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LongText Report for: 4Q1V-pdb

Name Class
4Q1V-pdb
HEADER    HYDROLASE                               04-APR-14   4Q1V              
TITLE     CRYSTAL STRUCTURE OF A PUTATIVE DIPEPTIDYL AMINOPEPTIDASE IV          
TITLE    2 (BACOVA_01349) FROM BACTEROIDES OVATUS ATCC 8483 AT 2.48 A RESOLUTION
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE DIPEPTIDYL AMINOPEPTIDASE IV;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PEPTIDASE, S9A/B/C FAMILY, CATALYTIC DOMAIN PROTEIN;        
COMPND   5 EC: 3.4.-.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACTEROIDES OVATUS;                             
SOURCE   3 ORGANISM_TAXID: 411476;                                              
SOURCE   4 STRAIN: ATCC 8483;                                                   
SOURCE   5 GENE: BACOVA_01349, ZP_02064383.1;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: PB1;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    TWO DOMAIN PROTEIN, DIPEPTIDYL-PEPTIDASE IV FAMILY (PF00930), PROLYL  
KEYWDS   2 OLIGOPEPTIDASE FAMILY (PF00326), STRUCTURAL GENOMICS, JOINT CENTER   
KEYWDS   3 FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-    
KEYWDS   4 BIOLOGY, HYDROLASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   1   07-MAY-14 4Q1V    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF A PUTATIVE DIPEPTIDYL AMINOPEPTIDASE IV 
JRNL        TITL 2 (BACOVA_01349) FROM BACTEROIDES OVATUS ATCC 8483 AT 2.48 A   
JRNL        TITL 3 RESOLUTION                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.48 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 70548                          
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)  : 0.173                          
REMARK   3   R VALUE            (WORKING SET)  : 0.171                          
REMARK   3   FREE R VALUE                      : 0.207                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3561                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.48                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.54                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.97                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 5125                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1981                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4886                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1958                   
REMARK   3   BIN FREE R VALUE                        : 0.2430                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.66                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 239                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11272                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 641                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.69                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.64940                                              
REMARK   3    B22 (A**2) : -4.79360                                             
REMARK   3    B33 (A**2) : 2.14420                                              
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) : 0.260               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 11748  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 15965  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 5360   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 314    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1718   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 11748  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1485   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 13169  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.10                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.65                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.84                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4Q1V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085499.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
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) : 0.97915                            
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70624                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.304                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.15200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 6.8400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.91900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SAD                                            
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   (%): 59.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10.0% POLYETHYLENE GLYCOL 6000, 0.1M     
REMARK 280  MES PH 6.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  293K                                                                
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       46.24350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.56350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.85150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.56350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.24350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.85150            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 54720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLN A    24                                                      
REMARK 465     GLU A    25                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     GLN B    24                                                      
REMARK 465     GLU B    25                                                      
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     LYS A 290    CE                                                  
REMARK 470     ALA A 508    CB                                                  
REMARK 470     LYS A 509    CE   NZ                                             
REMARK 470     LYS A 667    NZ                                                  
REMARK 470     GLU B 470    CD   OE1  OE2                                       
REMARK 470     LYS B 667    CE   NZ                                             
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 157     -116.49     62.23                                   
REMARK 500    ASN A 163     -119.58     60.24                                   
REMARK 500    LYS A 312      -82.08    -86.62                                   
REMARK 500    ALA A 464      142.58   -170.34                                   
REMARK 500    TYR A 518      -78.99   -123.03                                   
REMARK 500    ARG A 570       55.62   -143.48                                   
REMARK 500    SER A 603     -111.45     70.24                                   
REMARK 500    ASP A 645     -155.07     60.81                                   
REMARK 500    LYS A 709     -158.46    -84.86                                   
REMARK 500    VAL B  78      -63.98   -101.47                                   
REMARK 500    ASP B 157     -117.00     60.83                                   
REMARK 500    ASN B 163     -119.47     61.38                                   
REMARK 500    LYS B 312      -82.37    -88.67                                   
REMARK 500    TYR B 518      -78.93   -123.31                                   
REMARK 500    ARG B 570       47.35   -141.55                                   
REMARK 500    SER B 603     -111.63     71.33                                   
REMARK 500    ASP B 645     -155.14     60.89                                   
REMARK 500    LYS B 709     -159.41    -84.40                                   
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                              MG B 802  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B1171   O                                                      
REMARK 620 2 HOH B1024   O    88.6                                              
REMARK 620 3 ASP B 285   OD1  89.8 173.6                                        
REMARK 620 4 ASP B 285   O    77.7  91.2  82.4                                  
REMARK 620 5 ASP B 645   OD1  88.7  88.2  98.0 166.4                            
REMARK 620 6 HOH B1056   O   173.0  84.6  96.9 101.0  92.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 803  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 925   O                                                      
REMARK 620 2 ASP A 285   OD1  98.7                                              
REMARK 620 3 HOH A 924   O    74.4 167.2                                        
REMARK 620 4 ASP A 285   O    79.7  84.4  83.8                                  
REMARK 620 5 HOH A1235   O   164.5  96.7  90.1  99.5                            
REMARK 620 6 ASP A 645   OD1  89.7  97.8  93.0 169.4  90.6                      
REMARK 620 N                    1     2     3     4     5                       
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 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 802                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: JCSG-420002   RELATED DB: TARGETTRACK                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG                  
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING   
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 24-732 OF THE TARGET         
REMARK 999 SEQUENCE.                                                            
DBREF  4Q1V A   24   732  UNP    A7LU53   A7LU53_BACO1    24    732             
DBREF  4Q1V B   24   732  UNP    A7LU53   A7LU53_BACO1    24    732             
SEQADV 4Q1V GLY A    0  UNP  A7LU53              LEADER SEQUENCE                
SEQADV 4Q1V GLY B    0  UNP  A7LU53              LEADER SEQUENCE                
SEQRES   1 A  710  GLY GLN GLU THR LYS LYS PRO THR LEU GLU GLU LEU ILE          
SEQRES   2 A  710  PRO GLY GLY GLU SER TYR LEU TYR ALA GLU ASN LEU TYR          
SEQRES   3 A  710  GLY LEU GLN TRP TRP GLY ASP GLU CYS ILE LYS PRO GLY          
SEQRES   4 A  710  VAL ASP THR LEU TYR SER ILE GLN PRO LYS THR GLY LYS          
SEQRES   5 A  710  GLU THR MSE VAL ILE THR ARG GLU GLN ILE ASN LYS VAL          
SEQRES   6 A  710  LEU GLU GLU ASN LYS ALA GLY LYS LEU SER HIS LEU TYR          
SEQRES   7 A  710  SER VAL ARG PHE PRO TRP THR ASP LYS ALA GLN MSE LEU          
SEQRES   8 A  710  PHE THR ILE ALA GLY LYS PHE ILE VAL TYR ASN PHE LYS          
SEQRES   9 A  710  ASN ASN GLN VAL VAL SER THR PHE LYS PRO LYS ASP GLY          
SEQRES  10 A  710  ALA ASN ASN GLU ASP TYR CYS ALA ALA SER GLY ASN VAL          
SEQRES  11 A  710  ALA TYR THR ILE ASP ASN ASN LEU TYR VAL ASN GLU LYS          
SEQRES  12 A  710  ALA VAL THR ASN GLU PRO GLU GLY ILE VAL CYS GLY GLN          
SEQRES  13 A  710  THR VAL HIS ARG ASN GLU PHE GLY ILE ASN LYS GLY THR          
SEQRES  14 A  710  PHE TRP SER PRO LYS GLY ASN LEU LEU ALA PHE TYR ARG          
SEQRES  15 A  710  MSE ASP GLU SER MSE VAL THR GLN TYR PRO LEU VAL ASP          
SEQRES  16 A  710  ILE THR ALA ARG VAL GLY GLU VAL ASN ASN VAL ARG TYR          
SEQRES  17 A  710  PRO MSE ALA GLY MSE THR SER HIS GLN VAL LYS VAL GLY          
SEQRES  18 A  710  ILE TYR ASN PRO ALA THR GLY LYS SER ILE TYR LEU ASN          
SEQRES  19 A  710  ALA GLY ASP PRO THR ASP ARG TYR PHE THR ASN ILE SER          
SEQRES  20 A  710  TRP ALA PRO ASP GLU LYS SER LEU TYR LEU ILE GLU VAL          
SEQRES  21 A  710  ASN ARG ASP GLN ASN HIS ALA LYS LEU CYS GLN TYR ASN          
SEQRES  22 A  710  ALA GLU THR GLY GLU PRO MSE GLY VAL LEU TYR GLU GLU          
SEQRES  23 A  710  MSE HIS PRO LYS TYR VAL GLU PRO GLN ASN PRO ILE VAL          
SEQRES  24 A  710  PHE LEU PRO TRP ASP PRO THR LYS PHE ILE TYR GLN SER          
SEQRES  25 A  710  GLN ARG ASP GLY TYR ASN HIS LEU TYR LEU PHE GLU THR          
SEQRES  26 A  710  ASN ALA ALA ASN MSE LYS GLY GLU THR TYR ASN SER ALA          
SEQRES  27 A  710  ASN GLY GLY SER TYR PHE GLN ALA GLY LYS VAL LYS GLN          
SEQRES  28 A  710  LEU THR LYS GLY ASN TRP LEU VAL SER GLU ILE LEU GLY          
SEQRES  29 A  710  PHE ASN THR LYS ARG LYS GLU VAL ILE PHE THR ALA VAL          
SEQRES  30 A  710  GLU GLY LEU ARG SER GLY HIS PHE ALA VAL ASN VAL SER          
SEQRES  31 A  710  ASN GLY LYS ILE SER GLN PRO PHE GLU ASN CYS LYS GLU          
SEQRES  32 A  710  SER GLU HIS SER GLY THR LEU SER ALA SER GLY THR TYR          
SEQRES  33 A  710  LEU ILE ASP ARG TYR SER THR LYS ASP GLN PRO ARG VAL          
SEQRES  34 A  710  ILE ASN LEU VAL ASP THR LYS ASN PHE LYS GLU THR ALA          
SEQRES  35 A  710  ASN LEU LEU THR ALA GLU ASN PRO TYR ASP GLY TYR GLN          
SEQRES  36 A  710  MSE PRO SER ILE GLU THR GLY THR ILE LYS ALA ALA ASP          
SEQRES  37 A  710  GLY THR THR ASP LEU HIS TYR ARG LEU MSE LYS PRO ALA          
SEQRES  38 A  710  ASN PHE ASP PRO ALA LYS LYS TYR PRO VAL ILE VAL TYR          
SEQRES  39 A  710  VAL TYR GLY GLY PRO HIS ALA GLN CYS VAL THR GLY GLY          
SEQRES  40 A  710  TRP GLN ASN GLY ALA ARG GLY TRP ASP THR TYR MSE ALA          
SEQRES  41 A  710  SER LYS GLY TYR ILE MSE PHE THR ILE ASP ASN ARG GLY          
SEQRES  42 A  710  SER SER ASN ARG GLY LEU THR PHE GLU ASN ALA THR PHE          
SEQRES  43 A  710  ARG ARG LEU GLY ILE GLU GLU GLY LYS ASP GLN VAL LYS          
SEQRES  44 A  710  GLY VAL GLU PHE LEU LYS SER LEU PRO TYR VAL ASP SER          
SEQRES  45 A  710  GLU ARG ILE GLY VAL HIS GLY TRP SER PHE GLY GLY HIS          
SEQRES  46 A  710  MSE THR THR ALA LEU MSE LEU ARG TYR PRO GLU ILE PHE          
SEQRES  47 A  710  LYS VAL GLY VAL ALA GLY GLY PRO VAL ILE ASP TRP GLY          
SEQRES  48 A  710  TYR TYR GLU ILE MSE TYR GLY GLU ARG TYR MSE ASP THR          
SEQRES  49 A  710  PRO GLU SER ASN PRO GLU GLY TYR LYS GLU CYS ASN LEU          
SEQRES  50 A  710  LYS ASN LEU ALA ASP GLN LEU LYS GLY HIS LEU LEU ILE          
SEQRES  51 A  710  ILE HIS ASP ASP HIS ASP ASP THR CYS VAL PRO GLN HIS          
SEQRES  52 A  710  THR LEU SER PHE MSE LYS ALA CYS VAL ASP ALA ARG THR          
SEQRES  53 A  710  TYR PRO ASP LEU PHE ILE TYR PRO CYS HIS LYS HIS ASN          
SEQRES  54 A  710  VAL ALA GLY ARG ASP ARG VAL HIS LEU HIS GLU LYS ILE          
SEQRES  55 A  710  THR ARG TYR PHE GLU GLN ASN LEU                              
SEQRES   1 B  710  GLY GLN GLU THR LYS LYS PRO THR LEU GLU GLU LEU ILE          
SEQRES   2 B  710  PRO GLY GLY GLU SER TYR LEU TYR ALA GLU ASN LEU TYR          
SEQRES   3 B  710  GLY LEU GLN TRP TRP GLY ASP GLU CYS ILE LYS PRO GLY          
SEQRES   4 B  710  VAL ASP THR LEU TYR SER ILE GLN PRO LYS THR GLY LYS          
SEQRES   5 B  710  GLU THR MSE VAL ILE THR ARG GLU GLN ILE ASN LYS VAL          
SEQRES   6 B  710  LEU GLU GLU ASN LYS ALA GLY LYS LEU SER HIS LEU TYR          
SEQRES   7 B  710  SER VAL ARG PHE PRO TRP THR ASP LYS ALA GLN MSE LEU          
SEQRES   8 B  710  PHE THR ILE ALA GLY LYS PHE ILE VAL TYR ASN PHE LYS          
SEQRES   9 B  710  ASN ASN GLN VAL VAL SER THR PHE LYS PRO LYS ASP GLY          
SEQRES  10 B  710  ALA ASN ASN GLU ASP TYR CYS ALA ALA SER GLY ASN VAL          
SEQRES  11 B  710  ALA TYR THR ILE ASP ASN ASN LEU TYR VAL ASN GLU LYS          
SEQRES  12 B  710  ALA VAL THR ASN GLU PRO GLU GLY ILE VAL CYS GLY GLN          
SEQRES  13 B  710  THR VAL HIS ARG ASN GLU PHE GLY ILE ASN LYS GLY THR          
SEQRES  14 B  710  PHE TRP SER PRO LYS GLY ASN LEU LEU ALA PHE TYR ARG          
SEQRES  15 B  710  MSE ASP GLU SER MSE VAL THR GLN TYR PRO LEU VAL ASP          
SEQRES  16 B  710  ILE THR ALA ARG VAL GLY GLU VAL ASN ASN VAL ARG TYR          
SEQRES  17 B  710  PRO MSE ALA GLY MSE THR SER HIS GLN VAL LYS VAL GLY          
SEQRES  18 B  710  ILE TYR ASN PRO ALA THR GLY LYS SER ILE TYR LEU ASN          
SEQRES  19 B  710  ALA GLY ASP PRO THR ASP ARG TYR PHE THR ASN ILE SER          
SEQRES  20 B  710  TRP ALA PRO ASP GLU LYS SER LEU TYR LEU ILE GLU VAL          
SEQRES  21 B  710  ASN ARG ASP GLN ASN HIS ALA LYS LEU CYS GLN TYR ASN          
SEQRES  22 B  710  ALA GLU THR GLY GLU PRO MSE GLY VAL LEU TYR GLU GLU          
SEQRES  23 B  710  MSE HIS PRO LYS TYR VAL GLU PRO GLN ASN PRO ILE VAL          
SEQRES  24 B  710  PHE LEU PRO TRP ASP PRO THR LYS PHE ILE TYR GLN SER          
SEQRES  25 B  710  GLN ARG ASP GLY TYR ASN HIS LEU TYR LEU PHE GLU THR          
SEQRES  26 B  710  ASN ALA ALA ASN MSE LYS GLY GLU THR TYR ASN SER ALA          
SEQRES  27 B  710  ASN GLY GLY SER TYR PHE GLN ALA GLY LYS VAL LYS GLN          
SEQRES  28 B  710  LEU THR LYS GLY ASN TRP LEU VAL SER GLU ILE LEU GLY          
SEQRES  29 B  710  PHE ASN THR LYS ARG LYS GLU VAL ILE PHE THR ALA VAL          
SEQRES  30 B  710  GLU GLY LEU ARG SER GLY HIS PHE ALA VAL ASN VAL SER          
SEQRES  31 B  710  ASN GLY LYS ILE SER GLN PRO PHE GLU ASN CYS LYS GLU          
SEQRES  32 B  710  SER GLU HIS SER GLY THR LEU SER ALA SER GLY THR TYR          
SEQRES  33 B  710  LEU ILE ASP ARG TYR SER THR LYS ASP GLN PRO ARG VAL          
SEQRES  34 B  710  ILE ASN LEU VAL ASP THR LYS ASN PHE LYS GLU THR ALA          
SEQRES  35 B  710  ASN LEU LEU THR ALA GLU ASN PRO TYR ASP GLY TYR GLN          
SEQRES  36 B  710  MSE PRO SER ILE GLU THR GLY THR ILE LYS ALA ALA ASP          
SEQRES  37 B  710  GLY THR THR ASP LEU HIS TYR ARG LEU MSE LYS PRO ALA          
SEQRES  38 B  710  ASN PHE ASP PRO ALA LYS LYS TYR PRO VAL ILE VAL TYR          
SEQRES  39 B  710  VAL TYR GLY GLY PRO HIS ALA GLN CYS VAL THR GLY GLY          
SEQRES  40 B  710  TRP GLN ASN GLY ALA ARG GLY TRP ASP THR TYR MSE ALA          
SEQRES  41 B  710  SER LYS GLY TYR ILE MSE PHE THR ILE ASP ASN ARG GLY          
SEQRES  42 B  710  SER SER ASN ARG GLY LEU THR PHE GLU ASN ALA THR PHE          
SEQRES  43 B  710  ARG ARG LEU GLY ILE GLU GLU GLY LYS ASP GLN VAL LYS          
SEQRES  44 B  710  GLY VAL GLU PHE LEU LYS SER LEU PRO TYR VAL ASP SER          
SEQRES  45 B  710  GLU ARG ILE GLY VAL HIS GLY TRP SER PHE GLY GLY HIS          
SEQRES  46 B  710  MSE THR THR ALA LEU MSE LEU ARG TYR PRO GLU ILE PHE          
SEQRES  47 B  710  LYS VAL GLY VAL ALA GLY GLY PRO VAL ILE ASP TRP GLY          
SEQRES  48 B  710  TYR TYR GLU ILE MSE TYR GLY GLU ARG TYR MSE ASP THR          
SEQRES  49 B  710  PRO GLU SER ASN PRO GLU GLY TYR LYS GLU CYS ASN LEU          
SEQRES  50 B  710  LYS ASN LEU ALA ASP GLN LEU LYS GLY HIS LEU LEU ILE          
SEQRES  51 B  710  ILE HIS ASP ASP HIS ASP ASP THR CYS VAL PRO GLN HIS          
SEQRES  52 B  710  THR LEU SER PHE MSE LYS ALA CYS VAL ASP ALA ARG THR          
SEQRES  53 B  710  TYR PRO ASP LEU PHE ILE TYR PRO CYS HIS LYS HIS ASN          
SEQRES  54 B  710  VAL ALA GLY ARG ASP ARG VAL HIS LEU HIS GLU LYS ILE          
SEQRES  55 B  710  THR ARG TYR PHE GLU GLN ASN LEU                              
MODRES 4Q1V MSE A   77  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  112  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  205  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  209  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  232  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  235  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  302  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  309  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  352  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  478  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  500  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  541  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  548  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  608  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  613  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  638  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  644  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE A  690  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B   77  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  112  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  205  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  209  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  232  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  235  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  302  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  309  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  352  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  478  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  500  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  541  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  548  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  608  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  613  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  638  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  644  MET  SELENOMETHIONINE                                   
MODRES 4Q1V MSE B  690  MET  SELENOMETHIONINE                                   
HET    MSE  A  77       8                                                       
HET    MSE  A 112       8                                                       
HET    MSE  A 205       8                                                       
HET    MSE  A 209       8                                                       
HET    MSE  A 232       8                                                       
HET    MSE  A 235       8                                                       
HET    MSE  A 302       8                                                       
HET    MSE  A 309       8                                                       
HET    MSE  A 352       8                                                       
HET    MSE  A 478       8                                                       
HET    MSE  A 500       8                                                       
HET    MSE  A 541       8                                                       
HET    MSE  A 548       8                                                       
HET    MSE  A 608       8                                                       
HET    MSE  A 613       8                                                       
HET    MSE  A 638       8                                                       
HET    MSE  A 644       8                                                       
HET    MSE  A 690       8                                                       
HET    MSE  B  77       8                                                       
HET    MSE  B 112       8                                                       
HET    MSE  B 205       8                                                       
HET    MSE  B 209       8                                                       
HET    MSE  B 232       8                                                       
HET    MSE  B 235       8                                                       
HET    MSE  B 302       8                                                       
HET    MSE  B 309       8                                                       
HET    MSE  B 352       8                                                       
HET    MSE  B 478       8                                                       
HET    MSE  B 500       8                                                       
HET    MSE  B 541       8                                                       
HET    MSE  B 548       8                                                       
HET    MSE  B 608       8                                                       
HET    MSE  B 613       8                                                       
HET    MSE  B 638       8                                                       
HET    MSE  B 644       8                                                       
HET    MSE  B 690       8                                                       
HET    PEG  A 801       7                                                       
HET    PEG  A 802       7                                                       
HET     MG  A 803       1                                                       
HET    PEG  B 801       7                                                       
HET     MG  B 802       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   1  MSE    36(C5 H11 N O2 SE)                                           
FORMUL   3  PEG    3(C4 H10 O3)                                                 
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   8  HOH   *641(H2 O)                                                    
HELIX    1   1 THR A   30  ILE A   35  1                                   6    
HELIX    2   2 ARG A   81  ASN A   91  1                                  11    
HELIX    3   3 VAL A  180  GLU A  184  5                                   5    
HELIX    4   4 ASN A  348  MSE A  352  5                                   5    
HELIX    5   5 PRO A  419  CYS A  423  5                                   5    
HELIX    6   6 GLY A  529  ALA A  534  5                                   6    
HELIX    7   7 ARG A  535  LYS A  544  1                                  10    
HELIX    8   8 GLY A  560  ASN A  565  1                                   6    
HELIX    9   9 ALA A  566  PHE A  568  5                                   3    
HELIX   10  10 GLY A  572  SER A  588  1                                  17    
HELIX   11  11 SER A  603  TYR A  616  1                                  14    
HELIX   12  12 ASP A  631  TYR A  635  5                                   5    
HELIX   13  13 GLU A  636  ASP A  645  1                                  10    
HELIX   14  14 ASN A  650  CYS A  657  1                                   8    
HELIX   15  15 ASN A  658  LEU A  666  5                                   9    
HELIX   16  16 PRO A  683  ARG A  697  1                                  15    
HELIX   17  17 ARG A  715  LEU A  732  1                                  18    
HELIX   18  18 THR B   30  ILE B   35  1                                   6    
HELIX   19  19 ARG B   81  ASN B   91  1                                  11    
HELIX   20  20 VAL B  180  GLU B  184  5                                   5    
HELIX   21  21 ASN B  348  MSE B  352  5                                   5    
HELIX   22  22 PRO B  419  CYS B  423  5                                   5    
HELIX   23  23 GLY B  529  ALA B  534  5                                   6    
HELIX   24  24 ARG B  535  LYS B  544  1                                  10    
HELIX   25  25 GLY B  560  ALA B  566  1                                   7    
HELIX   26  26 GLY B  572  SER B  588  1                                  17    
HELIX   27  27 SER B  603  TYR B  616  1                                  14    
HELIX   28  28 ASP B  631  TYR B  635  5                                   5    
HELIX   29  29 GLU B  636  ASP B  645  1                                  10    
HELIX   30  30 ASN B  650  CYS B  657  1                                   8    
HELIX   31  31 ASN B  658  LEU B  666  5                                   9    
HELIX   32  32 PRO B  683  ARG B  697  1                                  15    
HELIX   33  33 ARG B  715  LEU B  732  1                                  18    
SHEET    1   A 4 GLN A  51  TRP A  53  0                                        
SHEET    2   A 4 GLU A  56  PRO A  60 -1  O  GLU A  56   N  TRP A  53           
SHEET    3   A 4 THR A  64  ILE A  68 -1  O  ILE A  68   N  CYS A  57           
SHEET    4   A 4 GLU A  75  THR A  80 -1  O  THR A  76   N  SER A  67           
SHEET    1   B 3 GLN A 111  ILE A 116  0                                        
SHEET    2   B 3 LYS A 119  ASN A 124 -1  O  ILE A 121   N  PHE A 114           
SHEET    3   B 3 GLN A 129  PHE A 134 -1  O  PHE A 134   N  PHE A 120           
SHEET    1   C 4 ASN A 141  TYR A 145  0                                        
SHEET    2   C 4 VAL A 152  ILE A 156 -1  O  ALA A 153   N  ASP A 144           
SHEET    3   C 4 ASN A 159  VAL A 162 -1  O  TYR A 161   N  TYR A 154           
SHEET    4   C 4 LYS A 165  ALA A 166 -1  O  LYS A 165   N  VAL A 162           
SHEET    1   D 3 ILE A 174  CYS A 176  0                                        
SHEET    2   D 3 LEU A 200  ASP A 206 -1  O  MSE A 205   N  VAL A 175           
SHEET    3   D 3 THR A 191  TRP A 193 -1  N  PHE A 192   O  ALA A 201           
SHEET    1   E 4 ILE A 174  CYS A 176  0                                        
SHEET    2   E 4 LEU A 200  ASP A 206 -1  O  MSE A 205   N  VAL A 175           
SHEET    3   E 4 GLN A 239  TYR A 245 -1  O  TYR A 245   N  LEU A 200           
SHEET    4   E 4 SER A 252  TYR A 254 -1  O  ILE A 253   N  ILE A 244           
SHEET    1   F 2 GLN A 212  ASP A 217  0                                        
SHEET    2   F 2 GLU A 224  ARG A 229 -1  O  ASN A 226   N  LEU A 215           
SHEET    1   G 6 ARG A 263  TRP A 270  0                                        
SHEET    2   G 6 SER A 276  ASN A 283 -1  O  TYR A 278   N  SER A 269           
SHEET    3   G 6 HIS A 288  ASN A 295 -1  O  TYR A 294   N  LEU A 277           
SHEET    4   G 6 PRO A 301  MSE A 309 -1  O  GLU A 308   N  ALA A 289           
SHEET    5   G 6 SER A 364  ALA A 368 -1  O  SER A 364   N  MSE A 309           
SHEET    6   G 6 GLY A 354  ASN A 358 -1  N  GLU A 355   O  GLN A 367           
SHEET    1   H 4 VAL A 321  LEU A 323  0                                        
SHEET    2   H 4 ASP A 326  SER A 334 -1  O  ILE A 331   N  VAL A 321           
SHEET    3   H 4 HIS A 341  GLU A 346 -1  O  PHE A 345   N  PHE A 330           
SHEET    4   H 4 LYS A 372  GLN A 373 -1  O  LYS A 372   N  LEU A 344           
SHEET    1   I 3 LEU A 380  ASN A 388  0                                        
SHEET    2   I 3 GLU A 393  GLU A 400 -1  O  ILE A 395   N  GLY A 386           
SHEET    3   I 3 ARG A 403  ASN A 410 -1  O  PHE A 407   N  PHE A 396           
SHEET    1   J 4 GLU A 427  LEU A 432  0                                        
SHEET    2   J 4 TYR A 438  THR A 445 -1  O  ILE A 440   N  THR A 431           
SHEET    3   J 4 GLN A 448  ASP A 456 -1  O  ASN A 453   N  ASP A 441           
SHEET    4   J 4 GLU A 462  THR A 468 -1  O  THR A 463   N  LEU A 454           
SHEET    1   K 8 SER A 480  LYS A 487  0                                        
SHEET    2   K 8 ASP A 494  LYS A 501 -1  O  LEU A 499   N  GLU A 482           
SHEET    3   K 8 ILE A 547  ILE A 551 -1  O  MSE A 548   N  MSE A 500           
SHEET    4   K 8 TYR A 511  TYR A 516  1  N  TYR A 516   O  PHE A 549           
SHEET    5   K 8 VAL A 592  TRP A 602  1  O  GLY A 598   N  VAL A 513           
SHEET    6   K 8 VAL A 622  GLY A 626  1  O  GLY A 626   N  GLY A 601           
SHEET    7   K 8 HIS A 669  ASP A 675  1  O  ILE A 673   N  ALA A 625           
SHEET    8   K 8 ASP A 701  TYR A 705  1  O  ASP A 701   N  LEU A 670           
SHEET    1   L 4 GLN B  51  TRP B  53  0                                        
SHEET    2   L 4 GLU B  56  PRO B  60 -1  O  ILE B  58   N  GLN B  51           
SHEET    3   L 4 THR B  64  ILE B  68 -1  O  ILE B  68   N  CYS B  57           
SHEET    4   L 4 GLU B  75  THR B  80 -1  O  THR B  76   N  SER B  67           
SHEET    1   M 3 GLN B 111  ILE B 116  0                                        
SHEET    2   M 3 LYS B 119  ASN B 124 -1  O  ILE B 121   N  PHE B 114           
SHEET    3   M 3 GLN B 129  PHE B 134 -1  O  PHE B 134   N  PHE B 120           
SHEET    1   N 4 ASN B 141  TYR B 145  0                                        
SHEET    2   N 4 VAL B 152  ILE B 156 -1  O  ALA B 153   N  ASP B 144           
SHEET    3   N 4 ASN B 159  VAL B 162 -1  O  TYR B 161   N  TYR B 154           
SHEET    4   N 4 LYS B 165  ALA B 166 -1  O  LYS B 165   N  VAL B 162           
SHEET    1   O 3 ILE B 174  CYS B 176  0                                        
SHEET    2   O 3 LEU B 200  ASP B 206 -1  O  MSE B 205   N  VAL B 175           
SHEET    3   O 3 THR B 191  TRP B 193 -1  N  PHE B 192   O  ALA B 201           
SHEET    1   P 4 ILE B 174  CYS B 176  0                                        
SHEET    2   P 4 LEU B 200  ASP B 206 -1  O  MSE B 205   N  VAL B 175           
SHEET    3   P 4 GLN B 239  TYR B 245 -1  O  TYR B 245   N  LEU B 200           
SHEET    4   P 4 SER B 252  TYR B 254 -1  O  ILE B 253   N  ILE B 244           
SHEET    1   Q 2 GLN B 212  ASP B 217  0                                        
SHEET    2   Q 2 GLU B 224  ARG B 229 -1  O  ASN B 226   N  LEU B 215           
SHEET    1   R 6 ARG B 263  TRP B 270  0                                        
SHEET    2   R 6 SER B 276  ASN B 283 -1  O  TYR B 278   N  SER B 269           
SHEET    3   R 6 HIS B 288  ASN B 295 -1  O  TYR B 294   N  LEU B 277           
SHEET    4   R 6 PRO B 301  MSE B 309 -1  O  GLU B 308   N  ALA B 289           
SHEET    5   R 6 SER B 364  ALA B 368 -1  O  SER B 364   N  MSE B 309           
SHEET    6   R 6 GLY B 354  ASN B 358 -1  N  GLU B 355   O  GLN B 367           
SHEET    1   S 4 VAL B 321  LEU B 323  0                                        
SHEET    2   S 4 ASP B 326  SER B 334 -1  O  ILE B 331   N  VAL B 321           
SHEET    3   S 4 HIS B 341  GLU B 346 -1  O  PHE B 345   N  PHE B 330           
SHEET    4   S 4 LYS B 372  GLN B 373 -1  O  LYS B 372   N  LEU B 344           
SHEET    1   T 3 LEU B 380  ASN B 388  0                                        
SHEET    2   T 3 GLU B 393  GLU B 400 -1  O  ILE B 395   N  GLY B 386           
SHEET    3   T 3 ARG B 403  ASN B 410 -1  O  PHE B 407   N  PHE B 396           
SHEET    1   U 4 GLU B 427  LEU B 432  0                                        
SHEET    2   U 4 TYR B 438  SER B 444 -1  O  ILE B 440   N  THR B 431           
SHEET    3   U 4 VAL B 451  ASP B 456 -1  O  ASN B 453   N  ASP B 441           
SHEET    4   U 4 GLU B 462  THR B 468 -1  O  THR B 463   N  LEU B 454           
SHEET    1   V 8 SER B 480  LYS B 487  0                                        
SHEET    2   V 8 ASP B 494  LYS B 501 -1  O  LEU B 499   N  GLU B 482           
SHEET    3   V 8 ILE B 547  ILE B 551 -1  O  THR B 550   N  ARG B 498           
SHEET    4   V 8 TYR B 511  TYR B 516  1  N  TYR B 516   O  PHE B 549           
SHEET    5   V 8 VAL B 592  TRP B 602  1  O  ARG B 596   N  VAL B 513           
SHEET    6   V 8 VAL B 622  GLY B 626  1  O  GLY B 626   N  GLY B 601           
SHEET    7   V 8 HIS B 669  ASP B 675  1  O  LEU B 671   N  ALA B 625           
SHEET    8   V 8 ASP B 701  TYR B 705  1  O  ASP B 701   N  LEU B 670           
LINK         C   THR A  76                 N   MSE A  77     1555   1555  1.33  
LINK         C   MSE A  77                 N   VAL A  78     1555   1555  1.33  
LINK         C   GLN A 111                 N   MSE A 112     1555   1555  1.35  
LINK         C   MSE A 112                 N   LEU A 113     1555   1555  1.34  
LINK         C   ARG A 204                 N   MSE A 205     1555   1555  1.32  
LINK         C   MSE A 205                 N   ASP A 206     1555   1555  1.33  
LINK         C   SER A 208                 N   MSE A 209     1555   1555  1.34  
LINK         C   MSE A 209                 N   VAL A 210     1555   1555  1.35  
LINK         C   PRO A 231                 N   MSE A 232     1555   1555  1.34  
LINK         C   MSE A 232                 N   ALA A 233     1555   1555  1.37  
LINK         C   GLY A 234                 N   MSE A 235     1555   1555  1.33  
LINK         C   MSE A 235                 N   THR A 236     1555   1555  1.34  
LINK         C   PRO A 301                 N   MSE A 302     1555   1555  1.34  
LINK         C   MSE A 302                 N   GLY A 303     1555   1555  1.32  
LINK         C   GLU A 308                 N   MSE A 309     1555   1555  1.34  
LINK         C   MSE A 309                 N   HIS A 310     1555   1555  1.34  
LINK         C   ASN A 351                 N   MSE A 352     1555   1555  1.35  
LINK         C   MSE A 352                 N   LYS A 353     1555   1555  1.35  
LINK         C   GLN A 477                 N   MSE A 478     1555   1555  1.33  
LINK         C   MSE A 478                 N   PRO A 479     1555   1555  1.34  
LINK         C   LEU A 499                 N   MSE A 500     1555   1555  1.33  
LINK         C   MSE A 500                 N   LYS A 501     1555   1555  1.34  
LINK         C   TYR A 540                 N   MSE A 541     1555   1555  1.34  
LINK         C   MSE A 541                 N   ALA A 542     1555   1555  1.35  
LINK         C   ILE A 547                 N   MSE A 548     1555   1555  1.32  
LINK         C   MSE A 548                 N   PHE A 549     1555   1555  1.33  
LINK         C   HIS A 607                 N   MSE A 608     1555   1555  1.34  
LINK         C   MSE A 608                 N   THR A 609     1555   1555  1.34  
LINK         C   LEU A 612                 N   MSE A 613     1555   1555  1.35  
LINK         C   MSE A 613                 N   LEU A 614     1555   1555  1.36  
LINK         C   ILE A 637                 N   MSE A 638     1555   1555  1.36  
LINK         C   MSE A 638                 N   TYR A 639     1555   1555  1.34  
LINK         C   TYR A 643                 N   MSE A 644     1555   1555  1.34  
LINK         C   MSE A 644                 N   ASP A 645     1555   1555  1.35  
LINK         C   PHE A 689                 N   MSE A 690     1555   1555  1.35  
LINK         C   MSE A 690                 N   LYS A 691     1555   1555  1.36  
LINK         C   THR B  76                 N   MSE B  77     1555   1555  1.33  
LINK         C   MSE B  77                 N   VAL B  78     1555   1555  1.33  
LINK         C   GLN B 111                 N   MSE B 112     1555   1555  1.32  
LINK         C   MSE B 112                 N   LEU B 113     1555   1555  1.34  
LINK         C   ARG B 204                 N   MSE B 205     1555   1555  1.33  
LINK         C   MSE B 205                 N   ASP B 206     1555   1555  1.34  
LINK         C   SER B 208                 N   MSE B 209     1555   1555  1.34  
LINK         C   MSE B 209                 N   VAL B 210     1555   1555  1.34  
LINK         C   PRO B 231                 N   MSE B 232     1555   1555  1.33  
LINK         C   MSE B 232                 N   ALA B 233     1555   1555  1.35  
LINK         C   GLY B 234                 N   MSE B 235     1555   1555  1.33  
LINK         C   MSE B 235                 N   THR B 236     1555   1555  1.33  
LINK         C   PRO B 301                 N   MSE B 302     1555   1555  1.34  
LINK         C   MSE B 302                 N   GLY B 303     1555   1555  1.33  
LINK         C   GLU B 308                 N   MSE B 309     1555   1555  1.34  
LINK         C   MSE B 309                 N   HIS B 310     1555   1555  1.35  
LINK         C   ASN B 351                 N   MSE B 352     1555   1555  1.35  
LINK         C   MSE B 352                 N   LYS B 353     1555   1555  1.34  
LINK         C   GLN B 477                 N   MSE B 478     1555   1555  1.33  
LINK         C   MSE B 478                 N   PRO B 479     1555   1555  1.34  
LINK         C   LEU B 499                 N   MSE B 500     1555   1555  1.33  
LINK         C   MSE B 500                 N   LYS B 501     1555   1555  1.34  
LINK         C   TYR B 540                 N   MSE B 541     1555   1555  1.34  
LINK         C   MSE B 541                 N   ALA B 542     1555   1555  1.35  
LINK         C   ILE B 547                 N   MSE B 548     1555   1555  1.32  
LINK         C   MSE B 548                 N   PHE B 549     1555   1555  1.34  
LINK         C   HIS B 607                 N   MSE B 608     1555   1555  1.34  
LINK         C   MSE B 608                 N   THR B 609     1555   1555  1.37  
LINK         C   LEU B 612                 N   MSE B 613     1555   1555  1.35  
LINK         C   MSE B 613                 N   LEU B 614     1555   1555  1.37  
LINK         C   ILE B 637                 N   MSE B 638     1555   1555  1.34  
LINK         C   MSE B 638                 N   TYR B 639     1555   1555  1.34  
LINK         C   TYR B 643                 N   MSE B 644     1555   1555  1.34  
LINK         C   MSE B 644                 N   ASP B 645     1555   1555  1.35  
LINK         C   PHE B 689                 N   MSE B 690     1555   1555  1.35  
LINK         C   MSE B 690                 N   LYS B 691     1555   1555  1.35  
LINK        MG    MG B 802                 O   HOH B1171     1555   1555  1.95  
LINK        MG    MG B 802                 O   HOH B1024     1555   1555  2.04  
LINK        MG    MG A 803                 O   HOH A 925     1555   1555  2.05  
LINK         OD1 ASP A 285                MG    MG A 803     1555   1555  2.08  
LINK         OD1 ASP B 285                MG    MG B 802     1555   1555  2.12  
LINK        MG    MG A 803                 O   HOH A 924     1555   1555  2.15  
LINK         O   ASP A 285                MG    MG A 803     1555   1555  2.23  
LINK        MG    MG A 803                 O   HOH A1235     1555   1555  2.24  
LINK         O   ASP B 285                MG    MG B 802     1555   1555  2.25  
LINK         OD1 ASP B 645                MG    MG B 802     1555   1555  2.26  
LINK         OD1 ASP A 645                MG    MG A 803     1555   1555  2.32  
LINK        MG    MG B 802                 O   HOH B1056     1555   1555  2.52  
SITE     1 AC1  1 GLN A 524                                                     
SITE     1 AC2  3 ARG A 204  LYS A 241  TYR A 254                               
SITE     1 AC3  5 ASP A 285  ASP A 645  HOH A 924  HOH A 925                    
SITE     2 AC3  5 HOH A1235                                                     
SITE     1 AC4  6 HIS B 406  GLN B 418  HIS B 428  ASP B 441                    
SITE     2 AC4  6 PHE B 460  GLU B 462                                          
SITE     1 AC5  5 ASP B 285  ASP B 645  HOH B1024  HOH B1056                    
SITE     2 AC5  5 HOH B1171                                                     
CRYST1   92.487  133.703  159.127  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010812  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007479  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006284        0.00000                         
TER    5727      LEU A 732                                                      
TER   11413      LEU B 732                                                      
MASTER      334    0   41   33   90    0    8    611936    2  397  110          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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