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LongText Report for: 7f5w-pdb

Name Class
7f5w-pdb
HEADER    PLANT PROTEIN                           23-JUN-21   7F5W              
TITLE     CONSERVED AND DIVERGENT STRIGOLACTONE SIGNALING IN SACCHARUM          
TITLE    2 SPONTANEUM                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HIGH TILLERING AND DWARF 2 PROTEIN;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHARUM HYBRID CULTIVAR ROC22;                
SOURCE   3 ORGANISM_TAXID: 676074;                                              
SOURCE   4 GENE: HTD2;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 866768                                      
KEYWDS    HYDROLASE PROTEIN DWARF 14 SL RECEPTOR, PLANT PROTEIN                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.Q.ZHAO,Z.H.MING                                                     
REVDAT   1   04-MAY-22 7F5W    0                                                
JRNL        AUTH   A.HU,Q.ZHAO,L.CHEN,J.ZHAO,Y.WANG,K.FENG,L.WU,M.XIE,X.ZHOU,   
JRNL        AUTH 2 L.XIAO,Z.MING,M.ZHANG,R.YAO                                  
JRNL        TITL   IDENTIFICATION OF CONSERVED AND DIVERGENT STRIGOLACTONE      
JRNL        TITL 2 RECEPTORS IN SUGARCANE REVEALS A KEY RESIDUE CRUCIAL FOR     
JRNL        TITL 3 PLANT BRANCHING CONTROL.                                     
JRNL        REF    FRONT PLANT SCI               V.  12 47160 2021              
JRNL        REFN                   ESSN 1664-462X                               
JRNL        PMID   34858455                                                     
JRNL        DOI    10.3389/FPLS.2021.747160                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.15_3459                                     
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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.81                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 110054                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.440                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3790                            
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  4.9665 -  4.9627    0.99     4186   147  0.1680 0.1771        
REMARK   3     2  4.9627 -  3.9391    1.00     4238   154  0.1410 0.1613        
REMARK   3     3  3.9391 -  3.4412    0.89     3667   132  0.1565 0.2187        
REMARK   3     4  3.4412 -  3.1266    0.99     3996   147  0.1717 0.2279        
REMARK   3     5  3.1266 -  2.9025    1.00     4220   152  0.1771 0.2024        
REMARK   3     6  2.9025 -  2.7313    1.00     4191   144  0.1864 0.2479        
REMARK   3     7  2.7313 -  2.5945    1.00     4240   152  0.1840 0.2222        
REMARK   3     8  2.5945 -  2.4816    1.00     4256   153  0.1903 0.2020        
REMARK   3     9  2.4816 -  2.3861    1.00     4195   143  0.1907 0.2548        
REMARK   3    10  2.3861 -  2.3037    1.00     4226   150  0.1790 0.2144        
REMARK   3    11  2.3037 -  2.2317    1.00     4197   151  0.1965 0.2523        
REMARK   3    12  2.2317 -  2.1679    1.00     4239   151  0.1950 0.2393        
REMARK   3    13  2.1679 -  2.1108    1.00     4183   150  0.1923 0.1935        
REMARK   3    14  2.1108 -  2.0593    0.91      918    31  0.2016 0.2350        
REMARK   3    15  2.0593 -  2.0125    0.99     3601   128  0.2272 0.2543        
REMARK   3    16  2.0125 -  1.9697    1.00     4184   154  0.2292 0.2543        
REMARK   3    17  1.9697 -  1.9303    1.00     4263   150  0.2333 0.2565        
REMARK   3    18  1.9303 -  1.8938    0.38     1599    55  0.2523 0.2965        
REMARK   3    19  1.8938 -  1.8600    1.00     4173   148  0.2596 0.2792        
REMARK   3    20  1.8600 -  1.8285    0.99     4181   153  0.2762 0.3508        
REMARK   3    21  1.8285 -  1.7990    1.00     4223   153  0.2866 0.3566        
REMARK   3    22  1.7990 -  1.7713    1.00     4203   151  0.2945 0.3196        
REMARK   3    23  1.7713 -  1.7452    1.00     4203   146  0.3134 0.4001        
REMARK   3    24  1.7452 -  1.7207    0.99     4242   153  0.3215 0.3507        
REMARK   3    25  1.7207 -  1.6974    0.99     4173   150  0.3167 0.3315        
REMARK   3    26  1.6974 -  1.6754    0.98     4151   140  0.3402 0.4174        
REMARK   3    27  1.6754 -  1.6544    0.98     4116   152  0.3477 0.3982        
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)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.810           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.35                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4898   2.9856  -4.7336              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0834 T22:   0.1121                                     
REMARK   3      T33:   0.1126 T12:   0.0232                                     
REMARK   3      T13:  -0.0113 T23:  -0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1212 L22:   0.4140                                     
REMARK   3      L33:   0.4720 L12:   0.1350                                     
REMARK   3      L13:  -0.1864 L23:  -0.1198                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0489 S12:  -0.0062 S13:  -0.0100                       
REMARK   3      S21:  -0.0506 S22:   0.0513 S23:  -0.0439                       
REMARK   3      S31:   0.1244 S32:   0.0226 S33:   0.0049                       
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 7F5W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUN-21.                  
REMARK 100 THE DEPOSITION ID IS D_1300022939.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-SEP-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979183                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 110054                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.810                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : 6.144                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 3VXK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01 M MAGNESIUM CHLORIDE HEXAHYDRATE,   
REMARK 280  0.05 M TRIS HYDROCHLORIDE PH 7.5, 5% V/V 2-PROPANOL, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 289K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.40500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.26050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.14750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.26050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.40500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.14750            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -39                                                      
REMARK 465     LEU A   -38                                                      
REMARK 465     ARG A   -37                                                      
REMARK 465     SER A   -36                                                      
REMARK 465     THR A   -35                                                      
REMARK 465     HIS A   -34                                                      
REMARK 465     SER A   -33                                                      
REMARK 465     PRO A   -32                                                      
REMARK 465     SER A   -31                                                      
REMARK 465     GLY A   -30                                                      
REMARK 465     SER A   -29                                                      
REMARK 465     SER A   -28                                                      
REMARK 465     SER A   -27                                                      
REMARK 465     ALA A   -26                                                      
REMARK 465     ALA A   -25                                                      
REMARK 465     PRO A   -24                                                      
REMARK 465     ALA A   -23                                                      
REMARK 465     SER A   -22                                                      
REMARK 465     SER A   -21                                                      
REMARK 465     SER A   -20                                                      
REMARK 465     SER A   -19                                                      
REMARK 465     ASP A   -18                                                      
REMARK 465     ALA A   -17                                                      
REMARK 465     ALA A   -16                                                      
REMARK 465     MET A   -15                                                      
REMARK 465     VAL A   -14                                                      
REMARK 465     GLY A   -13                                                      
REMARK 465     GLY A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     ALA A    -9                                                      
REMARK 465     ALA A    -8                                                      
REMARK 465     ALA A    -7                                                      
REMARK 465     ALA A    -6                                                      
REMARK 465     ALA A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     MET B   -39                                                      
REMARK 465     LEU B   -38                                                      
REMARK 465     ARG B   -37                                                      
REMARK 465     SER B   -36                                                      
REMARK 465     THR B   -35                                                      
REMARK 465     HIS B   -34                                                      
REMARK 465     SER B   -33                                                      
REMARK 465     PRO B   -32                                                      
REMARK 465     SER B   -31                                                      
REMARK 465     GLY B   -30                                                      
REMARK 465     SER B   -29                                                      
REMARK 465     SER B   -28                                                      
REMARK 465     SER B   -27                                                      
REMARK 465     ALA B   -26                                                      
REMARK 465     ALA B   -25                                                      
REMARK 465     PRO B   -24                                                      
REMARK 465     ALA B   -23                                                      
REMARK 465     SER B   -22                                                      
REMARK 465     SER B   -21                                                      
REMARK 465     SER B   -20                                                      
REMARK 465     SER B   -19                                                      
REMARK 465     ASP B   -18                                                      
REMARK 465     ALA B   -17                                                      
REMARK 465     ALA B   -16                                                      
REMARK 465     MET B   -15                                                      
REMARK 465     VAL B   -14                                                      
REMARK 465     GLY B   -13                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     ALA B    -9                                                      
REMARK 465     ALA B    -8                                                      
REMARK 465     ALA B    -7                                                      
REMARK 465     ALA B    -6                                                      
REMARK 465     ALA B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     SER B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     ALA B     0                                                      
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   OE2  GLU B   174     O    HOH B   301              1.82            
REMARK 500   NH1  ARG A    47     O    HOH A   301              1.93            
REMARK 500   O    HOH B   449     O    HOH B   475              1.99            
REMARK 500   O    HOH A   356     O    HOH A   438              2.01            
REMARK 500   O    HOH A   465     O    HOH A   472              2.02            
REMARK 500   O    PRO B     1     O    HOH B   302              2.04            
REMARK 500   O    HOH A   452     O    HOH A   473              2.05            
REMARK 500   ND1  HIS A   133     O    HOH A   302              2.05            
REMARK 500   O    HOH A   385     O    HOH A   427              2.07            
REMARK 500   NH1  ARG B   262     O    HOH B   303              2.08            
REMARK 500   OH   TYR B   159     O    HOH B   304              2.19            
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   OE2  GLU A   140     NH1  ARG A   230     4545     1.90            
REMARK 500   O    HOH A   457     O    HOH B   412     4455     1.97            
REMARK 500   O    HOH A   461     O    HOH B   446     2555     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 230   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  97     -123.23     62.83                                   
REMARK 500    ARG A 125      127.37   -172.16                                   
REMARK 500    ASP A 129       85.55   -166.29                                   
REMARK 500    ASN A 130     -110.38     56.13                                   
REMARK 500    ASN A 151       83.12   -154.70                                   
REMARK 500    ASN B  17       29.05   -146.91                                   
REMARK 500    SER B  97     -123.39     66.29                                   
REMARK 500    GLN B 243       20.94    -78.40                                   
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 B 484        DISTANCE =  5.95 ANGSTROMS                       
DBREF1 7F5W A  -39   268  UNP                  A0A0D5NT23_9POAL                 
DBREF2 7F5W A     A0A0D5NT23                          1         308             
DBREF1 7F5W B  -39   268  UNP                  A0A0D5NT23_9POAL                 
DBREF2 7F5W B     A0A0D5NT23                          1         308             
SEQRES   1 A  308  MET LEU ARG SER THR HIS SER PRO SER GLY SER SER SER          
SEQRES   2 A  308  ALA ALA PRO ALA SER SER SER SER ASP ALA ALA MET VAL          
SEQRES   3 A  308  GLY GLY GLY GLY ALA ALA ALA ALA ALA GLY SER GLY GLY          
SEQRES   4 A  308  ALA PRO SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL          
SEQRES   5 A  308  ARG VAL VAL GLY ASN GLY ASP ARG VAL VAL VAL LEU SER          
SEQRES   6 A  308  HIS GLY PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL          
SEQRES   7 A  308  LEU PRO TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR          
SEQRES   8 A  308  ASP LEU VAL CYS ALA GLY SER VAL ASN PRO GLU HIS PHE          
SEQRES   9 A  308  ASP PHE ARG ARG TYR ASP THR LEU ASP SER TYR VAL ASP          
SEQRES  10 A  308  ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG          
SEQRES  11 A  308  CYS ALA PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY          
SEQRES  12 A  308  ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE ALA LYS          
SEQRES  13 A  308  LEU VAL LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP          
SEQRES  14 A  308  ASN ASP TYR HIS GLY GLY PHE GLU LEU PRO GLU ILE GLN          
SEQRES  15 A  308  GLN VAL PHE ASP ALA MET ALA ALA ASN TYR SER ALA TRP          
SEQRES  16 A  308  ALA VAL GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL          
SEQRES  17 A  308  PRO ALA ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN          
SEQRES  18 A  308  MET ARG PRO ASP ILE SER LEU HIS VAL CYS ARG THR VAL          
SEQRES  19 A  308  PHE ASN THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG          
SEQRES  20 A  308  SER PRO CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER          
SEQRES  21 A  308  VAL PRO ALA SER VAL ALA ALA TYR LEU ARG ALA HIS LEU          
SEQRES  22 A  308  GLY GLY ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY          
SEQRES  23 A  308  HIS LEU PRO HIS LEU SER ALA PRO GLY LEU LEU ALA GLN          
SEQRES  24 A  308  VAL LEU ARG ARG ALA LEU ALA ARG TYR                          
SEQRES   1 B  308  MET LEU ARG SER THR HIS SER PRO SER GLY SER SER SER          
SEQRES   2 B  308  ALA ALA PRO ALA SER SER SER SER ASP ALA ALA MET VAL          
SEQRES   3 B  308  GLY GLY GLY GLY ALA ALA ALA ALA ALA GLY SER GLY GLY          
SEQRES   4 B  308  ALA PRO SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL          
SEQRES   5 B  308  ARG VAL VAL GLY ASN GLY ASP ARG VAL VAL VAL LEU SER          
SEQRES   6 B  308  HIS GLY PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL          
SEQRES   7 B  308  LEU PRO TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR          
SEQRES   8 B  308  ASP LEU VAL CYS ALA GLY SER VAL ASN PRO GLU HIS PHE          
SEQRES   9 B  308  ASP PHE ARG ARG TYR ASP THR LEU ASP SER TYR VAL ASP          
SEQRES  10 B  308  ASP LEU LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG          
SEQRES  11 B  308  CYS ALA PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY          
SEQRES  12 B  308  ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE ALA LYS          
SEQRES  13 B  308  LEU VAL LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP          
SEQRES  14 B  308  ASN ASP TYR HIS GLY GLY PHE GLU LEU PRO GLU ILE GLN          
SEQRES  15 B  308  GLN VAL PHE ASP ALA MET ALA ALA ASN TYR SER ALA TRP          
SEQRES  16 B  308  ALA VAL GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL          
SEQRES  17 B  308  PRO ALA ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN          
SEQRES  18 B  308  MET ARG PRO ASP ILE SER LEU HIS VAL CYS ARG THR VAL          
SEQRES  19 B  308  PHE ASN THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG          
SEQRES  20 B  308  SER PRO CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER          
SEQRES  21 B  308  VAL PRO ALA SER VAL ALA ALA TYR LEU ARG ALA HIS LEU          
SEQRES  22 B  308  GLY GLY ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY          
SEQRES  23 B  308  HIS LEU PRO HIS LEU SER ALA PRO GLY LEU LEU ALA GLN          
SEQRES  24 B  308  VAL LEU ARG ARG ALA LEU ALA ARG TYR                          
FORMUL   3  HOH   *357(H2 O)                                                    
HELIX    1 AA1 SER A    2  LEU A   10  1                                   9    
HELIX    2 AA2 ASP A   31  SER A   36  5                                   6    
HELIX    3 AA3 VAL A   38  LEU A   42  5                                   5    
HELIX    4 AA4 ASN A   60  PHE A   64  5                                   5    
HELIX    5 AA5 ARG A   67  ASP A   70  5                                   4    
HELIX    6 AA6 THR A   71  LEU A   86  1                                  16    
HELIX    7 AA7 SER A   97  ARG A  110  1                                  14    
HELIX    8 AA8 GLU A  137  ASN A  151  1                                  15    
HELIX    9 AA9 ASN A  151  GLY A  165  1                                  15    
HELIX   10 AB1 VAL A  168  MET A  182  1                                  15    
HELIX   11 AB2 ARG A  183  ASN A  196  1                                  14    
HELIX   12 AB3 LEU A  199  VAL A  206  5                                   8    
HELIX   13 AB4 ALA A  223  LEU A  233  1                                  11    
HELIX   14 AB5 LEU A  248  ALA A  253  1                                   6    
HELIX   15 AB6 ALA A  253  LEU A  265  1                                  13    
HELIX   16 AB7 SER B    2  LEU B   10  1                                   9    
HELIX   17 AB8 ASP B   31  SER B   36  5                                   6    
HELIX   18 AB9 VAL B   38  LEU B   42  5                                   5    
HELIX   19 AC1 ASN B   60  PHE B   64  5                                   5    
HELIX   20 AC2 ARG B   67  ASP B   70  5                                   4    
HELIX   21 AC3 THR B   71  LEU B   86  1                                  16    
HELIX   22 AC4 SER B   97  ARG B  110  1                                  14    
HELIX   23 AC5 GLU B  137  ASN B  151  1                                  15    
HELIX   24 AC6 ASN B  151  GLY B  165  1                                  15    
HELIX   25 AC7 VAL B  168  ASN B  181  1                                  14    
HELIX   26 AC8 ARG B  183  ASN B  196  1                                  14    
HELIX   27 AC9 LEU B  199  VAL B  206  5                                   8    
HELIX   28 AD1 PRO B  222  LEU B  233  1                                  12    
HELIX   29 AD2 LEU B  248  ALA B  253  1                                   6    
HELIX   30 AD3 ALA B  253  LEU B  265  1                                  13    
SHEET    1 AA1 7 ARG A  13  GLY A  16  0                                        
SHEET    2 AA1 7 ARG A  47  LEU A  50 -1  O  VAL A  48   N  VAL A  15           
SHEET    3 AA1 7 VAL A  21  SER A  25  1  N  VAL A  22   O  VAL A  49           
SHEET    4 AA1 7 CYS A  91  HIS A  96  1  O  VAL A  94   N  VAL A  23           
SHEET    5 AA1 7 PHE A 114  ILE A 120  1  O  ILE A 120   N  GLY A  95           
SHEET    6 AA1 7 CYS A 210  THR A 215  1  O  VAL A 213   N  LEU A 119           
SHEET    7 AA1 7 THR A 237  LEU A 242  1  O  GLU A 240   N  GLN A 214           
SHEET    1 AA2 7 ARG B  13  VAL B  15  0                                        
SHEET    2 AA2 7 HIS B  46  LEU B  50 -1  O  VAL B  48   N  VAL B  15           
SHEET    3 AA2 7 ARG B  20  SER B  25  1  N  ARG B  20   O  ARG B  47           
SHEET    4 AA2 7 CYS B  91  HIS B  96  1  O  VAL B  94   N  VAL B  23           
SHEET    5 AA2 7 PHE B 114  ILE B 120  1  O  ALA B 115   N  CYS B  91           
SHEET    6 AA2 7 CYS B 210  GLN B 214  1  O  VAL B 213   N  LEU B 119           
SHEET    7 AA2 7 THR B 237  PHE B 241  1  O  GLU B 240   N  GLN B 214           
CRYST1   48.810   88.295  118.521  90.00  90.00  90.00 P 21 21 21    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      0.020488  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011326  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008437        0.00000                         
TER    2079      TYR A 268                                                      
TER    4153      TYR B 268                                                      
MASTER      420    0    0   30   14    0    0    6 4508    2    0   48          
END                                                                             

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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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