Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 3MUN-pdb

Name Class
3MUN-pdb
HEADER    HYDROLASE                               03-MAY-10   3MUN              
TITLE     APPEP_PEPCLOSE CLOSED STATE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLYL ENDOPEPTIDASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEROMONAS PUNCTATA;                             
SOURCE   3 ORGANISM_COMMON: AEROMONAS CAVIAE;                                   
SOURCE   4 ORGANISM_TAXID: 648;                                                 
SOURCE   5 GENE: PROLYL ENDOPEPTIDASE;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    PROLYL ENDOPEPTIDASE, HYDROLASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.K.CHIU                                                              
REVDAT   1   18-MAY-11 3MUN    0                                                
JRNL        AUTH   T.K.CHIU,M.LI                                                
JRNL        TITL   ROUTE OF SUBSTRATE ENTRY IN PROLYL ENDOPEPTIDASE             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2689839.060                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 58674                          
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 SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2966                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.18                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5538                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1980                       
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 289                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5407                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 403                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.13000                                              
REMARK   3    B22 (A**2) : 4.13000                                              
REMARK   3    B33 (A**2) : -8.26000                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.13                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.25                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.21                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.75                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.850 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.500 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.610 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.240 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 55.95                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP_SPP.PARAM                          
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : ZPPOH.PARAM                                    
REMARK   3  PARAMETER FILE  5  : SUCROSE.PARAM                                  
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_SPP.TOP                                
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : ZPPOH.TOP                                      
REMARK   3  TOPOLOGY FILE  5   : SUCROSE.TOP                                    
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3MUN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059014.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59247                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14900                            
REMARK 200   FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.53700                            
REMARK 200   FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 3IUJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8MG/ML PROTEIN IN 20MM HEPES (PH7.5),    
REMARK 280  100MM NACL, 5% W/V GLYCEROL, AND 1MM EDTA. EQUAL VOLUME OF          
REMARK 280  PROTEIN AND PRECIPITANT (1.5M AMSO4, 100MM TRIS, PH 8.5 AND 12%     
REMARK 280  W/V GLYCEROL) WERE EQUILIBRATED BY VAPOR DIFFUSION AT 14C.          
REMARK 280  CRYOSOLUTION IS 2.2M AMSO4, 30% W/V SUCROSE, 12% W/V GLYCEROL,      
REMARK 280  AND 100MM TRIS (PH 8.5).                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.10000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       98.20000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       98.20000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       49.10000            
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 300 REMARK: 1                                                            
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 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    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ARG A     6                                                      
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    PRO A 312   C   -  N   -  CA  ANGL. DEV. =   9.7 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    ASP A 129      -91.02   -106.41                                   
REMARK 500    GLU A 166     -175.85     45.16                                   
REMARK 500    ASP A 285     -178.49   -177.35                                   
REMARK 500    ALA A 299       87.22   -156.10                                   
REMARK 500    ARG A 302      158.15     73.67                                   
REMARK 500    ASN A 311       66.59   -154.42                                   
REMARK 500    TYR A 458      -77.44   -133.13                                   
REMARK 500    GLN A 504     -114.84     46.54                                   
REMARK 500    SER A 538     -115.83     66.64                                   
REMARK 500    VAL A 562       49.61     30.95                                   
REMARK 500    THR A 574     -113.10     26.58                                   
REMARK 500    SER A 589      169.39    179.53                                   
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 A1275        DISTANCE =  5.19 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     SUC A  809                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SUC A 809                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3IUJ   RELATED DB: PDB                                   
REMARK 900 APPEP_WT2 OPENED STATE                                               
REMARK 900 RELATED ID: 3IUL   RELATED DB: PDB                                   
REMARK 900 APPEP_WT1 OPENED STATE                                               
REMARK 900 RELATED ID: 3IUN   RELATED DB: PDB                                   
REMARK 900 APPEP_D622N OPENED STATE                                             
REMARK 900 RELATED ID: 3IUQ   RELATED DB: PDB                                   
REMARK 900 APPEP_D622N+PP CLOSED STATE                                          
REMARK 900 RELATED ID: 3IUR   RELATED DB: PDB                                   
REMARK 900 AEPPEP_D266NX+H2H3 OPENED STATE                                      
REMARK 900 RELATED ID: 3IVM   RELATED DB: PDB                                   
REMARK 900 APPEP_WT+PP CLOSED STATE                                             
REMARK 900 RELATED ID: 3IUM   RELATED DB: PDB                                   
REMARK 900 APPEP_WTX OPENED STATE                                               
REMARK 900 RELATED ID: 3MUO   RELATED DB: PDB                                   
REMARK 900 APPEP_PEPCLOSE+PP CLOSED STATE                                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AUTHORS STATE THAT THESE ARE NOT MUTATIONS, BUT                      
REMARK 999 ERROR IN DNA SEQUENCING OF THE ORIGINAL DEPOSITED                    
REMARK 999 FILE. THEY CONFIRMED THIS WITH DNA SEQUENCING                        
DBREF  3MUN A    1   690  UNP    Q9X6R4   Q9X6R4_AERPU     1    690             
SEQADV 3MUN GLY A   -2  UNP  Q9X6R4              EXPRESSION TAG                 
SEQADV 3MUN SER A   -1  UNP  Q9X6R4              EXPRESSION TAG                 
SEQADV 3MUN HIS A    0  UNP  Q9X6R4              EXPRESSION TAG                 
SEQADV 3MUN TRP A   83  UNP  Q9X6R4    ARG    83 ENGINEERED MUTATION            
SEQADV 3MUN TRP A   84  UNP  Q9X6R4    GLU    84 ENGINEERED MUTATION            
SEQADV 3MUN GLN A  106  UNP  Q9X6R4    LYS   106 SEE REMARK 999                 
SEQADV 3MUN GLN A  242  UNP  Q9X6R4    ASP   242 ENGINEERED MUTATION            
SEQADV 3MUN GLN A  325  UNP  Q9X6R4    HIS   325 SEE REMARK 999                 
SEQADV 3MUN GLN A  326  UNP  Q9X6R4    ARG   326 SEE REMARK 999                 
SEQADV 3MUN SER A  334  UNP  Q9X6R4    THR   334 SEE REMARK 999                 
SEQADV 3MUN GLY A  335  UNP  Q9X6R4    ALA   335 SEE REMARK 999                 
SEQADV 3MUN ARG A  348  UNP  Q9X6R4    PRO   348 SEE REMARK 999                 
SEQADV 3MUN TYR A  376  UNP  Q9X6R4    LYS   376 ENGINEERED MUTATION            
SEQADV 3MUN TRP A  377  UNP  Q9X6R4    HIS   377 ENGINEERED MUTATION            
SEQADV 3MUN TRP A  378  UNP  Q9X6R4    ASP   378 ENGINEERED MUTATION            
SEQADV 3MUN THR A  577  UNP  Q9X6R4    ALA   577 SEE REMARK 999                 
SEQRES   1 A  693  GLY SER HIS MET SER GLY LYS ALA ARG LEU HIS TYR PRO          
SEQRES   2 A  693  VAL THR ARG GLN GLY GLU GLN VAL ASP HIS TYR PHE GLY          
SEQRES   3 A  693  GLN ALA VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP ASP          
SEQRES   4 A  693  ARG SER PRO GLU THR GLU ALA TRP VAL LYS ALA GLN ASN          
SEQRES   5 A  693  ALA VAL THR GLN ASP TYR LEU ALA GLN ILE PRO TYR ARG          
SEQRES   6 A  693  ALA ALA ILE LYS GLU LYS LEU ALA ALA SER TRP ASN TYR          
SEQRES   7 A  693  ALA LYS GLU GLY ALA PRO PHE TRP TRP GLY ARG TYR HIS          
SEQRES   8 A  693  TYR PHE PHE LYS ASN ASP GLY LEU GLN ASN GLN ASN VAL          
SEQRES   9 A  693  LEU TRP ARG GLN GLN GLU GLY LYS PRO ALA GLU VAL PHE          
SEQRES  10 A  693  LEU ASP PRO ASN THR LEU SER PRO ASP GLY THR THR ALA          
SEQRES  11 A  693  LEU ASP GLN LEU SER PHE SER ARG ASP GLY ARG ILE LEU          
SEQRES  12 A  693  ALA TYR SER LEU SER LEU ALA GLY SER ASP TRP ARG GLU          
SEQRES  13 A  693  ILE HIS LEU MET ASP VAL GLU SER LYS GLN PRO LEU GLU          
SEQRES  14 A  693  THR PRO LEU LYS ASP VAL LYS PHE SER GLY ILE SER TRP          
SEQRES  15 A  693  LEU GLY ASN GLU GLY PHE PHE TYR SER SER TYR ASP LYS          
SEQRES  16 A  693  PRO ASP GLY SER GLU LEU SER ALA ARG THR ASP GLN HIS          
SEQRES  17 A  693  LYS VAL TYR PHE HIS ARG LEU GLY THR ALA GLN GLU ASP          
SEQRES  18 A  693  ASP ARG LEU VAL PHE GLY ALA ILE PRO ALA GLN HIS HIS          
SEQRES  19 A  693  ARG TYR VAL GLY ALA THR VAL THR GLU ASP GLN ARG PHE          
SEQRES  20 A  693  LEU LEU ILE SER ALA ALA ASN SER THR SER GLY ASN ARG          
SEQRES  21 A  693  LEU TYR VAL LYS ASP LEU SER GLN GLU ASN ALA PRO LEU          
SEQRES  22 A  693  LEU THR VAL GLN GLY ASP LEU ASP ALA ASP VAL SER LEU          
SEQRES  23 A  693  VAL ASP ASN LYS GLY SER THR LEU TYR LEU LEU THR ASN          
SEQRES  24 A  693  ARG ASP ALA PRO ASN ARG ARG LEU VAL THR VAL ASP ALA          
SEQRES  25 A  693  ALA ASN PRO GLY PRO ALA HIS TRP ARG ASP LEU ILE PRO          
SEQRES  26 A  693  GLU ARG GLN GLN VAL LEU THR VAL HIS SER GLY SER GLY          
SEQRES  27 A  693  TYR LEU PHE ALA GLU TYR MET VAL ASP ALA THR ALA ARG          
SEQRES  28 A  693  VAL GLU GLN PHE ASP TYR GLU GLY LYS ARG VAL ARG GLU          
SEQRES  29 A  693  VAL ALA LEU PRO GLY LEU GLY SER VAL SER GLY PHE ASN          
SEQRES  30 A  693  GLY TYR TRP TRP ASP PRO ALA LEU TYR PHE GLY PHE GLU          
SEQRES  31 A  693  ASN TYR ALA GLN PRO PRO THR LEU TYR ARG PHE GLU PRO          
SEQRES  32 A  693  LYS SER GLY ALA ILE SER LEU TYR ARG ALA SER ALA ALA          
SEQRES  33 A  693  PRO PHE LYS PRO GLU ASP TYR VAL SER GLU GLN ARG PHE          
SEQRES  34 A  693  TYR GLN SER LYS ASP GLY THR ARG VAL PRO LEU ILE ILE          
SEQRES  35 A  693  SER TYR ARG LYS GLY LEU LYS LEU ASP GLY SER ASN PRO          
SEQRES  36 A  693  THR ILE LEU TYR GLY TYR GLY GLY PHE ASP VAL SER LEU          
SEQRES  37 A  693  THR PRO SER PHE SER VAL SER VAL ALA ASN TRP LEU ASP          
SEQRES  38 A  693  LEU GLY GLY VAL TYR ALA VAL ALA ASN LEU ARG GLY GLY          
SEQRES  39 A  693  GLY GLU TYR GLY GLN ALA TRP HIS LEU ALA GLY THR GLN          
SEQRES  40 A  693  GLN ASN LYS GLN ASN VAL PHE ASP ASP PHE ILE ALA ALA          
SEQRES  41 A  693  ALA GLU TYR LEU LYS ALA GLU GLY TYR THR ARG THR ASP          
SEQRES  42 A  693  ARG LEU ALA ILE ARG GLY GLY SER ASN GLY GLY LEU LEU          
SEQRES  43 A  693  VAL GLY ALA VAL MET THR GLN ARG PRO ASP LEU MET ARG          
SEQRES  44 A  693  VAL ALA LEU PRO ALA VAL GLY VAL LEU ASP MET LEU ARG          
SEQRES  45 A  693  TYR HIS THR PHE THR ALA GLY THR GLY TRP ALA TYR ASP          
SEQRES  46 A  693  TYR GLY THR SER ALA ASP SER GLU ALA MET PHE ASP TYR          
SEQRES  47 A  693  LEU LYS GLY TYR SER PRO LEU HIS ASN VAL ARG PRO GLY          
SEQRES  48 A  693  VAL SER TYR PRO SER THR MET VAL THR THR ALA ASP HIS          
SEQRES  49 A  693  ASP ASP ARG VAL VAL PRO ALA HIS SER PHE LYS PHE ALA          
SEQRES  50 A  693  ALA THR LEU GLN ALA ASP ASN ALA GLY PRO HIS PRO GLN          
SEQRES  51 A  693  LEU ILE ARG ILE GLU THR ASN ALA GLY HIS GLY ALA GLY          
SEQRES  52 A  693  THR PRO VAL ALA LYS LEU ILE GLU GLN SER ALA ASP ILE          
SEQRES  53 A  693  TYR ALA PHE THR LEU TYR GLU MET GLY TYR ARG GLU LEU          
SEQRES  54 A  693  PRO ARG GLN PRO                                              
HET    SO4  A 801       5                                                       
HET    SO4  A 802       5                                                       
HET    SO4  A 803       5                                                       
HET    SO4  A 804       5                                                       
HET    SO4  A 805       5                                                       
HET    SO4  A 806       5                                                       
HET    GOL  A 807       6                                                       
HET    GOL  A 808       6                                                       
HET    SUC  A 809      14                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     SUC SUCROSE                                                          
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  SO4    6(O4 S 2-)                                                   
FORMUL   8  GOL    2(C3 H8 O3)                                                  
FORMUL  10  SUC    C12 H22 O11                                                  
FORMUL  11  HOH   *403(H2 O)                                                    
HELIX    1   1 TYR A   30  ASP A   35  5                                   6    
HELIX    2   2 SER A   38  GLN A   58  1                                  21    
HELIX    3   3 TYR A   61  ASN A   74  1                                  14    
HELIX    4   4 ASP A  116  LEU A  120  5                                   5    
HELIX    5   5 ALA A  215  ASP A  219  5                                   5    
HELIX    6   6 ILE A  226  HIS A  230  5                                   5    
HELIX    7   7 GLY A  313  TRP A  317  5                                   5    
HELIX    8   8 LYS A  416  GLU A  418  5                                   3    
HELIX    9   9 SER A  470  LEU A  479  1                                  10    
HELIX   10  10 TYR A  494  ALA A  501  1                                   8    
HELIX   11  11 GLY A  502  ASN A  506  5                                   5    
HELIX   12  12 LYS A  507  GLU A  524  1                                  18    
HELIX   13  13 ARG A  528  ASP A  530  5                                   3    
HELIX   14  14 SER A  538  ARG A  551  1                                  14    
HELIX   15  15 ARG A  569  PHE A  573  5                                   5    
HELIX   16  16 ALA A  575  GLY A  578  5                                   4    
HELIX   17  17 TRP A  579  GLY A  584  1                                   6    
HELIX   18  18 SER A  589  SER A  600  1                                  12    
HELIX   19  19 PRO A  601  VAL A  605  5                                   5    
HELIX   20  20 PRO A  627  ASN A  641  1                                  15    
HELIX   21  21 PRO A  662  MET A  681  1                                  20    
SHEET    1   A 2 VAL A  18  TYR A  21  0                                        
SHEET    2   A 2 GLN A  24  ALA A  27 -1  O  VAL A  26   N  ASP A  19           
SHEET    1   B 3 LYS A  77  GLU A  78  0                                        
SHEET    2   B 3 TYR A  87  ASN A  93 -1  O  ASN A  93   N  LYS A  77           
SHEET    3   B 3 PHE A  82  TRP A  84 -1  N  PHE A  82   O  TYR A  89           
SHEET    1   C 4 LYS A  77  GLU A  78  0                                        
SHEET    2   C 4 TYR A  87  ASN A  93 -1  O  ASN A  93   N  LYS A  77           
SHEET    3   C 4 VAL A 101  GLN A 105 -1  O  VAL A 101   N  LYS A  92           
SHEET    4   C 4 GLU A 112  LEU A 115 -1  O  PHE A 114   N  LEU A 102           
SHEET    1   D 4 THR A 126  PHE A 133  0                                        
SHEET    2   D 4 ILE A 139  LEU A 146 -1  O  SER A 143   N  ASP A 129           
SHEET    3   D 4 TRP A 151  ASP A 158 -1  O  HIS A 155   N  TYR A 142           
SHEET    4   D 4 PRO A 164  LYS A 173 -1  O  VAL A 172   N  ARG A 152           
SHEET    1   E 4 SER A 178  LEU A 180  0                                        
SHEET    2   E 4 GLY A 184  SER A 189 -1  O  GLY A 184   N  LEU A 180           
SHEET    3   E 4 LYS A 206  ARG A 211 -1  O  HIS A 210   N  PHE A 185           
SHEET    4   E 4 ARG A 220  PHE A 223 -1  O  VAL A 222   N  VAL A 207           
SHEET    1   F 4 TYR A 233  VAL A 238  0                                        
SHEET    2   F 4 PHE A 244  ALA A 250 -1  O  ALA A 250   N  TYR A 233           
SHEET    3   F 4 ARG A 257  ASP A 262 -1  O  ARG A 257   N  ALA A 249           
SHEET    4   F 4 LEU A 270  GLN A 274 -1  O  LEU A 271   N  VAL A 260           
SHEET    1   G 4 VAL A 281  LYS A 287  0                                        
SHEET    2   G 4 THR A 290  THR A 295 -1  O  TYR A 292   N  VAL A 284           
SHEET    3   G 4 ARG A 303  ASP A 308 -1  O  VAL A 307   N  LEU A 291           
SHEET    4   G 4 ARG A 318  ILE A 321 -1  O  LEU A 320   N  LEU A 304           
SHEET    1   H 4 LEU A 328  GLY A 333  0                                        
SHEET    2   H 4 TYR A 336  VAL A 343 -1  O  PHE A 338   N  HIS A 331           
SHEET    3   H 4 THR A 346  PHE A 352 -1  O  THR A 346   N  VAL A 343           
SHEET    4   H 4 ARG A 358  VAL A 362 -1  O  VAL A 359   N  GLN A 351           
SHEET    1   I 4 SER A 369  GLY A 372  0                                        
SHEET    2   I 4 LEU A 382  ASN A 388 -1  O  GLU A 387   N  SER A 369           
SHEET    3   I 4 GLN A 391  GLU A 399 -1  O  PHE A 398   N  LEU A 382           
SHEET    4   I 4 ALA A 404  ARG A 409 -1  O  SER A 406   N  ARG A 397           
SHEET    1   J 8 TYR A 420  GLN A 428  0                                        
SHEET    2   J 8 ARG A 434  ARG A 442 -1  O  TYR A 441   N  VAL A 421           
SHEET    3   J 8 VAL A 482  ALA A 486 -1  O  TYR A 483   N  SER A 440           
SHEET    4   J 8 THR A 453  TYR A 456  1  N  TYR A 456   O  ALA A 484           
SHEET    5   J 8 LEU A 532  GLY A 537  1  O  ALA A 533   N  LEU A 455           
SHEET    6   J 8 VAL A 557  ALA A 561  1  O  ALA A 561   N  GLY A 536           
SHEET    7   J 8 SER A 613  ALA A 619  1  O  SER A 613   N  ALA A 558           
SHEET    8   J 8 GLN A 647  GLU A 652  1  O  LEU A 648   N  VAL A 616           
SITE     1 AC1  4 ARG A  13  GLY A  15  GLU A  16  HOH A1244                    
SITE     1 AC2  4 ARG A 201  ARG A 569  HOH A1089  HOH A1398                    
SITE     1 AC3  3 ARG A 358  ARG A 360  GLU A 361                               
SITE     1 AC4  4 ARG A  86  ARG A 360  SER A 402  HOH A1260                    
SITE     1 AC5  2 ARG A 624  HOH A1315                                          
SITE     1 AC6  4 HIS A 331  SER A 371  GLY A 372  ASN A 374                    
SITE     1 AC7  3 SER A 450  ARG A 528  ARG A 531                               
SITE     1 AC8  7 TYR A 458  PHE A 461  SER A 538  ASN A 539                    
SITE     2 AC8  7 TYR A 583  ARG A 624  HOH A1354                               
SITE     1 AC9  6 ALA A 228  HIS A 231  ARG A 257  GLY A 275                    
SITE     2 AC9  6 TYR A 679  HOH A1476                                          
CRYST1  108.140  108.140  147.300  90.00  90.00 120.00 P 31 2 1      6          
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      0.009247  0.005339  0.000000        0.00000                         
SCALE2      0.000000  0.010678  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006789        0.00000                         
TER    5408      PRO A 690                                                      
MASTER      376    0    9   21   41    0   11    6 5866    1   56   54          
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