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Database: PDB
Entry: 4R8F
LinkDB: 4R8F
Original site: 4R8F 
HEADER    HYDROLASE                               02-SEP-14   4R8F              
TITLE     CRYSTAL STRUCTURE OF YEAST AMINOPEPTIDASE 1 (APE1)                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VACUOLAR AMINOPEPTIDASE 1;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: AMINOPEPTIDASE III, AMINOPEPTIDASE YSCI, LEUCINE            
COMPND   5 AMINOPEPTIDASE IV, LAPIV, POLYPEPTIDASE, VACUOLAR AMINOPEPTIDASE I;  
COMPND   6 EC: 3.4.11.22;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;                 
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 GENE: LAP4, APE1, API, YSC1, YKL103C, YKL455;                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    PEPTIDASE, CVT PATHWAY, AUTOPHAGY, HYDROLASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.-Y.SU,C.-I.CHANG                                                    
REVDAT   1   12-AUG-15 4R8F    0                                                
JRNL        AUTH   M.-Y.SU,W.-H.PENG,M.-R.HO,S.-C.SU,Y.-C.CHANG,G.-C.CHEN,      
JRNL        AUTH 2 C.-I.CHANG                                                   
JRNL        TITL   STRUCTURE OF YEAST APE1 AND ITS ROLE IN AUTOPHAGIC VESICLE   
JRNL        TITL 2 FORMATION                                                    
JRNL        REF    AUTOPHAGY                                  2015              
JRNL        REFN                   ESSN 1554-8635                               
JRNL        PMID   26208681                                                     
JRNL        DOI    10.1080/15548627.2015.1067363                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 116.23                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 80667                          
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4222                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4007                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 189                          
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13544                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 91                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.09000                                              
REMARK   3    B22 (A**2) : 0.09000                                              
REMARK   3    B33 (A**2) : -0.30000                                             
REMARK   3    B12 (A**2) : 0.05000                                              
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): 0.402         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.261         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.216         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.891         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13839 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 13214 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18723 ; 1.092 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 30428 ; 0.726 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1714 ; 6.245 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   617 ;35.785 ;24.295       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2329 ;19.056 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    64 ;19.996 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2092 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15566 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3170 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6919 ; 1.295 ; 4.165       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6918 ; 1.295 ; 4.165       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8612 ; 2.359 ; 6.228       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  8613 ; 2.359 ; 6.228       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6920 ; 1.018 ; 4.382       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  6921 ; 1.018 ; 4.382       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 10112 ; 1.886 ; 6.515       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 15203 ; 4.199 ;33.003       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 15204 ; 4.199 ;33.004       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4R8F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-SEP-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB087029.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL15A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2                                
REMARK 200  MONOCHROMATOR                  : LN2-COOLED, FIXED-EXIT DOUBLE      
REMARK 200                                   CRYSTAL MONOCHROMATOR              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84889                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 116.230                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.040                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLECULAR REPLACEMENT                                 
REMARK 200 STARTING MODEL: 4DYO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH7.2, 1.1M NACL, 42.5%    
REMARK 280  PEG 400, 0.1M MGCL2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE     
REMARK 280  293.0K                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
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+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        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       70.08550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.46388            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      116.22567            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       70.08550            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       40.46388            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      116.22567            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       70.08550            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       40.46388            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      116.22567            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       80.92776            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      232.45133            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       80.92776            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      232.45133            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       80.92776            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      232.45133            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 71010 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 160200 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -239.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000      -70.08550            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000     -121.39165            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       70.08550            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000     -121.39165            
REMARK 350   BIOMT3   3  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     GLU A     2                                                      
REMARK 465     PRO A   165                                                      
REMARK 465     HIS A   166                                                      
REMARK 465     PHE A   167                                                      
REMARK 465     GLY A   168                                                      
REMARK 465     LYS A   169                                                      
REMARK 465     PRO A   170                                                      
REMARK 465     ALA A   171                                                      
REMARK 465     GLU A   172                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     PRO A   174                                                      
REMARK 465     PHE A   175                                                      
REMARK 465     ASP A   176                                                      
REMARK 465     ILE A   185                                                      
REMARK 465     GLY A   186                                                      
REMARK 465     PHE A   187                                                      
REMARK 465     PRO A   188                                                      
REMARK 465     THR A   189                                                      
REMARK 465     PRO A   190                                                      
REMARK 465     ASP A   191                                                      
REMARK 465     GLU A   192                                                      
REMARK 465     GLU A   193                                                      
REMARK 465     GLY A   194                                                      
REMARK 465     ASN A   195                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     ASN A   404                                                      
REMARK 465     ASN A   405                                                      
REMARK 465     SER A   406                                                      
REMARK 465     ARG A   407                                                      
REMARK 465     SER A   408                                                      
REMARK 465     GLY A   409                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     ASP B   103                                                      
REMARK 465     THR B   104                                                      
REMARK 465     ALA B   105                                                      
REMARK 465     GLU B   106                                                      
REMARK 465     LEU B   163                                                      
REMARK 465     ALA B   164                                                      
REMARK 465     PRO B   165                                                      
REMARK 465     HIS B   166                                                      
REMARK 465     PHE B   167                                                      
REMARK 465     GLY B   168                                                      
REMARK 465     LYS B   169                                                      
REMARK 465     PRO B   170                                                      
REMARK 465     ALA B   171                                                      
REMARK 465     GLU B   172                                                      
REMARK 465     GLY B   173                                                      
REMARK 465     PRO B   174                                                      
REMARK 465     PHE B   175                                                      
REMARK 465     ASP B   176                                                      
REMARK 465     LYS B   177                                                      
REMARK 465     GLU B   178                                                      
REMARK 465     ASP B   179                                                      
REMARK 465     ILE B   185                                                      
REMARK 465     GLY B   186                                                      
REMARK 465     PHE B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     THR B   189                                                      
REMARK 465     PRO B   190                                                      
REMARK 465     ASP B   191                                                      
REMARK 465     GLU B   192                                                      
REMARK 465     GLU B   193                                                      
REMARK 465     GLY B   194                                                      
REMARK 465     ASN B   195                                                      
REMARK 465     LYS B   403                                                      
REMARK 465     ASN B   404                                                      
REMARK 465     ASN B   405                                                      
REMARK 465     SER B   406                                                      
REMARK 465     ARG B   407                                                      
REMARK 465     SER B   408                                                      
REMARK 465     GLY B   409                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     ALA C   164                                                      
REMARK 465     PRO C   165                                                      
REMARK 465     GLY C   168                                                      
REMARK 465     LYS C   169                                                      
REMARK 465     PRO C   170                                                      
REMARK 465     ALA C   171                                                      
REMARK 465     GLU C   172                                                      
REMARK 465     GLY C   173                                                      
REMARK 465     PRO C   174                                                      
REMARK 465     PHE C   175                                                      
REMARK 465     ASP C   176                                                      
REMARK 465     LYS C   177                                                      
REMARK 465     GLU C   178                                                      
REMARK 465     ASP C   179                                                      
REMARK 465     GLY C   186                                                      
REMARK 465     PHE C   187                                                      
REMARK 465     PRO C   188                                                      
REMARK 465     THR C   189                                                      
REMARK 465     PRO C   190                                                      
REMARK 465     ASP C   191                                                      
REMARK 465     GLU C   192                                                      
REMARK 465     GLU C   193                                                      
REMARK 465     GLY C   194                                                      
REMARK 465     LYS C   403                                                      
REMARK 465     ASN C   404                                                      
REMARK 465     ASN C   405                                                      
REMARK 465     SER C   406                                                      
REMARK 465     ARG C   407                                                      
REMARK 465     SER C   408                                                      
REMARK 465     GLY C   409                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     ALA D   164                                                      
REMARK 465     GLY D   168                                                      
REMARK 465     LYS D   169                                                      
REMARK 465     PRO D   170                                                      
REMARK 465     ALA D   171                                                      
REMARK 465     GLU D   172                                                      
REMARK 465     GLY D   173                                                      
REMARK 465     PRO D   174                                                      
REMARK 465     ASP D   179                                                      
REMARK 465     ILE D   185                                                      
REMARK 465     GLY D   186                                                      
REMARK 465     PHE D   187                                                      
REMARK 465     PRO D   188                                                      
REMARK 465     THR D   189                                                      
REMARK 465     PRO D   190                                                      
REMARK 465     ASP D   191                                                      
REMARK 465     GLU D   192                                                      
REMARK 465     GLU D   193                                                      
REMARK 465     GLY D   194                                                      
REMARK 465     ASN D   195                                                      
REMARK 465     PRO D   351                                                      
REMARK 465     GLU D   352                                                      
REMARK 465     VAL D   353                                                      
REMARK 465     TYR D   354                                                      
REMARK 465     LEU D   355                                                      
REMARK 465     LYS D   356                                                      
REMARK 465     ASN D   357                                                      
REMARK 465     HIS D   358                                                      
REMARK 465     LYS D   403                                                      
REMARK 465     ASN D   404                                                      
REMARK 465     ASN D   405                                                      
REMARK 465     SER D   406                                                      
REMARK 465     ARG D   407                                                      
REMARK 465     SER D   408                                                      
REMARK 465     GLY D   409                                                      
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   4      -19.72     69.19                                   
REMARK 500    ILE A   8      -27.86     67.02                                   
REMARK 500    ASN A 143       43.70   -140.26                                   
REMARK 500    SER A 299       -5.94     74.55                                   
REMARK 500    HIS A 358       45.83   -146.88                                   
REMARK 500    ASN B  37       31.72     71.13                                   
REMARK 500    ASN C 121     -168.09    -74.35                                   
REMARK 500    SER C 299       -4.33     75.09                                   
REMARK 500    LEU D 120       23.34     80.67                                   
REMARK 500    HIS D 166       70.93     58.56                                   
REMARK 500    LYS D 177       14.86     81.24                                   
REMARK 500    SER D 299       -7.34     75.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU B  352     VAL B  353                  145.53                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ILE A   8        22.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4R8F A    2   470  UNP    P14904   AMPL_YEAST      46    514             
DBREF  4R8F B    2   470  UNP    P14904   AMPL_YEAST      46    514             
DBREF  4R8F C    2   470  UNP    P14904   AMPL_YEAST      46    514             
DBREF  4R8F D    2   470  UNP    P14904   AMPL_YEAST      46    514             
SEQADV 4R8F MET A    1  UNP  P14904              EXPRESSION TAG                 
SEQADV 4R8F MET B    1  UNP  P14904              EXPRESSION TAG                 
SEQADV 4R8F MET C    1  UNP  P14904              EXPRESSION TAG                 
SEQADV 4R8F MET D    1  UNP  P14904              EXPRESSION TAG                 
SEQRES   1 A  470  MET GLU HIS ASN TYR GLU ASP ILE ALA GLN GLU PHE ILE          
SEQRES   2 A  470  ASP PHE ILE TYR LYS ASN PRO THR THR TYR HIS VAL VAL          
SEQRES   3 A  470  SER PHE PHE ALA GLU LEU LEU ASP LYS HIS ASN PHE LYS          
SEQRES   4 A  470  TYR LEU SER GLU LYS SER ASN TRP GLN ASP SER ILE GLY          
SEQRES   5 A  470  GLU ASP GLY GLY LYS PHE TYR THR ILE ARG ASN GLY THR          
SEQRES   6 A  470  ASN LEU SER ALA PHE ILE LEU GLY LYS ASN TRP ARG ALA          
SEQRES   7 A  470  GLU LYS GLY VAL GLY VAL ILE GLY SER HIS VAL ASP ALA          
SEQRES   8 A  470  LEU THR VAL LYS LEU LYS PRO VAL SER PHE LYS ASP THR          
SEQRES   9 A  470  ALA GLU GLY TYR GLY ARG ILE ALA VAL ALA PRO TYR GLY          
SEQRES  10 A  470  GLY THR LEU ASN GLU LEU TRP LEU ASP ARG ASP LEU GLY          
SEQRES  11 A  470  ILE GLY GLY ARG LEU LEU TYR LYS LYS LYS GLY THR ASN          
SEQRES  12 A  470  GLU ILE LYS SER ALA LEU VAL ASP SER THR PRO LEU PRO          
SEQRES  13 A  470  VAL CYS ARG ILE PRO SER LEU ALA PRO HIS PHE GLY LYS          
SEQRES  14 A  470  PRO ALA GLU GLY PRO PHE ASP LYS GLU ASP GLN THR ILE          
SEQRES  15 A  470  PRO VAL ILE GLY PHE PRO THR PRO ASP GLU GLU GLY ASN          
SEQRES  16 A  470  GLU PRO PRO THR ASP ASP GLU LYS LYS SER PRO LEU PHE          
SEQRES  17 A  470  GLY LYS HIS CYS ILE HIS LEU LEU ARG TYR VAL ALA LYS          
SEQRES  18 A  470  LEU ALA GLY VAL GLU VAL SER GLU LEU ILE GLN MET ASP          
SEQRES  19 A  470  LEU ASP LEU PHE ASP VAL GLN LYS GLY THR ILE GLY GLY          
SEQRES  20 A  470  ILE GLY LYS HIS PHE LEU PHE ALA PRO ARG LEU ASP ASP          
SEQRES  21 A  470  ARG LEU CYS SER PHE ALA ALA MET ILE ALA LEU ILE CYS          
SEQRES  22 A  470  TYR ALA LYS ASP VAL ASN THR GLU GLU SER ASP LEU PHE          
SEQRES  23 A  470  SER THR VAL THR LEU TYR ASP ASN GLU GLU ILE GLY SER          
SEQRES  24 A  470  LEU THR ARG GLN GLY ALA LYS GLY GLY LEU LEU GLU SER          
SEQRES  25 A  470  VAL VAL GLU ARG SER SER SER ALA PHE THR LYS LYS PRO          
SEQRES  26 A  470  VAL ASP LEU HIS THR VAL TRP ALA ASN SER ILE ILE LEU          
SEQRES  27 A  470  SER ALA ASP VAL ASN HIS LEU TYR ASN PRO ASN PHE PRO          
SEQRES  28 A  470  GLU VAL TYR LEU LYS ASN HIS PHE PRO VAL PRO ASN VAL          
SEQRES  29 A  470  GLY ILE THR LEU SER LEU ASP PRO ASN GLY HIS MET ALA          
SEQRES  30 A  470  THR ASP VAL VAL GLY THR ALA LEU VAL GLU GLU LEU ALA          
SEQRES  31 A  470  ARG ARG ASN GLY ASP LYS VAL GLN TYR PHE GLN ILE LYS          
SEQRES  32 A  470  ASN ASN SER ARG SER GLY GLY THR ILE GLY PRO SER LEU          
SEQRES  33 A  470  ALA SER GLN THR GLY ALA ARG THR ILE ASP LEU GLY ILE          
SEQRES  34 A  470  ALA GLN LEU SER MET HIS SER ILE ARG ALA ALA THR GLY          
SEQRES  35 A  470  SER LYS ASP VAL GLY LEU GLY VAL LYS PHE PHE ASN GLY          
SEQRES  36 A  470  PHE PHE LYS HIS TRP ARG SER VAL TYR ASP GLU PHE GLY          
SEQRES  37 A  470  GLU LEU                                                      
SEQRES   1 B  470  MET GLU HIS ASN TYR GLU ASP ILE ALA GLN GLU PHE ILE          
SEQRES   2 B  470  ASP PHE ILE TYR LYS ASN PRO THR THR TYR HIS VAL VAL          
SEQRES   3 B  470  SER PHE PHE ALA GLU LEU LEU ASP LYS HIS ASN PHE LYS          
SEQRES   4 B  470  TYR LEU SER GLU LYS SER ASN TRP GLN ASP SER ILE GLY          
SEQRES   5 B  470  GLU ASP GLY GLY LYS PHE TYR THR ILE ARG ASN GLY THR          
SEQRES   6 B  470  ASN LEU SER ALA PHE ILE LEU GLY LYS ASN TRP ARG ALA          
SEQRES   7 B  470  GLU LYS GLY VAL GLY VAL ILE GLY SER HIS VAL ASP ALA          
SEQRES   8 B  470  LEU THR VAL LYS LEU LYS PRO VAL SER PHE LYS ASP THR          
SEQRES   9 B  470  ALA GLU GLY TYR GLY ARG ILE ALA VAL ALA PRO TYR GLY          
SEQRES  10 B  470  GLY THR LEU ASN GLU LEU TRP LEU ASP ARG ASP LEU GLY          
SEQRES  11 B  470  ILE GLY GLY ARG LEU LEU TYR LYS LYS LYS GLY THR ASN          
SEQRES  12 B  470  GLU ILE LYS SER ALA LEU VAL ASP SER THR PRO LEU PRO          
SEQRES  13 B  470  VAL CYS ARG ILE PRO SER LEU ALA PRO HIS PHE GLY LYS          
SEQRES  14 B  470  PRO ALA GLU GLY PRO PHE ASP LYS GLU ASP GLN THR ILE          
SEQRES  15 B  470  PRO VAL ILE GLY PHE PRO THR PRO ASP GLU GLU GLY ASN          
SEQRES  16 B  470  GLU PRO PRO THR ASP ASP GLU LYS LYS SER PRO LEU PHE          
SEQRES  17 B  470  GLY LYS HIS CYS ILE HIS LEU LEU ARG TYR VAL ALA LYS          
SEQRES  18 B  470  LEU ALA GLY VAL GLU VAL SER GLU LEU ILE GLN MET ASP          
SEQRES  19 B  470  LEU ASP LEU PHE ASP VAL GLN LYS GLY THR ILE GLY GLY          
SEQRES  20 B  470  ILE GLY LYS HIS PHE LEU PHE ALA PRO ARG LEU ASP ASP          
SEQRES  21 B  470  ARG LEU CYS SER PHE ALA ALA MET ILE ALA LEU ILE CYS          
SEQRES  22 B  470  TYR ALA LYS ASP VAL ASN THR GLU GLU SER ASP LEU PHE          
SEQRES  23 B  470  SER THR VAL THR LEU TYR ASP ASN GLU GLU ILE GLY SER          
SEQRES  24 B  470  LEU THR ARG GLN GLY ALA LYS GLY GLY LEU LEU GLU SER          
SEQRES  25 B  470  VAL VAL GLU ARG SER SER SER ALA PHE THR LYS LYS PRO          
SEQRES  26 B  470  VAL ASP LEU HIS THR VAL TRP ALA ASN SER ILE ILE LEU          
SEQRES  27 B  470  SER ALA ASP VAL ASN HIS LEU TYR ASN PRO ASN PHE PRO          
SEQRES  28 B  470  GLU VAL TYR LEU LYS ASN HIS PHE PRO VAL PRO ASN VAL          
SEQRES  29 B  470  GLY ILE THR LEU SER LEU ASP PRO ASN GLY HIS MET ALA          
SEQRES  30 B  470  THR ASP VAL VAL GLY THR ALA LEU VAL GLU GLU LEU ALA          
SEQRES  31 B  470  ARG ARG ASN GLY ASP LYS VAL GLN TYR PHE GLN ILE LYS          
SEQRES  32 B  470  ASN ASN SER ARG SER GLY GLY THR ILE GLY PRO SER LEU          
SEQRES  33 B  470  ALA SER GLN THR GLY ALA ARG THR ILE ASP LEU GLY ILE          
SEQRES  34 B  470  ALA GLN LEU SER MET HIS SER ILE ARG ALA ALA THR GLY          
SEQRES  35 B  470  SER LYS ASP VAL GLY LEU GLY VAL LYS PHE PHE ASN GLY          
SEQRES  36 B  470  PHE PHE LYS HIS TRP ARG SER VAL TYR ASP GLU PHE GLY          
SEQRES  37 B  470  GLU LEU                                                      
SEQRES   1 C  470  MET GLU HIS ASN TYR GLU ASP ILE ALA GLN GLU PHE ILE          
SEQRES   2 C  470  ASP PHE ILE TYR LYS ASN PRO THR THR TYR HIS VAL VAL          
SEQRES   3 C  470  SER PHE PHE ALA GLU LEU LEU ASP LYS HIS ASN PHE LYS          
SEQRES   4 C  470  TYR LEU SER GLU LYS SER ASN TRP GLN ASP SER ILE GLY          
SEQRES   5 C  470  GLU ASP GLY GLY LYS PHE TYR THR ILE ARG ASN GLY THR          
SEQRES   6 C  470  ASN LEU SER ALA PHE ILE LEU GLY LYS ASN TRP ARG ALA          
SEQRES   7 C  470  GLU LYS GLY VAL GLY VAL ILE GLY SER HIS VAL ASP ALA          
SEQRES   8 C  470  LEU THR VAL LYS LEU LYS PRO VAL SER PHE LYS ASP THR          
SEQRES   9 C  470  ALA GLU GLY TYR GLY ARG ILE ALA VAL ALA PRO TYR GLY          
SEQRES  10 C  470  GLY THR LEU ASN GLU LEU TRP LEU ASP ARG ASP LEU GLY          
SEQRES  11 C  470  ILE GLY GLY ARG LEU LEU TYR LYS LYS LYS GLY THR ASN          
SEQRES  12 C  470  GLU ILE LYS SER ALA LEU VAL ASP SER THR PRO LEU PRO          
SEQRES  13 C  470  VAL CYS ARG ILE PRO SER LEU ALA PRO HIS PHE GLY LYS          
SEQRES  14 C  470  PRO ALA GLU GLY PRO PHE ASP LYS GLU ASP GLN THR ILE          
SEQRES  15 C  470  PRO VAL ILE GLY PHE PRO THR PRO ASP GLU GLU GLY ASN          
SEQRES  16 C  470  GLU PRO PRO THR ASP ASP GLU LYS LYS SER PRO LEU PHE          
SEQRES  17 C  470  GLY LYS HIS CYS ILE HIS LEU LEU ARG TYR VAL ALA LYS          
SEQRES  18 C  470  LEU ALA GLY VAL GLU VAL SER GLU LEU ILE GLN MET ASP          
SEQRES  19 C  470  LEU ASP LEU PHE ASP VAL GLN LYS GLY THR ILE GLY GLY          
SEQRES  20 C  470  ILE GLY LYS HIS PHE LEU PHE ALA PRO ARG LEU ASP ASP          
SEQRES  21 C  470  ARG LEU CYS SER PHE ALA ALA MET ILE ALA LEU ILE CYS          
SEQRES  22 C  470  TYR ALA LYS ASP VAL ASN THR GLU GLU SER ASP LEU PHE          
SEQRES  23 C  470  SER THR VAL THR LEU TYR ASP ASN GLU GLU ILE GLY SER          
SEQRES  24 C  470  LEU THR ARG GLN GLY ALA LYS GLY GLY LEU LEU GLU SER          
SEQRES  25 C  470  VAL VAL GLU ARG SER SER SER ALA PHE THR LYS LYS PRO          
SEQRES  26 C  470  VAL ASP LEU HIS THR VAL TRP ALA ASN SER ILE ILE LEU          
SEQRES  27 C  470  SER ALA ASP VAL ASN HIS LEU TYR ASN PRO ASN PHE PRO          
SEQRES  28 C  470  GLU VAL TYR LEU LYS ASN HIS PHE PRO VAL PRO ASN VAL          
SEQRES  29 C  470  GLY ILE THR LEU SER LEU ASP PRO ASN GLY HIS MET ALA          
SEQRES  30 C  470  THR ASP VAL VAL GLY THR ALA LEU VAL GLU GLU LEU ALA          
SEQRES  31 C  470  ARG ARG ASN GLY ASP LYS VAL GLN TYR PHE GLN ILE LYS          
SEQRES  32 C  470  ASN ASN SER ARG SER GLY GLY THR ILE GLY PRO SER LEU          
SEQRES  33 C  470  ALA SER GLN THR GLY ALA ARG THR ILE ASP LEU GLY ILE          
SEQRES  34 C  470  ALA GLN LEU SER MET HIS SER ILE ARG ALA ALA THR GLY          
SEQRES  35 C  470  SER LYS ASP VAL GLY LEU GLY VAL LYS PHE PHE ASN GLY          
SEQRES  36 C  470  PHE PHE LYS HIS TRP ARG SER VAL TYR ASP GLU PHE GLY          
SEQRES  37 C  470  GLU LEU                                                      
SEQRES   1 D  470  MET GLU HIS ASN TYR GLU ASP ILE ALA GLN GLU PHE ILE          
SEQRES   2 D  470  ASP PHE ILE TYR LYS ASN PRO THR THR TYR HIS VAL VAL          
SEQRES   3 D  470  SER PHE PHE ALA GLU LEU LEU ASP LYS HIS ASN PHE LYS          
SEQRES   4 D  470  TYR LEU SER GLU LYS SER ASN TRP GLN ASP SER ILE GLY          
SEQRES   5 D  470  GLU ASP GLY GLY LYS PHE TYR THR ILE ARG ASN GLY THR          
SEQRES   6 D  470  ASN LEU SER ALA PHE ILE LEU GLY LYS ASN TRP ARG ALA          
SEQRES   7 D  470  GLU LYS GLY VAL GLY VAL ILE GLY SER HIS VAL ASP ALA          
SEQRES   8 D  470  LEU THR VAL LYS LEU LYS PRO VAL SER PHE LYS ASP THR          
SEQRES   9 D  470  ALA GLU GLY TYR GLY ARG ILE ALA VAL ALA PRO TYR GLY          
SEQRES  10 D  470  GLY THR LEU ASN GLU LEU TRP LEU ASP ARG ASP LEU GLY          
SEQRES  11 D  470  ILE GLY GLY ARG LEU LEU TYR LYS LYS LYS GLY THR ASN          
SEQRES  12 D  470  GLU ILE LYS SER ALA LEU VAL ASP SER THR PRO LEU PRO          
SEQRES  13 D  470  VAL CYS ARG ILE PRO SER LEU ALA PRO HIS PHE GLY LYS          
SEQRES  14 D  470  PRO ALA GLU GLY PRO PHE ASP LYS GLU ASP GLN THR ILE          
SEQRES  15 D  470  PRO VAL ILE GLY PHE PRO THR PRO ASP GLU GLU GLY ASN          
SEQRES  16 D  470  GLU PRO PRO THR ASP ASP GLU LYS LYS SER PRO LEU PHE          
SEQRES  17 D  470  GLY LYS HIS CYS ILE HIS LEU LEU ARG TYR VAL ALA LYS          
SEQRES  18 D  470  LEU ALA GLY VAL GLU VAL SER GLU LEU ILE GLN MET ASP          
SEQRES  19 D  470  LEU ASP LEU PHE ASP VAL GLN LYS GLY THR ILE GLY GLY          
SEQRES  20 D  470  ILE GLY LYS HIS PHE LEU PHE ALA PRO ARG LEU ASP ASP          
SEQRES  21 D  470  ARG LEU CYS SER PHE ALA ALA MET ILE ALA LEU ILE CYS          
SEQRES  22 D  470  TYR ALA LYS ASP VAL ASN THR GLU GLU SER ASP LEU PHE          
SEQRES  23 D  470  SER THR VAL THR LEU TYR ASP ASN GLU GLU ILE GLY SER          
SEQRES  24 D  470  LEU THR ARG GLN GLY ALA LYS GLY GLY LEU LEU GLU SER          
SEQRES  25 D  470  VAL VAL GLU ARG SER SER SER ALA PHE THR LYS LYS PRO          
SEQRES  26 D  470  VAL ASP LEU HIS THR VAL TRP ALA ASN SER ILE ILE LEU          
SEQRES  27 D  470  SER ALA ASP VAL ASN HIS LEU TYR ASN PRO ASN PHE PRO          
SEQRES  28 D  470  GLU VAL TYR LEU LYS ASN HIS PHE PRO VAL PRO ASN VAL          
SEQRES  29 D  470  GLY ILE THR LEU SER LEU ASP PRO ASN GLY HIS MET ALA          
SEQRES  30 D  470  THR ASP VAL VAL GLY THR ALA LEU VAL GLU GLU LEU ALA          
SEQRES  31 D  470  ARG ARG ASN GLY ASP LYS VAL GLN TYR PHE GLN ILE LYS          
SEQRES  32 D  470  ASN ASN SER ARG SER GLY GLY THR ILE GLY PRO SER LEU          
SEQRES  33 D  470  ALA SER GLN THR GLY ALA ARG THR ILE ASP LEU GLY ILE          
SEQRES  34 D  470  ALA GLN LEU SER MET HIS SER ILE ARG ALA ALA THR GLY          
SEQRES  35 D  470  SER LYS ASP VAL GLY LEU GLY VAL LYS PHE PHE ASN GLY          
SEQRES  36 D  470  PHE PHE LYS HIS TRP ARG SER VAL TYR ASP GLU PHE GLY          
SEQRES  37 D  470  GLU LEU                                                      
FORMUL   5  HOH   *91(H2 O)                                                     
HELIX    1   1 ILE A    8  ASN A   19  1                                  12    
HELIX    2   2 THR A   21  LYS A   35  1                                  15    
HELIX    3   3 ARG A   77  GLY A   81  5                                   5    
HELIX    4   4 ASN A  121  LEU A  125  5                                   5    
HELIX    5   5 THR A  199  LYS A  204  1                                   6    
HELIX    6   6 CYS A  212  GLY A  224  1                                  13    
HELIX    7   7 GLU A  226  SER A  228  5                                   3    
HELIX    8   8 ARG A  257  ASP A  277  1                                  21    
HELIX    9   9 VAL A  278  SER A  283  5                                   6    
HELIX   10  10 GLY A  304  GLY A  307  5                                   4    
HELIX   11  11 GLY A  308  THR A  322  1                                  15    
HELIX   12  12 ASP A  327  ASN A  334  1                                   8    
HELIX   13  13 PHE A  350  TYR A  354  5                                   5    
HELIX   14  14 ASP A  379  GLY A  394  1                                  16    
HELIX   15  15 THR A  411  GLY A  421  1                                  11    
HELIX   16  16 LYS A  444  GLU A  466  1                                  23    
HELIX   17  17 TYR B    5  ASN B   19  1                                  15    
HELIX   18  18 THR B   21  HIS B   36  1                                  16    
HELIX   19  19 ARG B   77  GLY B   81  5                                   5    
HELIX   20  20 THR B  199  LYS B  204  1                                   6    
HELIX   21  21 CYS B  212  GLY B  224  1                                  13    
HELIX   22  22 GLU B  226  SER B  228  5                                   3    
HELIX   23  23 ARG B  257  ASP B  277  1                                  21    
HELIX   24  24 ASN B  294  GLY B  298  5                                   5    
HELIX   25  25 GLY B  304  GLY B  307  5                                   4    
HELIX   26  26 GLY B  308  THR B  322  1                                  15    
HELIX   27  27 ASP B  327  ASN B  334  1                                   8    
HELIX   28  28 VAL B  380  GLY B  394  1                                  15    
HELIX   29  29 THR B  411  GLY B  421  1                                  11    
HELIX   30  30 LYS B  444  GLU B  466  1                                  23    
HELIX   31  31 TYR C    5  ASN C   19  1                                  15    
HELIX   32  32 THR C   21  HIS C   36  1                                  16    
HELIX   33  33 ARG C   77  GLY C   81  5                                   5    
HELIX   34  34 ASN C  121  LEU C  125  5                                   5    
HELIX   35  35 THR C  199  LYS C  204  1                                   6    
HELIX   36  36 CYS C  212  GLY C  224  1                                  13    
HELIX   37  37 GLU C  226  SER C  228  5                                   3    
HELIX   38  38 ARG C  257  ASP C  277  1                                  21    
HELIX   39  39 GLY C  304  GLY C  307  5                                   4    
HELIX   40  40 GLY C  308  THR C  322  1                                  15    
HELIX   41  41 ASP C  327  ASN C  334  1                                   8    
HELIX   42  42 PHE C  350  TYR C  354  5                                   5    
HELIX   43  43 ASP C  379  GLY C  394  1                                  16    
HELIX   44  44 THR C  411  GLY C  421  1                                  11    
HELIX   45  45 LYS C  444  GLU C  466  1                                  23    
HELIX   46  46 TYR D    5  ASN D   19  1                                  15    
HELIX   47  47 THR D   21  HIS D   36  1                                  16    
HELIX   48  48 ARG D   77  GLY D   81  5                                   5    
HELIX   49  49 ASN D  121  LEU D  125  5                                   5    
HELIX   50  50 ASP D  201  SER D  205  5                                   5    
HELIX   51  51 CYS D  212  GLY D  224  1                                  13    
HELIX   52  52 ARG D  261  ASP D  277  1                                  17    
HELIX   53  53 GLY D  304  GLY D  307  5                                   4    
HELIX   54  54 GLY D  308  THR D  322  1                                  15    
HELIX   55  55 ASP D  327  ASN D  334  1                                   8    
HELIX   56  56 GLY D  374  THR D  378  5                                   5    
HELIX   57  57 ASP D  379  ASN D  393  1                                  15    
HELIX   58  58 THR D  411  GLY D  421  1                                  11    
HELIX   59  59 LYS D  444  GLU D  466  1                                  23    
SHEET    1   A 9 LYS A  39  TYR A  40  0                                        
SHEET    2   A 9 GLY A  56  ARG A  62  1  O  LYS A  57   N  LYS A  39           
SHEET    3   A 9 ASN A  66  LEU A  72 -1  O  ASN A  66   N  ARG A  62           
SHEET    4   A 9 PHE A 286  TYR A 292 -1  O  LEU A 291   N  LEU A  67           
SHEET    5   A 9 GLY A  83  HIS A  88  1  N  SER A  87   O  TYR A 292           
SHEET    6   A 9 ILE A 336  ALA A 340  1  O  LEU A 338   N  GLY A  86           
SHEET    7   A 9 ARG A 423  GLY A 428  1  O  ILE A 425   N  ILE A 337           
SHEET    8   A 9 ILE A 366  LEU A 370 -1  N  THR A 367   O  GLY A 428           
SHEET    9   A 9 VAL A 397  GLN A 401  1  O  GLN A 398   N  LEU A 368           
SHEET    1   B 6 LYS A 146  ASP A 151  0                                        
SHEET    2   B 6 LEU A 129  TYR A 137 -1  N  LEU A 135   O  ALA A 148           
SHEET    3   B 6 LEU A 230  ASP A 239 -1  O  GLN A 232   N  LEU A 136           
SHEET    4   B 6 THR A  93  ALA A 105 -1  N  VAL A  94   O  LEU A 237           
SHEET    5   B 6 TYR A 108  TYR A 116 -1  O  TYR A 116   N  THR A  93           
SHEET    6   B 6 ILE A 182  PRO A 183 -1  O  ILE A 182   N  ILE A 111           
SHEET    1   C 3 THR A 244  GLY A 246  0                                        
SHEET    2   C 3 PHE A 252  ALA A 255 -1  O  PHE A 254   N  THR A 244           
SHEET    3   C 3 ALA A 439  GLY A 442 -1  O  ALA A 439   N  ALA A 255           
SHEET    1   D 9 LYS B  39  TYR B  40  0                                        
SHEET    2   D 9 GLY B  56  ARG B  62  1  O  LYS B  57   N  LYS B  39           
SHEET    3   D 9 ASN B  66  LEU B  72 -1  O  PHE B  70   N  PHE B  58           
SHEET    4   D 9 PHE B 286  TYR B 292 -1  O  LEU B 291   N  LEU B  67           
SHEET    5   D 9 GLY B  83  HIS B  88  1  N  SER B  87   O  TYR B 292           
SHEET    6   D 9 ILE B 336  ALA B 340  1  O  LEU B 338   N  GLY B  86           
SHEET    7   D 9 ARG B 423  GLY B 428  1  O  ILE B 425   N  ILE B 337           
SHEET    8   D 9 THR B 367  LEU B 370 -1  N  THR B 367   O  GLY B 428           
SHEET    9   D 9 GLN B 398  GLN B 401  1  O  GLN B 398   N  LEU B 368           
SHEET    1   E 6 ILE B 145  ASP B 151  0                                        
SHEET    2   E 6 LEU B 129  LYS B 138 -1  N  TYR B 137   O  LYS B 146           
SHEET    3   E 6 LEU B 230  ASP B 239 -1  O  ILE B 231   N  LEU B 136           
SHEET    4   E 6 THR B  93  PHE B 101 -1  N  VAL B  94   O  LEU B 237           
SHEET    5   E 6 ARG B 110  TYR B 116 -1  O  ALA B 114   N  LYS B  95           
SHEET    6   E 6 ILE B 182  PRO B 183 -1  O  ILE B 182   N  ILE B 111           
SHEET    1   F 3 THR B 244  GLY B 246  0                                        
SHEET    2   F 3 PHE B 252  ALA B 255 -1  O  PHE B 252   N  GLY B 246           
SHEET    3   F 3 ALA B 439  GLY B 442 -1  O  THR B 441   N  LEU B 253           
SHEET    1   G 9 LYS C  39  TYR C  40  0                                        
SHEET    2   G 9 GLY C  56  ARG C  62  1  O  LYS C  57   N  LYS C  39           
SHEET    3   G 9 ASN C  66  LEU C  72 -1  O  ASN C  66   N  ARG C  62           
SHEET    4   G 9 PHE C 286  TYR C 292 -1  O  LEU C 291   N  LEU C  67           
SHEET    5   G 9 GLY C  83  HIS C  88  1  N  SER C  87   O  TYR C 292           
SHEET    6   G 9 ILE C 336  ALA C 340  1  O  ALA C 340   N  GLY C  86           
SHEET    7   G 9 ARG C 423  GLY C 428  1  O  ILE C 425   N  ILE C 337           
SHEET    8   G 9 ILE C 366  LEU C 370 -1  N  THR C 367   O  GLY C 428           
SHEET    9   G 9 VAL C 397  GLN C 401  1  O  GLN C 398   N  LEU C 368           
SHEET    1   H 6 LYS C 146  ASP C 151  0                                        
SHEET    2   H 6 LEU C 129  TYR C 137 -1  N  LEU C 135   O  ALA C 148           
SHEET    3   H 6 LEU C 230  ASP C 239 -1  O  ASP C 236   N  GLY C 132           
SHEET    4   H 6 THR C  93  PHE C 101 -1  N  VAL C  94   O  LEU C 237           
SHEET    5   H 6 GLY C 109  TYR C 116 -1  O  TYR C 116   N  THR C  93           
SHEET    6   H 6 ILE C 182  ILE C 185 -1  O  VAL C 184   N  GLY C 109           
SHEET    1   I 3 THR C 244  GLY C 246  0                                        
SHEET    2   I 3 PHE C 252  ALA C 255 -1  O  PHE C 254   N  THR C 244           
SHEET    3   I 3 ALA C 439  GLY C 442 -1  O  THR C 441   N  LEU C 253           
SHEET    1   J 9 LYS D  39  TYR D  40  0                                        
SHEET    2   J 9 GLY D  56  ARG D  62  1  O  LYS D  57   N  LYS D  39           
SHEET    3   J 9 ASN D  66  LEU D  72 -1  O  ASN D  66   N  ARG D  62           
SHEET    4   J 9 PHE D 286  TYR D 292 -1  O  LEU D 291   N  LEU D  67           
SHEET    5   J 9 GLY D  83  HIS D  88  1  N  SER D  87   O  TYR D 292           
SHEET    6   J 9 ILE D 336  ALA D 340  1  O  LEU D 338   N  VAL D  84           
SHEET    7   J 9 ARG D 423  GLY D 428  1  O  ILE D 425   N  ILE D 337           
SHEET    8   J 9 GLY D 365  LEU D 370 -1  N  THR D 367   O  GLY D 428           
SHEET    9   J 9 LYS D 396  GLN D 401  1  O  GLN D 398   N  LEU D 368           
SHEET    1   K 5 ILE D 111  TYR D 116  0                                        
SHEET    2   K 5 THR D  93  PHE D 101 -1  N  LYS D  95   O  ALA D 114           
SHEET    3   K 5 LEU D 230  ASP D 239 -1  O  LEU D 237   N  VAL D  94           
SHEET    4   K 5 LEU D 129  LYS D 138 -1  N  GLY D 132   O  ASP D 236           
SHEET    5   K 5 ILE D 145  ASP D 151 -1  O  ALA D 148   N  LEU D 135           
SHEET    1   L 3 THR D 244  GLY D 246  0                                        
SHEET    2   L 3 PHE D 252  ALA D 255 -1  O  PHE D 252   N  GLY D 246           
SHEET    3   L 3 ALA D 439  GLY D 442 -1  O  THR D 441   N  LEU D 253           
SHEET    1   M 2 ASN D 343  HIS D 344  0                                        
SHEET    2   M 2 ALA D 430  GLN D 431  1  O  GLN D 431   N  ASN D 343           
CISPEP   1 ASP A    7    ILE A    8          0       -11.79                     
CISPEP   2 THR A  153    PRO A  154          0         5.93                     
CISPEP   3 ASP A  259    ASP A  260          0        -1.94                     
CISPEP   4 THR B  119    LEU B  120          0        -1.40                     
CISPEP   5 THR B  153    PRO B  154          0        11.04                     
CISPEP   6 ASP B  259    ASP B  260          0        -1.82                     
CISPEP   7 THR C  153    PRO C  154          0         8.26                     
CISPEP   8 ASP C  259    ASP C  260          0        -5.99                     
CISPEP   9 THR D  153    PRO D  154          0         7.18                     
CISPEP  10 PRO D  165    HIS D  166          0         1.36                     
CISPEP  11 ASP D  259    ASP D  260          0        -0.31                     
CISPEP  12 ASN D  349    PHE D  350          0        15.76                     
CRYST1  140.171  140.171  348.677  90.00  90.00 120.00 H 3          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      0.007134  0.004119  0.000000        0.00000                         
SCALE2      0.000000  0.008238  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002868        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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