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LongText Report for: 4EZI-pdb

Name Class
4EZI-pdb
HEADER    UNKNOWN FUNCTION                        02-MAY-12   4EZI              
TITLE     CRYSTAL STRUCTURE OF A HYPOTHETICAL PROTEIN (LPG1103) FROM LEGIONELLA 
TITLE    2 PNEUMOPHILA SUBSP. PNEUMOPHILA STR. PHILADELPHIA 1 AT 1.15 A         
TITLE    3 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNCHARACTERIZED PROTEIN;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA STR.  
SOURCE   3 PHILADELPHIA 1;                                                      
SOURCE   4 ORGANISM_TAXID: 272624;                                              
SOURCE   5 STRAIN: PHILADELPHIA 1 / ATCC 33152 / DSM 7513;                      
SOURCE   6 GENE: LPG1103;                                                       
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: PB1;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    ALPHA-BETA HYDROLASES FOLD, STRUCTURAL GENOMICS, JOINT CENTER FOR     
KEYWDS   2 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-        
KEYWDS   3 BIOLOGY, UNKNOWN FUNCTION                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   1   27-JUN-12 4EZI    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF A HYPOTHETICAL PROTEIN (LPG1103) FROM   
JRNL        TITL 2 LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA STR. PHILADELPHIA  
JRNL        TITL 3 1 AT 1.15 A RESOLUTION                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 131826                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.137                           
REMARK   3   R VALUE            (WORKING SET) : 0.135                           
REMARK   3   FREE R VALUE                     : 0.157                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6631                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9084                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 545                          
REMARK   3   BIN FREE R VALUE                    : 0.2960                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2962                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 536                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 9.25                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.20000                                              
REMARK   3    B22 (A**2) : -0.11000                                             
REMARK   3    B33 (A**2) : -0.09000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.032         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.032         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.020         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.002         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.980                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.975                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3292 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2214 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4507 ; 1.428 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5439 ; 0.951 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   416 ; 5.845 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   160 ;37.149 ;24.563       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   541 ;11.786 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;21.892 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   485 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3696 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   680 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1972 ; 1.898 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   778 ; 1.390 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3221 ; 2.691 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1320 ; 3.642 ; 8.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1269 ; 5.188 ;11.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  5506 ; 1.464 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   539 ; 6.748 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  5395 ; 3.568 ; 3.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE       
REMARK   3  RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR         
REMARK   3  SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE       
REMARK   3  OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75   
REMARK   3  FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET               
REMARK   3  INCORPORATION. 3. POLYETHYLENE GLYCOL (PEG) AND CHLORIDE (CL)       
REMARK   3  FROM THE CRYSTALLIZATION SOLUTION HAVE BEEN MODELED INTO THE        
REMARK   3  STRUCTURE.                                                          
REMARK   4                                                                      
REMARK   4 4EZI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072264.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97916                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : VERTICAL FOCUSING MIRROR; DOUBLE   
REMARK 200                                   CRYSTAL SI(111) MONOCHROMATOR      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 131916                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.637                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10600                            
REMARK 200   FOR THE DATA SET  : 7.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.78700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.78700                            
REMARK 200   FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD,SHARP                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.20M SODIUM ACETATE, 30.00%             
REMARK 280  POLYETHYLENE GLYCOL 4000, 0.1M TRIS HYDROCHLORIDE PH 8.5,           
REMARK 280  NANODROP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.43750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.27450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.74400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.27450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.43750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.74400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     LEU A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     LYS A   403                                                      
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     GLU A  32    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  53    CE   NZ                                             
REMARK 470     MSE A 401    CG  SE    CE                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 120       62.78     37.89                                   
REMARK 500    SER A 134      -64.05    -90.37                                   
REMARK 500    TYR A 144      157.60     86.64                                   
REMARK 500    SER A 195     -123.44     63.74                                   
REMARK 500    PHE A 365       58.66    -91.35                                   
REMARK 500    ALA A 374      -17.32   -140.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: JCSG-418740   RELATED DB: TARGETTRACK                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT (RESIDUES 28-403) WAS EXPRESSED WITH A PURIFICATION    
REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE       
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.          
DBREF  4EZI A   28   403  UNP    Q5ZWI2   Q5ZWI2_LEGPH    28    403             
SEQADV 4EZI GLY A    0  UNP  Q5ZWI2              LEADER SEQUENCE                
SEQRES   1 A  377  GLY ALA LEU GLU HIS GLU LYS LEU VAL ASN TYR ILE ALA          
SEQRES   2 A  377  LEU GLY GLU PHE SER ARG GLU THR ALA GLU ILE ALA LEU          
SEQRES   3 A  377  LYS LYS MSE PRO PRO LEU ASP THR LEU THR VAL HIS TYR          
SEQRES   4 A  377  ASP LEU GLN LEU TYR LYS ILE ASN TYR LYS THR GLN SER          
SEQRES   5 A  377  PRO ASP GLY ASN LEU THR ILE ALA SER GLY LEU VAL ALA          
SEQRES   6 A  377  MSE PRO ILE HIS PRO VAL GLY GLN VAL GLY ILE ILE SER          
SEQRES   7 A  377  TYR GLN HIS GLY THR ARG PHE GLU ARG ASN ASP VAL PRO          
SEQRES   8 A  377  SER ARG ASN ASN GLU LYS ASN TYR ILE TYR LEU ALA ALA          
SEQRES   9 A  377  TYR GLY ASN SER ALA GLY TYR MSE THR VAL MSE PRO ASP          
SEQRES  10 A  377  TYR LEU GLY LEU GLY ASP ASN GLU LEU THR LEU HIS PRO          
SEQRES  11 A  377  TYR VAL GLN ALA GLU THR LEU ALA SER SER SER ILE ASP          
SEQRES  12 A  377  MSE LEU PHE ALA ALA LYS GLU LEU ALA ASN ARG LEU HIS          
SEQRES  13 A  377  TYR PRO ILE SER ASP LYS LEU TYR LEU ALA GLY TYR SER          
SEQRES  14 A  377  GLU GLY GLY PHE SER THR ILE VAL MSE PHE GLU MSE LEU          
SEQRES  15 A  377  ALA LYS GLU TYR PRO ASP LEU PRO VAL SER ALA VAL ALA          
SEQRES  16 A  377  PRO GLY SER ALA PRO TYR GLY TRP GLU GLU THR MSE HIS          
SEQRES  17 A  377  PHE VAL MSE LEU GLU PRO GLY PRO ARG ALA THR ALA TYR          
SEQRES  18 A  377  LEU ALA TYR PHE PHE TYR SER LEU GLN THR TYR LYS SER          
SEQRES  19 A  377  TYR TRP SER GLY PHE ASP GLU ILE PHE ALA PRO PRO TYR          
SEQRES  20 A  377  ASN THR LEU ILE PRO GLU LEU MSE ASP GLY TYR HIS ALA          
SEQRES  21 A  377  VAL ASP GLU ILE LEU GLN ALA LEU PRO GLN ASP PRO LEU          
SEQRES  22 A  377  LEU ILE PHE GLN PRO LYS PHE SER ASN GLY ILE ILE SER          
SEQRES  23 A  377  LYS THR ASP ARG ASN THR GLU ILE LEU LYS ILE ASN PHE          
SEQRES  24 A  377  ASN HIS TYR ASP PHE LYS PRO THR ALA PRO LEU LEU LEU          
SEQRES  25 A  377  VAL GLY THR LYS GLY ASP ARG ASP VAL PRO TYR ALA GLY          
SEQRES  26 A  377  ALA GLU MSE ALA TYR HIS SER PHE ARG LYS TYR SER ASP          
SEQRES  27 A  377  PHE VAL TRP ILE LYS SER VAL SER ASP ALA LEU ASP HIS          
SEQRES  28 A  377  VAL GLN ALA HIS PRO PHE VAL LEU LYS GLU GLN VAL ASP          
SEQRES  29 A  377  PHE PHE LYS GLN PHE GLU ARG GLN GLU ALA MSE ASN LYS          
MODRES 4EZI MSE A   55  MET  SELENOMETHIONINE                                   
MODRES 4EZI MSE A   92  MET  SELENOMETHIONINE                                   
MODRES 4EZI MSE A  138  MET  SELENOMETHIONINE                                   
MODRES 4EZI MSE A  141  MET  SELENOMETHIONINE                                   
MODRES 4EZI MSE A  170  MET  SELENOMETHIONINE                                   
MODRES 4EZI MSE A  204  MET  SELENOMETHIONINE                                   
MODRES 4EZI MSE A  207  MET  SELENOMETHIONINE                                   
MODRES 4EZI MSE A  233  MET  SELENOMETHIONINE                                   
MODRES 4EZI MSE A  237  MET  SELENOMETHIONINE                                   
MODRES 4EZI MSE A  281  MET  SELENOMETHIONINE                                   
MODRES 4EZI MSE A  354  MET  SELENOMETHIONINE                                   
MODRES 4EZI MSE A  401  MET  SELENOMETHIONINE                                   
HET    MSE  A  55      13                                                       
HET    MSE  A  92       8                                                       
HET    MSE  A 138       8                                                       
HET    MSE  A 141       8                                                       
HET    MSE  A 170       8                                                       
HET    MSE  A 204       8                                                       
HET    MSE  A 207       8                                                       
HET    MSE  A 233       8                                                       
HET    MSE  A 237      13                                                       
HET    MSE  A 281       8                                                       
HET    MSE  A 354      13                                                       
HET    MSE  A 401       5                                                       
HET    PEG  A 501       7                                                       
HET     CL  A 502       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   2  PEG    C4 H10 O3                                                    
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  HOH   *536(H2 O)                                                    
HELIX    1   1 SER A   44  LYS A   54  1                                  11    
HELIX    2   2 PRO A   57  LEU A   61  5                                   5    
HELIX    3   3 VAL A  116  ASN A  120  5                                   5    
HELIX    4   4 ASN A  121  LYS A  123  5                                   3    
HELIX    5   5 ASN A  124  GLY A  132  1                                   9    
HELIX    6   6 GLN A  159  LEU A  181  1                                  23    
HELIX    7   7 SER A  195  TYR A  212  1                                  18    
HELIX    8   8 GLY A  228  GLU A  239  1                                  12    
HELIX    9   9 ARG A  243  SER A  260  1                                  18    
HELIX   10  10 GLY A  264  PHE A  269  1                                   6    
HELIX   11  11 PRO A  272  MSE A  281  1                                  10    
HELIX   12  12 ALA A  286  LEU A  294  1                                   9    
HELIX   13  13 ASP A  297  PHE A  302  5                                   6    
HELIX   14  14 GLN A  303  SER A  312  1                                  10    
HELIX   15  15 ASN A  317  ASN A  326  1                                  10    
HELIX   16  16 PRO A  348  LYS A  361  1                                  14    
HELIX   17  17 ALA A  380  ARG A  397  1                                  18    
SHEET    1   A 7 LEU A  34  PHE A  43  0                                        
SHEET    2   A 7 LEU A  67  GLN A  77 -1  O  ASN A  73   N  VAL A  35           
SHEET    3   A 7 LEU A  83  PRO A  93 -1  O  MSE A  92   N  GLN A  68           
SHEET    4   A 7 MSE A 138  PRO A 142 -1  O  MSE A 141   N  LEU A  89           
SHEET    5   A 7 VAL A 100  GLN A 106  1  N  ILE A 103   O  VAL A 140           
SHEET    6   A 7 ILE A 185  TYR A 194  1  O  SER A 186   N  VAL A 100           
SHEET    7   A 7 ALA A 219  GLY A 223  1  O  ALA A 221   N  LEU A 191           
SHEET    1   B 2 LEU A 336  GLY A 340  0                                        
SHEET    2   B 2 VAL A 366  SER A 370  1  O  TRP A 367   N  LEU A 338           
LINK         C   LYS A  54                 N   MSE A  55     1555   1555  1.34  
LINK         C   MSE A  55                 N   PRO A  56     1555   1555  1.34  
LINK         C   ALA A  91                 N   MSE A  92     1555   1555  1.34  
LINK         C   MSE A  92                 N   PRO A  93     1555   1555  1.34  
LINK         C   TYR A 137                 N   MSE A 138     1555   1555  1.33  
LINK         C   MSE A 138                 N   THR A 139     1555   1555  1.33  
LINK         C   VAL A 140                 N   MSE A 141     1555   1555  1.34  
LINK         C   MSE A 141                 N   PRO A 142     1555   1555  1.34  
LINK         C   ASP A 169                 N   MSE A 170     1555   1555  1.33  
LINK         C   MSE A 170                 N   LEU A 171     1555   1555  1.32  
LINK         C   VAL A 203                 N   MSE A 204     1555   1555  1.33  
LINK         C   MSE A 204                 N   PHE A 205     1555   1555  1.32  
LINK         C   GLU A 206                 N   MSE A 207     1555   1555  1.33  
LINK         C   MSE A 207                 N   LEU A 208     1555   1555  1.32  
LINK         C   THR A 232                 N   MSE A 233     1555   1555  1.33  
LINK         C   MSE A 233                 N   HIS A 234     1555   1555  1.32  
LINK         C   VAL A 236                 N   MSE A 237     1555   1555  1.34  
LINK         C   MSE A 237                 N   LEU A 238     1555   1555  1.34  
LINK         C   LEU A 280                 N   MSE A 281     1555   1555  1.34  
LINK         C   MSE A 281                 N   ASP A 282     1555   1555  1.33  
LINK         C   GLU A 353                 N   MSE A 354     1555   1555  1.33  
LINK         C   MSE A 354                 N   ALA A 355     1555   1555  1.34  
LINK         C   ALA A 400                 N   MSE A 401     1555   1555  1.34  
LINK         C   MSE A 401                 N   ASN A 402     1555   1555  1.33  
CISPEP   1 PRO A   56    PRO A   57          0        11.27                     
CISPEP   2 PRO A  271    PRO A  272          0        -2.42                     
SITE     1 AC1  4 TYR A 157  GLU A 196  PHE A 251  VAL A 347                    
SITE     1 AC2  3 GLU A 230  ASN A 326  HOH A 729                               
CRYST1   50.875   63.488  114.549  90.00  90.00  90.00 P 21 21 21    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      0.019656  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015751  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008730        0.00000                         
TER    3175      ASN A 402                                                      
MASTER      300    0   14   17    9    0    2    6 3506    1  139   29          
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.
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