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LongText Report for: 5fv4-pdb

Name Class
5fv4-pdb
HEADER    HYDROLASE                               03-FEB-16   5FV4              
TITLE     PIG LIVER ESTERASE 5 (PLE5)                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;                                
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: PLE5;                                                       
COMPND   5 EC: 3.1.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: LIVER;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: K-12;                                      
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: SHUFFLE T7 EXPRESS;                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PET-15B                                    
KEYWDS    HYDROLASE, ESTERASE, ESTERASE-LIPASE SUPERFAMILY, CARBOXYLESTERASE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.WERTEN,G.J.PALM,L.BERNDT,W.HINRICHS                                 
REVDAT   1   15-FEB-17 5FV4    0                                                
JRNL        AUTH   S.WERTEN,G.J.PALM,L.BERNDT,W.HINRICHS                        
JRNL        TITL   PIG LIVER ESTERASE 5                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.74                          
REMARK   3   NUMBER OF REFLECTIONS             : 137701                         
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) : 0.18043                         
REMARK   3   R VALUE            (WORKING SET) : 0.17912                         
REMARK   3   FREE R VALUE                     : 0.20510                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 7248                            
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) : 2.400                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.462                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10152                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.300                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 534                          
REMARK   3   BIN FREE R VALUE                    : 0.319                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 24570                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 517                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 62.262                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.180                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.97                                                 
REMARK   3    B22 (A**2) : -1.01                                                
REMARK   3    B33 (A**2) : 0.12                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.33                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.359         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.214         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.179         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.945        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 25254 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 23880 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 34368 ; 1.562 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 55176 ; 1.282 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3174 ; 6.036 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1062 ;36.055 ;24.294       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4038 ;15.055 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   108 ;18.059 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3762 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 28560 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  5628 ; 0.007 ; 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): 12714 ; 2.003 ; 3.808       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 12713 ; 2.002 ; 3.807       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15882 ; 3.201 ; 5.706       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 12540 ; 2.379 ; 4.050       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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   NUMBER OF DIFFERENT NCS GROUPS : 6                                 
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  :  15                               
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     5    534       B     5    534   65956  0.04  0.05     
REMARK   3    2     A     5    534       C     5    534   66270  0.03  0.05     
REMARK   3    3     A     5    534       D     5    534   65952  0.04  0.05     
REMARK   3    4     A     5    534       E     5    534   66352  0.03  0.05     
REMARK   3    5     A     5    534       F     5    534   66070  0.04  0.05     
REMARK   3    6     B     5    534       C     5    534   66236  0.04  0.05     
REMARK   3    7     B     5    534       D     5    534   65930  0.04  0.05     
REMARK   3    8     B     5    534       E     5    534   66124  0.03  0.05     
REMARK   3    9     B     5    534       F     5    534   66236  0.04  0.05     
REMARK   3   10     C     5    534       D     5    534   66184  0.04  0.05     
REMARK   3   11     C     5    534       E     5    534   66416  0.03  0.05     
REMARK   3   12     C     5    534       F     5    534   66314  0.04  0.05     
REMARK   3   13     D     5    534       E     5    534   66212  0.03  0.05     
REMARK   3   14     D     5    534       F     5    534   66080  0.04  0.05     
REMARK   3   15     E     5    534       F     5    534   66338  0.03  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP :     1                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     5        A   534                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3369 146.5089 110.4509              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0269 T22:   0.2745                                     
REMARK   3      T33:   0.0074 T12:   0.0389                                     
REMARK   3      T13:   0.0076 T23:   0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9714 L22:   1.0485                                     
REMARK   3      L33:   1.1799 L12:  -0.2950                                     
REMARK   3      L13:  -0.4756 L23:   0.4712                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0239 S12:   0.1959 S13:   0.0227                       
REMARK   3      S21:  -0.1300 S22:  -0.0318 S23:  -0.0361                       
REMARK   3      S31:   0.0206 S32:  -0.0032 S33:   0.0079                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     2                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     5        B   534                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.7178 154.3572  56.2409              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0305 T22:   0.3959                                     
REMARK   3      T33:   0.1845 T12:  -0.0291                                     
REMARK   3      T13:  -0.0054 T23:   0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3205 L22:   0.8905                                     
REMARK   3      L33:   1.2975 L12:   0.2764                                     
REMARK   3      L13:  -0.2420 L23:  -0.1655                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0429 S12:  -0.4293 S13:  -0.0522                       
REMARK   3      S21:   0.1499 S22:  -0.1249 S23:  -0.0471                       
REMARK   3      S31:   0.0518 S32:   0.0424 S33:   0.0820                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     3                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     5        C   534                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.2740  96.7865  69.7522              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0492 T22:   0.1365                                     
REMARK   3      T33:   0.2327 T12:   0.0221                                     
REMARK   3      T13:  -0.0027 T23:  -0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8455 L22:   1.7606                                     
REMARK   3      L33:   1.1773 L12:  -0.3445                                     
REMARK   3      L13:  -0.0100 L23:  -0.0193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0199 S12:   0.0460 S13:   0.3000                       
REMARK   3      S21:  -0.0770 S22:  -0.0838 S23:  -0.1897                       
REMARK   3      S31:  -0.2305 S32:  -0.0605 S33:   0.0639                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     4                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     5        D   534                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.0960 130.3568 112.2242              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1627 T22:   0.3425                                     
REMARK   3      T33:   0.3671 T12:  -0.0105                                     
REMARK   3      T13:  -0.1352 T23:  -0.1993                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9309 L22:   1.1792                                     
REMARK   3      L33:   2.4881 L12:   0.0454                                     
REMARK   3      L13:   1.1763 L23:   0.0819                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3264 S12:   0.4432 S13:  -0.5249                       
REMARK   3      S21:  -0.1121 S22:   0.0943 S23:   0.1280                       
REMARK   3      S31:   0.5905 S32:   0.0460 S33:  -0.4208                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     5                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     5        E   534                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1109  93.8800  99.4280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2557 T22:   0.2868                                     
REMARK   3      T33:   0.5836 T12:  -0.1157                                     
REMARK   3      T13:  -0.0891 T23:  -0.1660                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9888 L22:   2.1139                                     
REMARK   3      L33:   2.0673 L12:   0.2367                                     
REMARK   3      L13:   0.1507 L23:  -0.2170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0570 S12:  -0.2457 S13:   0.4233                       
REMARK   3      S21:   0.3215 S22:  -0.0632 S23:  -0.0158                       
REMARK   3      S31:  -0.6580 S32:   0.2641 S33:   0.1201                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :     6                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     5        F   534                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8107 136.9797  58.7750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0855 T22:   0.3078                                     
REMARK   3      T33:   0.0804 T12:   0.0626                                     
REMARK   3      T13:  -0.0037 T23:   0.1072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2649 L22:   0.9915                                     
REMARK   3      L33:   2.2907 L12:  -0.3363                                     
REMARK   3      L13:   0.5522 L23:  -0.3044                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0952 S12:  -0.1613 S13:  -0.2429                       
REMARK   3      S21:  -0.0094 S22:   0.0198 S23:   0.1559                       
REMARK   3      S31:   0.4210 S32:   0.1237 S33:  -0.1149                       
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   3  U  VALUES WITH TLS ADDED                                            
REMARK   4                                                                      
REMARK   4 5FV4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-16.                  
REMARK 100 THE PDBE ID CODE IS EBI-66170.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III                          
REMARK 200  BEAMLINE                       : P13 (MX1)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 144950                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.14                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.3                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.77                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.02                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1MX9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.5, 18% PEG             
REMARK 280  4000 AT 295 K                                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       94.01000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 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: 4                                                       
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: 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                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
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: E                                     
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: 6                                                       
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: F                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     GLU A   535                                                      
REMARK 465     ALA A   536                                                      
REMARK 465     ALA A   537                                                      
REMARK 465     LYS A   538                                                      
REMARK 465     LYS A   539                                                      
REMARK 465     PRO A   540                                                      
REMARK 465     PRO A   541                                                      
REMARK 465     LYS A   542                                                      
REMARK 465     ILE A   543                                                      
REMARK 465     LYS A   544                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     GLU B   535                                                      
REMARK 465     ALA B   536                                                      
REMARK 465     ALA B   537                                                      
REMARK 465     LYS B   538                                                      
REMARK 465     LYS B   539                                                      
REMARK 465     PRO B   540                                                      
REMARK 465     PRO B   541                                                      
REMARK 465     LYS B   542                                                      
REMARK 465     ILE B   543                                                      
REMARK 465     LYS B   544                                                      
REMARK 465     GLY C     1                                                      
REMARK 465     GLN C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     GLU C   535                                                      
REMARK 465     ALA C   536                                                      
REMARK 465     ALA C   537                                                      
REMARK 465     LYS C   538                                                      
REMARK 465     LYS C   539                                                      
REMARK 465     PRO C   540                                                      
REMARK 465     PRO C   541                                                      
REMARK 465     LYS C   542                                                      
REMARK 465     ILE C   543                                                      
REMARK 465     LYS C   544                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     GLU D   535                                                      
REMARK 465     ALA D   536                                                      
REMARK 465     ALA D   537                                                      
REMARK 465     LYS D   538                                                      
REMARK 465     LYS D   539                                                      
REMARK 465     PRO D   540                                                      
REMARK 465     PRO D   541                                                      
REMARK 465     LYS D   542                                                      
REMARK 465     ILE D   543                                                      
REMARK 465     LYS D   544                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     GLN E     2                                                      
REMARK 465     PRO E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     GLU E   535                                                      
REMARK 465     ALA E   536                                                      
REMARK 465     ALA E   537                                                      
REMARK 465     LYS E   538                                                      
REMARK 465     LYS E   539                                                      
REMARK 465     PRO E   540                                                      
REMARK 465     PRO E   541                                                      
REMARK 465     LYS E   542                                                      
REMARK 465     ILE E   543                                                      
REMARK 465     LYS E   544                                                      
REMARK 465     GLY F     1                                                      
REMARK 465     GLN F     2                                                      
REMARK 465     PRO F     3                                                      
REMARK 465     ALA F     4                                                      
REMARK 465     GLU F   535                                                      
REMARK 465     ALA F   536                                                      
REMARK 465     ALA F   537                                                      
REMARK 465     LYS F   538                                                      
REMARK 465     LYS F   539                                                      
REMARK 465     PRO F   540                                                      
REMARK 465     PRO F   541                                                      
REMARK 465     LYS F   542                                                      
REMARK 465     ILE F   543                                                      
REMARK 465     LYS F   544                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    GLY D   492     OE1  GLU E   493     1455     1.85            
REMARK 500   O    LEU D   495     OE2  GLU E   493     1455     1.91            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG B  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG B 295   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG C 295   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    LEU D  26   CB  -  CG  -  CD1 ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ARG D 113   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG E 113   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG F  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP F 465   CB  -  CG  -  OD1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP F 465   CB  -  CG  -  OD2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  59     -167.52     62.48                                   
REMARK 500    CYS A  99       11.38   -140.98                                   
REMARK 500    ARG A 115       53.75   -140.88                                   
REMARK 500    SER A 168       82.24   -157.65                                   
REMARK 500    SER A 204     -122.98     63.07                                   
REMARK 500    MET A 243       25.04   -141.40                                   
REMARK 500    VAL A 308      -71.58   -131.42                                   
REMARK 500    TRP A 339      -57.25   -153.70                                   
REMARK 500    ASP A 502     -150.85   -110.72                                   
REMARK 500    ARG A 519       56.56     70.47                                   
REMARK 500    GLN B  28      109.46    -49.90                                   
REMARK 500    PHE B  59     -166.37     63.34                                   
REMARK 500    THR B  63       61.56   -119.40                                   
REMARK 500    SER B 168       84.61   -160.90                                   
REMARK 500    SER B 204     -121.51     62.66                                   
REMARK 500    VAL B 308      -72.07   -131.29                                   
REMARK 500    TRP B 339      -58.22   -153.81                                   
REMARK 500    ASP B 502     -152.78   -111.58                                   
REMARK 500    ARG B 519       57.05     70.18                                   
REMARK 500    PHE C  59     -167.62     63.55                                   
REMARK 500    THR C  63       61.05   -119.89                                   
REMARK 500    ARG C 113       79.79   -110.92                                   
REMARK 500    SER C 168       84.04   -162.29                                   
REMARK 500    SER C 204     -121.34     63.98                                   
REMARK 500    MET C 243       28.10   -142.93                                   
REMARK 500    VAL C 308      -71.01   -131.12                                   
REMARK 500    TRP C 339      -56.24   -153.84                                   
REMARK 500    ASP C 502     -152.00   -110.59                                   
REMARK 500    ARG C 519       56.83     70.65                                   
REMARK 500    GLN D  28      109.22    -49.36                                   
REMARK 500    PHE D  59     -165.06     63.21                                   
REMARK 500    SER D 168       82.35   -160.40                                   
REMARK 500    SER D 204     -124.23     61.75                                   
REMARK 500    VAL D 308      -73.15   -131.43                                   
REMARK 500    TRP D 339      -57.22   -153.47                                   
REMARK 500    GLU D 351      -30.17    -39.97                                   
REMARK 500    ASP D 502     -152.66   -112.14                                   
REMARK 500    ARG D 519       56.85     70.40                                   
REMARK 500    PHE E  59     -167.36     62.34                                   
REMARK 500    THR E  63       63.08   -117.13                                   
REMARK 500    SER E 168       83.05   -160.44                                   
REMARK 500    SER E 204     -122.59     60.45                                   
REMARK 500    VAL E 308      -70.52   -130.89                                   
REMARK 500    TRP E 339      -57.16   -153.42                                   
REMARK 500    ASP E 502     -151.66   -111.88                                   
REMARK 500    ARG E 519       57.29     70.00                                   
REMARK 500    PHE F  59     -163.70     61.91                                   
REMARK 500    THR F  63       61.45   -118.38                                   
REMARK 500    SER F 168       84.37   -159.60                                   
REMARK 500    SER F 197       80.76   -150.90                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE DIFFERENCES BETWEEN UNIPROT AND THE SAMPLE ARE              
REMARK 999 DUE TO A LOCAL CLONE BEING USED.                                     
DBREF  5FV4 A    1   544  UNP    A9GYW6   A9GYW6_PIG       1    544             
DBREF  5FV4 B    1   544  UNP    A9GYW6   A9GYW6_PIG       1    544             
DBREF  5FV4 C    1   544  UNP    A9GYW6   A9GYW6_PIG       1    544             
DBREF  5FV4 D    1   544  UNP    A9GYW6   A9GYW6_PIG       1    544             
DBREF  5FV4 E    1   544  UNP    A9GYW6   A9GYW6_PIG       1    544             
DBREF  5FV4 F    1   544  UNP    A9GYW6   A9GYW6_PIG       1    544             
SEQADV 5FV4 ASP A   73  UNP  A9GYW6    GLU    73 CONFLICT                       
SEQADV 5FV4 VAL A   75  UNP  A9GYW6    ILE    75 CONFLICT                       
SEQADV 5FV4 ALA A   76  UNP  A9GYW6    GLY    76 CONFLICT                       
SEQADV 5FV4 THR A   80  UNP  A9GYW6    LEU    80 CONFLICT                       
SEQADV 5FV4 ALA A  459  UNP  A9GYW6    PHE   459 CONFLICT                       
SEQADV 5FV4 PHE A  461  UNP  A9GYW6    LEU   461 CONFLICT                       
SEQADV 5FV4 ARG A  463  UNP  A9GYW6    LYS   463 CONFLICT                       
SEQADV 5FV4 ASP B   73  UNP  A9GYW6    GLU    73 CONFLICT                       
SEQADV 5FV4 VAL B   75  UNP  A9GYW6    ILE    75 CONFLICT                       
SEQADV 5FV4 ALA B   76  UNP  A9GYW6    GLY    76 CONFLICT                       
SEQADV 5FV4 THR B   80  UNP  A9GYW6    LEU    80 CONFLICT                       
SEQADV 5FV4 ALA B  459  UNP  A9GYW6    PHE   459 CONFLICT                       
SEQADV 5FV4 PHE B  461  UNP  A9GYW6    LEU   461 CONFLICT                       
SEQADV 5FV4 ARG B  463  UNP  A9GYW6    LYS   463 CONFLICT                       
SEQADV 5FV4 ASP C   73  UNP  A9GYW6    GLU    73 CONFLICT                       
SEQADV 5FV4 VAL C   75  UNP  A9GYW6    ILE    75 CONFLICT                       
SEQADV 5FV4 ALA C   76  UNP  A9GYW6    GLY    76 CONFLICT                       
SEQADV 5FV4 THR C   80  UNP  A9GYW6    LEU    80 CONFLICT                       
SEQADV 5FV4 ALA C  459  UNP  A9GYW6    PHE   459 CONFLICT                       
SEQADV 5FV4 PHE C  461  UNP  A9GYW6    LEU   461 CONFLICT                       
SEQADV 5FV4 ARG C  463  UNP  A9GYW6    LYS   463 CONFLICT                       
SEQADV 5FV4 ASP D   73  UNP  A9GYW6    GLU    73 CONFLICT                       
SEQADV 5FV4 VAL D   75  UNP  A9GYW6    ILE    75 CONFLICT                       
SEQADV 5FV4 ALA D   76  UNP  A9GYW6    GLY    76 CONFLICT                       
SEQADV 5FV4 THR D   80  UNP  A9GYW6    LEU    80 CONFLICT                       
SEQADV 5FV4 ALA D  459  UNP  A9GYW6    PHE   459 CONFLICT                       
SEQADV 5FV4 PHE D  461  UNP  A9GYW6    LEU   461 CONFLICT                       
SEQADV 5FV4 ARG D  463  UNP  A9GYW6    LYS   463 CONFLICT                       
SEQADV 5FV4 ASP E   73  UNP  A9GYW6    GLU    73 CONFLICT                       
SEQADV 5FV4 VAL E   75  UNP  A9GYW6    ILE    75 CONFLICT                       
SEQADV 5FV4 ALA E   76  UNP  A9GYW6    GLY    76 CONFLICT                       
SEQADV 5FV4 THR E   80  UNP  A9GYW6    LEU    80 CONFLICT                       
SEQADV 5FV4 ALA E  459  UNP  A9GYW6    PHE   459 CONFLICT                       
SEQADV 5FV4 PHE E  461  UNP  A9GYW6    LEU   461 CONFLICT                       
SEQADV 5FV4 ARG E  463  UNP  A9GYW6    LYS   463 CONFLICT                       
SEQADV 5FV4 ASP F   73  UNP  A9GYW6    GLU    73 CONFLICT                       
SEQADV 5FV4 VAL F   75  UNP  A9GYW6    ILE    75 CONFLICT                       
SEQADV 5FV4 ALA F   76  UNP  A9GYW6    GLY    76 CONFLICT                       
SEQADV 5FV4 THR F   80  UNP  A9GYW6    LEU    80 CONFLICT                       
SEQADV 5FV4 ALA F  459  UNP  A9GYW6    PHE   459 CONFLICT                       
SEQADV 5FV4 PHE F  461  UNP  A9GYW6    LEU   461 CONFLICT                       
SEQADV 5FV4 ARG F  463  UNP  A9GYW6    LYS   463 CONFLICT                       
SEQRES   1 A  544  GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN          
SEQRES   2 A  544  GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU          
SEQRES   3 A  544  ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA          
SEQRES   4 A  544  LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN          
SEQRES   5 A  544  PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER          
SEQRES   6 A  544  TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN          
SEQRES   7 A  544  MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU          
SEQRES   8 A  544  ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE          
SEQRES   9 A  544  TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO          
SEQRES  10 A  544  VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY          
SEQRES  11 A  544  GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS          
SEQRES  12 A  544  GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY          
SEQRES  13 A  544  ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG          
SEQRES  14 A  544  GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS          
SEQRES  15 A  544  TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO          
SEQRES  16 A  544  GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU          
SEQRES  17 A  544  SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN          
SEQRES  18 A  544  LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE          
SEQRES  19 A  544  THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA          
SEQRES  20 A  544  LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR          
SEQRES  21 A  544  SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU          
SEQRES  22 A  544  ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE          
SEQRES  23 A  544  ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO          
SEQRES  24 A  544  PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS          
SEQRES  25 A  544  MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR          
SEQRES  26 A  544  VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY          
SEQRES  27 A  544  TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU          
SEQRES  28 A  544  GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP          
SEQRES  29 A  544  LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR          
SEQRES  30 A  544  PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP          
SEQRES  31 A  544  PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY          
SEQRES  32 A  544  ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG          
SEQRES  33 A  544  GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU          
SEQRES  34 A  544  PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO          
SEQRES  35 A  544  LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER          
SEQRES  36 A  544  VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU          
SEQRES  37 A  544  GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP          
SEQRES  38 A  544  ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY          
SEQRES  39 A  544  LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR          
SEQRES  40 A  544  LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU          
SEQRES  41 A  544  LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER          
SEQRES  42 A  544  LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS                  
SEQRES   1 B  544  GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN          
SEQRES   2 B  544  GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU          
SEQRES   3 B  544  ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA          
SEQRES   4 B  544  LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN          
SEQRES   5 B  544  PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER          
SEQRES   6 B  544  TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN          
SEQRES   7 B  544  MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU          
SEQRES   8 B  544  ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE          
SEQRES   9 B  544  TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO          
SEQRES  10 B  544  VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY          
SEQRES  11 B  544  GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS          
SEQRES  12 B  544  GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY          
SEQRES  13 B  544  ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG          
SEQRES  14 B  544  GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS          
SEQRES  15 B  544  TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO          
SEQRES  16 B  544  GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU          
SEQRES  17 B  544  SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN          
SEQRES  18 B  544  LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE          
SEQRES  19 B  544  THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA          
SEQRES  20 B  544  LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR          
SEQRES  21 B  544  SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU          
SEQRES  22 B  544  ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE          
SEQRES  23 B  544  ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO          
SEQRES  24 B  544  PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS          
SEQRES  25 B  544  MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR          
SEQRES  26 B  544  VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY          
SEQRES  27 B  544  TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU          
SEQRES  28 B  544  GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP          
SEQRES  29 B  544  LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR          
SEQRES  30 B  544  PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP          
SEQRES  31 B  544  PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY          
SEQRES  32 B  544  ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG          
SEQRES  33 B  544  GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU          
SEQRES  34 B  544  PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO          
SEQRES  35 B  544  LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER          
SEQRES  36 B  544  VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU          
SEQRES  37 B  544  GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP          
SEQRES  38 B  544  ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY          
SEQRES  39 B  544  LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR          
SEQRES  40 B  544  LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU          
SEQRES  41 B  544  LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER          
SEQRES  42 B  544  LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS                  
SEQRES   1 C  544  GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN          
SEQRES   2 C  544  GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU          
SEQRES   3 C  544  ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA          
SEQRES   4 C  544  LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN          
SEQRES   5 C  544  PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER          
SEQRES   6 C  544  TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN          
SEQRES   7 C  544  MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU          
SEQRES   8 C  544  ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE          
SEQRES   9 C  544  TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO          
SEQRES  10 C  544  VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY          
SEQRES  11 C  544  GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS          
SEQRES  12 C  544  GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY          
SEQRES  13 C  544  ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG          
SEQRES  14 C  544  GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS          
SEQRES  15 C  544  TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO          
SEQRES  16 C  544  GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU          
SEQRES  17 C  544  SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN          
SEQRES  18 C  544  LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE          
SEQRES  19 C  544  THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA          
SEQRES  20 C  544  LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR          
SEQRES  21 C  544  SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU          
SEQRES  22 C  544  ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE          
SEQRES  23 C  544  ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO          
SEQRES  24 C  544  PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS          
SEQRES  25 C  544  MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR          
SEQRES  26 C  544  VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY          
SEQRES  27 C  544  TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU          
SEQRES  28 C  544  GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP          
SEQRES  29 C  544  LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR          
SEQRES  30 C  544  PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP          
SEQRES  31 C  544  PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY          
SEQRES  32 C  544  ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG          
SEQRES  33 C  544  GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU          
SEQRES  34 C  544  PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO          
SEQRES  35 C  544  LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER          
SEQRES  36 C  544  VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU          
SEQRES  37 C  544  GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP          
SEQRES  38 C  544  ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY          
SEQRES  39 C  544  LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR          
SEQRES  40 C  544  LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU          
SEQRES  41 C  544  LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER          
SEQRES  42 C  544  LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS                  
SEQRES   1 D  544  GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN          
SEQRES   2 D  544  GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU          
SEQRES   3 D  544  ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA          
SEQRES   4 D  544  LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN          
SEQRES   5 D  544  PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER          
SEQRES   6 D  544  TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN          
SEQRES   7 D  544  MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU          
SEQRES   8 D  544  ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE          
SEQRES   9 D  544  TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO          
SEQRES  10 D  544  VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY          
SEQRES  11 D  544  GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS          
SEQRES  12 D  544  GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY          
SEQRES  13 D  544  ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG          
SEQRES  14 D  544  GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS          
SEQRES  15 D  544  TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO          
SEQRES  16 D  544  GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU          
SEQRES  17 D  544  SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN          
SEQRES  18 D  544  LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE          
SEQRES  19 D  544  THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA          
SEQRES  20 D  544  LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR          
SEQRES  21 D  544  SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU          
SEQRES  22 D  544  ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE          
SEQRES  23 D  544  ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO          
SEQRES  24 D  544  PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS          
SEQRES  25 D  544  MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR          
SEQRES  26 D  544  VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY          
SEQRES  27 D  544  TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU          
SEQRES  28 D  544  GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP          
SEQRES  29 D  544  LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR          
SEQRES  30 D  544  PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP          
SEQRES  31 D  544  PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY          
SEQRES  32 D  544  ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG          
SEQRES  33 D  544  GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU          
SEQRES  34 D  544  PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO          
SEQRES  35 D  544  LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER          
SEQRES  36 D  544  VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU          
SEQRES  37 D  544  GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP          
SEQRES  38 D  544  ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY          
SEQRES  39 D  544  LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR          
SEQRES  40 D  544  LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU          
SEQRES  41 D  544  LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER          
SEQRES  42 D  544  LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS                  
SEQRES   1 E  544  GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN          
SEQRES   2 E  544  GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU          
SEQRES   3 E  544  ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA          
SEQRES   4 E  544  LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN          
SEQRES   5 E  544  PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER          
SEQRES   6 E  544  TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN          
SEQRES   7 E  544  MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU          
SEQRES   8 E  544  ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE          
SEQRES   9 E  544  TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO          
SEQRES  10 E  544  VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY          
SEQRES  11 E  544  GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS          
SEQRES  12 E  544  GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY          
SEQRES  13 E  544  ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG          
SEQRES  14 E  544  GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS          
SEQRES  15 E  544  TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO          
SEQRES  16 E  544  GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU          
SEQRES  17 E  544  SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN          
SEQRES  18 E  544  LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE          
SEQRES  19 E  544  THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA          
SEQRES  20 E  544  LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR          
SEQRES  21 E  544  SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU          
SEQRES  22 E  544  ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE          
SEQRES  23 E  544  ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO          
SEQRES  24 E  544  PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS          
SEQRES  25 E  544  MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR          
SEQRES  26 E  544  VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY          
SEQRES  27 E  544  TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU          
SEQRES  28 E  544  GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP          
SEQRES  29 E  544  LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR          
SEQRES  30 E  544  PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP          
SEQRES  31 E  544  PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY          
SEQRES  32 E  544  ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG          
SEQRES  33 E  544  GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU          
SEQRES  34 E  544  PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO          
SEQRES  35 E  544  LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER          
SEQRES  36 E  544  VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU          
SEQRES  37 E  544  GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP          
SEQRES  38 E  544  ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY          
SEQRES  39 E  544  LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR          
SEQRES  40 E  544  LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU          
SEQRES  41 E  544  LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER          
SEQRES  42 E  544  LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS                  
SEQRES   1 F  544  GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN          
SEQRES   2 F  544  GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU          
SEQRES   3 F  544  ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA          
SEQRES   4 F  544  LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN          
SEQRES   5 F  544  PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER          
SEQRES   6 F  544  TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN          
SEQRES   7 F  544  MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU          
SEQRES   8 F  544  ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE          
SEQRES   9 F  544  TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO          
SEQRES  10 F  544  VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY          
SEQRES  11 F  544  GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS          
SEQRES  12 F  544  GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY          
SEQRES  13 F  544  ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG          
SEQRES  14 F  544  GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS          
SEQRES  15 F  544  TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO          
SEQRES  16 F  544  GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU          
SEQRES  17 F  544  SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN          
SEQRES  18 F  544  LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE          
SEQRES  19 F  544  THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA          
SEQRES  20 F  544  LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR          
SEQRES  21 F  544  SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU          
SEQRES  22 F  544  ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE          
SEQRES  23 F  544  ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO          
SEQRES  24 F  544  PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS          
SEQRES  25 F  544  MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR          
SEQRES  26 F  544  VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY          
SEQRES  27 F  544  TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU          
SEQRES  28 F  544  GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP          
SEQRES  29 F  544  LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR          
SEQRES  30 F  544  PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP          
SEQRES  31 F  544  PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY          
SEQRES  32 F  544  ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG          
SEQRES  33 F  544  GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU          
SEQRES  34 F  544  PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO          
SEQRES  35 F  544  LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER          
SEQRES  36 F  544  VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU          
SEQRES  37 F  544  GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP          
SEQRES  38 F  544  ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY          
SEQRES  39 F  544  LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR          
SEQRES  40 F  544  LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU          
SEQRES  41 F  544  LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER          
SEQRES  42 F  544  LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS                  
FORMUL   7  HOH   *517(H2 O)                                                    
HELIX    1   1 LEU A   43  ARG A   47  5                                   5    
HELIX    2   2 ASP A   73  THR A   85  1                                  13    
HELIX    3   3 GLY A  131  TYR A  135  5                                   5    
HELIX    4   4 GLY A  137  ASN A  145  1                                   9    
HELIX    5   5 LEU A  155  PHE A  161  1                                   7    
HELIX    6   6 ASN A  171  ILE A  188  1                                  18    
HELIX    7   7 ALA A  189  PHE A  191  5                                   3    
HELIX    8   8 SER A  204  SER A  216  1                                  13    
HELIX    9   9 PRO A  217  LYS A  220  5                                   4    
HELIX   10  10 PHE A  234  GLY A  237  5                                   4    
HELIX   11  11 MET A  243  GLY A  255  1                                  13    
HELIX   12  12 THR A  260  LYS A  271  1                                  12    
HELIX   13  13 SER A  272  LYS A  284  1                                  13    
HELIX   14  14 ASP A  293  SER A  297  5                                   5    
HELIX   15  15 MET A  313  LYS A  321  1                                   9    
HELIX   16  16 TRP A  339  MET A  345  1                                   7    
HELIX   17  17 ASP A  355  SER A  366  1                                  12    
HELIX   18  18 SER A  366  ASN A  371  1                                   6    
HELIX   19  19 PRO A  373  GLU A  375  5                                   3    
HELIX   20  20 LEU A  376  GLY A  386  1                                  11    
HELIX   21  21 ASP A  390  PHE A  407  1                                  18    
HELIX   22  22 PHE A  407  ALA A  421  1                                  15    
HELIX   23  23 GLY A  450  PHE A  457  1                                   8    
HELIX   24  24 GLY A  458  LEU A  462  5                                   5    
HELIX   25  25 PRO A  467  GLY A  488  1                                  22    
HELIX   26  26 LYS A  521  LEU A  532  1                                  12    
HELIX   27  27 LEU B   43  ARG B   47  5                                   5    
HELIX   28  28 ASP B   73  THR B   85  1                                  13    
HELIX   29  29 GLY B  131  TYR B  135  5                                   5    
HELIX   30  30 GLY B  137  ASN B  145  1                                   9    
HELIX   31  31 LEU B  155  PHE B  161  1                                   7    
HELIX   32  32 ASN B  171  ILE B  188  1                                  18    
HELIX   33  33 ALA B  189  PHE B  191  5                                   3    
HELIX   34  34 SER B  204  SER B  216  1                                  13    
HELIX   35  35 PRO B  217  LYS B  220  5                                   4    
HELIX   36  36 PHE B  234  GLY B  237  5                                   4    
HELIX   37  37 MET B  243  GLY B  255  1                                  13    
HELIX   38  38 THR B  260  LYS B  271  1                                  12    
HELIX   39  39 SER B  272  LYS B  284  1                                  13    
HELIX   40  40 ASP B  293  SER B  297  5                                   5    
HELIX   41  41 MET B  313  LYS B  321  1                                   9    
HELIX   42  42 TRP B  339  GLY B  346  1                                   8    
HELIX   43  43 ASP B  355  SER B  366  1                                  12    
HELIX   44  44 SER B  366  ASN B  371  1                                   6    
HELIX   45  45 PRO B  373  GLU B  375  5                                   3    
HELIX   46  46 LEU B  376  GLY B  386  1                                  11    
HELIX   47  47 ASP B  390  PHE B  407  1                                  18    
HELIX   48  48 PHE B  407  ALA B  421  1                                  15    
HELIX   49  49 GLY B  450  PHE B  457  1                                   8    
HELIX   50  50 GLY B  458  LEU B  462  5                                   5    
HELIX   51  51 PRO B  467  GLY B  488  1                                  22    
HELIX   52  52 LYS B  521  LEU B  532  1                                  12    
HELIX   53  53 LEU C   43  ARG C   47  5                                   5    
HELIX   54  54 ASP C   73  THR C   85  1                                  13    
HELIX   55  55 GLY C  131  TYR C  135  5                                   5    
HELIX   56  56 GLY C  137  ASN C  145  1                                   9    
HELIX   57  57 LEU C  155  PHE C  161  1                                   7    
HELIX   58  58 ASN C  171  ILE C  188  1                                  18    
HELIX   59  59 ALA C  189  PHE C  191  5                                   3    
HELIX   60  60 SER C  204  SER C  216  1                                  13    
HELIX   61  61 PRO C  217  LYS C  220  5                                   4    
HELIX   62  62 PHE C  234  GLY C  237  5                                   4    
HELIX   63  63 MET C  243  GLY C  255  1                                  13    
HELIX   64  64 THR C  260  LYS C  271  1                                  12    
HELIX   65  65 SER C  272  LYS C  284  1                                  13    
HELIX   66  66 ASP C  293  SER C  297  5                                   5    
HELIX   67  67 MET C  313  LYS C  321  1                                   9    
HELIX   68  68 TRP C  339  MET C  345  1                                   7    
HELIX   69  69 ASP C  355  SER C  366  1                                  12    
HELIX   70  70 SER C  366  ASN C  371  1                                   6    
HELIX   71  71 PRO C  373  GLU C  375  5                                   3    
HELIX   72  72 LEU C  376  GLY C  386  1                                  11    
HELIX   73  73 ASP C  390  PHE C  407  1                                  18    
HELIX   74  74 PHE C  407  ALA C  421  1                                  15    
HELIX   75  75 GLY C  450  PHE C  457  1                                   8    
HELIX   76  76 GLY C  458  LEU C  462  5                                   5    
HELIX   77  77 PRO C  467  GLY C  488  1                                  22    
HELIX   78  78 LYS C  521  LEU C  532  1                                  12    
HELIX   79  79 LEU D   43  ARG D   47  5                                   5    
HELIX   80  80 ASP D   73  THR D   85  1                                  13    
HELIX   81  81 GLY D  131  TYR D  135  5                                   5    
HELIX   82  82 GLY D  137  ASN D  145  1                                   9    
HELIX   83  83 LEU D  155  PHE D  161  1                                   7    
HELIX   84  84 ASN D  171  ILE D  188  1                                  18    
HELIX   85  85 ALA D  189  PHE D  191  5                                   3    
HELIX   86  86 SER D  204  SER D  216  1                                  13    
HELIX   87  87 PRO D  217  LYS D  220  5                                   4    
HELIX   88  88 PHE D  234  GLY D  237  5                                   4    
HELIX   89  89 MET D  243  GLY D  255  1                                  13    
HELIX   90  90 THR D  260  LYS D  271  1                                  12    
HELIX   91  91 SER D  272  LYS D  284  1                                  13    
HELIX   92  92 ASP D  293  SER D  297  5                                   5    
HELIX   93  93 MET D  313  LYS D  321  1                                   9    
HELIX   94  94 TRP D  339  MET D  345  1                                   7    
HELIX   95  95 ASP D  355  SER D  366  1                                  12    
HELIX   96  96 SER D  366  ASN D  371  1                                   6    
HELIX   97  97 PRO D  373  GLU D  375  5                                   3    
HELIX   98  98 LEU D  376  GLY D  386  1                                  11    
HELIX   99  99 ASP D  390  PHE D  407  1                                  18    
HELIX  100 100 PHE D  407  ALA D  421  1                                  15    
HELIX  101 101 GLY D  450  PHE D  457  1                                   8    
HELIX  102 102 GLY D  458  LEU D  462  5                                   5    
HELIX  103 103 PRO D  467  GLY D  488  1                                  22    
HELIX  104 104 LYS D  521  LEU D  532  1                                  12    
HELIX  105 105 LEU E   43  ARG E   47  5                                   5    
HELIX  106 106 ASP E   73  THR E   85  1                                  13    
HELIX  107 107 GLY E  131  TYR E  135  5                                   5    
HELIX  108 108 GLY E  137  ASN E  145  1                                   9    
HELIX  109 109 LEU E  155  PHE E  161  1                                   7    
HELIX  110 110 ASN E  171  ILE E  188  1                                  18    
HELIX  111 111 ALA E  189  PHE E  191  5                                   3    
HELIX  112 112 SER E  204  SER E  216  1                                  13    
HELIX  113 113 PRO E  217  LYS E  220  5                                   4    
HELIX  114 114 PHE E  234  GLY E  237  5                                   4    
HELIX  115 115 MET E  243  GLY E  255  1                                  13    
HELIX  116 116 THR E  260  LYS E  271  1                                  12    
HELIX  117 117 SER E  272  LYS E  284  1                                  13    
HELIX  118 118 ASP E  293  SER E  297  5                                   5    
HELIX  119 119 MET E  313  LYS E  321  1                                   9    
HELIX  120 120 TRP E  339  MET E  345  1                                   7    
HELIX  121 121 ASP E  355  SER E  366  1                                  12    
HELIX  122 122 SER E  366  ASN E  371  1                                   6    
HELIX  123 123 PRO E  373  GLU E  375  5                                   3    
HELIX  124 124 LEU E  376  GLY E  386  1                                  11    
HELIX  125 125 ASP E  390  PHE E  407  1                                  18    
HELIX  126 126 PHE E  407  ALA E  421  1                                  15    
HELIX  127 127 GLY E  450  PHE E  457  1                                   8    
HELIX  128 128 GLY E  458  LEU E  462  5                                   5    
HELIX  129 129 PRO E  467  GLY E  488  1                                  22    
HELIX  130 130 LYS E  521  LEU E  532  1                                  12    
HELIX  131 131 LEU F   43  ARG F   47  5                                   5    
HELIX  132 132 ASP F   73  THR F   85  1                                  13    
HELIX  133 133 GLY F  131  TYR F  135  5                                   5    
HELIX  134 134 GLY F  137  ASN F  145  1                                   9    
HELIX  135 135 LEU F  155  PHE F  161  1                                   7    
HELIX  136 136 ASN F  171  ILE F  188  1                                  18    
HELIX  137 137 ALA F  189  PHE F  191  5                                   3    
HELIX  138 138 SER F  204  SER F  216  1                                  13    
HELIX  139 139 PRO F  217  LYS F  220  5                                   4    
HELIX  140 140 PHE F  234  GLY F  237  5                                   4    
HELIX  141 141 MET F  243  GLY F  255  1                                  13    
HELIX  142 142 THR F  260  LYS F  271  1                                  12    
HELIX  143 143 SER F  272  LYS F  284  1                                  13    
HELIX  144 144 ASP F  293  SER F  297  5                                   5    
HELIX  145 145 MET F  313  LYS F  321  1                                   9    
HELIX  146 146 TRP F  339  MET F  345  1                                   7    
HELIX  147 147 ASP F  355  SER F  366  1                                  12    
HELIX  148 148 SER F  366  ASN F  371  1                                   6    
HELIX  149 149 PRO F  373  GLU F  375  5                                   3    
HELIX  150 150 LEU F  376  GLY F  386  1                                  11    
HELIX  151 151 ASP F  390  PHE F  407  1                                  18    
HELIX  152 152 PHE F  407  ALA F  421  1                                  15    
HELIX  153 153 GLY F  450  PHE F  457  1                                   8    
HELIX  154 154 GLY F  458  ARG F  463  1                                   6    
HELIX  155 155 PRO F  467  GLY F  488  1                                  22    
HELIX  156 156 LYS F  521  LEU F  532  1                                  12    
SHEET    1  AA 3 VAL A   8  VAL A   9  0                                        
SHEET    2  AA 3 ARG A  15  LEU A  17 -1  O  VAL A  16   N  VAL A   9           
SHEET    3  AA 3 VAL A  60  ASN A  62  1  O  LYS A  61   N  LEU A  17           
SHEET    1  AB11 LYS A  19  SER A  22  0                                        
SHEET    2  AB11 PRO A  29  PRO A  37 -1  O  VAL A  30   N  VAL A  21           
SHEET    3  AB11 TYR A 101  THR A 106 -1  O  LEU A 102   N  VAL A  36           
SHEET    4  AB11 VAL A 147  ILE A 151 -1  O  VAL A 148   N  TYR A 105           
SHEET    5  AB11 LEU A 116  ILE A 122  1  O  PRO A 117   N  VAL A 147           
SHEET    6  AB11 GLY A 193  GLU A 203  1  N  ASP A 194   O  LEU A 116           
SHEET    7  AB11 ARG A 225  GLU A 229  1  O  ARG A 225   N  ILE A 200           
SHEET    8  AB11 TYR A 328  ASN A 333  1  O  ILE A 329   N  SER A 228           
SHEET    9  AB11 THR A 425  GLN A 431  1  O  TYR A 426   N  VAL A 330           
SHEET   10  AB11 GLY A 506  GLY A 511  1  O  LEU A 508   N  GLU A 429           
SHEET   11  AB11 GLN A 515  LYS A 518 -1  O  GLN A 515   N  GLN A 509           
SHEET    1  AC 2 MET A  69  CYS A  70  0                                        
SHEET    2  AC 2 PHE A  95  SER A  96  1  N  SER A  96   O  MET A  69           
SHEET    1  AD 2 VAL A 239  ARG A 240  0                                        
SHEET    2  AD 2 THR A 303  VAL A 304  1  O  THR A 303   N  ARG A 240           
SHEET    1  BA 3 VAL B   8  VAL B   9  0                                        
SHEET    2  BA 3 ARG B  15  LEU B  17 -1  O  VAL B  16   N  VAL B   9           
SHEET    3  BA 3 VAL B  60  ASN B  62  1  O  LYS B  61   N  LEU B  17           
SHEET    1  BB11 LYS B  19  SER B  22  0                                        
SHEET    2  BB11 PRO B  29  PRO B  37 -1  O  VAL B  30   N  VAL B  21           
SHEET    3  BB11 TYR B 101  THR B 106 -1  O  LEU B 102   N  VAL B  36           
SHEET    4  BB11 VAL B 147  ILE B 151 -1  O  VAL B 148   N  TYR B 105           
SHEET    5  BB11 LEU B 116  ILE B 122  1  O  PRO B 117   N  VAL B 147           
SHEET    6  BB11 GLY B 193  GLU B 203  1  N  ASP B 194   O  LEU B 116           
SHEET    7  BB11 ARG B 225  GLU B 229  1  O  ARG B 225   N  ILE B 200           
SHEET    8  BB11 TYR B 328  ASN B 333  1  O  ILE B 329   N  SER B 228           
SHEET    9  BB11 THR B 425  GLN B 431  1  O  TYR B 426   N  VAL B 330           
SHEET   10  BB11 GLY B 506  GLY B 511  1  O  LEU B 508   N  GLU B 429           
SHEET   11  BB11 GLN B 515  LYS B 518 -1  O  GLN B 515   N  GLN B 509           
SHEET    1  BC 2 MET B  69  CYS B  70  0                                        
SHEET    2  BC 2 PHE B  95  SER B  96  1  N  SER B  96   O  MET B  69           
SHEET    1  BD 2 VAL B 239  ARG B 240  0                                        
SHEET    2  BD 2 THR B 303  VAL B 304  1  O  THR B 303   N  ARG B 240           
SHEET    1  CA 3 VAL C   8  VAL C   9  0                                        
SHEET    2  CA 3 ARG C  15  LEU C  17 -1  O  VAL C  16   N  VAL C   9           
SHEET    3  CA 3 VAL C  60  ASN C  62  1  O  LYS C  61   N  LEU C  17           
SHEET    1  CB11 LYS C  19  SER C  22  0                                        
SHEET    2  CB11 PRO C  29  PRO C  37 -1  O  VAL C  30   N  VAL C  21           
SHEET    3  CB11 TYR C 101  THR C 106 -1  O  LEU C 102   N  VAL C  36           
SHEET    4  CB11 VAL C 147  ILE C 151 -1  O  VAL C 148   N  TYR C 105           
SHEET    5  CB11 LEU C 116  ILE C 122  1  O  PRO C 117   N  VAL C 147           
SHEET    6  CB11 GLY C 193  GLU C 203  1  N  ASP C 194   O  LEU C 116           
SHEET    7  CB11 ARG C 225  GLU C 229  1  O  ARG C 225   N  ILE C 200           
SHEET    8  CB11 TYR C 328  ASN C 333  1  O  ILE C 329   N  SER C 228           
SHEET    9  CB11 THR C 425  GLN C 431  1  O  TYR C 426   N  VAL C 330           
SHEET   10  CB11 GLY C 506  GLY C 511  1  O  LEU C 508   N  GLU C 429           
SHEET   11  CB11 GLN C 515  LYS C 518 -1  O  GLN C 515   N  GLN C 509           
SHEET    1  CC 2 MET C  69  CYS C  70  0                                        
SHEET    2  CC 2 PHE C  95  SER C  96  1  N  SER C  96   O  MET C  69           
SHEET    1  CD 2 VAL C 239  ARG C 240  0                                        
SHEET    2  CD 2 THR C 303  VAL C 304  1  O  THR C 303   N  ARG C 240           
SHEET    1  DA 3 VAL D   8  VAL D   9  0                                        
SHEET    2  DA 3 ARG D  15  LEU D  17 -1  O  VAL D  16   N  VAL D   9           
SHEET    3  DA 3 VAL D  60  ASN D  62  1  O  LYS D  61   N  LEU D  17           
SHEET    1  DB11 LYS D  19  SER D  22  0                                        
SHEET    2  DB11 PRO D  29  PRO D  37 -1  O  VAL D  30   N  VAL D  21           
SHEET    3  DB11 TYR D 101  THR D 106 -1  O  LEU D 102   N  VAL D  36           
SHEET    4  DB11 VAL D 147  ILE D 151 -1  O  VAL D 148   N  TYR D 105           
SHEET    5  DB11 LEU D 116  ILE D 122  1  O  PRO D 117   N  VAL D 147           
SHEET    6  DB11 GLY D 193  GLU D 203  1  N  ASP D 194   O  LEU D 116           
SHEET    7  DB11 ARG D 225  GLU D 229  1  O  ARG D 225   N  ILE D 200           
SHEET    8  DB11 TYR D 328  ASN D 333  1  O  ILE D 329   N  SER D 228           
SHEET    9  DB11 THR D 425  GLN D 431  1  O  TYR D 426   N  VAL D 330           
SHEET   10  DB11 GLY D 506  GLY D 511  1  O  LEU D 508   N  GLU D 429           
SHEET   11  DB11 GLN D 515  LYS D 518 -1  O  GLN D 515   N  GLN D 509           
SHEET    1  DC 2 MET D  69  CYS D  70  0                                        
SHEET    2  DC 2 PHE D  95  SER D  96  1  N  SER D  96   O  MET D  69           
SHEET    1  DD 2 VAL D 239  ARG D 240  0                                        
SHEET    2  DD 2 THR D 303  VAL D 304  1  O  THR D 303   N  ARG D 240           
SHEET    1  EA 3 VAL E   8  VAL E   9  0                                        
SHEET    2  EA 3 ARG E  15  LEU E  17 -1  O  VAL E  16   N  VAL E   9           
SHEET    3  EA 3 VAL E  60  ASN E  62  1  O  LYS E  61   N  LEU E  17           
SHEET    1  EB11 LYS E  19  SER E  22  0                                        
SHEET    2  EB11 PRO E  29  PRO E  37 -1  O  VAL E  30   N  VAL E  21           
SHEET    3  EB11 TYR E 101  THR E 106 -1  O  LEU E 102   N  VAL E  36           
SHEET    4  EB11 VAL E 147  ILE E 151 -1  O  VAL E 148   N  TYR E 105           
SHEET    5  EB11 LEU E 116  ILE E 122  1  O  PRO E 117   N  VAL E 147           
SHEET    6  EB11 GLY E 193  GLU E 203  1  N  ASP E 194   O  LEU E 116           
SHEET    7  EB11 ARG E 225  GLU E 229  1  O  ARG E 225   N  ILE E 200           
SHEET    8  EB11 TYR E 328  ASN E 333  1  O  ILE E 329   N  SER E 228           
SHEET    9  EB11 THR E 425  GLN E 431  1  O  TYR E 426   N  VAL E 330           
SHEET   10  EB11 GLY E 506  GLY E 511  1  O  LEU E 508   N  GLU E 429           
SHEET   11  EB11 GLN E 515  LYS E 518 -1  O  GLN E 515   N  GLN E 509           
SHEET    1  EC 2 MET E  69  CYS E  70  0                                        
SHEET    2  EC 2 PHE E  95  SER E  96  1  N  SER E  96   O  MET E  69           
SHEET    1  ED 2 VAL E 239  ARG E 240  0                                        
SHEET    2  ED 2 THR E 303  VAL E 304  1  O  THR E 303   N  ARG E 240           
SHEET    1  FA 3 VAL F   8  VAL F   9  0                                        
SHEET    2  FA 3 ARG F  15  LEU F  17 -1  O  VAL F  16   N  VAL F   9           
SHEET    3  FA 3 VAL F  60  ASN F  62  1  O  LYS F  61   N  LEU F  17           
SHEET    1  FB11 LYS F  19  SER F  22  0                                        
SHEET    2  FB11 PRO F  29  PRO F  37 -1  O  VAL F  30   N  VAL F  21           
SHEET    3  FB11 TYR F 101  THR F 106 -1  O  LEU F 102   N  VAL F  36           
SHEET    4  FB11 VAL F 147  ILE F 151 -1  O  VAL F 148   N  TYR F 105           
SHEET    5  FB11 LEU F 116  ILE F 122  1  O  PRO F 117   N  VAL F 147           
SHEET    6  FB11 GLY F 193  GLU F 203  1  N  ASP F 194   O  LEU F 116           
SHEET    7  FB11 ARG F 225  GLU F 229  1  O  ARG F 225   N  ILE F 200           
SHEET    8  FB11 TYR F 328  ASN F 333  1  O  ILE F 329   N  SER F 228           
SHEET    9  FB11 THR F 425  GLN F 431  1  O  TYR F 426   N  VAL F 330           
SHEET   10  FB11 GLY F 506  GLY F 511  1  O  LEU F 508   N  GLU F 429           
SHEET   11  FB11 GLN F 515  LYS F 518 -1  O  GLN F 515   N  GLN F 509           
SHEET    1  FC 2 MET F  69  CYS F  70  0                                        
SHEET    2  FC 2 PHE F  95  SER F  96  1  N  SER F  96   O  MET F  69           
SHEET    1  FD 2 VAL F 239  ARG F 240  0                                        
SHEET    2  FD 2 THR F 303  VAL F 304  1  O  THR F 303   N  ARG F 240           
SSBOND   1 CYS A   70    CYS A   99                          1555   1555  1.99  
SSBOND   2 CYS A  256    CYS A  267                          1555   1555  2.17  
SSBOND   3 CYS B   70    CYS B   99                          1555   1555  1.98  
SSBOND   4 CYS B  256    CYS B  267                          1555   1555  2.13  
SSBOND   5 CYS C   70    CYS C   99                          1555   1555  1.99  
SSBOND   6 CYS C  256    CYS C  267                          1555   1555  2.15  
SSBOND   7 CYS D   70    CYS D   99                          1555   1555  1.99  
SSBOND   8 CYS D  256    CYS D  267                          1555   1555  2.18  
SSBOND   9 CYS E   70    CYS E   99                          1555   1555  1.99  
SSBOND  10 CYS E  256    CYS E  267                          1555   1555  2.14  
SSBOND  11 CYS F   70    CYS F   99                          1555   1555  1.98  
SSBOND  12 CYS F  256    CYS F  267                          1555   1555  2.19  
CRYST1   92.860  188.020  109.500  90.00  96.44  90.00 P 1 21 1     12          
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      0.010769  0.000000  0.001216        0.00000                         
SCALE2      0.000000  0.005319  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009190        0.00000                         
MTRIX1   1 -0.974020 -0.222240  0.043530        9.26110    1                    
MTRIX2   1 -0.226290  0.947660 -0.225250       41.37080    1                    
MTRIX3   1  0.008810 -0.229250 -0.973330      197.43523    1                    
MTRIX1   2 -0.970090 -0.242510  0.010780       11.23982    1                    
MTRIX2   2  0.106610 -0.465500 -0.878610      261.74030    1                    
MTRIX3   2  0.218090 -0.851180  0.477420      140.72946    1                    
MTRIX1   3 -0.999360  0.008690  0.034720      -37.88942    1                    
MTRIX2   3  0.030940 -0.278090  0.960060       64.84949    1                    
MTRIX3   3  0.018000  0.960520  0.277640      -59.24981    1                    
MTRIX1   4  0.982740  0.084070 -0.164760       17.75239    1                    
MTRIX2   4 -0.060960 -0.693790 -0.717590      275.16031    1                    
MTRIX3   4 -0.174630  0.715250 -0.676690       70.20776    1                    
MTRIX1   5  0.972270  0.038490 -0.230660       39.43866    1                    
MTRIX2   5  0.217440 -0.511760  0.831160      119.08277    1                    
MTRIX3   5 -0.086050 -0.858270 -0.505940      240.81943    1                    
TER    4096      LYS A 534                                                      
TER    8192      LYS B 534                                                      
TER   12288      LYS C 534                                                      
TER   16384      LYS D 534                                                      
TER   20480      LYS E 534                                                      
TER   24576      LYS F 534                                                      
MASTER      609    0    0  156  108    0    0   2125087    6   24  252          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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