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LongText Report for: 5l8s-pdb

Name Class
5l8s-pdb
HEADER    HYDROLASE                               08-JUN-16   5L8S              
TITLE     THE CRYSTAL STRUCTURE OF A COLD-ADAPTED ACYLAMINOACYL PEPTIDASE       
TITLE    2 REVEALS A NOVEL QUATERNARY ARCHITECTURE BASED ON THE ARM-EXCHANGE    
TITLE    3 MECHANISM                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AMINO ACYL PEPTIDASE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: PEPTIDASE S9;                                               
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SPOROSARCINA PSYCHROPHILA;                      
SOURCE   3 ORGANISM_TAXID: 1476;                                                
SOURCE   4 GENE: APH, AZE41_09720;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ACYL AMINOACYL PEPTIDASE, ALPHA/BETA HYDROLASE DOMAIN, ARM EXCHANGE,  
KEYWDS   2 BETA-PROPELLER DOMAIN, COLD ADAPTATION, DIMERIZATION, PROLINE HINGE, 
KEYWDS   3 SPOROSARCINA PSYCHROPHILA, HYDROLASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BROCCA,C.FERRARI,A.BARBIROLI,A.PESCE,M.LOTTI,M.NARDINI              
REVDAT   1   16-NOV-16 5L8S    0                                                
JRNL        AUTH   S.BROCCA,C.FERRARI,A.BARBIROLI,A.PESCE,M.LOTTI,M.NARDINI     
JRNL        TITL   A BACTERIAL ACYL AMINOACYL PEPTIDASE COUPLES FLEXIBILITY AND 
JRNL        TITL 2 STABILITY AS A RESULT OF COLD ADAPTATION.                    
JRNL        REF    FEBS J.                                    2016              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   27739253                                                     
JRNL        DOI    10.1111/FEBS.13925                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 140806                         
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) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7433                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10301                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 545                          
REMARK   3   BIN FREE R VALUE                    : 0.3680                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19524                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 476                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.37000                                              
REMARK   3    B22 (A**2) : 0.36000                                              
REMARK   3    B33 (A**2) : -0.73000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.311         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.238         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.174         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.858         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 20113 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 18451 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 27265 ; 1.282 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 42610 ; 0.727 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2426 ; 6.175 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1027 ;35.123 ;24.430       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3358 ;15.325 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    96 ;15.653 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2871 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 22893 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  4783 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  9674 ; 2.282 ; 4.219       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  9673 ; 2.280 ; 4.219       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12089 ; 3.658 ; 6.323       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 12090 ; 3.659 ; 6.323       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 10439 ; 2.702 ; 4.555       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 10436 ; 2.689 ; 4.555       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 15164 ; 4.415 ; 6.685       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 22014 ; 6.374 ;33.424       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 21975 ; 6.365 ;33.419       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5L8S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000331.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-12                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93929                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 148344                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.500                              
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: 1VE6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 400, 0.1 M NA-HEPES (PH 7.5),    
REMARK 280  AND 0.2 M MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       74.04000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       95.61500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.55000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       95.61500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       74.04000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.55000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 45900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LYS D   518     OH   TYR D   524              2.11            
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    ASN A  20      143.83   -179.63                                   
REMARK 500    ARG A  58      -28.65   -157.22                                   
REMARK 500    ASP A  79     -163.61   -111.45                                   
REMARK 500    ASP A  83      -53.58    -27.43                                   
REMARK 500    LEU A 101      -61.34   -123.87                                   
REMARK 500    LYS A 128      -70.06    -43.44                                   
REMARK 500    ASN A 130       74.44   -151.96                                   
REMARK 500    LEU A 134      141.53     75.26                                   
REMARK 500    VAL A 154      -61.36     74.15                                   
REMARK 500    MET A 186      -67.01   -130.67                                   
REMARK 500    ASP A 280       42.65     36.07                                   
REMARK 500    SER A 383     -153.68   -130.91                                   
REMARK 500    ASP A 425       54.44   -155.82                                   
REMARK 500    GLU A 428      -85.21   -105.08                                   
REMARK 500    SER A 458     -122.13     62.69                                   
REMARK 500    HIS A 471       33.95   -142.26                                   
REMARK 500    PHE A 482       67.15     27.54                                   
REMARK 500    LEU A 506      -60.72   -107.58                                   
REMARK 500    HIS A 603       93.87    -68.88                                   
REMARK 500    ARG B  58      -35.86   -139.23                                   
REMARK 500    ASP B  79     -156.29   -119.31                                   
REMARK 500    ASP B  81       65.57     35.66                                   
REMARK 500    GLU B  84       -9.76     66.48                                   
REMARK 500    SER B 113      -53.00   -121.72                                   
REMARK 500    LEU B 134      147.85     73.41                                   
REMARK 500    VAL B 154      -47.28     80.39                                   
REMARK 500    MET B 186      -50.62   -120.44                                   
REMARK 500    SER B 383     -157.43   -132.88                                   
REMARK 500    ASP B 425       59.26   -163.16                                   
REMARK 500    GLU B 428      -79.11   -130.44                                   
REMARK 500    ASN B 450       -0.33     70.50                                   
REMARK 500    SER B 458     -119.93     65.78                                   
REMARK 500    HIS B 471       40.73   -146.10                                   
REMARK 500    PHE B 482       61.95     37.32                                   
REMARK 500    ARG C  58      -27.41   -158.25                                   
REMARK 500    ASP C  79     -161.51   -110.56                                   
REMARK 500    LEU C 134      152.99     76.82                                   
REMARK 500    VAL C 154      -61.08     67.53                                   
REMARK 500    LYS C 258       53.79     35.23                                   
REMARK 500    ASN C 321       17.82   -156.33                                   
REMARK 500    ASP C 369      116.82    -35.55                                   
REMARK 500    ASP C 425       70.81   -156.66                                   
REMARK 500    GLU C 428      -85.31   -128.41                                   
REMARK 500    SER C 458     -126.72     61.53                                   
REMARK 500    HIS C 471       35.70   -149.00                                   
REMARK 500    PHE C 482       64.05     30.83                                   
REMARK 500    ARG D  58      -25.03   -158.39                                   
REMARK 500    ASP D  79     -166.14   -108.79                                   
REMARK 500    LYS D 128      -71.86    -37.18                                   
REMARK 500    ASN D 130       71.12   -157.05                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 975        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH A 976        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A 977        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH B 907        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH C 905        DISTANCE =  7.36 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 701                 
DBREF  5L8S A    1   596  UNP    E1VFE0   E1VFE0_SPOPS     1    596             
DBREF  5L8S B    1   596  UNP    E1VFE0   E1VFE0_SPOPS     1    596             
DBREF  5L8S C    1   596  UNP    E1VFE0   E1VFE0_SPOPS     1    596             
DBREF  5L8S D    1   596  UNP    E1VFE0   E1VFE0_SPOPS     1    596             
SEQADV 5L8S LEU A  597  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S GLU A  598  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS A  599  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS A  600  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS A  601  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS A  602  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS A  603  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS A  604  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S LEU B  597  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S GLU B  598  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS B  599  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS B  600  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS B  601  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS B  602  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS B  603  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS B  604  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S LEU C  597  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S GLU C  598  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS C  599  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS C  600  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS C  601  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS C  602  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS C  603  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS C  604  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S LEU D  597  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S GLU D  598  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS D  599  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS D  600  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS D  601  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS D  602  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS D  603  UNP  E1VFE0              EXPRESSION TAG                 
SEQADV 5L8S HIS D  604  UNP  E1VFE0              EXPRESSION TAG                 
SEQRES   1 A  604  MET ILE ASN PHE PRO LYS PRO THR VAL GLU GLN PHE PHE          
SEQRES   2 A  604  ARG THR TYR THR ILE THR ASN PHE ALA VAL SER SER ASP          
SEQRES   3 A  604  GLU LYS ARG LEU VAL PHE ASN ALA ASN LEU ASN GLY LYS          
SEQRES   4 A  604  MET ASN LEU TRP ALA MET ASP LEU PRO ASP THR TYR PRO          
SEQRES   5 A  604  TYR LEU PHE ALA HIS ARG ASP GLU SER CYS ASN PHE ILE          
SEQRES   6 A  604  LYS PHE ASP PRO GLU ASN ARG TYR VAL LEU ALA GLY PHE          
SEQRES   7 A  604  ASP LYS ASP GLY ASP GLU ASN TYR GLN ILE TYR ALA ILE          
SEQRES   8 A  604  PRO ASN GLU GLY GLY LEU PRO HIS PRO LEU ILE THR GLY          
SEQRES   9 A  604  ASP ALA SER GLU LYS TYR TYR PHE SER HIS LEU SER ALA          
SEQRES  10 A  604  ASP GLY LYS CYS VAL TYR TYR GLU THR SER LYS GLU ASN          
SEQRES  11 A  604  PRO SER PHE LEU ASN THR ARG ILE ARG ASN LEU GLU THR          
SEQRES  12 A  604  GLY GLU ASP ARG LEU LEU ASN VAL GLY GLU VAL SER THR          
SEQRES  13 A  604  THR GLU LEU ALA ALA VAL SER GLU ASN GLU GLU SER PHE          
SEQRES  14 A  604  VAL TYR LEU ARG ALA PHE ALA ASN THR TYR ILE VAL GLY          
SEQRES  15 A  604  PHE VAL LYS MET GLY GLU GLU THR PHE ASN ILE THR PRO          
SEQRES  16 A  604  ASP PRO GLU LYS VAL HIS VAL ALA MET GLU PRO VAL PHE          
SEQRES  17 A  604  THR ASP ASN GLU THR ILE TYR PHE ALA THR ASP TYR ASP          
SEQRES  18 A  604  SER ASP GLU MET TYR LEU ALA LYS PHE ASP LEU THR SER          
SEQRES  19 A  604  LYS GLU PHE SER LYS VAL LEU ALA PHE ASP GLY GLU SER          
SEQRES  20 A  604  ILE GLN SER VAL LYS TRP ASP LYS ASP ASN LYS ALA PHE          
SEQRES  21 A  604  TYR LEU ILE THR VAL LYS GLY VAL THR ASP ILE LEU TYR          
SEQRES  22 A  604  ARG TYR ASP VAL ALA THR ASP LYS VAL GLU GLU CYS SER          
SEQRES  23 A  604  LEU PRO VAL ASP ILE ILE GLU GLN ILE GLN VAL ALA LYS          
SEQRES  24 A  604  SER GLY ASN LEU TYR ILE LEU GLY ARG SER ALA THR VAL          
SEQRES  25 A  604  PRO HIS ASN VAL TYR GLN SER SER ASN GLY VAL GLU TRP          
SEQRES  26 A  604  LYS GLN LEU THR ASN ASN ARG VAL LEU GLY LEU SER PRO          
SEQRES  27 A  604  GLU ASP MET VAL GLU PRO ASP ILE VAL SER TYR THR SER          
SEQRES  28 A  604  PHE ASP GLY MET GLU ILE GLU ALA LEU LEU PHE LYS ALA          
SEQRES  29 A  604  LYS PRO GLU ASN ASP ASN GLY TYR THR ILE PHE TRP PRO          
SEQRES  30 A  604  HIS GLY GLY PRO GLN SER ALA GLU ARG LYS MET PHE ARG          
SEQRES  31 A  604  SER MET PHE GLN CYS PHE ILE ASN ARG GLY TYR THR ILE          
SEQRES  32 A  604  PHE ALA PRO ASN PHE ARG GLY SER THR GLY TYR GLY SER          
SEQRES  33 A  604  ALA PHE THR LYS LEU VAL GLU LEU ASP TRP GLY GLU GLY          
SEQRES  34 A  604  PRO ARG LEU ASP CYS ILE ALA GLY ILE GLU TRP LEU PHE          
SEQRES  35 A  604  GLU SER GLY PHE THR ASP ARG ASN LYS LEU PHE LEU VAL          
SEQRES  36 A  604  GLY GLY SER TYR GLY GLY TYR MET ALA LEU LEU LEU HIS          
SEQRES  37 A  604  GLY ARG HIS SER ASP TYR PHE ARG ALA VAL VAL ASP ILE          
SEQRES  38 A  604  PHE GLY PRO SER ASP LEU PHE THR PHE ILE ASN SER VAL          
SEQRES  39 A  604  PRO PRO HIS TRP LYS PRO ILE MET GLU ARG TRP LEU GLY          
SEQRES  40 A  604  ASP PRO GLU ARG ASP LYS GLU ARG PHE ILE LYS ASP SER          
SEQRES  41 A  604  PRO VAL THR TYR LEU ASP GLY MET VAL LYS PRO MET LEU          
SEQRES  42 A  604  VAL ILE GLN GLY ALA LYS ASP PRO ARG VAL VAL LYS GLU          
SEQRES  43 A  604  GLU SER ASP GLN ILE VAL ALA LYS LEU LYS GLU LYS GLY          
SEQRES  44 A  604  ARG ASP VAL GLU TYR LEU VAL LEU GLU ASP GLU GLY HIS          
SEQRES  45 A  604  GLY PHE SER LYS LYS GLU ASN GLU ILE LYS VAL TYR SER          
SEQRES  46 A  604  LEU MET LEU ALA PHE LEU GLU LYS HIS GLN ALA LEU GLU          
SEQRES  47 A  604  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  604  MET ILE ASN PHE PRO LYS PRO THR VAL GLU GLN PHE PHE          
SEQRES   2 B  604  ARG THR TYR THR ILE THR ASN PHE ALA VAL SER SER ASP          
SEQRES   3 B  604  GLU LYS ARG LEU VAL PHE ASN ALA ASN LEU ASN GLY LYS          
SEQRES   4 B  604  MET ASN LEU TRP ALA MET ASP LEU PRO ASP THR TYR PRO          
SEQRES   5 B  604  TYR LEU PHE ALA HIS ARG ASP GLU SER CYS ASN PHE ILE          
SEQRES   6 B  604  LYS PHE ASP PRO GLU ASN ARG TYR VAL LEU ALA GLY PHE          
SEQRES   7 B  604  ASP LYS ASP GLY ASP GLU ASN TYR GLN ILE TYR ALA ILE          
SEQRES   8 B  604  PRO ASN GLU GLY GLY LEU PRO HIS PRO LEU ILE THR GLY          
SEQRES   9 B  604  ASP ALA SER GLU LYS TYR TYR PHE SER HIS LEU SER ALA          
SEQRES  10 B  604  ASP GLY LYS CYS VAL TYR TYR GLU THR SER LYS GLU ASN          
SEQRES  11 B  604  PRO SER PHE LEU ASN THR ARG ILE ARG ASN LEU GLU THR          
SEQRES  12 B  604  GLY GLU ASP ARG LEU LEU ASN VAL GLY GLU VAL SER THR          
SEQRES  13 B  604  THR GLU LEU ALA ALA VAL SER GLU ASN GLU GLU SER PHE          
SEQRES  14 B  604  VAL TYR LEU ARG ALA PHE ALA ASN THR TYR ILE VAL GLY          
SEQRES  15 B  604  PHE VAL LYS MET GLY GLU GLU THR PHE ASN ILE THR PRO          
SEQRES  16 B  604  ASP PRO GLU LYS VAL HIS VAL ALA MET GLU PRO VAL PHE          
SEQRES  17 B  604  THR ASP ASN GLU THR ILE TYR PHE ALA THR ASP TYR ASP          
SEQRES  18 B  604  SER ASP GLU MET TYR LEU ALA LYS PHE ASP LEU THR SER          
SEQRES  19 B  604  LYS GLU PHE SER LYS VAL LEU ALA PHE ASP GLY GLU SER          
SEQRES  20 B  604  ILE GLN SER VAL LYS TRP ASP LYS ASP ASN LYS ALA PHE          
SEQRES  21 B  604  TYR LEU ILE THR VAL LYS GLY VAL THR ASP ILE LEU TYR          
SEQRES  22 B  604  ARG TYR ASP VAL ALA THR ASP LYS VAL GLU GLU CYS SER          
SEQRES  23 B  604  LEU PRO VAL ASP ILE ILE GLU GLN ILE GLN VAL ALA LYS          
SEQRES  24 B  604  SER GLY ASN LEU TYR ILE LEU GLY ARG SER ALA THR VAL          
SEQRES  25 B  604  PRO HIS ASN VAL TYR GLN SER SER ASN GLY VAL GLU TRP          
SEQRES  26 B  604  LYS GLN LEU THR ASN ASN ARG VAL LEU GLY LEU SER PRO          
SEQRES  27 B  604  GLU ASP MET VAL GLU PRO ASP ILE VAL SER TYR THR SER          
SEQRES  28 B  604  PHE ASP GLY MET GLU ILE GLU ALA LEU LEU PHE LYS ALA          
SEQRES  29 B  604  LYS PRO GLU ASN ASP ASN GLY TYR THR ILE PHE TRP PRO          
SEQRES  30 B  604  HIS GLY GLY PRO GLN SER ALA GLU ARG LYS MET PHE ARG          
SEQRES  31 B  604  SER MET PHE GLN CYS PHE ILE ASN ARG GLY TYR THR ILE          
SEQRES  32 B  604  PHE ALA PRO ASN PHE ARG GLY SER THR GLY TYR GLY SER          
SEQRES  33 B  604  ALA PHE THR LYS LEU VAL GLU LEU ASP TRP GLY GLU GLY          
SEQRES  34 B  604  PRO ARG LEU ASP CYS ILE ALA GLY ILE GLU TRP LEU PHE          
SEQRES  35 B  604  GLU SER GLY PHE THR ASP ARG ASN LYS LEU PHE LEU VAL          
SEQRES  36 B  604  GLY GLY SER TYR GLY GLY TYR MET ALA LEU LEU LEU HIS          
SEQRES  37 B  604  GLY ARG HIS SER ASP TYR PHE ARG ALA VAL VAL ASP ILE          
SEQRES  38 B  604  PHE GLY PRO SER ASP LEU PHE THR PHE ILE ASN SER VAL          
SEQRES  39 B  604  PRO PRO HIS TRP LYS PRO ILE MET GLU ARG TRP LEU GLY          
SEQRES  40 B  604  ASP PRO GLU ARG ASP LYS GLU ARG PHE ILE LYS ASP SER          
SEQRES  41 B  604  PRO VAL THR TYR LEU ASP GLY MET VAL LYS PRO MET LEU          
SEQRES  42 B  604  VAL ILE GLN GLY ALA LYS ASP PRO ARG VAL VAL LYS GLU          
SEQRES  43 B  604  GLU SER ASP GLN ILE VAL ALA LYS LEU LYS GLU LYS GLY          
SEQRES  44 B  604  ARG ASP VAL GLU TYR LEU VAL LEU GLU ASP GLU GLY HIS          
SEQRES  45 B  604  GLY PHE SER LYS LYS GLU ASN GLU ILE LYS VAL TYR SER          
SEQRES  46 B  604  LEU MET LEU ALA PHE LEU GLU LYS HIS GLN ALA LEU GLU          
SEQRES  47 B  604  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 C  604  MET ILE ASN PHE PRO LYS PRO THR VAL GLU GLN PHE PHE          
SEQRES   2 C  604  ARG THR TYR THR ILE THR ASN PHE ALA VAL SER SER ASP          
SEQRES   3 C  604  GLU LYS ARG LEU VAL PHE ASN ALA ASN LEU ASN GLY LYS          
SEQRES   4 C  604  MET ASN LEU TRP ALA MET ASP LEU PRO ASP THR TYR PRO          
SEQRES   5 C  604  TYR LEU PHE ALA HIS ARG ASP GLU SER CYS ASN PHE ILE          
SEQRES   6 C  604  LYS PHE ASP PRO GLU ASN ARG TYR VAL LEU ALA GLY PHE          
SEQRES   7 C  604  ASP LYS ASP GLY ASP GLU ASN TYR GLN ILE TYR ALA ILE          
SEQRES   8 C  604  PRO ASN GLU GLY GLY LEU PRO HIS PRO LEU ILE THR GLY          
SEQRES   9 C  604  ASP ALA SER GLU LYS TYR TYR PHE SER HIS LEU SER ALA          
SEQRES  10 C  604  ASP GLY LYS CYS VAL TYR TYR GLU THR SER LYS GLU ASN          
SEQRES  11 C  604  PRO SER PHE LEU ASN THR ARG ILE ARG ASN LEU GLU THR          
SEQRES  12 C  604  GLY GLU ASP ARG LEU LEU ASN VAL GLY GLU VAL SER THR          
SEQRES  13 C  604  THR GLU LEU ALA ALA VAL SER GLU ASN GLU GLU SER PHE          
SEQRES  14 C  604  VAL TYR LEU ARG ALA PHE ALA ASN THR TYR ILE VAL GLY          
SEQRES  15 C  604  PHE VAL LYS MET GLY GLU GLU THR PHE ASN ILE THR PRO          
SEQRES  16 C  604  ASP PRO GLU LYS VAL HIS VAL ALA MET GLU PRO VAL PHE          
SEQRES  17 C  604  THR ASP ASN GLU THR ILE TYR PHE ALA THR ASP TYR ASP          
SEQRES  18 C  604  SER ASP GLU MET TYR LEU ALA LYS PHE ASP LEU THR SER          
SEQRES  19 C  604  LYS GLU PHE SER LYS VAL LEU ALA PHE ASP GLY GLU SER          
SEQRES  20 C  604  ILE GLN SER VAL LYS TRP ASP LYS ASP ASN LYS ALA PHE          
SEQRES  21 C  604  TYR LEU ILE THR VAL LYS GLY VAL THR ASP ILE LEU TYR          
SEQRES  22 C  604  ARG TYR ASP VAL ALA THR ASP LYS VAL GLU GLU CYS SER          
SEQRES  23 C  604  LEU PRO VAL ASP ILE ILE GLU GLN ILE GLN VAL ALA LYS          
SEQRES  24 C  604  SER GLY ASN LEU TYR ILE LEU GLY ARG SER ALA THR VAL          
SEQRES  25 C  604  PRO HIS ASN VAL TYR GLN SER SER ASN GLY VAL GLU TRP          
SEQRES  26 C  604  LYS GLN LEU THR ASN ASN ARG VAL LEU GLY LEU SER PRO          
SEQRES  27 C  604  GLU ASP MET VAL GLU PRO ASP ILE VAL SER TYR THR SER          
SEQRES  28 C  604  PHE ASP GLY MET GLU ILE GLU ALA LEU LEU PHE LYS ALA          
SEQRES  29 C  604  LYS PRO GLU ASN ASP ASN GLY TYR THR ILE PHE TRP PRO          
SEQRES  30 C  604  HIS GLY GLY PRO GLN SER ALA GLU ARG LYS MET PHE ARG          
SEQRES  31 C  604  SER MET PHE GLN CYS PHE ILE ASN ARG GLY TYR THR ILE          
SEQRES  32 C  604  PHE ALA PRO ASN PHE ARG GLY SER THR GLY TYR GLY SER          
SEQRES  33 C  604  ALA PHE THR LYS LEU VAL GLU LEU ASP TRP GLY GLU GLY          
SEQRES  34 C  604  PRO ARG LEU ASP CYS ILE ALA GLY ILE GLU TRP LEU PHE          
SEQRES  35 C  604  GLU SER GLY PHE THR ASP ARG ASN LYS LEU PHE LEU VAL          
SEQRES  36 C  604  GLY GLY SER TYR GLY GLY TYR MET ALA LEU LEU LEU HIS          
SEQRES  37 C  604  GLY ARG HIS SER ASP TYR PHE ARG ALA VAL VAL ASP ILE          
SEQRES  38 C  604  PHE GLY PRO SER ASP LEU PHE THR PHE ILE ASN SER VAL          
SEQRES  39 C  604  PRO PRO HIS TRP LYS PRO ILE MET GLU ARG TRP LEU GLY          
SEQRES  40 C  604  ASP PRO GLU ARG ASP LYS GLU ARG PHE ILE LYS ASP SER          
SEQRES  41 C  604  PRO VAL THR TYR LEU ASP GLY MET VAL LYS PRO MET LEU          
SEQRES  42 C  604  VAL ILE GLN GLY ALA LYS ASP PRO ARG VAL VAL LYS GLU          
SEQRES  43 C  604  GLU SER ASP GLN ILE VAL ALA LYS LEU LYS GLU LYS GLY          
SEQRES  44 C  604  ARG ASP VAL GLU TYR LEU VAL LEU GLU ASP GLU GLY HIS          
SEQRES  45 C  604  GLY PHE SER LYS LYS GLU ASN GLU ILE LYS VAL TYR SER          
SEQRES  46 C  604  LEU MET LEU ALA PHE LEU GLU LYS HIS GLN ALA LEU GLU          
SEQRES  47 C  604  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 D  604  MET ILE ASN PHE PRO LYS PRO THR VAL GLU GLN PHE PHE          
SEQRES   2 D  604  ARG THR TYR THR ILE THR ASN PHE ALA VAL SER SER ASP          
SEQRES   3 D  604  GLU LYS ARG LEU VAL PHE ASN ALA ASN LEU ASN GLY LYS          
SEQRES   4 D  604  MET ASN LEU TRP ALA MET ASP LEU PRO ASP THR TYR PRO          
SEQRES   5 D  604  TYR LEU PHE ALA HIS ARG ASP GLU SER CYS ASN PHE ILE          
SEQRES   6 D  604  LYS PHE ASP PRO GLU ASN ARG TYR VAL LEU ALA GLY PHE          
SEQRES   7 D  604  ASP LYS ASP GLY ASP GLU ASN TYR GLN ILE TYR ALA ILE          
SEQRES   8 D  604  PRO ASN GLU GLY GLY LEU PRO HIS PRO LEU ILE THR GLY          
SEQRES   9 D  604  ASP ALA SER GLU LYS TYR TYR PHE SER HIS LEU SER ALA          
SEQRES  10 D  604  ASP GLY LYS CYS VAL TYR TYR GLU THR SER LYS GLU ASN          
SEQRES  11 D  604  PRO SER PHE LEU ASN THR ARG ILE ARG ASN LEU GLU THR          
SEQRES  12 D  604  GLY GLU ASP ARG LEU LEU ASN VAL GLY GLU VAL SER THR          
SEQRES  13 D  604  THR GLU LEU ALA ALA VAL SER GLU ASN GLU GLU SER PHE          
SEQRES  14 D  604  VAL TYR LEU ARG ALA PHE ALA ASN THR TYR ILE VAL GLY          
SEQRES  15 D  604  PHE VAL LYS MET GLY GLU GLU THR PHE ASN ILE THR PRO          
SEQRES  16 D  604  ASP PRO GLU LYS VAL HIS VAL ALA MET GLU PRO VAL PHE          
SEQRES  17 D  604  THR ASP ASN GLU THR ILE TYR PHE ALA THR ASP TYR ASP          
SEQRES  18 D  604  SER ASP GLU MET TYR LEU ALA LYS PHE ASP LEU THR SER          
SEQRES  19 D  604  LYS GLU PHE SER LYS VAL LEU ALA PHE ASP GLY GLU SER          
SEQRES  20 D  604  ILE GLN SER VAL LYS TRP ASP LYS ASP ASN LYS ALA PHE          
SEQRES  21 D  604  TYR LEU ILE THR VAL LYS GLY VAL THR ASP ILE LEU TYR          
SEQRES  22 D  604  ARG TYR ASP VAL ALA THR ASP LYS VAL GLU GLU CYS SER          
SEQRES  23 D  604  LEU PRO VAL ASP ILE ILE GLU GLN ILE GLN VAL ALA LYS          
SEQRES  24 D  604  SER GLY ASN LEU TYR ILE LEU GLY ARG SER ALA THR VAL          
SEQRES  25 D  604  PRO HIS ASN VAL TYR GLN SER SER ASN GLY VAL GLU TRP          
SEQRES  26 D  604  LYS GLN LEU THR ASN ASN ARG VAL LEU GLY LEU SER PRO          
SEQRES  27 D  604  GLU ASP MET VAL GLU PRO ASP ILE VAL SER TYR THR SER          
SEQRES  28 D  604  PHE ASP GLY MET GLU ILE GLU ALA LEU LEU PHE LYS ALA          
SEQRES  29 D  604  LYS PRO GLU ASN ASP ASN GLY TYR THR ILE PHE TRP PRO          
SEQRES  30 D  604  HIS GLY GLY PRO GLN SER ALA GLU ARG LYS MET PHE ARG          
SEQRES  31 D  604  SER MET PHE GLN CYS PHE ILE ASN ARG GLY TYR THR ILE          
SEQRES  32 D  604  PHE ALA PRO ASN PHE ARG GLY SER THR GLY TYR GLY SER          
SEQRES  33 D  604  ALA PHE THR LYS LEU VAL GLU LEU ASP TRP GLY GLU GLY          
SEQRES  34 D  604  PRO ARG LEU ASP CYS ILE ALA GLY ILE GLU TRP LEU PHE          
SEQRES  35 D  604  GLU SER GLY PHE THR ASP ARG ASN LYS LEU PHE LEU VAL          
SEQRES  36 D  604  GLY GLY SER TYR GLY GLY TYR MET ALA LEU LEU LEU HIS          
SEQRES  37 D  604  GLY ARG HIS SER ASP TYR PHE ARG ALA VAL VAL ASP ILE          
SEQRES  38 D  604  PHE GLY PRO SER ASP LEU PHE THR PHE ILE ASN SER VAL          
SEQRES  39 D  604  PRO PRO HIS TRP LYS PRO ILE MET GLU ARG TRP LEU GLY          
SEQRES  40 D  604  ASP PRO GLU ARG ASP LYS GLU ARG PHE ILE LYS ASP SER          
SEQRES  41 D  604  PRO VAL THR TYR LEU ASP GLY MET VAL LYS PRO MET LEU          
SEQRES  42 D  604  VAL ILE GLN GLY ALA LYS ASP PRO ARG VAL VAL LYS GLU          
SEQRES  43 D  604  GLU SER ASP GLN ILE VAL ALA LYS LEU LYS GLU LYS GLY          
SEQRES  44 D  604  ARG ASP VAL GLU TYR LEU VAL LEU GLU ASP GLU GLY HIS          
SEQRES  45 D  604  GLY PHE SER LYS LYS GLU ASN GLU ILE LYS VAL TYR SER          
SEQRES  46 D  604  LEU MET LEU ALA PHE LEU GLU LYS HIS GLN ALA LEU GLU          
SEQRES  47 D  604  HIS HIS HIS HIS HIS HIS                                      
HET    SO4  A 701       5                                                       
HET    SO4  B 701       5                                                       
HET    SO4  C 701       5                                                       
HET    SO4  D 701       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   9  HOH   *476(H2 O)                                                    
HELIX    1 AA1 THR A    8  ARG A   14  5                                   7    
HELIX    2 AA2 LYS A  255  ASN A  257  5                                   3    
HELIX    3 AA3 SER A  337  MET A  341  5                                   5    
HELIX    4 AA4 ARG A  390  GLY A  400  1                                  11    
HELIX    5 AA5 GLY A  415  LEU A  421  1                                   7    
HELIX    6 AA6 GLU A  428  GLY A  445  1                                  18    
HELIX    7 AA7 SER A  458  SER A  472  1                                  15    
HELIX    8 AA8 ASP A  473  PHE A  475  5                                   3    
HELIX    9 AA9 ASP A  486  VAL A  494  1                                   9    
HELIX   10 AB1 PRO A  495  HIS A  497  5                                   3    
HELIX   11 AB2 TRP A  498  LEU A  506  1                                   9    
HELIX   12 AB3 ASP A  512  SER A  520  1                                   9    
HELIX   13 AB4 PRO A  521  MET A  528  5                                   8    
HELIX   14 AB5 LYS A  545  LYS A  558  1                                  14    
HELIX   15 AB6 LYS A  576  HIS A  594  1                                  19    
HELIX   16 AB7 THR B    8  THR B   15  5                                   8    
HELIX   17 AB8 SER B  337  MET B  341  5                                   5    
HELIX   18 AB9 ARG B  390  GLY B  400  1                                  11    
HELIX   19 AC1 GLY B  415  LEU B  421  1                                   7    
HELIX   20 AC2 GLU B  428  GLY B  445  1                                  18    
HELIX   21 AC3 SER B  458  SER B  472  1                                  15    
HELIX   22 AC4 ASP B  473  PHE B  475  5                                   3    
HELIX   23 AC5 ASP B  486  VAL B  494  1                                   9    
HELIX   24 AC6 PRO B  495  HIS B  497  5                                   3    
HELIX   25 AC7 TRP B  498  LEU B  506  1                                   9    
HELIX   26 AC8 ASP B  512  ASP B  519  1                                   8    
HELIX   27 AC9 SER B  520  MET B  528  5                                   9    
HELIX   28 AD1 VAL B  544  GLU B  557  1                                  14    
HELIX   29 AD2 LYS B  576  HIS B  594  1                                  19    
HELIX   30 AD3 THR C    8  PHE C   13  5                                   6    
HELIX   31 AD4 SER C  337  MET C  341  5                                   5    
HELIX   32 AD5 ARG C  390  ARG C  399  1                                  10    
HELIX   33 AD6 GLY C  415  LEU C  421  1                                   7    
HELIX   34 AD7 GLU C  428  GLY C  445  1                                  18    
HELIX   35 AD8 SER C  458  SER C  472  1                                  15    
HELIX   36 AD9 ASP C  473  PHE C  475  5                                   3    
HELIX   37 AE1 ASP C  486  VAL C  494  1                                   9    
HELIX   38 AE2 PRO C  495  HIS C  497  5                                   3    
HELIX   39 AE3 TRP C  498  LEU C  506  1                                   9    
HELIX   40 AE4 ASP C  512  ASP C  519  1                                   8    
HELIX   41 AE5 SER C  520  MET C  528  5                                   9    
HELIX   42 AE6 VAL C  544  LYS C  558  1                                  15    
HELIX   43 AE7 LYS C  576  HIS C  594  1                                  19    
HELIX   44 AE8 THR D    8  PHE D   13  5                                   6    
HELIX   45 AE9 LYS D  255  ASN D  257  5                                   3    
HELIX   46 AF1 SER D  337  MET D  341  5                                   5    
HELIX   47 AF2 ARG D  390  GLY D  400  1                                  11    
HELIX   48 AF3 GLY D  415  LYS D  420  1                                   6    
HELIX   49 AF4 LEU D  421  GLU D  423  5                                   3    
HELIX   50 AF5 GLU D  428  GLY D  445  1                                  18    
HELIX   51 AF6 SER D  458  SER D  472  1                                  15    
HELIX   52 AF7 ASP D  473  PHE D  475  5                                   3    
HELIX   53 AF8 ASP D  486  VAL D  494  1                                   9    
HELIX   54 AF9 PRO D  495  HIS D  497  5                                   3    
HELIX   55 AG1 TRP D  498  LEU D  506  1                                   9    
HELIX   56 AG2 ASP D  512  ASP D  519  1                                   8    
HELIX   57 AG3 SER D  520  MET D  528  5                                   9    
HELIX   58 AG4 VAL D  544  LYS D  558  1                                  15    
HELIX   59 AG5 LYS D  576  HIS D  594  1                                  19    
SHEET    1 AA1 4 ILE A  18  VAL A  23  0                                        
SHEET    2 AA1 4 LEU A  30  ALA A  34 -1  O  ASN A  33   N  ASN A  20           
SHEET    3 AA1 4 ASN A  41  MET A  45 -1  O  TRP A  43   N  PHE A  32           
SHEET    4 AA1 4 TYR A  53  ALA A  56 -1  O  TYR A  53   N  ALA A  44           
SHEET    1 AA2 4 CYS A  62  PHE A  67  0                                        
SHEET    2 AA2 4 VAL A  74  PHE A  78 -1  O  LEU A  75   N  LYS A  66           
SHEET    3 AA2 4 GLN A  87  ILE A  91 -1  O  TYR A  89   N  ALA A  76           
SHEET    4 AA2 4 HIS A  99  ILE A 102 -1  O  HIS A  99   N  ALA A  90           
SHEET    1 AA3 4 TYR A 110  LEU A 115  0                                        
SHEET    2 AA3 4 CYS A 121  THR A 126 -1  O  TYR A 123   N  HIS A 114           
SHEET    3 AA3 4 ASN A 135  ASN A 140 -1  O  ARG A 139   N  VAL A 122           
SHEET    4 AA3 4 ASP A 146  VAL A 151 -1  O  LEU A 149   N  THR A 136           
SHEET    1 AA4 4 THR A 156  VAL A 162  0                                        
SHEET    2 AA4 4 PHE A 169  ALA A 176 -1  O  LEU A 172   N  GLU A 158           
SHEET    3 AA4 4 TYR A 179  LYS A 185 -1  O  PHE A 183   N  TYR A 171           
SHEET    4 AA4 4 THR A 190  ASN A 192 -1  O  PHE A 191   N  VAL A 184           
SHEET    1 AA5 4 ALA A 203  ASP A 210  0                                        
SHEET    2 AA5 4 THR A 213  THR A 218 -1  O  ALA A 217   N  MET A 204           
SHEET    3 AA5 4 TYR A 226  ASP A 231 -1  O  TYR A 226   N  THR A 218           
SHEET    4 AA5 4 GLU A 236  LEU A 241 -1  O  LEU A 241   N  LEU A 227           
SHEET    1 AA6 4 SER A 247  ASP A 254  0                                        
SHEET    2 AA6 4 ALA A 259  LYS A 266 -1  O  ALA A 259   N  ASP A 254           
SHEET    3 AA6 4 THR A 269  ASP A 276 -1  O  TYR A 275   N  PHE A 260           
SHEET    4 AA6 4 LYS A 281  GLU A 284 -1  O  GLU A 283   N  ARG A 274           
SHEET    1 AA7 4 ILE A 291  VAL A 297  0                                        
SHEET    2 AA7 4 LEU A 303  ARG A 308 -1  O  LEU A 306   N  GLU A 293           
SHEET    3 AA7 4 ASN A 315  SER A 319 -1  O  SER A 319   N  LEU A 303           
SHEET    4 AA7 4 LYS A 326  GLN A 327 -1  O  LYS A 326   N  GLN A 318           
SHEET    1 AA8 8 ASP A 345  THR A 350  0                                        
SHEET    2 AA8 8 GLU A 356  PHE A 362 -1  O  ILE A 357   N  TYR A 349           
SHEET    3 AA8 8 THR A 402  PRO A 406 -1  O  ILE A 403   N  PHE A 362           
SHEET    4 AA8 8 THR A 373  PHE A 375  1  N  ILE A 374   O  THR A 402           
SHEET    5 AA8 8 LEU A 452  GLY A 457  1  O  PHE A 453   N  THR A 373           
SHEET    6 AA8 8 ALA A 477  ILE A 481  1  O  ILE A 481   N  GLY A 456           
SHEET    7 AA8 8 MET A 532  GLY A 537  1  O  LEU A 533   N  ASP A 480           
SHEET    8 AA8 8 VAL A 562  LEU A 567  1  O  GLU A 563   N  VAL A 534           
SHEET    1 AA9 4 ILE B  18  VAL B  23  0                                        
SHEET    2 AA9 4 LEU B  30  ALA B  34 -1  O  ASN B  33   N  ASN B  20           
SHEET    3 AA9 4 ASN B  41  MET B  45 -1  O  TRP B  43   N  PHE B  32           
SHEET    4 AA9 4 TYR B  53  ALA B  56 -1  O  PHE B  55   N  LEU B  42           
SHEET    1 AB1 4 CYS B  62  PHE B  67  0                                        
SHEET    2 AB1 4 TYR B  73  PHE B  78 -1  O  LEU B  75   N  LYS B  66           
SHEET    3 AB1 4 GLN B  87  PRO B  92 -1  O  ILE B  91   N  VAL B  74           
SHEET    4 AB1 4 HIS B  99  ILE B 102 -1  O  HIS B  99   N  ALA B  90           
SHEET    1 AB2 4 TYR B 110  LEU B 115  0                                        
SHEET    2 AB2 4 CYS B 121  THR B 126 -1  O  TYR B 123   N  HIS B 114           
SHEET    3 AB2 4 ASN B 135  ASN B 140 -1  O  ARG B 137   N  TYR B 124           
SHEET    4 AB2 4 ASP B 146  VAL B 151 -1  O  LEU B 149   N  THR B 136           
SHEET    1 AB3 4 THR B 156  VAL B 162  0                                        
SHEET    2 AB3 4 PHE B 169  ALA B 176 -1  O  VAL B 170   N  ALA B 161           
SHEET    3 AB3 4 TYR B 179  LYS B 185 -1  O  TYR B 179   N  PHE B 175           
SHEET    4 AB3 4 THR B 190  ASN B 192 -1  O  PHE B 191   N  VAL B 184           
SHEET    1 AB4 4 ALA B 203  PHE B 208  0                                        
SHEET    2 AB4 4 THR B 213  THR B 218 -1  O  ALA B 217   N  MET B 204           
SHEET    3 AB4 4 TYR B 226  ASP B 231 -1  O  TYR B 226   N  THR B 218           
SHEET    4 AB4 4 GLU B 236  LEU B 241 -1  O  LEU B 241   N  LEU B 227           
SHEET    1 AB5 4 SER B 247  ASP B 254  0                                        
SHEET    2 AB5 4 ALA B 259  LYS B 266 -1  O  ALA B 259   N  ASP B 254           
SHEET    3 AB5 4 THR B 269  ASP B 276 -1  O  TYR B 273   N  LEU B 262           
SHEET    4 AB5 4 LYS B 281  CYS B 285 -1  O  CYS B 285   N  LEU B 272           
SHEET    1 AB6 4 ILE B 291  VAL B 297  0                                        
SHEET    2 AB6 4 LEU B 303  ARG B 308 -1  O  LEU B 306   N  GLU B 293           
SHEET    3 AB6 4 ASN B 315  SER B 319 -1  O  SER B 319   N  LEU B 303           
SHEET    4 AB6 4 LYS B 326  GLN B 327 -1  O  LYS B 326   N  GLN B 318           
SHEET    1 AB7 8 ASP B 345  THR B 350  0                                        
SHEET    2 AB7 8 GLU B 356  PHE B 362 -1  O  LEU B 361   N  ASP B 345           
SHEET    3 AB7 8 THR B 402  PRO B 406 -1  O  ALA B 405   N  LEU B 360           
SHEET    4 AB7 8 THR B 373  PHE B 375  1  N  ILE B 374   O  PHE B 404           
SHEET    5 AB7 8 LEU B 452  GLY B 457  1  O  PHE B 453   N  THR B 373           
SHEET    6 AB7 8 ALA B 477  ILE B 481  1  O  ILE B 481   N  GLY B 456           
SHEET    7 AB7 8 MET B 532  GLY B 537  1  O  LEU B 533   N  ASP B 480           
SHEET    8 AB7 8 VAL B 562  LEU B 567  1  O  GLU B 563   N  VAL B 534           
SHEET    1 AB8 4 ILE C  18  VAL C  23  0                                        
SHEET    2 AB8 4 LEU C  30  ALA C  34 -1  O  VAL C  31   N  ALA C  22           
SHEET    3 AB8 4 ASN C  41  MET C  45 -1  O  TRP C  43   N  PHE C  32           
SHEET    4 AB8 4 TYR C  53  ALA C  56 -1  O  PHE C  55   N  LEU C  42           
SHEET    1 AB9 4 CYS C  62  PHE C  67  0                                        
SHEET    2 AB9 4 TYR C  73  PHE C  78 -1  O  LEU C  75   N  LYS C  66           
SHEET    3 AB9 4 GLN C  87  PRO C  92 -1  O  ILE C  91   N  VAL C  74           
SHEET    4 AB9 4 HIS C  99  ILE C 102 -1  O  HIS C  99   N  ALA C  90           
SHEET    1 AC1 4 TYR C 110  LEU C 115  0                                        
SHEET    2 AC1 4 CYS C 121  THR C 126 -1  O  TYR C 123   N  HIS C 114           
SHEET    3 AC1 4 ASN C 135  ASN C 140 -1  O  ARG C 139   N  VAL C 122           
SHEET    4 AC1 4 ASP C 146  VAL C 151 -1  O  LEU C 149   N  THR C 136           
SHEET    1 AC2 4 THR C 156  VAL C 162  0                                        
SHEET    2 AC2 4 SER C 168  ALA C 176 -1  O  LEU C 172   N  GLU C 158           
SHEET    3 AC2 4 TYR C 179  MET C 186 -1  O  TYR C 179   N  PHE C 175           
SHEET    4 AC2 4 GLU C 189  ASN C 192 -1  O  PHE C 191   N  VAL C 184           
SHEET    1 AC3 4 ALA C 203  ASP C 210  0                                        
SHEET    2 AC3 4 THR C 213  THR C 218 -1  O  ALA C 217   N  MET C 204           
SHEET    3 AC3 4 TYR C 226  ASP C 231 -1  O  TYR C 226   N  THR C 218           
SHEET    4 AC3 4 GLU C 236  LEU C 241 -1  O  LEU C 241   N  LEU C 227           
SHEET    1 AC4 4 SER C 247  ASP C 254  0                                        
SHEET    2 AC4 4 ALA C 259  LYS C 266 -1  O  ALA C 259   N  ASP C 254           
SHEET    3 AC4 4 THR C 269  ASP C 276 -1  O  TYR C 273   N  LEU C 262           
SHEET    4 AC4 4 LYS C 281  GLU C 284 -1  O  GLU C 283   N  ARG C 274           
SHEET    1 AC5 4 ILE C 291  VAL C 297  0                                        
SHEET    2 AC5 4 LEU C 303  SER C 309 -1  O  LEU C 306   N  GLU C 293           
SHEET    3 AC5 4 VAL C 312  SER C 319 -1  O  SER C 319   N  LEU C 303           
SHEET    4 AC5 4 LYS C 326  GLN C 327 -1  O  LYS C 326   N  GLN C 318           
SHEET    1 AC6 8 ASP C 345  THR C 350  0                                        
SHEET    2 AC6 8 GLU C 356  PHE C 362 -1  O  LEU C 361   N  ASP C 345           
SHEET    3 AC6 8 THR C 402  PRO C 406 -1  O  ILE C 403   N  PHE C 362           
SHEET    4 AC6 8 THR C 373  PHE C 375  1  N  ILE C 374   O  THR C 402           
SHEET    5 AC6 8 LEU C 452  GLY C 457  1  O  PHE C 453   N  THR C 373           
SHEET    6 AC6 8 VAL C 478  ILE C 481  1  O  ILE C 481   N  GLY C 456           
SHEET    7 AC6 8 MET C 532  GLY C 537  1  O  LEU C 533   N  VAL C 478           
SHEET    8 AC6 8 VAL C 562  LEU C 567  1  O  LEU C 565   N  VAL C 534           
SHEET    1 AC7 4 ILE D  18  VAL D  23  0                                        
SHEET    2 AC7 4 LEU D  30  ALA D  34 -1  O  VAL D  31   N  ALA D  22           
SHEET    3 AC7 4 ASN D  41  MET D  45 -1  O  TRP D  43   N  PHE D  32           
SHEET    4 AC7 4 TYR D  53  ALA D  56 -1  O  PHE D  55   N  LEU D  42           
SHEET    1 AC8 4 CYS D  62  PHE D  67  0                                        
SHEET    2 AC8 4 VAL D  74  PHE D  78 -1  O  LEU D  75   N  LYS D  66           
SHEET    3 AC8 4 GLN D  87  ILE D  91 -1  O  TYR D  89   N  ALA D  76           
SHEET    4 AC8 4 HIS D  99  ILE D 102 -1  O  ILE D 102   N  ILE D  88           
SHEET    1 AC9 4 TYR D 110  LEU D 115  0                                        
SHEET    2 AC9 4 CYS D 121  THR D 126 -1  O  TYR D 123   N  HIS D 114           
SHEET    3 AC9 4 ASN D 135  ASN D 140 -1  O  ARG D 137   N  TYR D 124           
SHEET    4 AC9 4 ASP D 146  VAL D 151 -1  O  ASN D 150   N  THR D 136           
SHEET    1 AD1 4 THR D 156  VAL D 162  0                                        
SHEET    2 AD1 4 SER D 168  ALA D 176 -1  O  VAL D 170   N  ALA D 161           
SHEET    3 AD1 4 TYR D 179  MET D 186 -1  O  TYR D 179   N  PHE D 175           
SHEET    4 AD1 4 GLU D 189  ASN D 192 -1  O  PHE D 191   N  VAL D 184           
SHEET    1 AD2 4 ALA D 203  ASP D 210  0                                        
SHEET    2 AD2 4 THR D 213  THR D 218 -1  O  ALA D 217   N  MET D 204           
SHEET    3 AD2 4 TYR D 226  ASP D 231 -1  O  TYR D 226   N  THR D 218           
SHEET    4 AD2 4 GLU D 236  LEU D 241 -1  O  LEU D 241   N  LEU D 227           
SHEET    1 AD3 4 SER D 247  ASP D 254  0                                        
SHEET    2 AD3 4 ALA D 259  LYS D 266 -1  O  ALA D 259   N  ASP D 254           
SHEET    3 AD3 4 THR D 269  ASP D 276 -1  O  THR D 269   N  LYS D 266           
SHEET    4 AD3 4 LYS D 281  GLU D 284 -1  O  GLU D 283   N  ARG D 274           
SHEET    1 AD4 4 ILE D 291  VAL D 297  0                                        
SHEET    2 AD4 4 LEU D 303  SER D 309 -1  O  LEU D 306   N  GLU D 293           
SHEET    3 AD4 4 VAL D 312  SER D 319 -1  O  SER D 319   N  LEU D 303           
SHEET    4 AD4 4 LYS D 326  GLN D 327 -1  O  LYS D 326   N  GLN D 318           
SHEET    1 AD5 8 ASP D 345  THR D 350  0                                        
SHEET    2 AD5 8 GLU D 356  PHE D 362 -1  O  LEU D 361   N  ASP D 345           
SHEET    3 AD5 8 THR D 402  PRO D 406 -1  O  ILE D 403   N  PHE D 362           
SHEET    4 AD5 8 THR D 373  PHE D 375  1  N  ILE D 374   O  THR D 402           
SHEET    5 AD5 8 LEU D 452  GLY D 457  1  O  PHE D 453   N  THR D 373           
SHEET    6 AD5 8 VAL D 478  ILE D 481  1  O  VAL D 479   N  LEU D 454           
SHEET    7 AD5 8 MET D 532  GLY D 537  1  O  LEU D 533   N  ASP D 480           
SHEET    8 AD5 8 VAL D 562  LEU D 567  1  O  LEU D 565   N  VAL D 534           
CISPEP   1 LEU A   47    PRO A   48          0         4.39                     
CISPEP   2 GLY A  380    PRO A  381          0         0.00                     
CISPEP   3 LEU B   47    PRO B   48          0         4.47                     
CISPEP   4 GLY B  380    PRO B  381          0         0.38                     
CISPEP   5 LEU C   47    PRO C   48          0         6.55                     
CISPEP   6 GLY C  380    PRO C  381          0         3.26                     
CISPEP   7 LEU D   47    PRO D   48          0         4.13                     
CISPEP   8 GLY D  380    PRO D  381          0         4.40                     
SITE     1 AC1  5 ASP A 369  GLY A 371  GLY A 445  PHE A 446                    
SITE     2 AC1  5 ASP A 448                                                     
SITE     1 AC2  5 GLY B 371  GLY B 445  PHE B 446  THR B 447                    
SITE     2 AC2  5 ASP B 448                                                     
SITE     1 AC3  5 ASP C 369  GLY C 371  GLY C 445  PHE C 446                    
SITE     2 AC3  5 ASP C 448                                                     
SITE     1 AC4  5 ASP D 369  GLY D 371  GLY D 445  PHE D 446                    
SITE     2 AC4  5 ASP D 448                                                     
CRYST1  148.080  151.100  191.230  90.00  90.00  90.00 P 21 21 21   16          
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      0.006753  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006618  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005229        0.00000                         
TER    4894      HIS A 604                                                      
TER    9788      HIS B 604                                                      
TER   14676      HIS C 604                                                      
TER   19570      HIS D 604                                                      
MASTER      363    0    4   59  144    0    8    620020    4   20  188          
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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