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LongText Report for: 5tnf-pdb

Name Class
5tnf-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           14-OCT-16   5TNF              
TITLE     CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR   
TITLE    2 CIF CONTAINING THE ADDUCTED 19,20-EPDPE HYDROLYSIS INTERMEDIATE      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CFTR INHIBITORY FACTOR;                                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN UCBPP-PA14);     
SOURCE   3 ORGANISM_TAXID: 208963;                                              
SOURCE   4 STRAIN: UCBPP-PA14;                                                  
SOURCE   5 GENE: PA14_26090;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TOP10                                      
KEYWDS    EPOXIDE HYDROLASE, HYDROXYALKYL-ENZYME INTERMEDIATE, HYDROLASE-       
KEYWDS   2 HYDROLASE INHIBITOR COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.L.HVORECNY,D.R.MADDEN                                               
REVDAT   1   11-OCT-17 5TNF    0                                                
JRNL        AUTH   K.L.HVORECNY,C.D.BAHL,S.KITAMURA,K.S.S.LEE,B.D.HAMMOCK,      
JRNL        AUTH 2 C.MORISSEAU,D.R.MADDEN                                       
JRNL        TITL   ACTIVE-SITE FLEXIBILITY AND SUBSTRATE SPECIFICITY IN A       
JRNL        TITL 2 BACTERIAL VIRULENCE FACTOR: CRYSTALLOGRAPHIC SNAPSHOTS OF AN 
JRNL        TITL 3 EPOXIDE HYDROLASE.                                           
JRNL        REF    STRUCTURE                     V.  25   697 2017              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   28392259                                                     
JRNL        DOI    10.1016/J.STR.2017.03.002                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.16                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 120849                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.148                           
REMARK   3   R VALUE            (WORKING SET) : 0.146                           
REMARK   3   FREE R VALUE                     : 0.175                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6053                            
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  1.7699 -  1.7500    0.96     3637   297  0.1668 0.2060        
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)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.320           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.006          10032                                  
REMARK   3   ANGLE     :  0.816          13634                                  
REMARK   3   CHIRALITY :  0.052           1395                                  
REMARK   3   PLANARITY :  0.006           1790                                  
REMARK   3   DIHEDRAL  : 16.028           5958                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 25:321 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7867  11.9910 -27.3390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0824 T22:   0.0869                                     
REMARK   3      T33:   0.0627 T12:  -0.0025                                     
REMARK   3      T13:   0.0049 T23:  -0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8616 L22:   0.8283                                     
REMARK   3      L33:   0.7585 L12:   0.0452                                     
REMARK   3      L13:   0.1643 L23:   0.0164                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0128 S12:   0.0995 S13:  -0.0919                       
REMARK   3      S21:  -0.0765 S22:  -0.0143 S23:  -0.0515                       
REMARK   3      S31:   0.1007 S32:   0.0402 S33:   0.0060                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 25:321 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  31.0493  51.7358 -15.7387              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0890 T22:   0.0770                                     
REMARK   3      T33:   0.1019 T12:  -0.0181                                     
REMARK   3      T13:  -0.0213 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0975 L22:   1.2267                                     
REMARK   3      L33:   0.6600 L12:   0.3980                                     
REMARK   3      L13:   0.0147 L23:   0.1012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0222 S12:  -0.0215 S13:   0.1472                       
REMARK   3      S21:   0.0407 S22:   0.0127 S23:  -0.0562                       
REMARK   3      S31:  -0.1107 S32:   0.0253 S33:   0.0052                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 25:321 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5768  44.9447 -27.2865              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0807 T22:   0.0782                                     
REMARK   3      T33:   0.1096 T12:  -0.0040                                     
REMARK   3      T13:   0.0014 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8369 L22:   1.0941                                     
REMARK   3      L33:   0.8324 L12:  -0.0075                                     
REMARK   3      L13:  -0.0510 L23:  -0.0218                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0161 S12:   0.0489 S13:   0.1511                       
REMARK   3      S21:  -0.0618 S22:  -0.0267 S23:   0.1001                       
REMARK   3      S31:  -0.1103 S32:  -0.0495 S33:   0.0103                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 25:321 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8947   5.2015 -15.7423              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0894 T22:   0.0961                                     
REMARK   3      T33:   0.0637 T12:  -0.0268                                     
REMARK   3      T13:   0.0118 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0852 L22:   1.0014                                     
REMARK   3      L33:   0.5982 L12:   0.2939                                     
REMARK   3      L13:  -0.0981 L23:  -0.1411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0180 S12:  -0.0701 S13:  -0.0822                       
REMARK   3      S21:   0.0145 S22:  -0.0208 S23:   0.0840                       
REMARK   3      S31:   0.0686 S32:  -0.0037 S33:   0.0047                       
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 5TNF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222797.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS DEC 6, 2010                    
REMARK 200  DATA SCALING SOFTWARE          : XDS DEC 6, 2010                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 120855                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.158                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 5.750                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 20.7600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.79                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.240                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.10_2155: ???                                 
REMARK 200 STARTING MODEL: 3KD2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PH5 CALCIUM CHLORIDE     
REMARK 280  PEG 8000, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       84.27550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.96100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.27550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.96100            
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: 2780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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: 2770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     HIS B   322                                                      
REMARK 465     HIS B   323                                                      
REMARK 465     HIS B   324                                                      
REMARK 465     HIS B   325                                                      
REMARK 465     HIS C   322                                                      
REMARK 465     HIS C   323                                                      
REMARK 465     HIS C   324                                                      
REMARK 465     HIS C   325                                                      
REMARK 465     HIS D   322                                                      
REMARK 465     HIS D   323                                                      
REMARK 465     HIS D   324                                                      
REMARK 465     HIS D   325                                                      
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   NH1  ARG B   319     O    HOH B   501              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   703     O    HOH A   703     2554     2.03            
REMARK 500   NH2  ARG B   163     OE1  GLU C   285     2554     2.17            
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    ASP A 129     -130.79     60.40                                   
REMARK 500    ALA A 154      144.20   -174.59                                   
REMARK 500    CYS A 303       55.91   -141.81                                   
REMARK 500    THR B  99      -65.41    -94.42                                   
REMARK 500    ASP B 129     -130.23     58.63                                   
REMARK 500    ALA B 154      143.78   -174.28                                   
REMARK 500    CYS B 303       55.18   -141.77                                   
REMARK 500    ASP C 129     -129.42     60.42                                   
REMARK 500    ALA C 154      144.69   -172.33                                   
REMARK 500    ASP C 185       19.73     59.74                                   
REMARK 500    CYS C 303       56.65   -141.88                                   
REMARK 500    THR D  99      -65.56    -92.93                                   
REMARK 500    ASP D 129     -129.01     57.22                                   
REMARK 500    ALA D 154      144.60   -174.75                                   
REMARK 500    CYS D 303       53.13   -141.71                                   
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 768        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH C 762        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH D 779        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH D 780        DISTANCE =  6.26 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7HW A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7HW B 401 and ASP B    
REMARK 800  129                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7HW C 401 and ASP C    
REMARK 800  129                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7HW D 401 and ASP D    
REMARK 800  129                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KD2, 4DMC   RELATED DB: PDB                             
REMARK 900 3KD2 - WILD TYPE VERSION OF THE CURRENT SUBMISSION 4DMC - APO        
REMARK 900 VERSION OF SAME PROTEIN AS CURRENT SUBMISSION (CIF WITH E153Q        
REMARK 900 MUTATION)                                                            
DBREF1 5TNF A   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNF A     A0A0M3KL26                          1         301             
DBREF1 5TNF B   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNF B     A0A0M3KL26                          1         301             
DBREF1 5TNF C   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNF C     A0A0M3KL26                          1         301             
DBREF1 5TNF D   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNF D     A0A0M3KL26                          1         301             
SEQADV 5TNF GLN A  153  UNP  A0A0M3KL2 GLU   129 ENGINEERED MUTATION            
SEQADV 5TNF GLN B  153  UNP  A0A0M3KL2 GLU   129 ENGINEERED MUTATION            
SEQADV 5TNF GLN C  153  UNP  A0A0M3KL2 GLU   129 ENGINEERED MUTATION            
SEQADV 5TNF GLN D  153  UNP  A0A0M3KL2 GLU   129 ENGINEERED MUTATION            
SEQRES   1 A  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 A  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 A  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 A  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 A  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 A  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 A  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 A  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 A  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 A  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA          
SEQRES  11 A  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 A  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 A  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 A  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 A  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 A  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 A  301  ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER          
SEQRES  18 A  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 A  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 A  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 A  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 A  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 A  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 A  301  HIS HIS                                                      
SEQRES   1 B  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 B  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 B  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 B  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 B  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 B  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 B  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 B  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 B  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 B  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA          
SEQRES  11 B  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 B  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 B  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 B  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 B  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 B  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 B  301  ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER          
SEQRES  18 B  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 B  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 B  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 B  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 B  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 B  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 B  301  HIS HIS                                                      
SEQRES   1 C  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 C  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 C  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 C  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 C  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 C  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 C  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 C  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 C  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 C  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA          
SEQRES  11 C  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 C  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 C  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 C  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 C  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 C  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 C  301  ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER          
SEQRES  18 C  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 C  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 C  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 C  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 C  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 C  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 C  301  HIS HIS                                                      
SEQRES   1 D  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 D  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 D  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 D  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 D  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 D  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 D  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 D  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 D  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 D  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA          
SEQRES  11 D  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 D  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 D  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 D  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 D  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 D  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 D  301  ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER          
SEQRES  18 D  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 D  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 D  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 D  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 D  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 D  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 D  301  HIS HIS                                                      
HET    7HW  A 401      25                                                       
HET    7HW  B 401      25                                                       
HET    7HW  C 401      25                                                       
HET    7HW  D 401      25                                                       
HETNAM     7HW (4Z,7Z,10Z,13Z,16Z,19R,20R)-19,20-DIHYDROXYDOCOSA-4,7,           
HETNAM   2 7HW  10,13,16-PENTAENOIC ACID                                        
FORMUL   5  7HW    4(C22 H34 O4)                                                
FORMUL   9  HOH   *1065(H2 O)                                                   
HELIX    1 AA1 THR A   66  HIS A   71  5                                   6    
HELIX    2 AA2 LEU A   73  ALA A   78  1                                   6    
HELIX    3 AA3 SER A  102  SER A  118  1                                  17    
HELIX    4 AA4 ASP A  129  ASN A  134  1                                   6    
HELIX    5 AA5 THR A  135  ASN A  142  1                                   8    
HELIX    6 AA6 ASP A  158  PHE A  164  5                                   7    
HELIX    7 AA7 TRP A  176  ALA A  183  1                                   8    
HELIX    8 AA8 ARG A  186  ALA A  193  1                                   8    
HELIX    9 AA9 LYS A  195  HIS A  207  1                                  13    
HELIX   10 AB1 ASN A  210  PHE A  214  5                                   5    
HELIX   11 AB2 SER A  215  ALA A  227  1                                  13    
HELIX   12 AB3 LYS A  228  ALA A  241  1                                  14    
HELIX   13 AB4 ALA A  241  ALA A  253  1                                  13    
HELIX   14 AB5 THR A  274  ALA A  284  1                                  11    
HELIX   15 AB6 TRP A  298  CYS A  303  1                                   6    
HELIX   16 AB7 CYS A  303  ARG A  317  1                                  15    
HELIX   17 AB8 THR B   66  HIS B   71  5                                   6    
HELIX   18 AB9 GLN B   72  ALA B   78  1                                   7    
HELIX   19 AC1 SER B  102  SER B  118  1                                  17    
HELIX   20 AC2 ASP B  129  ASN B  134  1                                   6    
HELIX   21 AC3 THR B  135  ASN B  142  1                                   8    
HELIX   22 AC4 ASP B  158  PHE B  164  5                                   7    
HELIX   23 AC5 TRP B  176  ALA B  183  1                                   8    
HELIX   24 AC6 ARG B  186  ALA B  193  1                                   8    
HELIX   25 AC7 LYS B  195  HIS B  207  1                                  13    
HELIX   26 AC8 ASN B  210  PHE B  214  5                                   5    
HELIX   27 AC9 SER B  215  LYS B  228  1                                  14    
HELIX   28 AD1 LYS B  228  ALA B  241  1                                  14    
HELIX   29 AD2 ALA B  241  ALA B  253  1                                  13    
HELIX   30 AD3 THR B  274  ALA B  284  1                                  11    
HELIX   31 AD4 TRP B  298  CYS B  303  1                                   6    
HELIX   32 AD5 CYS B  303  ARG B  317  1                                  15    
HELIX   33 AD6 THR C   66  HIS C   71  5                                   6    
HELIX   34 AD7 LEU C   73  ALA C   78  1                                   6    
HELIX   35 AD8 SER C  102  SER C  118  1                                  17    
HELIX   36 AD9 ASP C  129  ASN C  134  1                                   6    
HELIX   37 AE1 THR C  135  ASN C  142  1                                   8    
HELIX   38 AE2 ASP C  158  PHE C  164  5                                   7    
HELIX   39 AE3 TRP C  176  ALA C  183  1                                   8    
HELIX   40 AE4 ARG C  186  ALA C  193  1                                   8    
HELIX   41 AE5 LYS C  195  HIS C  207  1                                  13    
HELIX   42 AE6 ASN C  210  PHE C  214  5                                   5    
HELIX   43 AE7 SER C  215  ALA C  227  1                                  13    
HELIX   44 AE8 LYS C  228  ALA C  241  1                                  14    
HELIX   45 AE9 ALA C  241  ALA C  253  1                                  13    
HELIX   46 AF1 THR C  274  ALA C  284  1                                  11    
HELIX   47 AF2 TRP C  298  CYS C  303  1                                   6    
HELIX   48 AF3 CYS C  303  SER C  316  1                                  14    
HELIX   49 AF4 THR D   66  HIS D   71  5                                   6    
HELIX   50 AF5 GLN D   72  ALA D   78  1                                   7    
HELIX   51 AF6 SER D  102  SER D  118  1                                  17    
HELIX   52 AF7 ASP D  129  ASN D  134  1                                   6    
HELIX   53 AF8 THR D  135  ASN D  142  1                                   8    
HELIX   54 AF9 ASP D  158  PHE D  164  5                                   7    
HELIX   55 AG1 TRP D  176  ALA D  183  1                                   8    
HELIX   56 AG2 ARG D  186  ALA D  193  1                                   8    
HELIX   57 AG3 LYS D  195  HIS D  207  1                                  13    
HELIX   58 AG4 ASN D  210  PHE D  214  5                                   5    
HELIX   59 AG5 SER D  215  ALA D  227  1                                  13    
HELIX   60 AG6 LYS D  228  ALA D  241  1                                  14    
HELIX   61 AG7 ALA D  241  ALA D  253  1                                  13    
HELIX   62 AG8 THR D  274  ALA D  282  1                                   9    
HELIX   63 AG9 TRP D  298  CYS D  303  1                                   6    
HELIX   64 AH1 CYS D  303  ARG D  317  1                                  15    
SHEET    1 AA1 8 GLU A  35  VAL A  41  0                                        
SHEET    2 AA1 8 VAL A  44  GLY A  52 -1  O  VAL A  44   N  VAL A  41           
SHEET    3 AA1 8 THR A  82  PRO A  86 -1  O  VAL A  83   N  GLY A  51           
SHEET    4 AA1 8 LEU A  56  VAL A  60  1  N  VAL A  57   O  THR A  82           
SHEET    5 AA1 8 PHE A 123  HIS A 128  1  O  ASP A 124   N  LEU A  56           
SHEET    6 AA1 8 ILE A 146  MET A 152  1  O  VAL A 150   N  LEU A 125           
SHEET    7 AA1 8 THR A 261  GLY A 266  1  O  MET A 262   N  TYR A 151           
SHEET    8 AA1 8 VAL A 287  LEU A 292  1  O  LEU A 292   N  ALA A 265           
SHEET    1 AA2 2 PHE A 167  THR A 168  0                                        
SHEET    2 AA2 2 GLY A 171  GLU A 172 -1  O  GLY A 171   N  THR A 168           
SHEET    1 AA3 8 PHE B  34  VAL B  41  0                                        
SHEET    2 AA3 8 VAL B  44  GLY B  52 -1  O  TYR B  48   N  ALA B  37           
SHEET    3 AA3 8 THR B  82  PRO B  86 -1  O  VAL B  83   N  GLY B  51           
SHEET    4 AA3 8 LEU B  56  VAL B  60  1  N  VAL B  57   O  THR B  82           
SHEET    5 AA3 8 PHE B 123  HIS B 128  1  O  ASP B 124   N  LEU B  56           
SHEET    6 AA3 8 ILE B 146  MET B 152  1  O  VAL B 150   N  LEU B 125           
SHEET    7 AA3 8 THR B 261  GLY B 266  1  O  MET B 262   N  LEU B 149           
SHEET    8 AA3 8 VAL B 287  LEU B 292  1  O  LEU B 292   N  ALA B 265           
SHEET    1 AA4 2 PHE B 167  THR B 168  0                                        
SHEET    2 AA4 2 GLY B 171  GLU B 172 -1  O  GLY B 171   N  THR B 168           
SHEET    1 AA5 8 GLU C  35  VAL C  41  0                                        
SHEET    2 AA5 8 VAL C  44  GLY C  52 -1  O  VAL C  44   N  VAL C  41           
SHEET    3 AA5 8 THR C  82  PRO C  86 -1  O  VAL C  83   N  GLY C  51           
SHEET    4 AA5 8 LEU C  56  VAL C  60  1  N  VAL C  57   O  THR C  82           
SHEET    5 AA5 8 PHE C 123  HIS C 128  1  O  VAL C 126   N  VAL C  60           
SHEET    6 AA5 8 ILE C 146  MET C 152  1  O  ALA C 147   N  PHE C 123           
SHEET    7 AA5 8 THR C 261  GLY C 266  1  O  MET C 262   N  TYR C 151           
SHEET    8 AA5 8 VAL C 287  LEU C 292  1  O  LEU C 292   N  ALA C 265           
SHEET    1 AA6 2 PHE C 167  THR C 168  0                                        
SHEET    2 AA6 2 GLY C 171  GLU C 172 -1  O  GLY C 171   N  THR C 168           
SHEET    1 AA7 8 PHE D  34  VAL D  41  0                                        
SHEET    2 AA7 8 VAL D  44  GLY D  52 -1  O  LEU D  46   N  ARG D  39           
SHEET    3 AA7 8 THR D  82  PRO D  86 -1  O  VAL D  83   N  GLY D  51           
SHEET    4 AA7 8 LEU D  56  VAL D  60  1  N  VAL D  57   O  THR D  82           
SHEET    5 AA7 8 PHE D 123  HIS D 128  1  O  ASP D 124   N  MET D  58           
SHEET    6 AA7 8 ILE D 146  MET D 152  1  O  VAL D 150   N  LEU D 125           
SHEET    7 AA7 8 THR D 261  GLY D 266  1  O  MET D 262   N  TYR D 151           
SHEET    8 AA7 8 VAL D 287  LEU D 292  1  O  LEU D 292   N  ALA D 265           
SHEET    1 AA8 2 PHE D 167  THR D 168  0                                        
SHEET    2 AA8 2 GLY D 171  GLU D 172 -1  O  GLY D 171   N  THR D 168           
SSBOND   1 CYS A  295    CYS A  303                          1555   1555  2.01  
SSBOND   2 CYS B  295    CYS B  303                          1555   1555  1.99  
SSBOND   3 CYS C  295    CYS C  303                          1555   1555  2.00  
SSBOND   4 CYS D  295    CYS D  303                          1555   1555  1.99  
LINK         OD1 ASP A 129                 C3  7HW A 401     1555   1555  1.42  
LINK         OD1 ASP B 129                 C3  7HW B 401     1555   1555  1.42  
LINK         OD1 ASP C 129                 C3  7HW C 401     1555   1555  1.43  
LINK         OD1 ASP D 129                 C3  7HW D 401     1555   1555  1.43  
SITE     1 AC1 13 ASP A 129  GLN A 153  ALA A 154  LEU A 174                    
SITE     2 AC1 13 HIS A 177  PHE A 178  PHE A 203  TYR A 239                    
SITE     3 AC1 13 GLY A 270  MET A 272  PHE A 275  HIS A 297                    
SITE     4 AC1 13 HOH A 556                                                     
SITE     1 AC2 19 PHE B  63  HIS B 128  ILE B 130  GLY B 131                    
SITE     2 AC2 19 ILE B 132  MET B 152  GLN B 153  ALA B 154                    
SITE     3 AC2 19 PHE B 164  VAL B 175  HIS B 177  PHE B 178                    
SITE     4 AC2 19 PHE B 203  TYR B 239  GLY B 270  GLY B 271                    
SITE     5 AC2 19 MET B 272  HIS B 297  HOH B 658                               
SITE     1 AC3 19 PHE C  63  HIS C 128  ILE C 130  GLY C 131                    
SITE     2 AC3 19 ILE C 132  MET C 152  GLN C 153  ALA C 154                    
SITE     3 AC3 19 PHE C 164  LEU C 174  HIS C 177  PHE C 178                    
SITE     4 AC3 19 PHE C 203  TYR C 239  GLY C 270  MET C 272                    
SITE     5 AC3 19 PHE C 275  HIS C 297  HOH C 642                               
SITE     1 AC4 20 ARG A 256  PHE D  63  HIS D 128  ILE D 130                    
SITE     2 AC4 20 GLY D 131  ILE D 132  MET D 152  GLN D 153                    
SITE     3 AC4 20 ALA D 154  PHE D 164  PRO D 165  LEU D 174                    
SITE     4 AC4 20 HIS D 177  PHE D 178  PHE D 203  TYR D 239                    
SITE     5 AC4 20 GLY D 270  MET D 272  HIS D 297  HOH D 680                    
CRYST1  168.551   83.922   89.678  90.00 100.35  90.00 C 1 2 1      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      0.005933  0.000000  0.001084        0.00000                         
SCALE2      0.000000  0.011916  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011336        0.00000                         
TER    2423      HIS A 321                                                      
TER    4805      HIS B 321                                                      
TER    7209      HIS C 321                                                      
TER    9615      HIS D 321                                                      
MASTER      391    0    4   64   40    0   19    610657    4  112   96          
END                                                                             

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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.
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