Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 4KYV-pdb

Name Class
4KYV-pdb
HEADER    DE NOVO PROTEIN                         29-MAY-13   4KYV              
TITLE     CRYSTAL STRUCTURE OF DEHALOGENASE HALOTAG2 WITH HALTS AT THE          
TITLE    2 RESOLUTION 1.8A. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)     
TITLE    3 TARGET OR150                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DEHALOGENASE HALOTAG2;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE   3 ORGANISM_TAXID: 32630;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;                           
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET15_NESG                                
KEYWDS    STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE,       
KEYWDS   2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, HALTS, HALOGENASE,   
KEYWDS   3 DE NOVO PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.KUZIN,S.LEW,J.SEETHARAMAN,M.MAGLAQUI,R.XIAO,E.KOHAN,H.WANG,         
AUTHOR   2 J.K.EVERETT,G.ACTON,T.B.,KORNHABER,G.T.MONTELIONE,J.F.HUNT,L.TONG,   
AUTHOR   3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)                      
REVDAT   1   24-JUL-13 4KYV    0                                                
JRNL        AUTH   A.KUZIN,S.LEW,J.SEETHARAMAN,M.MAGLAQUI,R.XIAO,E.KOHAN,       
JRNL        AUTH 2 H.WANG,J.K.EVERETT,G.ACTON,T.B.,KORNHABER,G.T.MONTELIONE,    
JRNL        AUTH 3 J.F.HUNT,L.TONG                                              
JRNL        TITL   NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR150        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1269)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.61                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.460                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 101600                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.790                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3853                            
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 29.6140 -  5.4440    0.94     3477   136  0.1580 0.1740        
REMARK   3     2  5.4440 -  4.3250    0.96     3534   147  0.1250 0.1610        
REMARK   3     3  4.3250 -  3.7800    0.97     3629   139  0.1270 0.1400        
REMARK   3     4  3.7800 -  3.4350    0.98     3649   136  0.1420 0.1380        
REMARK   3     5  3.4350 -  3.1890    0.97     3584   131  0.1450 0.1850        
REMARK   3     6  3.1890 -  3.0010    0.97     3602   151  0.1510 0.1780        
REMARK   3     7  3.0010 -  2.8510    0.98     3584   143  0.1540 0.2110        
REMARK   3     8  2.8510 -  2.7270    0.97     3597   139  0.1480 0.1730        
REMARK   3     9  2.7270 -  2.6220    0.97     3619   140  0.1490 0.2000        
REMARK   3    10  2.6220 -  2.5320    0.97     3574   144  0.1490 0.1940        
REMARK   3    11  2.5320 -  2.4520    0.96     3621   137  0.1490 0.1930        
REMARK   3    12  2.4520 -  2.3820    0.96     3469   143  0.1450 0.1640        
REMARK   3    13  2.3820 -  2.3200    0.95     3585   148  0.1460 0.1760        
REMARK   3    14  2.3200 -  2.2630    0.95     3483   131  0.1450 0.1930        
REMARK   3    15  2.2630 -  2.2120    0.94     3512   132  0.1540 0.1800        
REMARK   3    16  2.2120 -  2.1650    0.94     3445   148  0.1540 0.1920        
REMARK   3    17  2.1650 -  2.1210    0.93     3488   144  0.1590 0.2120        
REMARK   3    18  2.1210 -  2.0810    0.93     3466   119  0.1620 0.2210        
REMARK   3    19  2.0810 -  2.0440    0.93     3363   147  0.1640 0.2240        
REMARK   3    20  2.0440 -  2.0100    0.92     3509   116  0.1720 0.2060        
REMARK   3    21  2.0100 -  1.9770    0.93     3390   154  0.1690 0.2240        
REMARK   3    22  1.9770 -  1.9470    0.92     3407   120  0.1790 0.2410        
REMARK   3    23  1.9470 -  1.9180    0.91     3449   132  0.1800 0.2260        
REMARK   3    24  1.9180 -  1.8910    0.92     3333   138  0.1880 0.2370        
REMARK   3    25  1.8910 -  1.8650    0.92     3375   141  0.1900 0.2570        
REMARK   3    26  1.8650 -  1.8410    0.91     3428   121  0.1970 0.2460        
REMARK   3    27  1.8410 -  1.8180    0.91     3325   127  0.2050 0.2470        
REMARK   3    28  1.8180 -  1.7960    0.88     3250   149  0.2120 0.2610        
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)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.030           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.43                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.57                          
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      :  0.007           5010                                  
REMARK   3   ANGLE     :  1.122           6853                                  
REMARK   3   CHIRALITY :  0.077            715                                  
REMARK   3   PLANARITY :  0.007            901                                  
REMARK   3   DIHEDRAL  : 12.773           1825                                  
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):  10.4718  10.2827  20.2585              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0832 T22:   0.0984                                     
REMARK   3      T33:   0.1173 T12:  -0.0007                                     
REMARK   3      T13:  -0.0134 T23:   0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1144 L22:   0.3206                                     
REMARK   3      L33:   0.5163 L12:  -0.1004                                     
REMARK   3      L13:  -0.1862 L23:   0.2758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0066 S12:   0.0090 S13:   0.0057                       
REMARK   3      S21:  -0.0075 S22:  -0.0203 S23:   0.0221                       
REMARK   3      S31:  -0.0009 S32:  -0.0161 S33:   0.0304                       
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 4KYV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079967.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56625                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 26.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4KAC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 100MM NACL, 5MM DTT,   
REMARK 280  0.02% NAN3, 10MM TRIS-HCL (PH 7.5) . RESERVOIR SOLUTION:.1M         
REMARK 280  NH4NO3 .1M SODIUM ACETATE 24% PEG 20000 , MICROBATCH UNDER OIL      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.38500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MSE A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     SER A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     MSE A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     MSE B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER B  13    OG                                                  
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   OD1  ASP B    42     NH2  ARG B   157     2546     2.16            
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    PRO A  53       49.81    -99.94                                   
REMARK 500    THR A  54     -160.06   -108.12                                   
REMARK 500    SER A  55     -168.77   -161.54                                   
REMARK 500    GLU A 109      -94.00   -104.96                                   
REMARK 500    ASP A 117     -127.08     54.00                                   
REMARK 500    ARG A 164       47.89    -88.91                                   
REMARK 500    ASP A 167      -72.67    -97.76                                   
REMARK 500    VAL A 256      -67.87   -136.26                                   
REMARK 500    LEU A 282      -93.94   -118.51                                   
REMARK 500    PRO B  53       50.18   -100.51                                   
REMARK 500    THR B  54     -158.32   -109.36                                   
REMARK 500    SER B  55     -169.40   -162.66                                   
REMARK 500    GLU B 109      -91.05   -110.66                                   
REMARK 500    ASP B 117     -129.48     54.37                                   
REMARK 500    ARG B 164       41.65    -89.79                                   
REMARK 500    ASP B 167      -72.65    -97.39                                   
REMARK 500    VAL B 256      -68.33   -138.40                                   
REMARK 500    LEU B 282      -96.67   -120.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  52   OD1                                                    
REMARK 620 2 LEU B 213   O   148.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 291   OD1                                                    
REMARK 620 2 HOH A 599   O   143.4                                              
REMARK 620 3 ASN A  61   O   151.2  58.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 291   OD1                                                    
REMARK 620 2 HOH B 623   O   138.4                                              
REMARK 620 3 ASN B  61   O   156.5  57.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 213   O                                                      
REMARK 620 2 ASN A  52   OD1 119.2                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Q9 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Q9 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 403                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KAC   RELATED DB: PDB                                   
REMARK 900 100% IDENTITY                                                        
REMARK 900 RELATED ID: NESG-OR150   RELATED DB: TARGETTRACK                     
DBREF  4KYV A    1   306  PDB    4KYV     4KYV             1    306             
DBREF  4KYV B    1   306  PDB    4KYV     4KYV             1    306             
SEQRES   1 A  306  MSE GLY HIS HIS HIS HIS HIS HIS SER HIS MSE GLY SER          
SEQRES   2 A  306  GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL          
SEQRES   3 A  306  GLU VAL LEU GLY GLU ARG MSE HIS TYR VAL ASP VAL GLY          
SEQRES   4 A  306  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN          
SEQRES   5 A  306  PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS          
SEQRES   6 A  306  VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE          
SEQRES   7 A  306  GLY MSE GLY LYS SER ASP LYS PRO ASP LEU ASP TYR PHE          
SEQRES   8 A  306  PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU          
SEQRES   9 A  306  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP          
SEQRES  10 A  306  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN          
SEQRES  11 A  306  PRO GLU ARG VAL LYS GLY ILE ALA CYS MSE GLU PHE ILE          
SEQRES  12 A  306  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA          
SEQRES  13 A  306  ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY          
SEQRES  14 A  306  ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY          
SEQRES  15 A  306  ALA LEU PRO MSE GLY VAL VAL ARG PRO LEU THR GLU VAL          
SEQRES  16 A  306  GLU MSE ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL          
SEQRES  17 A  306  ASP ARG GLU PRO LEU TRP ARG LEU PRO ASN GLU LEU PRO          
SEQRES  18 A  306  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU          
SEQRES  19 A  306  ALA TYR MSE ASN TRP LEU HIS GLN SER PRO VAL PRO LYS          
SEQRES  20 A  306  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO          
SEQRES  21 A  306  ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS          
SEQRES  22 A  306  LYS THR VAL ASP ILE GLY PRO GLY LEU PHE LEU LEU GLN          
SEQRES  23 A  306  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG          
SEQRES  24 A  306  TRP LEU PRO GLY LEU ALA GLY                                  
SEQRES   1 B  306  MSE GLY HIS HIS HIS HIS HIS HIS SER HIS MSE GLY SER          
SEQRES   2 B  306  GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL          
SEQRES   3 B  306  GLU VAL LEU GLY GLU ARG MSE HIS TYR VAL ASP VAL GLY          
SEQRES   4 B  306  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN          
SEQRES   5 B  306  PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS          
SEQRES   6 B  306  VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE          
SEQRES   7 B  306  GLY MSE GLY LYS SER ASP LYS PRO ASP LEU ASP TYR PHE          
SEQRES   8 B  306  PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU          
SEQRES   9 B  306  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP          
SEQRES  10 B  306  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN          
SEQRES  11 B  306  PRO GLU ARG VAL LYS GLY ILE ALA CYS MSE GLU PHE ILE          
SEQRES  12 B  306  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA          
SEQRES  13 B  306  ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY          
SEQRES  14 B  306  ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY          
SEQRES  15 B  306  ALA LEU PRO MSE GLY VAL VAL ARG PRO LEU THR GLU VAL          
SEQRES  16 B  306  GLU MSE ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL          
SEQRES  17 B  306  ASP ARG GLU PRO LEU TRP ARG LEU PRO ASN GLU LEU PRO          
SEQRES  18 B  306  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU          
SEQRES  19 B  306  ALA TYR MSE ASN TRP LEU HIS GLN SER PRO VAL PRO LYS          
SEQRES  20 B  306  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO          
SEQRES  21 B  306  ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS          
SEQRES  22 B  306  LYS THR VAL ASP ILE GLY PRO GLY LEU PHE LEU LEU GLN          
SEQRES  23 B  306  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG          
SEQRES  24 B  306  TRP LEU PRO GLY LEU ALA GLY                                  
MODRES 4KYV MSE A   33  MET  SELENOMETHIONINE                                   
MODRES 4KYV MSE A   80  MET  SELENOMETHIONINE                                   
MODRES 4KYV MSE A  140  MET  SELENOMETHIONINE                                   
MODRES 4KYV MSE A  186  MET  SELENOMETHIONINE                                   
MODRES 4KYV MSE A  197  MET  SELENOMETHIONINE                                   
MODRES 4KYV MSE A  237  MET  SELENOMETHIONINE                                   
MODRES 4KYV MSE B   33  MET  SELENOMETHIONINE                                   
MODRES 4KYV MSE B   80  MET  SELENOMETHIONINE                                   
MODRES 4KYV MSE B  140  MET  SELENOMETHIONINE                                   
MODRES 4KYV MSE B  186  MET  SELENOMETHIONINE                                   
MODRES 4KYV MSE B  197  MET  SELENOMETHIONINE                                   
MODRES 4KYV MSE B  237  MET  SELENOMETHIONINE                                   
HET    MSE  A  33       8                                                       
HET    MSE  A  80       8                                                       
HET    MSE  A 140       8                                                       
HET    MSE  A 186       8                                                       
HET    MSE  A 197      13                                                       
HET    MSE  A 237       8                                                       
HET    MSE  B  33       8                                                       
HET    MSE  B  80       8                                                       
HET    MSE  B 140       8                                                       
HET    MSE  B 186       8                                                       
HET    MSE  B 197       8                                                       
HET    MSE  B 237       8                                                       
HET    1Q9  A 401      18                                                       
HET     NA  A 402       1                                                       
HET     NA  A 403       1                                                       
HET    1Q9  B 401      18                                                       
HET     NA  B 402       1                                                       
HET     NA  B 403       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     1Q9 N-(2-ETHOXY-3,5-DIMETHYLBENZYL)-1H-TETRAZOL-5-AMINE              
HETNAM      NA SODIUM ION                                                       
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   3  1Q9    2(C12 H17 N5 O)                                              
FORMUL   4   NA    4(NA 1+)                                                     
FORMUL   9  HOH   *680(H2 O)                                                    
HELIX    1   1 SER A   55  ARG A   60  5                                   6    
HELIX    2   2 ILE A   62  ALA A   67  1                                   6    
HELIX    3   3 PHE A   91  LEU A  106  1                                  16    
HELIX    4   4 ASP A  117  ASN A  130  1                                  14    
HELIX    5   5 THR A  148  TRP A  152  5                                   5    
HELIX    6   6 PRO A  153  PHE A  155  5                                   3    
HELIX    7   7 ALA A  156  ARG A  164  1                                   9    
HELIX    8   8 ASP A  167  ILE A  174  1                                   8    
HELIX    9   9 ASN A  177  GLY A  182  1                                   6    
HELIX   10  10 GLY A  182  GLY A  187  1                                   6    
HELIX   11  11 THR A  193  GLU A  202  1                                  10    
HELIX   12  12 PRO A  203  LEU A  205  5                                   3    
HELIX   13  13 LYS A  206  ASP A  209  5                                   4    
HELIX   14  14 ARG A  210  LEU A  220  1                                  11    
HELIX   15  15 PRO A  226  SER A  243  1                                  18    
HELIX   16  16 PRO A  259  LEU A  270  1                                  12    
HELIX   17  17 LEU A  284  ASN A  289  1                                   6    
HELIX   18  18 ASN A  289  LEU A  301  1                                  13    
HELIX   19  19 PRO A  302  ALA A  305  5                                   4    
HELIX   20  20 SER B   55  ARG B   60  5                                   6    
HELIX   21  21 ILE B   62  ALA B   67  1                                   6    
HELIX   22  22 PHE B   91  GLY B  107  1                                  17    
HELIX   23  23 ASP B  117  ASN B  130  1                                  14    
HELIX   24  24 THR B  148  TRP B  152  5                                   5    
HELIX   25  25 PRO B  153  ARG B  164  1                                  12    
HELIX   26  26 ASP B  167  ILE B  174  1                                   8    
HELIX   27  27 ASN B  177  GLY B  182  1                                   6    
HELIX   28  28 GLY B  182  GLY B  187  1                                   6    
HELIX   29  29 THR B  193  GLU B  202  1                                  10    
HELIX   30  30 PRO B  203  LEU B  205  5                                   3    
HELIX   31  31 LYS B  206  ASP B  209  5                                   4    
HELIX   32  32 ARG B  210  LEU B  216  1                                   7    
HELIX   33  33 PRO B  217  LEU B  220  5                                   4    
HELIX   34  34 PRO B  226  SER B  243  1                                  18    
HELIX   35  35 PRO B  259  LEU B  270  1                                  12    
HELIX   36  36 LEU B  284  ASP B  288  5                                   5    
HELIX   37  37 ASN B  289  LEU B  301  1                                  13    
HELIX   38  38 PRO B  302  ALA B  305  5                                   4    
SHEET    1   A 8 HIS A  24  VAL A  28  0                                        
SHEET    2   A 8 GLU A  31  VAL A  38 -1  O  GLU A  31   N  VAL A  28           
SHEET    3   A 8 CYS A  72  PRO A  75 -1  O  CYS A  72   N  VAL A  38           
SHEET    4   A 8 VAL A  46  LEU A  49  1  N  PHE A  48   O  ILE A  73           
SHEET    5   A 8 VAL A 111  HIS A 116  1  O  VAL A 112   N  LEU A  47           
SHEET    6   A 8 VAL A 134  MSE A 140  1  O  ALA A 138   N  LEU A 113           
SHEET    7   A 8 LYS A 247  PRO A 254  1  O  LEU A 248   N  CYS A 139           
SHEET    8   A 8 CYS A 273  GLY A 281  1  O  LYS A 274   N  LEU A 249           
SHEET    1   B 8 HIS B  24  VAL B  28  0                                        
SHEET    2   B 8 GLU B  31  VAL B  38 -1  O  GLU B  31   N  VAL B  28           
SHEET    3   B 8 CYS B  72  PRO B  75 -1  O  CYS B  72   N  VAL B  38           
SHEET    4   B 8 VAL B  46  LEU B  49  1  N  PHE B  48   O  ILE B  73           
SHEET    5   B 8 VAL B 111  HIS B 116  1  O  VAL B 112   N  LEU B  47           
SHEET    6   B 8 VAL B 134  MSE B 140  1  O  ALA B 138   N  LEU B 113           
SHEET    7   B 8 LYS B 247  PRO B 254  1  O  LEU B 248   N  CYS B 139           
SHEET    8   B 8 CYS B 273  GLY B 281  1  O  LYS B 274   N  LEU B 249           
LINK         C   ARG A  32                 N   MSE A  33     1555   1555  1.33  
LINK         C   MSE A  33                 N   HIS A  34     1555   1555  1.32  
LINK         C   GLY A  79                 N   MSE A  80     1555   1555  1.33  
LINK         C   MSE A  80                 N   GLY A  81     1555   1555  1.33  
LINK         C   CYS A 139                 N   MSE A 140     1555   1555  1.33  
LINK         C   MSE A 140                 N   GLU A 141     1555   1555  1.33  
LINK         C   PRO A 185                 N   MSE A 186     1555   1555  1.33  
LINK         C   MSE A 186                 N   GLY A 187     1555   1555  1.33  
LINK         C   GLU A 196                 N   MSE A 197     1555   1555  1.33  
LINK         C   MSE A 197                 N   ASP A 198     1555   1555  1.33  
LINK         C   TYR A 236                 N   MSE A 237     1555   1555  1.33  
LINK         C   MSE A 237                 N   ASN A 238     1555   1555  1.34  
LINK         C   ARG B  32                 N   MSE B  33     1555   1555  1.33  
LINK         C   MSE B  33                 N   HIS B  34     1555   1555  1.32  
LINK         C   GLY B  79                 N   MSE B  80     1555   1555  1.33  
LINK         C   MSE B  80                 N   GLY B  81     1555   1555  1.33  
LINK         C   CYS B 139                 N   MSE B 140     1555   1555  1.33  
LINK         C   MSE B 140                 N   GLU B 141     1555   1555  1.33  
LINK         C   PRO B 185                 N   MSE B 186     1555   1555  1.33  
LINK         C   MSE B 186                 N   GLY B 187     1555   1555  1.33  
LINK         C   GLU B 196                 N   MSE B 197     1555   1555  1.33  
LINK         C   MSE B 197                 N   ASP B 198     1555   1555  1.33  
LINK         C   TYR B 236                 N   MSE B 237     1555   1555  1.33  
LINK         C   MSE B 237                 N   ASN B 238     1555   1555  1.33  
LINK         OD1 ASN B  52                NA    NA B 403     1555   1555  2.19  
LINK         OD1 ASP A 291                NA    NA A 402     1555   1555  2.22  
LINK         OD1 ASP B 291                NA    NA B 402     1555   1555  2.27  
LINK         O   LEU B 213                NA    NA B 403     1555   1555  2.59  
LINK         O   LEU A 213                NA    NA A 403     1555   1555  2.67  
LINK         OD1 ASN A  52                NA    NA A 403     1555   1555  2.76  
LINK        NA    NA A 402                 O   HOH A 599     1555   1555  2.88  
LINK        NA    NA B 402                 O   HOH B 623     1555   1555  2.99  
LINK         O   ASN B  61                NA    NA B 402     1555   1555  3.00  
LINK         O   ASN A  61                NA    NA A 402     1555   1555  3.16  
CISPEP   1 ASN A   52    PRO A   53          0       -11.41                     
CISPEP   2 GLU A  225    PRO A  226          0        -3.59                     
CISPEP   3 THR A  253    PRO A  254          0         6.88                     
CISPEP   4 ASN B   52    PRO B   53          0        -8.76                     
CISPEP   5 GLU B  225    PRO B  226          0        -3.18                     
CISPEP   6 THR B  253    PRO B  254          0         2.64                     
SITE     1 AC1 12 PRO A  53  ASP A 117  TRP A 118  TRP A 152                    
SITE     2 AC1 12 ALA A 156  PHE A 160  PHE A 179  ALA A 183                    
SITE     3 AC1 12 PRO A 217  LEU A 220  VAL A 256  PHE A 283                    
SITE     1 AC2  4 ASN A  61  HIS A  65  ASP A 291  HOH A 599                    
SITE     1 AC3  4 ASN A  52  PHE A 179  LEU A 213  PRO A 217                    
SITE     1 AC4 13 ASN B  52  PRO B  53  ASP B 117  TRP B 118                    
SITE     2 AC4 13 TRP B 152  PHE B 160  PHE B 179  ALA B 183                    
SITE     3 AC4 13 MSE B 186  PRO B 217  LEU B 220  VAL B 256                    
SITE     4 AC4 13 PHE B 283                                                     
SITE     1 AC5  4 ASN B  61  HIS B  65  ASP B 291  HOH B 623                    
SITE     1 AC6  4 ASN B  52  PHE B 179  LEU B 213  PRO B 217                    
CRYST1   42.938   94.770   73.483  90.00  93.11  90.00 P 1 21 1      4          
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      0.023289  0.000000  0.001267        0.00000                         
SCALE2      0.000000  0.010552  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013629        0.00000                         
TER    2406      GLY A 306                                                      
TER    4805      GLY B 306                                                      
MASTER      380    0   18   38   16    0   11    6 5505    2  175   48          
END                                                                             

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

Acknowledgements and disclaimer