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LongText Report for: 7x0d-pdb

Name Class
7x0d-pdb
HEADER    HYDROLASE                               21-FEB-22   7X0D              
TITLE     CRYSTAL STRUCTURE OF PHOSPHOLIPASE A1, CAPLA1                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOLIPASE A1;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.1.1.-;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAPSICUM ANNUUM;                                
SOURCE   3 ORGANISM_TAXID: 4072;                                                
SOURCE   4 GENE: PLA1, T459_03599;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PHOSPHOLIPASE A1, HYDROLASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.HEO,I.LEE,S.MOON,W.LEE                                              
REVDAT   1   13-APR-22 7X0D    0                                                
JRNL        AUTH   Y.HEO,I.LEE,S.MOON,J.YUN,E.KIM,S.PARK,J.PARK,W.KIM,W.LEE     
JRNL        TITL   CRYSTAL STRUCTURES OF THE PLANT PHOSPHOLIPASE A1 PROTEINS    
JRNL        TITL 2 REVEAL A UNIQUE DIMERIZATION DOMAIN                          
JRNL        REF    MOLECULES                                  2022              
JRNL        REFN                   ESSN 1420-3049                               
JRNL        DOI    10.3390/MOLECULES27072317                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.11                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.333                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 67351                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.062                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3409                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.1061 -  6.9087    1.00     2943   136  0.1681 0.1891        
REMARK   3     2  6.9087 -  5.4860    1.00     2806   176  0.1862 0.2339        
REMARK   3     3  5.4860 -  4.7932    1.00     2832   140  0.1710 0.2120        
REMARK   3     4  4.7932 -  4.3552    0.99     2755   150  0.1579 0.2004        
REMARK   3     5  4.3552 -  4.0432    0.97     2710   143  0.1683 0.2178        
REMARK   3     6  4.0432 -  3.8050    0.96     2675   135  0.1796 0.2394        
REMARK   3     7  3.8050 -  3.6145    0.95     2630   157  0.1874 0.2670        
REMARK   3     8  3.6145 -  3.4572    0.96     2650   141  0.1990 0.2628        
REMARK   3     9  3.4572 -  3.3241    0.95     2599   150  0.2019 0.2364        
REMARK   3    10  3.3241 -  3.2094    0.95     2660   124  0.2197 0.2554        
REMARK   3    11  3.2094 -  3.1091    0.95     2634   152  0.2226 0.2501        
REMARK   3    12  3.1091 -  3.0202    0.95     2657   133  0.2299 0.2686        
REMARK   3    13  3.0202 -  2.9407    0.95     2601   143  0.2298 0.2769        
REMARK   3    14  2.9407 -  2.8690    0.95     2635   143  0.2349 0.3173        
REMARK   3    15  2.8690 -  2.8038    0.95     2613   145  0.2315 0.2915        
REMARK   3    16  2.8038 -  2.7441    0.95     2639   135  0.2424 0.3304        
REMARK   3    17  2.7441 -  2.6892    0.95     2574   156  0.2368 0.3378        
REMARK   3    18  2.6892 -  2.6385    0.95     2636   152  0.2462 0.2986        
REMARK   3    19  2.6385 -  2.5914    0.95     2615   147  0.2505 0.3170        
REMARK   3    20  2.5914 -  2.5474    0.96     2691   133  0.2601 0.3341        
REMARK   3    21  2.5474 -  2.5063    0.96     2632   142  0.2702 0.3492        
REMARK   3    22  2.5063 -  2.4678    0.96     2624   128  0.2703 0.3610        
REMARK   3    23  2.4678 -  2.4315    0.96     2702   128  0.2996 0.3449        
REMARK   3    24  2.4315 -  2.3973    0.89     2429   120  0.2910 0.3613        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.337            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.704           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.56                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002          12769                                  
REMARK   3   ANGLE     :  0.545          17315                                  
REMARK   3   CHIRALITY :  0.042           1848                                  
REMARK   3   PLANARITY :  0.004           2200                                  
REMARK   3   DIHEDRAL  : 13.668           7483                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7X0D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-FEB-22.                  
REMARK 100 THE DEPOSITION ID IS D_1300027809.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0082                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67379                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.390                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.11900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.9700                            
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) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.790                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 2YIJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES (PH 7.5), 0.2M AMMONIUM       
REMARK 280  SULFATE, 10% PEG 8000, 10% 2-PROPANOL, VAPOR DIFFUSION, SITTING     
REMARK 280  DROP, TEMPERATURE 293K                                              
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       29.78400            
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                                                    
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: 3060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 2970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
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 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      101.95560            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       29.78400            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      147.31857            
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     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ASP A   160                                                      
REMARK 465     GLY A   161                                                      
REMARK 465     GLY A   162                                                      
REMARK 465     LEU A   163                                                      
REMARK 465     LEU A   164                                                      
REMARK 465     PRO A   165                                                      
REMARK 465     LEU A   166                                                      
REMARK 465     PHE A   167                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     PRO B    91                                                      
REMARK 465     ASP B    92                                                      
REMARK 465     ASP B   160                                                      
REMARK 465     GLY B   161                                                      
REMARK 465     GLY B   162                                                      
REMARK 465     LEU B   163                                                      
REMARK 465     LEU B   164                                                      
REMARK 465     PRO B   165                                                      
REMARK 465     LEU B   166                                                      
REMARK 465     PHE B   167                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     LEU C    90                                                      
REMARK 465     PRO C    91                                                      
REMARK 465     ASP C    92                                                      
REMARK 465     ASP C   160                                                      
REMARK 465     GLY C   161                                                      
REMARK 465     GLY C   162                                                      
REMARK 465     LEU C   163                                                      
REMARK 465     LEU C   164                                                      
REMARK 465     PRO C   165                                                      
REMARK 465     LEU C   166                                                      
REMARK 465     PHE C   167                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     PRO D    91                                                      
REMARK 465     ASP D    92                                                      
REMARK 465     ASP D   160                                                      
REMARK 465     GLY D   161                                                      
REMARK 465     GLY D   162                                                      
REMARK 465     LEU D   163                                                      
REMARK 465     LEU D   164                                                      
REMARK 465     PRO D   165                                                      
REMARK 465     LEU D   166                                                      
REMARK 465     PHE D   167                                                      
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    PHE B   110     NH1  ARG B   135              1.91            
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    ALA A  93       -4.00   -156.86                                   
REMARK 500    GLU A 102       30.82    -98.59                                   
REMARK 500    TRP A 143      -34.73   -144.96                                   
REMARK 500    SER A 221     -125.16     63.05                                   
REMARK 500    ASP A 262     -156.16   -103.16                                   
REMARK 500    ILE A 360      -41.35   -136.12                                   
REMARK 500    VAL B 140      -66.65   -127.73                                   
REMARK 500    TRP B 143      -30.83   -144.50                                   
REMARK 500    ARG B 185      -23.87    120.38                                   
REMARK 500    SER B 221     -127.27     61.99                                   
REMARK 500    ASP B 262     -158.40    -92.65                                   
REMARK 500    PRO B 288       -8.09    -59.90                                   
REMARK 500    ILE B 360      -42.64   -136.11                                   
REMARK 500    TRP C 143      -38.20   -141.54                                   
REMARK 500    SER C 221     -127.48     58.76                                   
REMARK 500    ASP C 262     -163.36    -77.95                                   
REMARK 500    ILE C 360      -42.06   -136.73                                   
REMARK 500    VAL C 380      109.36     57.09                                   
REMARK 500    LEU C 389      103.02    -56.92                                   
REMARK 500    GLU C 396      122.05     85.25                                   
REMARK 500    VAL D 140      -65.25   -127.18                                   
REMARK 500    TRP D 143      -31.63   -140.11                                   
REMARK 500    ASN D 210       22.30    -77.00                                   
REMARK 500    SER D 221     -126.13     60.02                                   
REMARK 500    ASP D 262     -154.94    -97.76                                   
REMARK 500    ILE D 360      -41.37   -137.33                                   
REMARK 500    TYR D 395       -3.90   -140.30                                   
REMARK 500    GLU D 396      126.05     66.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7X0D A    1   397  UNP    A5YW95   A5YW95_CAPAN     1    397             
DBREF  7X0D B    1   397  UNP    A5YW95   A5YW95_CAPAN     1    397             
DBREF  7X0D C    1   397  UNP    A5YW95   A5YW95_CAPAN     1    397             
DBREF  7X0D D    1   397  UNP    A5YW95   A5YW95_CAPAN     1    397             
SEQADV 7X0D GLY A    0  UNP  A5YW95              EXPRESSION TAG                 
SEQADV 7X0D TRP A  113  UNP  A5YW95    TYR   113 ENGINEERED MUTATION            
SEQADV 7X0D GLY B    0  UNP  A5YW95              EXPRESSION TAG                 
SEQADV 7X0D TRP B  113  UNP  A5YW95    TYR   113 ENGINEERED MUTATION            
SEQADV 7X0D GLY C    0  UNP  A5YW95              EXPRESSION TAG                 
SEQADV 7X0D TRP C  113  UNP  A5YW95    TYR   113 ENGINEERED MUTATION            
SEQADV 7X0D GLY D    0  UNP  A5YW95              EXPRESSION TAG                 
SEQADV 7X0D TRP D  113  UNP  A5YW95    TYR   113 ENGINEERED MUTATION            
SEQRES   1 A  398  GLY MET GLY SER MET ALA GLU LYS TRP GLU GLU LEU SER          
SEQRES   2 A  398  GLY LYS ASN ASN TRP GLU GLY LEU LEU ASN PRO LEU ASP          
SEQRES   3 A  398  LEU ASP LEU ARG LYS TYR ILE ILE GLN TYR GLY GLU LEU          
SEQRES   4 A  398  ALA GLN ALA THR TYR ASP THR PHE ILE SER GLU ARG ALA          
SEQRES   5 A  398  SER LYS TYR ALA GLY ALA SER ARG TYR SER MET GLU ASN          
SEQRES   6 A  398  PHE PHE THR LYS VAL GLY LEU ASP PRO SER LYS TYR HIS          
SEQRES   7 A  398  VAL THR LYS PHE PHE TYR GLY THR SER SER ILE PRO LEU          
SEQRES   8 A  398  PRO ASP ALA PHE MET THR ARG SER LEU SER ARG GLU ALA          
SEQRES   9 A  398  TRP SER LYS GLU SER ASN PHE MET GLY TRP ILE ALA VAL          
SEQRES  10 A  398  ALA THR ASP GLU GLY LYS VAL ALA LEU GLY ARG ARG ASP          
SEQRES  11 A  398  ILE VAL ILE ASN TRP ARG GLY THR LEU GLN VAL LEU GLU          
SEQRES  12 A  398  TRP VAL ASN ASP LEU GLN PHE LEU LEU VAL PRO ALA PRO          
SEQRES  13 A  398  LYS VAL PHE GLY ASP GLY GLY LEU LEU PRO LEU PHE HIS          
SEQRES  14 A  398  PRO LEU VAL HIS HIS GLY PHE HIS ASN ILE TYR THR THR          
SEQRES  15 A  398  GLU ASN PRO ARG SER GLN PHE ASN LYS THR CYS VAL ARG          
SEQRES  16 A  398  ASP GLN VAL MET GLU GLU VAL LYS ARG LEU VAL GLU GLU          
SEQRES  17 A  398  TYR LYS ASN GLU GLU VAL SER ILE THR VAL THR GLY HIS          
SEQRES  18 A  398  SER LEU GLY ALA SER LEU ALA THR LEU ASN ALA VAL ASP          
SEQRES  19 A  398  ILE ALA PHE ASN GLY ILE ASN LYS SER SER ASN GLY LYS          
SEQRES  20 A  398  GLU PHE PRO VAL THR ALA PHE VAL PHE ALA SER PRO LYS          
SEQRES  21 A  398  VAL GLY ASP LEU ASN PHE HIS LYS ALA PHE SER LYS LEU          
SEQRES  22 A  398  LYS HIS LEU HIS ILE LEU ARG ILE HIS ASN LEU LEU ASP          
SEQRES  23 A  398  ILE VAL PRO LYS TYR PRO PRO VAL GLY TYR PHE ASP VAL          
SEQRES  24 A  398  GLY GLN GLU LEU MET ILE ASP THR THR LYS SER PRO TYR          
SEQRES  25 A  398  VAL LYS PRO PRO GLY GLU VAL VAL SER TRP HIS LEU LEU          
SEQRES  26 A  398  GLU PRO TYR LEU HIS GLY ILE ALA GLY THR GLN GLY ILE          
SEQRES  27 A  398  GLY MET THR ALA GLY PHE LYS LEU GLU VAL ASN ARG ASP          
SEQRES  28 A  398  ILE SER LEU VAL ASN LYS GLN TRP MET ILE LEU LYS ASP          
SEQRES  29 A  398  GLU TYR CYS ILE PRO PRO LEU TRP TRP SER GLU LYS HIS          
SEQRES  30 A  398  LYS GLY MET VAL GLN GLN GLN ASP GLY SER TRP LEU LEU          
SEQRES  31 A  398  GLN ASP ARG ASP ASP TYR GLU PHE                              
SEQRES   1 B  398  GLY MET GLY SER MET ALA GLU LYS TRP GLU GLU LEU SER          
SEQRES   2 B  398  GLY LYS ASN ASN TRP GLU GLY LEU LEU ASN PRO LEU ASP          
SEQRES   3 B  398  LEU ASP LEU ARG LYS TYR ILE ILE GLN TYR GLY GLU LEU          
SEQRES   4 B  398  ALA GLN ALA THR TYR ASP THR PHE ILE SER GLU ARG ALA          
SEQRES   5 B  398  SER LYS TYR ALA GLY ALA SER ARG TYR SER MET GLU ASN          
SEQRES   6 B  398  PHE PHE THR LYS VAL GLY LEU ASP PRO SER LYS TYR HIS          
SEQRES   7 B  398  VAL THR LYS PHE PHE TYR GLY THR SER SER ILE PRO LEU          
SEQRES   8 B  398  PRO ASP ALA PHE MET THR ARG SER LEU SER ARG GLU ALA          
SEQRES   9 B  398  TRP SER LYS GLU SER ASN PHE MET GLY TRP ILE ALA VAL          
SEQRES  10 B  398  ALA THR ASP GLU GLY LYS VAL ALA LEU GLY ARG ARG ASP          
SEQRES  11 B  398  ILE VAL ILE ASN TRP ARG GLY THR LEU GLN VAL LEU GLU          
SEQRES  12 B  398  TRP VAL ASN ASP LEU GLN PHE LEU LEU VAL PRO ALA PRO          
SEQRES  13 B  398  LYS VAL PHE GLY ASP GLY GLY LEU LEU PRO LEU PHE HIS          
SEQRES  14 B  398  PRO LEU VAL HIS HIS GLY PHE HIS ASN ILE TYR THR THR          
SEQRES  15 B  398  GLU ASN PRO ARG SER GLN PHE ASN LYS THR CYS VAL ARG          
SEQRES  16 B  398  ASP GLN VAL MET GLU GLU VAL LYS ARG LEU VAL GLU GLU          
SEQRES  17 B  398  TYR LYS ASN GLU GLU VAL SER ILE THR VAL THR GLY HIS          
SEQRES  18 B  398  SER LEU GLY ALA SER LEU ALA THR LEU ASN ALA VAL ASP          
SEQRES  19 B  398  ILE ALA PHE ASN GLY ILE ASN LYS SER SER ASN GLY LYS          
SEQRES  20 B  398  GLU PHE PRO VAL THR ALA PHE VAL PHE ALA SER PRO LYS          
SEQRES  21 B  398  VAL GLY ASP LEU ASN PHE HIS LYS ALA PHE SER LYS LEU          
SEQRES  22 B  398  LYS HIS LEU HIS ILE LEU ARG ILE HIS ASN LEU LEU ASP          
SEQRES  23 B  398  ILE VAL PRO LYS TYR PRO PRO VAL GLY TYR PHE ASP VAL          
SEQRES  24 B  398  GLY GLN GLU LEU MET ILE ASP THR THR LYS SER PRO TYR          
SEQRES  25 B  398  VAL LYS PRO PRO GLY GLU VAL VAL SER TRP HIS LEU LEU          
SEQRES  26 B  398  GLU PRO TYR LEU HIS GLY ILE ALA GLY THR GLN GLY ILE          
SEQRES  27 B  398  GLY MET THR ALA GLY PHE LYS LEU GLU VAL ASN ARG ASP          
SEQRES  28 B  398  ILE SER LEU VAL ASN LYS GLN TRP MET ILE LEU LYS ASP          
SEQRES  29 B  398  GLU TYR CYS ILE PRO PRO LEU TRP TRP SER GLU LYS HIS          
SEQRES  30 B  398  LYS GLY MET VAL GLN GLN GLN ASP GLY SER TRP LEU LEU          
SEQRES  31 B  398  GLN ASP ARG ASP ASP TYR GLU PHE                              
SEQRES   1 C  398  GLY MET GLY SER MET ALA GLU LYS TRP GLU GLU LEU SER          
SEQRES   2 C  398  GLY LYS ASN ASN TRP GLU GLY LEU LEU ASN PRO LEU ASP          
SEQRES   3 C  398  LEU ASP LEU ARG LYS TYR ILE ILE GLN TYR GLY GLU LEU          
SEQRES   4 C  398  ALA GLN ALA THR TYR ASP THR PHE ILE SER GLU ARG ALA          
SEQRES   5 C  398  SER LYS TYR ALA GLY ALA SER ARG TYR SER MET GLU ASN          
SEQRES   6 C  398  PHE PHE THR LYS VAL GLY LEU ASP PRO SER LYS TYR HIS          
SEQRES   7 C  398  VAL THR LYS PHE PHE TYR GLY THR SER SER ILE PRO LEU          
SEQRES   8 C  398  PRO ASP ALA PHE MET THR ARG SER LEU SER ARG GLU ALA          
SEQRES   9 C  398  TRP SER LYS GLU SER ASN PHE MET GLY TRP ILE ALA VAL          
SEQRES  10 C  398  ALA THR ASP GLU GLY LYS VAL ALA LEU GLY ARG ARG ASP          
SEQRES  11 C  398  ILE VAL ILE ASN TRP ARG GLY THR LEU GLN VAL LEU GLU          
SEQRES  12 C  398  TRP VAL ASN ASP LEU GLN PHE LEU LEU VAL PRO ALA PRO          
SEQRES  13 C  398  LYS VAL PHE GLY ASP GLY GLY LEU LEU PRO LEU PHE HIS          
SEQRES  14 C  398  PRO LEU VAL HIS HIS GLY PHE HIS ASN ILE TYR THR THR          
SEQRES  15 C  398  GLU ASN PRO ARG SER GLN PHE ASN LYS THR CYS VAL ARG          
SEQRES  16 C  398  ASP GLN VAL MET GLU GLU VAL LYS ARG LEU VAL GLU GLU          
SEQRES  17 C  398  TYR LYS ASN GLU GLU VAL SER ILE THR VAL THR GLY HIS          
SEQRES  18 C  398  SER LEU GLY ALA SER LEU ALA THR LEU ASN ALA VAL ASP          
SEQRES  19 C  398  ILE ALA PHE ASN GLY ILE ASN LYS SER SER ASN GLY LYS          
SEQRES  20 C  398  GLU PHE PRO VAL THR ALA PHE VAL PHE ALA SER PRO LYS          
SEQRES  21 C  398  VAL GLY ASP LEU ASN PHE HIS LYS ALA PHE SER LYS LEU          
SEQRES  22 C  398  LYS HIS LEU HIS ILE LEU ARG ILE HIS ASN LEU LEU ASP          
SEQRES  23 C  398  ILE VAL PRO LYS TYR PRO PRO VAL GLY TYR PHE ASP VAL          
SEQRES  24 C  398  GLY GLN GLU LEU MET ILE ASP THR THR LYS SER PRO TYR          
SEQRES  25 C  398  VAL LYS PRO PRO GLY GLU VAL VAL SER TRP HIS LEU LEU          
SEQRES  26 C  398  GLU PRO TYR LEU HIS GLY ILE ALA GLY THR GLN GLY ILE          
SEQRES  27 C  398  GLY MET THR ALA GLY PHE LYS LEU GLU VAL ASN ARG ASP          
SEQRES  28 C  398  ILE SER LEU VAL ASN LYS GLN TRP MET ILE LEU LYS ASP          
SEQRES  29 C  398  GLU TYR CYS ILE PRO PRO LEU TRP TRP SER GLU LYS HIS          
SEQRES  30 C  398  LYS GLY MET VAL GLN GLN GLN ASP GLY SER TRP LEU LEU          
SEQRES  31 C  398  GLN ASP ARG ASP ASP TYR GLU PHE                              
SEQRES   1 D  398  GLY MET GLY SER MET ALA GLU LYS TRP GLU GLU LEU SER          
SEQRES   2 D  398  GLY LYS ASN ASN TRP GLU GLY LEU LEU ASN PRO LEU ASP          
SEQRES   3 D  398  LEU ASP LEU ARG LYS TYR ILE ILE GLN TYR GLY GLU LEU          
SEQRES   4 D  398  ALA GLN ALA THR TYR ASP THR PHE ILE SER GLU ARG ALA          
SEQRES   5 D  398  SER LYS TYR ALA GLY ALA SER ARG TYR SER MET GLU ASN          
SEQRES   6 D  398  PHE PHE THR LYS VAL GLY LEU ASP PRO SER LYS TYR HIS          
SEQRES   7 D  398  VAL THR LYS PHE PHE TYR GLY THR SER SER ILE PRO LEU          
SEQRES   8 D  398  PRO ASP ALA PHE MET THR ARG SER LEU SER ARG GLU ALA          
SEQRES   9 D  398  TRP SER LYS GLU SER ASN PHE MET GLY TRP ILE ALA VAL          
SEQRES  10 D  398  ALA THR ASP GLU GLY LYS VAL ALA LEU GLY ARG ARG ASP          
SEQRES  11 D  398  ILE VAL ILE ASN TRP ARG GLY THR LEU GLN VAL LEU GLU          
SEQRES  12 D  398  TRP VAL ASN ASP LEU GLN PHE LEU LEU VAL PRO ALA PRO          
SEQRES  13 D  398  LYS VAL PHE GLY ASP GLY GLY LEU LEU PRO LEU PHE HIS          
SEQRES  14 D  398  PRO LEU VAL HIS HIS GLY PHE HIS ASN ILE TYR THR THR          
SEQRES  15 D  398  GLU ASN PRO ARG SER GLN PHE ASN LYS THR CYS VAL ARG          
SEQRES  16 D  398  ASP GLN VAL MET GLU GLU VAL LYS ARG LEU VAL GLU GLU          
SEQRES  17 D  398  TYR LYS ASN GLU GLU VAL SER ILE THR VAL THR GLY HIS          
SEQRES  18 D  398  SER LEU GLY ALA SER LEU ALA THR LEU ASN ALA VAL ASP          
SEQRES  19 D  398  ILE ALA PHE ASN GLY ILE ASN LYS SER SER ASN GLY LYS          
SEQRES  20 D  398  GLU PHE PRO VAL THR ALA PHE VAL PHE ALA SER PRO LYS          
SEQRES  21 D  398  VAL GLY ASP LEU ASN PHE HIS LYS ALA PHE SER LYS LEU          
SEQRES  22 D  398  LYS HIS LEU HIS ILE LEU ARG ILE HIS ASN LEU LEU ASP          
SEQRES  23 D  398  ILE VAL PRO LYS TYR PRO PRO VAL GLY TYR PHE ASP VAL          
SEQRES  24 D  398  GLY GLN GLU LEU MET ILE ASP THR THR LYS SER PRO TYR          
SEQRES  25 D  398  VAL LYS PRO PRO GLY GLU VAL VAL SER TRP HIS LEU LEU          
SEQRES  26 D  398  GLU PRO TYR LEU HIS GLY ILE ALA GLY THR GLN GLY ILE          
SEQRES  27 D  398  GLY MET THR ALA GLY PHE LYS LEU GLU VAL ASN ARG ASP          
SEQRES  28 D  398  ILE SER LEU VAL ASN LYS GLN TRP MET ILE LEU LYS ASP          
SEQRES  29 D  398  GLU TYR CYS ILE PRO PRO LEU TRP TRP SER GLU LYS HIS          
SEQRES  30 D  398  LYS GLY MET VAL GLN GLN GLN ASP GLY SER TRP LEU LEU          
SEQRES  31 D  398  GLN ASP ARG ASP ASP TYR GLU PHE                              
HET    SO4  A 401       5                                                       
HET    SO4  B 401       5                                                       
HET    SO4  C 401       5                                                       
HET    SO4  D 401       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   9  HOH   *508(H2 O)                                                    
HELIX    1 AA1 LYS A    7  SER A   12  1                                   6    
HELIX    2 AA2 ASP A   25  PHE A   46  1                                  22    
HELIX    3 AA3 ASN A   64  VAL A   69  1                                   6    
HELIX    4 AA4 THR A  118  GLY A  126  1                                   9    
HELIX    5 AA5 ALA A  154  GLY A  159  1                                   6    
HELIX    6 AA6 HIS A  173  THR A  181  1                                   9    
HELIX    7 AA7 CYS A  192  TYR A  208  1                                  17    
HELIX    8 AA8 SER A  221  ASN A  237  1                                  17    
HELIX    9 AA9 ASP A  262  LEU A  272  1                                  11    
HELIX   10 AB1 ILE A  286  TYR A  290  5                                   5    
HELIX   11 AB2 ASP A  305  SER A  309  5                                   5    
HELIX   12 AB3 LEU A  323  THR A  334  1                                  12    
HELIX   13 AB4 ASP A  350  LYS A  356  5                                   7    
HELIX   14 AB5 LYS A  362  CYS A  366  5                                   5    
HELIX   15 AB6 GLU A  374  LYS A  377  5                                   4    
HELIX   16 AB7 LYS B    7  SER B   12  1                                   6    
HELIX   17 AB8 ASP B   25  THR B   45  1                                  21    
HELIX   18 AB9 ASN B   64  VAL B   69  1                                   6    
HELIX   19 AC1 THR B  118  GLY B  126  1                                   9    
HELIX   20 AC2 ALA B  154  GLY B  159  1                                   6    
HELIX   21 AC3 HIS B  173  THR B  181  1                                   9    
HELIX   22 AC4 CYS B  192  TYR B  208  1                                  17    
HELIX   23 AC5 SER B  221  ASN B  237  1                                  17    
HELIX   24 AC6 ASP B  262  LYS B  271  1                                  10    
HELIX   25 AC7 ILE B  286  TYR B  290  5                                   5    
HELIX   26 AC8 ASP B  305  SER B  309  5                                   5    
HELIX   27 AC9 LEU B  323  THR B  334  1                                  12    
HELIX   28 AD1 ASP B  350  LYS B  356  5                                   7    
HELIX   29 AD2 LYS B  362  CYS B  366  5                                   5    
HELIX   30 AD3 GLU B  374  LYS B  377  5                                   4    
HELIX   31 AD4 LYS C    7  SER C   12  1                                   6    
HELIX   32 AD5 ASP C   25  PHE C   46  1                                  22    
HELIX   33 AD6 ASN C   64  VAL C   69  1                                   6    
HELIX   34 AD7 THR C  118  GLY C  126  1                                   9    
HELIX   35 AD8 VAL C  140  ASN C  145  1                                   6    
HELIX   36 AD9 ALA C  154  GLY C  159  1                                   6    
HELIX   37 AE1 HIS C  173  THR C  181  1                                   9    
HELIX   38 AE2 CYS C  192  TYR C  208  1                                  17    
HELIX   39 AE3 SER C  221  ASN C  237  1                                  17    
HELIX   40 AE4 ASP C  262  LYS C  271  1                                  10    
HELIX   41 AE5 ILE C  286  TYR C  290  5                                   5    
HELIX   42 AE6 ASP C  305  SER C  309  5                                   5    
HELIX   43 AE7 LEU C  323  THR C  334  1                                  12    
HELIX   44 AE8 ASP C  350  LYS C  356  5                                   7    
HELIX   45 AE9 LYS C  362  CYS C  366  5                                   5    
HELIX   46 AF1 GLU C  374  MET C  379  5                                   6    
HELIX   47 AF2 LYS D    7  SER D   12  1                                   6    
HELIX   48 AF3 ASP D   25  THR D   45  1                                  21    
HELIX   49 AF4 ASN D   64  VAL D   69  1                                   6    
HELIX   50 AF5 THR D  118  GLY D  126  1                                   9    
HELIX   51 AF6 HIS D  173  THR D  181  1                                   9    
HELIX   52 AF7 CYS D  192  TYR D  208  1                                  17    
HELIX   53 AF8 SER D  221  ASN D  237  1                                  17    
HELIX   54 AF9 ASP D  262  LYS D  271  1                                  10    
HELIX   55 AG1 ILE D  286  TYR D  290  5                                   5    
HELIX   56 AG2 ASP D  305  SER D  309  5                                   5    
HELIX   57 AG3 LEU D  323  THR D  334  1                                  12    
HELIX   58 AG4 ASP D  350  LYS D  356  5                                   7    
HELIX   59 AG5 LYS D  362  CYS D  366  5                                   5    
HELIX   60 AG6 GLU D  374  LYS D  377  5                                   4    
SHEET    1 AA1 7 TYR A  76  GLY A  84  0                                        
SHEET    2 AA1 7 ASN A 109  ALA A 117 -1  O  ILE A 114   N  THR A  79           
SHEET    3 AA1 7 ARG A 128  TRP A 134 -1  O  VAL A 131   N  ALA A 115           
SHEET    4 AA1 7 VAL A 213  HIS A 220  1  O  THR A 216   N  ILE A 130           
SHEET    5 AA1 7 VAL A 250  PHE A 255  1  O  THR A 251   N  VAL A 217           
SHEET    6 AA1 7 LEU A 275  ASN A 282  1  O  LEU A 278   N  ALA A 252           
SHEET    7 AA1 7 GLN A 300  ILE A 304  1  O  GLN A 300   N  ARG A 279           
SHEET    1 AA2 2 LEU A 151  PRO A 153  0                                        
SHEET    2 AA2 2 LEU A 170  HIS A 172 -1  O  VAL A 171   N  VAL A 152           
SHEET    1 AA3 2 MET A 379  GLN A 381  0                                        
SHEET    2 AA3 2 TRP A 387  LEU A 389 -1  O  LEU A 388   N  VAL A 380           
SHEET    1 AA4 7 TYR B  76  GLY B  84  0                                        
SHEET    2 AA4 7 ASN B 109  ALA B 117 -1  O  ILE B 114   N  THR B  79           
SHEET    3 AA4 7 ARG B 128  TRP B 134 -1  O  VAL B 131   N  ALA B 115           
SHEET    4 AA4 7 VAL B 213  HIS B 220  1  O  SER B 214   N  ILE B 130           
SHEET    5 AA4 7 VAL B 250  PHE B 255  1  O  THR B 251   N  VAL B 217           
SHEET    6 AA4 7 LEU B 275  ASN B 282  1  O  LEU B 278   N  ALA B 252           
SHEET    7 AA4 7 GLN B 300  ILE B 304  1  O  GLN B 300   N  ARG B 279           
SHEET    1 AA5 2 LEU B 151  PRO B 153  0                                        
SHEET    2 AA5 2 LEU B 170  HIS B 172 -1  O  VAL B 171   N  VAL B 152           
SHEET    1 AA6 2 MET B 379  GLN B 381  0                                        
SHEET    2 AA6 2 TRP B 387  LEU B 389 -1  O  LEU B 388   N  VAL B 380           
SHEET    1 AA7 7 TYR C  76  GLY C  84  0                                        
SHEET    2 AA7 7 ASN C 109  ALA C 117 -1  O  ILE C 114   N  THR C  79           
SHEET    3 AA7 7 ARG C 128  TRP C 134 -1  O  VAL C 131   N  ALA C 115           
SHEET    4 AA7 7 VAL C 213  HIS C 220  1  O  THR C 216   N  ILE C 130           
SHEET    5 AA7 7 VAL C 250  PHE C 255  1  O  THR C 251   N  ILE C 215           
SHEET    6 AA7 7 LEU C 275  ASN C 282  1  O  HIS C 276   N  ALA C 252           
SHEET    7 AA7 7 GLN C 300  ILE C 304  1  O  GLN C 300   N  ARG C 279           
SHEET    1 AA8 2 LEU C 151  PRO C 153  0                                        
SHEET    2 AA8 2 LEU C 170  HIS C 172 -1  O  VAL C 171   N  VAL C 152           
SHEET    1 AA9 7 TYR D  76  GLY D  84  0                                        
SHEET    2 AA9 7 ASN D 109  ALA D 117 -1  O  ILE D 114   N  THR D  79           
SHEET    3 AA9 7 ARG D 128  TRP D 134 -1  O  VAL D 131   N  ALA D 115           
SHEET    4 AA9 7 VAL D 213  HIS D 220  1  O  THR D 216   N  ILE D 130           
SHEET    5 AA9 7 VAL D 250  PHE D 255  1  O  THR D 251   N  ILE D 215           
SHEET    6 AA9 7 LEU D 275  ASN D 282  1  O  LEU D 278   N  ALA D 252           
SHEET    7 AA9 7 GLN D 300  ILE D 304  1  O  GLN D 300   N  ARG D 279           
SHEET    1 AB1 2 LEU D 151  PRO D 153  0                                        
SHEET    2 AB1 2 LEU D 170  HIS D 172 -1  O  VAL D 171   N  VAL D 152           
SHEET    1 AB2 2 MET D 379  GLN D 381  0                                        
SHEET    2 AB2 2 TRP D 387  LEU D 389 -1  O  LEU D 388   N  VAL D 380           
CISPEP   1 ASN A   22    PRO A   23          0         0.81                     
CISPEP   2 TYR A  290    PRO A  291          0        -5.44                     
CISPEP   3 PRO A  314    PRO A  315          0        -0.14                     
CISPEP   4 ASN B   22    PRO B   23          0         2.04                     
CISPEP   5 TYR B  290    PRO B  291          0        -5.46                     
CISPEP   6 PRO B  314    PRO B  315          0        -4.86                     
CISPEP   7 ASN C   22    PRO C   23          0         0.26                     
CISPEP   8 TYR C  290    PRO C  291          0        -5.20                     
CISPEP   9 PRO C  314    PRO C  315          0        -2.14                     
CISPEP  10 ASN D   22    PRO D   23          0         0.40                     
CISPEP  11 TYR D  290    PRO D  291          0        -3.67                     
CISPEP  12 PRO D  314    PRO D  315          0        -0.98                     
CRYST1  102.313   59.568  147.319  90.00  90.14  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009774  0.000000  0.000024        0.00000                         
SCALE2      0.000000  0.016788  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006788        0.00000                         
TER    3117      PHE A 397                                                      
TER    6219      PHE B 397                                                      
TER    9313      PHE C 397                                                      
TER   12415      PHE D 397                                                      
MASTER      341    0    4   60   42    0    0    612939    4   20  124          
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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