GenomeNet

Database: PDB
Entry: 6ENB
LinkDB: 6ENB
Original site: 6ENB 
HEADER    HYDROLASE                               04-OCT-17   6ENB              
TITLE     LTA4 HYDROLASE (E297Q) MUTANT IN COMPLEX WITH PRO-GLY-PRO PEPTIDE     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LTA-4 HYDROLASE,LEUKOTRIENE A(4) HYDROLASE;                 
COMPND   5 EC: 3.3.2.6;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PRO-GLY-PRO;                                               
COMPND  10 CHAIN: B;                                                            
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LTA4H, LTA4;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    LTA4H, SUBSTRATE, HYDROLASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.SRINIVAS                                                            
REVDAT   3   16-OCT-19 6ENB    1       REMARK                                   
REVDAT   2   24-OCT-18 6ENB    1       COMPND SOURCE SEQADV                     
REVDAT   1   13-DEC-17 6ENB    0                                                
JRNL        AUTH   S.NUMAO,F.HASLER,C.LAGUERRE,H.SRINIVAS,N.WACK,P.JAGER,       
JRNL        AUTH 2 A.SCHMID,A.OSMONT,P.ROTHLISBERGER,J.HOUGUENADE,C.BERGSDORF,  
JRNL        AUTH 3 J.DAWSON,N.CARTE,A.HOFMANN,C.MARKERT,L.HARDAKER,A.BILLICH,   
JRNL        AUTH 4 R.M.WOLF,C.A.PENNO,B.BOLLBUCK,W.MILTZ,T.A.ROHN               
JRNL        TITL   FEASIBILITY AND PHYSIOLOGICAL RELEVANCE OF DESIGNING HIGHLY  
JRNL        TITL 2 POTENT AMINOPEPTIDASE-SPARING LEUKOTRIENE A4 HYDROLASE       
JRNL        TITL 3 INHIBITORS.                                                  
JRNL        REF    SCI REP                       V.   7 13591 2017              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   29051536                                                     
JRNL        DOI    10.1038/S41598-017-13490-1                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.84 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
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) : 1.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 59014                          
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)  : 0.157                          
REMARK   3   R VALUE            (WORKING SET)  : 0.155                          
REMARK   3   FREE R VALUE                      : 0.186                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2951                           
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) : 1.84                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.89                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.85                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4324                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2118                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4108                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2089                   
REMARK   3   BIN FREE R VALUE                        : 0.2686                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.00                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 216                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4865                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 676                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.08980                                             
REMARK   3    B22 (A**2) : 5.17940                                              
REMARK   3    B33 (A**2) : -4.08960                                             
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) : 0.172               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.120               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.109               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.111               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.105               
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      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5006   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6806   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1710   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 121    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 719    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5006   ; 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   : 651    ; 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   : 6162   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.58                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 15.81                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    4.2957    3.6843    0.1249           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0218 T22:   -0.0199                                    
REMARK   3     T33:   -0.0333 T12:    0.0036                                    
REMARK   3     T13:    0.0047 T23:   -0.0014                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2291 L22:    0.6768                                    
REMARK   3     L33:    0.1435 L12:    0.0238                                    
REMARK   3     L13:    0.0312 L23:    0.0355                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0216 S12:   -0.0064 S13:   -0.0076                     
REMARK   3     S21:    0.0406 S22:    0.0182 S23:   -0.0449                     
REMARK   3     S31:    0.0196 S32:   -0.0009 S33:    0.0033                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ENB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006891.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59014                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.840                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 0.1 IMIDAZOLE PH 6.8,      
REMARK 280  0.1 M SODIUM ACETATE, 0.005 M YBCL3, VAPOR DIFFUSION, SITTING       
REMARK 280  DROP, TEMPERATURE 298K                                              
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       38.72150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.52900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.78800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.52900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.72150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.78800            
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: 1420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 437    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   801     O    HOH A   805     2555     1.14            
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    GLN A  79       68.22   -112.58                                   
REMARK 500    SER A  80     -128.77     49.27                                   
REMARK 500    ASN A  97       -4.73     78.82                                   
REMARK 500    GLU A 271       40.48    -76.91                                   
REMARK 500    CYS A 274      -17.77     76.66                                   
REMARK 500    PHE A 432       33.97    -98.44                                   
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 A1473        DISTANCE =  7.39 ANGSTROMS                       
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                              YB A 704  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 175   OD1                                                    
REMARK 620 2 HOH A1094   O    59.5                                              
REMARK 620 3 HOH A1227   O   151.4  95.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 295   NE2                                                    
REMARK 620 2 HIS A 299   NE2  82.3                                              
REMARK 620 3 GLU A 318   OE1  85.5  92.3                                        
REMARK 620 4 PRO B   1   O    84.8  93.0 168.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 703  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 481   OD1                                                    
REMARK 620 2 ASP A 481   OD2  53.4                                              
REMARK 620 3 ACT A 702   O   117.2 129.5                                        
REMARK 620 4 ACT A 702   OXT  72.1  81.0  52.9                                  
REMARK 620 5 HOH A 957   O    73.1  82.5 147.2 144.8                            
REMARK 620 6 HOH A1179   O   149.8 144.4  72.5 125.3  84.6                      
REMARK 620 7 ASP A  47   OD1  73.4 126.5  68.2  78.1  87.4  85.7                
REMARK 620 8 ASP A  47   OD2  73.9 126.8  66.8  76.8  88.9  85.8   1.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YB A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YB A 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 705                 
DBREF  6ENB A    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
DBREF  6ENB B    1     3  PDB    6ENB     6ENB             1      3             
SEQADV 6ENB GLY A    0  UNP  P09960              EXPRESSION TAG                 
SEQADV 6ENB GLN A  296  UNP  P09960    GLU   297 CONFLICT                       
SEQRES   1 A  611  GLY PRO GLU ILE VAL ASP THR CYS SER LEU ALA SER PRO          
SEQRES   2 A  611  ALA SER VAL CYS ARG THR LYS HIS LEU HIS LEU ARG CYS          
SEQRES   3 A  611  SER VAL ASP PHE THR ARG ARG THR LEU THR GLY THR ALA          
SEQRES   4 A  611  ALA LEU THR VAL GLN SER GLN GLU ASP ASN LEU ARG SER          
SEQRES   5 A  611  LEU VAL LEU ASP THR LYS ASP LEU THR ILE GLU LYS VAL          
SEQRES   6 A  611  VAL ILE ASN GLY GLN GLU VAL LYS TYR ALA LEU GLY GLU          
SEQRES   7 A  611  ARG GLN SER TYR LYS GLY SER PRO MET GLU ILE SER LEU          
SEQRES   8 A  611  PRO ILE ALA LEU SER LYS ASN GLN GLU ILE VAL ILE GLU          
SEQRES   9 A  611  ILE SER PHE GLU THR SER PRO LYS SER SER ALA LEU GLN          
SEQRES  10 A  611  TRP LEU THR PRO GLU GLN THR SER GLY LYS GLU HIS PRO          
SEQRES  11 A  611  TYR LEU PHE SER GLN CYS GLN ALA ILE HIS CYS ARG ALA          
SEQRES  12 A  611  ILE LEU PRO CYS GLN ASP THR PRO SER VAL LYS LEU THR          
SEQRES  13 A  611  TYR THR ALA GLU VAL SER VAL PRO LYS GLU LEU VAL ALA          
SEQRES  14 A  611  LEU MET SER ALA ILE ARG ASP GLY GLU THR PRO ASP PRO          
SEQRES  15 A  611  GLU ASP PRO SER ARG LYS ILE TYR LYS PHE ILE GLN LYS          
SEQRES  16 A  611  VAL PRO ILE PRO CYS TYR LEU ILE ALA LEU VAL VAL GLY          
SEQRES  17 A  611  ALA LEU GLU SER ARG GLN ILE GLY PRO ARG THR LEU VAL          
SEQRES  18 A  611  TRP SER GLU LYS GLU GLN VAL GLU LYS SER ALA TYR GLU          
SEQRES  19 A  611  PHE SER GLU THR GLU SER MET LEU LYS ILE ALA GLU ASP          
SEQRES  20 A  611  LEU GLY GLY PRO TYR VAL TRP GLY GLN TYR ASP LEU LEU          
SEQRES  21 A  611  VAL LEU PRO PRO SER PHE PRO TYR GLY GLY MET GLU ASN          
SEQRES  22 A  611  PRO CYS LEU THR PHE VAL THR PRO THR LEU LEU ALA GLY          
SEQRES  23 A  611  ASP LYS SER LEU SER ASN VAL ILE ALA HIS GLN ILE SER          
SEQRES  24 A  611  HIS SER TRP THR GLY ASN LEU VAL THR ASN LYS THR TRP          
SEQRES  25 A  611  ASP HIS PHE TRP LEU ASN GLU GLY HIS THR VAL TYR LEU          
SEQRES  26 A  611  GLU ARG HIS ILE CYS GLY ARG LEU PHE GLY GLU LYS PHE          
SEQRES  27 A  611  ARG HIS PHE ASN ALA LEU GLY GLY TRP GLY GLU LEU GLN          
SEQRES  28 A  611  ASN SER VAL LYS THR PHE GLY GLU THR HIS PRO PHE THR          
SEQRES  29 A  611  LYS LEU VAL VAL ASP LEU THR ASP ILE ASP PRO ASP VAL          
SEQRES  30 A  611  ALA TYR SER SER VAL PRO TYR GLU LYS GLY PHE ALA LEU          
SEQRES  31 A  611  LEU PHE TYR LEU GLU GLN LEU LEU GLY GLY PRO GLU ILE          
SEQRES  32 A  611  PHE LEU GLY PHE LEU LYS ALA TYR VAL GLU LYS PHE SER          
SEQRES  33 A  611  TYR LYS SER ILE THR THR ASP ASP TRP LYS ASP PHE LEU          
SEQRES  34 A  611  TYR SER TYR PHE LYS ASP LYS VAL ASP VAL LEU ASN GLN          
SEQRES  35 A  611  VAL ASP TRP ASN ALA TRP LEU TYR SER PRO GLY LEU PRO          
SEQRES  36 A  611  PRO ILE LYS PRO ASN TYR ASP MET THR LEU THR ASN ALA          
SEQRES  37 A  611  CYS ILE ALA LEU SER GLN ARG TRP ILE THR ALA LYS GLU          
SEQRES  38 A  611  ASP ASP LEU ASN SER PHE ASN ALA THR ASP LEU LYS ASP          
SEQRES  39 A  611  LEU SER SER HIS GLN LEU ASN GLU PHE LEU ALA GLN THR          
SEQRES  40 A  611  LEU GLN ARG ALA PRO LEU PRO LEU GLY HIS ILE LYS ARG          
SEQRES  41 A  611  MET GLN GLU VAL TYR ASN PHE ASN ALA ILE ASN ASN SER          
SEQRES  42 A  611  GLU ILE ARG PHE ARG TRP LEU ARG LEU CYS ILE GLN SER          
SEQRES  43 A  611  LYS TRP GLU ASP ALA ILE PRO LEU ALA LEU LYS MET ALA          
SEQRES  44 A  611  THR GLU GLN GLY ARG MET LYS PHE THR ARG PRO LEU PHE          
SEQRES  45 A  611  LYS ASP LEU ALA ALA PHE ASP LYS SER HIS ASP GLN ALA          
SEQRES  46 A  611  VAL ARG THR TYR GLN GLU HIS LYS ALA SER MET HIS PRO          
SEQRES  47 A  611  VAL THR ALA MET LEU VAL GLY LYS ASP LEU LYS VAL ASP          
SEQRES   1 B    3  PRO GLY PRO                                                  
HET     ZN  A 701       1                                                       
HET    ACT  A 702       4                                                       
HET     YB  A 703       1                                                       
HET     YB  A 704       1                                                       
HET    IMD  A 705       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     IMD IMIDAZOLE                                                        
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  ACT    C2 H3 O2 1-                                                  
FORMUL   5   YB    2(YB 3+)                                                     
FORMUL   7  IMD    C3 H5 N2 1+                                                  
FORMUL   8  HOH   *676(H2 O)                                                    
HELIX    1 AA1 GLN A   79  GLY A   83  5                                   5    
HELIX    2 AA2 THR A  119  THR A  123  5                                   5    
HELIX    3 AA3 HIS A  139  ILE A  143  5                                   5    
HELIX    4 AA4 TYR A  200  ILE A  202  5                                   3    
HELIX    5 AA5 GLU A  223  GLU A  225  5                                   3    
HELIX    6 AA6 GLN A  226  PHE A  234  1                                   9    
HELIX    7 AA7 GLU A  236  GLY A  249  1                                  14    
HELIX    8 AA8 PRO A  280  LEU A  283  5                                   4    
HELIX    9 AA9 SER A  290  HIS A  299  1                                  10    
HELIX   10 AB1 THR A  310  HIS A  313  5                                   4    
HELIX   11 AB2 PHE A  314  GLY A  334  1                                  21    
HELIX   12 AB3 GLY A  334  GLY A  357  1                                  24    
HELIX   13 AB4 HIS A  360  LYS A  364  5                                   5    
HELIX   14 AB5 ASP A  373  TYR A  378  1                                   6    
HELIX   15 AB6 SER A  380  GLY A  398  1                                  19    
HELIX   16 AB7 GLY A  399  SER A  415  1                                  17    
HELIX   17 AB8 THR A  420  PHE A  432  1                                  13    
HELIX   18 AB9 LYS A  435  ASN A  440  1                                   6    
HELIX   19 AC1 ASP A  443  SER A  450  1                                   8    
HELIX   20 AC2 THR A  465  ALA A  478  1                                  14    
HELIX   21 AC3 LYS A  479  PHE A  486  5                                   8    
HELIX   22 AC4 ASN A  487  LYS A  492  5                                   6    
HELIX   23 AC5 SER A  495  GLN A  508  1                                  14    
HELIX   24 AC6 PRO A  513  ASN A  525  1                                  13    
HELIX   25 AC7 PHE A  526  ILE A  529  5                                   4    
HELIX   26 AC8 ASN A  531  SER A  545  1                                  15    
HELIX   27 AC9 TRP A  547  ASP A  549  5                                   3    
HELIX   28 AD1 ALA A  550  GLN A  561  1                                  12    
HELIX   29 AD2 ARG A  563  PHE A  577  1                                  15    
HELIX   30 AD3 PHE A  577  LYS A  592  1                                  16    
HELIX   31 AD4 ALA A  593  MET A  595  5                                   3    
HELIX   32 AD5 HIS A  596  LYS A  608  1                                  13    
SHEET    1 AA1 8 GLN A  69  GLU A  70  0                                        
SHEET    2 AA1 8 LEU A  59  ILE A  66 -1  N  ILE A  66   O  GLN A  69           
SHEET    3 AA1 8 GLU A  99  THR A 108 -1  O  GLU A 107   N  THR A  60           
SHEET    4 AA1 8 THR A  33  SER A  44 -1  N  ALA A  38   O  ILE A 104           
SHEET    5 AA1 8 CYS A  16  ASP A  28 -1  N  LYS A  19   O  THR A  41           
SHEET    6 AA1 8 LYS A 153  PRO A 163  1  O  SER A 161   N  CYS A  25           
SHEET    7 AA1 8 ASP A 183  PRO A 198 -1  O  GLN A 193   N  TYR A 156           
SHEET    8 AA1 8 ILE A 173  ASP A 180 -1  N  THR A 178   O  ILE A 188           
SHEET    1 AA2 3 LEU A  49  THR A  56  0                                        
SHEET    2 AA2 3 SER A  84  LEU A  94 -1  O  ILE A  88   N  LEU A  52           
SHEET    3 AA2 3 TYR A  73  LEU A  75 -1  N  ALA A  74   O  GLU A  87           
SHEET    1 AA3 4 LEU A 115  LEU A 118  0                                        
SHEET    2 AA3 4 TYR A 130  SER A 133 -1  O  TYR A 130   N  LEU A 118           
SHEET    3 AA3 4 LEU A 204  GLY A 207 -1  O  VAL A 206   N  LEU A 131           
SHEET    4 AA3 4 VAL A 167  MET A 170 -1  N  VAL A 167   O  GLY A 207           
SHEET    1 AA4 5 GLU A 210  GLY A 215  0                                        
SHEET    2 AA4 5 THR A 218  SER A 222 -1  O  VAL A 220   N  ARG A 212           
SHEET    3 AA4 5 ASP A 257  VAL A 260  1  O  VAL A 260   N  TRP A 221           
SHEET    4 AA4 5 LEU A 275  VAL A 278  1  O  THR A 276   N  LEU A 259           
SHEET    5 AA4 5 GLY A 269  MET A 270 -1  N  MET A 270   O  PHE A 277           
SHEET    1 AA5 2 VAL A 306  ASN A 308  0                                        
SHEET    2 AA5 2 LYS A 417  ILE A 419  1  O  ILE A 419   N  THR A 307           
LINK         OD1 ASP A 175                YB    YB A 704     1555   1555  2.32  
LINK         NE2 HIS A 295                ZN    ZN A 701     1555   1555  2.33  
LINK         NE2 HIS A 299                ZN    ZN A 701     1555   1555  2.42  
LINK         OE1 GLU A 318                ZN    ZN A 701     1555   1555  2.09  
LINK         OD1 ASP A 481                YB    YB A 703     1555   1555  2.43  
LINK         OD2 ASP A 481                YB    YB A 703     1555   1555  2.44  
LINK         O   PRO B   1                ZN    ZN A 701     1555   1555  2.54  
LINK         O   ACT A 702                YB    YB A 703     1555   1555  2.57  
LINK         OXT ACT A 702                YB    YB A 703     1555   1555  2.41  
LINK        YB    YB A 703                 O   HOH A 957     1555   1555  2.49  
LINK        YB    YB A 703                 O   HOH A1179     1555   1555  2.50  
LINK        YB    YB A 704                 O   HOH A1094     1555   1555  3.22  
LINK         OD1 ASP A  47                YB    YB A 703     1555   1545  2.45  
LINK         OD2 ASP A  47                YB    YB A 703     1555   1545  2.45  
LINK        YB    YB A 704                 O   HOH A1227     1555   4445  2.92  
CISPEP   1 GLN A  136    ALA A  137          0        -0.11                     
CISPEP   2 ALA A  510    PRO A  511          0         5.32                     
SITE     1 AC1  5 HIS A 295  HIS A 299  GLU A 318  PRO B   1                    
SITE     2 AC1  5 GLY B   2                                                     
SITE     1 AC2  9 ASP A  47  ASN A  48  ARG A 174  LYS A 479                    
SITE     2 AC2  9 ASP A 481   YB A 703  HOH A 888  HOH A1179                    
SITE     3 AC2  9 HOH A1195                                                     
SITE     1 AC3  5 ASP A  47  ASP A 481  ACT A 702  HOH A 957                    
SITE     2 AC3  5 HOH A1179                                                     
SITE     1 AC4  2 ASP A 175  HOH A1227                                          
SITE     1 AC5  6 GLY A 344  GLY A 347  GLU A 348  GLU A 501                    
SITE     2 AC5  6 ALA A 504  GLN A 508                                          
CRYST1   77.443   87.576   99.058  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012913  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011419  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010095        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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