEU CYS ASN ILE ALA ILE LEU VAL          
SEQRES   9 A  606  ILE ASP ILE MET HIS GLY LEU GLU GLN GLN THR ILE GLU          
SEQRES  10 A  606  SER ILE LYS LEU LEU ARG ASP ARG LYS ALA PRO PHE VAL          
SEQRES  11 A  606  VAL ALA LEU ASN LYS ILE ASP ARG LEU TYR ASP TRP LYS          
SEQRES  12 A  606  ALA ILE PRO ASN ASN SER PHE ARG ASP SER PHE ALA LYS          
SEQRES  13 A  606  GLN SER ARG ALA VAL GLN GLU GLU PHE GLN SER ARG TYR          
SEQRES  14 A  606  SER LYS ILE GLN LEU GLU LEU ALA GLU GLN GLY LEU ASN          
SEQRES  15 A  606  SER GLU LEU TYR PHE GLN ASN LYS ASN MET SER LYS TYR          
SEQRES  16 A  606  VAL SER ILE VAL PRO THR SER ALA VAL THR GLY GLU GLY          
SEQRES  17 A  606  VAL PRO ASP LEU LEU TRP LEU LEU LEU GLU LEU THR GLN          
SEQRES  18 A  606  LYS ARG MET SER LYS GLN LEU MET TYR LEU SER HIS VAL          
SEQRES  19 A  606  GLU ALA THR ILE LEU GLU VAL LYS VAL VAL GLU GLY PHE          
SEQRES  20 A  606  GLY THR THR ILE ASP VAL ILE LEU SER ASN GLY TYR LEU          
SEQRES  21 A  606  ARG GLU GLY ASP ARG ILE VAL LEU CYS GLY MET ASN GLY          
SEQRES  22 A  606  PRO ILE VAL THR ASN ILE ARG ALA LEU LEU THR PRO GLN          
SEQRES  23 A  606  PRO LEU ARG GLU LEU ARG LEU LYS SER GLU TYR VAL HIS          
SEQRES  24 A  606  HIS LYS GLU VAL LYS ALA ALA LEU GLY VAL LYS ILE ALA          
SEQRES  25 A  606  ALA ASN ASP LEU GLU LYS ALA VAL SER GLY SER ARG LEU          
SEQRES  26 A  606  LEU VAL VAL GLY PRO GLU ASP ASP GLU ASP GLU LEU MET          
SEQRES  27 A  606  ASP ASP VAL MET ASP ASP LEU THR GLY LEU LEU ASP SER          
SEQRES  28 A  606  VAL ASP THR THR GLY LYS GLY VAL VAL VAL GLN ALA SER          
SEQRES  29 A  606  THR LEU GLY SER LEU GLU ALA LEU LEU ASP PHE LEU LYS          
SEQRES  30 A  606  ASP MET LYS ILE PRO VAL MET SER ILE GLY LEU GLY PRO          
SEQRES  31 A  606  VAL TYR LYS ARG ASP VAL MET LYS ALA SER THR MET LEU          
SEQRES  32 A  606  GLU LYS ALA PRO GLU TYR ALA VAL MET LEU CYS PHE ASP          
SEQRES  33 A  606  VAL LYS VAL ASP LYS GLU ALA GLU GLN TYR ALA GLU GLN          
SEQRES  34 A  606  GLU GLY ILE LYS ILE PHE ASN ALA ASP VAL ILE TYR HIS          
SEQRES  35 A  606  LEU PHE ASP SER PHE THR ALA TYR GLN GLU LYS LEU LEU          
SEQRES  36 A  606  GLU GLU ARG ARG LYS ASP PHE LEU ASP TYR ALA ILE PHE          
SEQRES  37 A  606  PRO CYS VAL LEU GLN THR LEU GLN ILE ILE ASN LYS ARG          
SEQRES  38 A  606  GLY PRO MET ILE ILE GLY VAL ASP VAL LEU GLU GLY THR          
SEQRES  39 A  606  LEU ARG VAL GLY THR PRO ILE CYS ALA VAL LYS THR ASP          
SEQRES  40 A  606  PRO THR THR LYS GLU ARG GLN THR LEU ILE LEU GLY LYS          
SEQRES  41 A  606  VAL ILE SER LEU GLU ILE ASN HIS GLN PRO VAL GLN GLU          
SEQRES  42 A  606  VAL LYS LYS GLY GLN THR ALA ALA GLY VAL ALA VAL ARG          
SEQRES  43 A  606  LEU GLU ASP PRO SER GLY GLN GLN PRO ILE TRP GLY ARG          
SEQRES  44 A  606  HIS VAL ASP GLU ASN ASP THR LEU TYR SER LEU VAL SER          
SEQRES  45 A  606  ARG ARG SER ILE ASP THR LEU LYS ASP LYS ALA PHE ARG          
SEQRES  46 A  606  ASP GLN VAL ALA ARG SER ASP TRP LEU LEU LEU LYS LYS          
SEQRES  47 A  606  LEU LYS VAL VAL PHE GLY ILE GLU                              
SEQRES   1 B  606  GLY SER HIS MET LYS ASP LEU ARG SER PRO ILE CYS CYS          
SEQRES   2 B  606  ILE LEU GLY HIS VAL ASP THR GLY LYS THR LYS LEU LEU          
SEQRES   3 B  606  ASP LYS ILE ARG GLN THR ASN VAL GLN GLY GLY GLU ALA          
SEQRES   4 B  606  GLY GLY ILE THR GLN GLN ILE GLY ALA THR TYR PHE PRO          
SEQRES   5 B  606  ILE ASP ALA ILE LYS ALA LYS THR LYS VAL MET ALA GLU          
SEQRES   6 B  606  TYR GLU LYS GLN THR PHE ASP VAL PRO GLY LEU LEU VAL          
SEQRES   7 B  606  ILE ASP THR PRO GLY HIS GLU SER PHE SER ASN LEU ARG          
SEQRES   8 B  606  SER ARG GLY SER SER LEU CYS ASN ILE ALA ILE LEU VAL          
SEQRES   9 B  606  ILE ASP ILE MET HIS GLY LEU GLU GLN GLN THR ILE GLU          
SEQRES  10 B  606  SER ILE LYS LEU LEU ARG ASP ARG LYS ALA PRO PHE VAL          
SEQRES  11 B  606  VAL ALA LEU ASN LYS ILE ASP ARG LEU TYR ASP TRP LYS          
SEQRES  12 B  606  ALA ILE PRO ASN ASN SER PHE ARG ASP SER PHE ALA LYS          
SEQRES  13 B  606  GLN SER ARG ALA VAL GLN GLU GLU PHE GLN SER ARG TYR          
SEQRES  14 B  606  SER LYS ILE GLN LEU GLU LEU ALA GLU GLN GLY LEU ASN          
SEQRES  15 B  606  SER GLU LEU TYR PHE GLN ASN LYS ASN MET SER LYS TYR          
SEQRES  16 B  606  VAL SER ILE VAL PRO THR SER ALA VAL THR GLY GLU GLY          
SEQRES  17 B  606  VAL PRO ASP LEU LEU TRP LEU LEU LEU GLU LEU THR GLN          
SEQRES  18 B  606  LYS ARG MET SER LYS GLN LEU MET TYR LEU SER HIS VAL          
SEQRES  19 B  606  GLU ALA THR ILE LEU GLU VAL LYS VAL VAL GLU GLY PHE          
SEQRES  20 B  606  GLY THR THR ILE ASP VAL ILE LEU SER ASN GLY TYR LEU          
SEQRES  21 B  606  ARG GLU GLY ASP ARG ILE VAL LEU CYS GLY MET ASN GLY          
SEQRES  22 B  606  PRO ILE VAL THR ASN ILE ARG ALA LEU LEU THR PRO GLN          
SEQRES  23 B  606  PRO LEU ARG GLU LEU ARG LEU LYS SER GLU TYR VAL HIS          
SEQRES  24 B  606  HIS LYS GLU VAL LYS ALA ALA LEU GLY VAL LYS ILE ALA          
SEQRES  25 B  606  ALA ASN ASP LEU GLU LYS ALA VAL SER GLY SER ARG LEU          
SEQRES  26 B  606  LEU VAL VAL GLY PRO GLU ASP ASP GLU ASP GLU LEU MET          
SEQRES  27 B  606  ASP ASP VAL MET ASP ASP LEU THR GLY LEU LEU ASP SER          
SEQRES  28 B  606  VAL ASP THR THR GLY LYS GLY VAL VAL VAL GLN ALA SER          
SEQRES  29 B  606  THR LEU GLY SER LEU GLU ALA LEU LEU ASP PHE LEU LYS          
SEQRES  30 B  606  ASP MET LYS ILE PRO VAL MET SER ILE GLY LEU GLY PRO          
SEQRES  31 B  606  VAL TYR LYS ARG ASP VAL MET LYS ALA SER THR MET LEU          
SEQRES  32 B  606  GLU LYS ALA PRO GLU TYR ALA VAL MET LEU CYS PHE ASP          
SEQRES  33 B  606  VAL LYS VAL ASP LYS GLU ALA GLU GLN TYR ALA GLU GLN          
SEQRES  34 B  606  GLU GLY ILE LYS ILE PHE ASN ALA ASP VAL ILE TYR HIS          
SEQRES  35 B  606  LEU PHE ASP SER PHE THR ALA TYR GLN GLU LYS LEU LEU          
SEQRES  36 B  606  GLU GLU ARG ARG LYS ASP PHE LEU ASP TYR ALA ILE PHE          
SEQRES  37 B  606  PRO CYS VAL LEU GLN THR LEU GLN ILE ILE ASN LYS ARG          
SEQRES  38 B  606  GLY PRO MET ILE ILE GLY VAL ASP VAL LEU GLU GLY THR          
SEQRES  39 B  606  LEU ARG VAL GLY THR PRO ILE CYS ALA VAL LYS THR ASP          
SEQRES  40 B  606  PRO THR THR LYS GLU ARG GLN THR LEU ILE LEU GLY LYS          
SEQRES  41 B  606  VAL ILE SER LEU GLU ILE ASN HIS GLN PRO VAL GLN GLU          
SEQRES  42 B  606  VAL LYS LYS GLY GLN THR ALA ALA GLY VAL ALA VAL ARG          
SEQRES  43 B  606  LEU GLU ASP PRO SER GLY GLN GLN PRO ILE TRP GLY ARG          
SEQRES  44 B  606  HIS VAL ASP GLU ASN ASP THR LEU TYR SER LEU VAL SER          
SEQRES  45 B  606  ARG ARG SER ILE ASP THR LEU LYS ASP LYS ALA PHE ARG          
SEQRES  46 B  606  ASP GLN VAL ALA ARG SER ASP TRP LEU LEU LEU LYS LYS          
SEQRES  47 B  606  LEU LYS VAL VAL PHE GLY ILE GLU                              
SEQRES   1 C  131  GLY SER HIS MET ILE TYR LYS GLU GLU GLY GLN GLU TYR          
SEQRES   2 C  131  ALA GLN ILE THR LYS MET LEU GLY ASN GLY ARG VAL GLU          
SEQRES   3 C  131  ALA SER CYS PHE ASP GLY ASN LYS ARG MET ALA HIS ILE          
SEQRES   4 C  131  ARG GLY LYS LEU ARG LYS LYS VAL TRP MET GLY GLN GLY          
SEQRES   5 C  131  ASP ILE ILE LEU VAL SER LEU ARG ASP PHE GLN ASP ASP          
SEQRES   6 C  131  GLN CYS ASP VAL VAL HIS LYS TYR ASN LEU ASP GLU ALA          
SEQRES   7 C  131  ARG THR LEU LYS ASN GLN GLY GLU LEU PRO GLU ASN ALA          
SEQRES   8 C  131  LYS ILE ASN GLU THR ASP ASN PHE GLY PHE GLU SER ASP          
SEQRES   9 C  131  GLU ASP VAL ASN PHE GLU PHE GLY ASN ALA ASP GLU ASP          
SEQRES  10 C  131  ASP GLU GLU GLY GLU ASP GLU GLU LEU ASP ILE ASP ASP          
SEQRES  11 C  131  ILE                                                          
HELIX    1   1 HIS A   13  THR A   16  5                                   4    
HELIX    2   2 GLY A   17  GLN A   27  1                                  11    
HELIX    3   3 ILE A   49  LYS A   57  1                                   9    
HELIX    4   4 VAL A   58  TYR A   62  5                                   5    
HELIX    5   5 PRO A   78  SER A   88  1                                  11    
HELIX    6   6 GLU A  108  LYS A  122  1                                  15    
HELIX    7   7 LYS A  131  LEU A  135  5                                   5    
HELIX    8   8 SER A  145  LYS A  152  1                                   8    
HELIX    9   9 SER A  154  GLN A  175  1                                  22    
HELIX   10  10 PHE A  183  ASN A  185  5                                   3    
HELIX   11  11 GLY A  204  GLN A  217  1                                  14    
HELIX   12  12 ASP A  329  VAL A  348  1                                  20    
HELIX   13  13 THR A  361  LYS A  376  1                                  16    
HELIX   14  14 TYR A  388  THR A  397  1                                  10    
HELIX   15  15 ALA A  402  TYR A  405  5                                   4    
HELIX   16  16 ASP A  416  GLU A  426  1                                  11    
HELIX   17  17 VAL A  435  ALA A  462  1                                  28    
HELIX   18  18 SER A  568  ASP A  577  1                                  10    
HELIX   19  19 ALA A  585  GLY A  600  1                                  16    
HELIX   20  20 HIS B   13  THR B   16  5                                   4    
HELIX   21  21 GLY B   17  GLN B   27  1                                  11    
HELIX   22  22 ILE B   49  LYS B   57  1                                   9    
HELIX   23  23 VAL B   58  TYR B   62  5                                   5    
HELIX   24  24 GLU B   81  ARG B   87  1                                   7    
HELIX   25  25 GLU B  108  LYS B  122  1                                  15    
HELIX   26  26 LYS B  131  LEU B  135  5                                   5    
HELIX   27  27 SER B  145  LYS B  152  1                                   8    
HELIX   28  28 SER B  154  GLN B  175  1                                  22    
HELIX   29  29 PHE B  183  ASN B  185  5                                   3    
HELIX   30  30 GLY B  204  GLN B  217  1                                  14    
HELIX   31  31 MET B  220  MET B  225  1                                   6    
HELIX   32  32 ASP B  329  VAL B  337  1                                   9    
HELIX   33  33 MET B  338  ASP B  346  1                                   9    
HELIX   34  34 THR B  361  LYS B  376  1                                  16    
HELIX   35  35 TYR B  388  ALA B  402  1                                  15    
HELIX   36  36 ASP B  416  GLU B  426  1                                  11    
HELIX   37  37 VAL B  435  TYR B  461  1                                  27    
HELIX   38  38 SER B  568  LEU B  575  1                                   8    
HELIX   39  39 ASP B  577  ASP B  582  1                                   6    
HELIX   40  40 ALA B  585  GLY B  600  1                                  16    
SHEET    1   A 7 THR A  45  PRO A  48  0                                        
SHEET    2   A 7 GLY A  71  ILE A  75 -1  O  LEU A  72   N  PHE A  47           
SHEET    3   A 7 ILE A   7  LEU A  11  1  N  CYS A   8   O  LEU A  73           
SHEET    4   A 7 ILE A  96  ASP A 102  1  O  ILE A  98   N  CYS A   9           
SHEET    5   A 7 PHE A 125  ASN A 130  1  O  ALA A 128   N  ILE A 101           
SHEET    6   A 7 VAL A 192  PRO A 196  1  O  VAL A 195   N  VAL A 127           
SHEET    7   A 7 SER A 179  LEU A 181  1  N  GLU A 180   O  VAL A 192           
SHEET    1   B 8 GLY A 269  ASN A 274  0                                        
SHEET    2   B 8 ARG A 261  GLY A 266 -1  N  LEU A 264   O  ILE A 271           
SHEET    3   B 8 ARG A 320  VAL A 323 -1  O  LEU A 322   N  VAL A 263           
SHEET    4   B 8 GLU A 231  VAL A 240 -1  N  ALA A 232   O  LEU A 321           
SHEET    5   B 8 GLY A 244  ASN A 253 -1  O  ASP A 248   N  GLU A 236           
SHEET    6   B 8 LEU A 303  ALA A 308 -1  O  ILE A 307   N  ILE A 247           
SHEET    7   B 8 ALA A 277  THR A 280 -1  N  LEU A 279   O  LYS A 306           
SHEET    8   B 8 VAL A 294  HIS A 295 -1  O  VAL A 294   N  THR A 280           
SHEET    1   C 2 LEU A 256  ARG A 257  0                                        
SHEET    2   C 2 GLU A 298  VAL A 299 -1  O  VAL A 299   N  LEU A 256           
SHEET    1   D 4 VAL A 379  LEU A 384  0                                        
SHEET    2   D 4 VAL A 355  ALA A 359  1  N  VAL A 357   O  SER A 381           
SHEET    3   D 4 VAL A 407  PHE A 411  1  O  LEU A 409   N  VAL A 356           
SHEET    4   D 4 LYS A 429  ALA A 433  1  O  PHE A 431   N  MET A 408           
SHEET    1   E 7 GLN A 525  VAL A 527  0                                        
SHEET    2   E 7 LEU A 512  ILE A 522 -1  N  ILE A 522   O  GLN A 525           
SHEET    3   E 7 PRO A 496  ALA A 499 -1  N  ILE A 497   O  GLY A 515           
SHEET    4   E 7 LEU A 563  SER A 565 -1  O  TYR A 564   N  CYS A 498           
SHEET    5   E 7 CYS A 466  ASN A 475 -1  N  LEU A 468   O  LEU A 563           
SHEET    6   E 7 ILE A 481  ARG A 492 -1  O  ASP A 485   N  GLN A 469           
SHEET    7   E 7 GLU A 529  LYS A 531 -1  O  VAL A 530   N  LEU A 491           
SHEET    1   F 5 GLN A 525  VAL A 527  0                                        
SHEET    2   F 5 LEU A 512  ILE A 522 -1  N  ILE A 522   O  GLN A 525           
SHEET    3   F 5 VAL A 539  GLU A 544 -1  O  ARG A 542   N  ILE A 518           
SHEET    4   F 5 ILE A 481  ARG A 492 -1  N  ILE A 482   O  VAL A 541           
SHEET    5   F 5 GLU A 529  LYS A 531 -1  O  VAL A 530   N  LEU A 491           
SHEET    1   G 8 THR B  39  GLN B  40  0                                        
SHEET    2   G 8 THR B  45  PRO B  48 -1  O  TYR B  46   N  THR B  39           
SHEET    3   G 8 GLY B  71  ILE B  75 -1  O  LEU B  72   N  PHE B  47           
SHEET    4   G 8 ILE B   7  LEU B  11  1  N  CYS B   8   O  LEU B  73           
SHEET    5   G 8 ILE B  96  ASP B 102  1  O  ILE B  98   N  CYS B   9           
SHEET    6   G 8 PHE B 125  ASN B 130  1  O  VAL B 126   N  LEU B  99           
SHEET    7   G 8 VAL B 192  PRO B 196  1  O  VAL B 195   N  VAL B 127           
SHEET    8   G 8 SER B 179  LEU B 181  1  N  GLU B 180   O  ILE B 194           
SHEET    1   H 8 ILE B 271  ASN B 274  0                                        
SHEET    2   H 8 ARG B 261  LEU B 264 -1  N  ILE B 262   O  THR B 273           
SHEET    3   H 8 ARG B 320  VAL B 323 -1  O  LEU B 322   N  VAL B 263           
SHEET    4   H 8 GLU B 231  VAL B 240 -1  N  ALA B 232   O  LEU B 321           
SHEET    5   H 8 GLY B 244  ASN B 253 -1  O  ILE B 250   N  THR B 233           
SHEET    6   H 8 GLY B 304  ALA B 308 -1  O  ILE B 307   N  ILE B 247           
SHEET    7   H 8 ALA B 277  PRO B 281 -1  N  ALA B 277   O  ALA B 308           
SHEET    8   H 8 TYR B 293  HIS B 295 -1  O  VAL B 294   N  THR B 280           
SHEET    1   I 2 TYR B 255  ARG B 257  0                                        
SHEET    2   I 2 GLU B 298  LYS B 300 -1  O  VAL B 299   N  LEU B 256           
SHEET    1   J 4 VAL B 379  GLY B 383  0                                        
SHEET    2   J 4 VAL B 355  GLN B 358  1  N  VAL B 357   O  SER B 381           
SHEET    3   J 4 VAL B 407  CYS B 410  1  O  LEU B 409   N  VAL B 356           
SHEET    4   J 4 LYS B 429  ASN B 432  1  O  PHE B 431   N  MET B 408           
SHEET    1   K 7 GLN B 525  VAL B 527  0                                        
SHEET    2   K 7 GLU B 508  ILE B 522 -1  N  ILE B 522   O  GLN B 525           
SHEET    3   K 7 PRO B 496  ASP B 503 -1  N  ILE B 497   O  GLY B 515           
SHEET    4   K 7 LEU B 563  SER B 565 -1  O  TYR B 564   N  CYS B 498           
SHEET    5   K 7 CYS B 466  ASN B 475 -1  N  LEU B 468   O  LEU B 563           
SHEET    6   K 7 MET B 480  ARG B 492 -1  O  GLY B 483   N  GLN B 472           
SHEET    7   K 7 GLU B 529  LYS B 531 -1  O  VAL B 530   N  LEU B 491           
SHEET    1   L 5 GLN B 525  VAL B 527  0                                        
SHEET    2   L 5 GLU B 508  ILE B 522 -1  N  ILE B 522   O  GLN B 525           
SHEET    3   L 5 VAL B 539  GLU B 544 -1  O  ALA B 540   N  GLU B 521           
SHEET    4   L 5 MET B 480  ARG B 492 -1  N  ILE B 482   O  VAL B 541           
SHEET    5   L 5 GLU B 529  LYS B 531 -1  O  VAL B 530   N  LEU B 491           
SSBOND   1 CYS A    9    CYS A   94                          1555   1555  2.02  
SSBOND   2 CYS B    9    CYS B   94                          1555   1555  2.03  
CISPEP   1 GLY A  478    PRO A  479          0        -1.88                     
CISPEP   2 LEU B  284    ARG B  285          0        -2.51                     
CISPEP   3 GLU C  120    GLU C  121          0         1.12                     
CRYST1  101.939  120.942  132.750  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009810  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008268  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007533        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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