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Database: PDB
Entry: 5KHN
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Original site: 5KHN 
HEADER    MEMBRANE PROTEIN                        15-JUN-16   5KHN              
TITLE     CRYSTAL STRUCTURES OF THE BURKHOLDERIA MULTIVORANS HOPANOID           
TITLE    2 TRANSPORTER HPNN                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RND TRANSPORTER;                                           
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA MULTIVORANS;                       
SOURCE   3 ORGANISM_TAXID: 87883;                                               
SOURCE   4 GENE: WM33_10510;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    TRANSMEMBRANE HELICES, MEMBRANE PROTEIN                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.-C.SU,E.W.YU                                                        
REVDAT   4   27-SEP-17 5KHN    1       REMARK                                   
REVDAT   3   05-JUL-17 5KHN    1       JRNL                                     
REVDAT   2   21-JUN-17 5KHN    1       JRNL                                     
REVDAT   1   14-JUN-17 5KHN    0                                                
JRNL        AUTH   N.KUMAR,C.C.SU,T.H.CHOU,A.RADHAKRISHNAN,J.A.DELMAR,          
JRNL        AUTH 2 K.R.RAJASHANKAR,E.W.YU                                       
JRNL        TITL   CRYSTAL STRUCTURES OF THE BURKHOLDERIA MULTIVORANS HOPANOID  
JRNL        TITL 2 TRANSPORTER HPNN.                                            
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 114  6557 2017              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   28584102                                                     
JRNL        DOI    10.1073/PNAS.1619660114                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 93.80                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 38512                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.285                           
REMARK   3   R VALUE            (WORKING SET) : 0.283                           
REMARK   3   FREE R VALUE                     : 0.319                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1927                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 93.8374 -  8.3000    0.99     2698   130  0.2450 0.2843        
REMARK   3     2  8.3000 -  6.5885    1.00     2624   136  0.2569 0.2935        
REMARK   3     3  6.5885 -  5.7558    1.00     2661   130  0.3192 0.3148        
REMARK   3     4  5.7558 -  5.2296    1.00     2590   169  0.2915 0.2883        
REMARK   3     5  5.2296 -  4.8548    1.00     2585   149  0.2667 0.3428        
REMARK   3     6  4.8548 -  4.5686    1.00     2636   133  0.2811 0.3006        
REMARK   3     7  4.5686 -  4.3398    1.00     2597   145  0.2713 0.3269        
REMARK   3     8  4.3398 -  4.1509    1.00     2629   113  0.2887 0.3014        
REMARK   3     9  4.1509 -  3.9911    1.00     2607   128  0.2937 0.3665        
REMARK   3    10  3.9911 -  3.8533    1.00     2609   149  0.3313 0.3692        
REMARK   3    11  3.8533 -  3.7328    1.00     2619   119  0.3456 0.3592        
REMARK   3    12  3.7328 -  3.6261    1.00     2618   120  0.3511 0.3914        
REMARK   3    13  3.6261 -  3.5307    1.00     2623   155  0.3964 0.4359        
REMARK   3    14  3.5307 -  3.4445    0.97     2489   151  0.4236 0.4727        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.720            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.310           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 126.0                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 127.5                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003          12872                                  
REMARK   3   ANGLE     :  0.604          17607                                  
REMARK   3   CHIRALITY :  0.039           2175                                  
REMARK   3   PLANARITY :  0.005           2232                                  
REMARK   3   DIHEDRAL  : 14.396           7726                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5KHN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222248.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 3.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SI(III)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38588                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 11.00                              
REMARK 200  R MERGE                    (I) : 0.12600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.69100                            
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: SIRAS                        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG2000, AND 0.2M LISO4, PH 3.5,     
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 298K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       64.77300            
REMARK 290   SMTRY3   2  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: 5030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 71940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     TYR B   227                                                      
REMARK 465     GLY B   228                                                      
REMARK 465     ALA B   229                                                      
REMARK 465     LEU B   230                                                      
REMARK 465     LYS B   231                                                      
REMARK 465     ALA B   232                                                      
REMARK 465     PRO B   432                                                      
REMARK 465     GLY B   433                                                      
REMARK 465     GLU B   434                                                      
REMARK 465     SER B   435                                                      
REMARK 465     LYS B   436                                                      
REMARK 465     THR B   437                                                      
REMARK 465     GLY B   861                                                      
REMARK 465     LYS B   862                                                      
REMARK 465     PRO B   863                                                      
REMARK 465     ARG B   864                                                      
REMARK 465     VAL B   865                                                      
REMARK 465     LYS B   866                                                      
REMARK 465     ARG B   867                                                      
REMARK 465     ALA B   868                                                      
REMARK 465     LYS B   869                                                      
REMARK 465     ASN B   870                                                      
REMARK 465     GLN B   871                                                      
REMARK 465     SER B   872                                                      
REMARK 465     GLN B   873                                                      
REMARK 465     GLY B   874                                                      
REMARK 465     ILE B   875                                                      
REMARK 465     ASN B   876                                                      
REMARK 465     GLU B   877                                                      
REMARK 465     HIS B   878                                                      
REMARK 465     HIS B   879                                                      
REMARK 465     HIS B   880                                                      
REMARK 465     HIS B   881                                                      
REMARK 465     HIS B   882                                                      
REMARK 465     HIS B   883                                                      
REMARK 465     TYR A   227                                                      
REMARK 465     GLY A   228                                                      
REMARK 465     ALA A   229                                                      
REMARK 465     LEU A   230                                                      
REMARK 465     LYS A   231                                                      
REMARK 465     ALA A   232                                                      
REMARK 465     GLY A   233                                                      
REMARK 465     PRO A   432                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     GLU A   434                                                      
REMARK 465     SER A   435                                                      
REMARK 465     LYS A   436                                                      
REMARK 465     GLY A   861                                                      
REMARK 465     LYS A   862                                                      
REMARK 465     PRO A   863                                                      
REMARK 465     ARG A   864                                                      
REMARK 465     VAL A   865                                                      
REMARK 465     LYS A   866                                                      
REMARK 465     ARG A   867                                                      
REMARK 465     ALA A   868                                                      
REMARK 465     LYS A   869                                                      
REMARK 465     ASN A   870                                                      
REMARK 465     GLN A   871                                                      
REMARK 465     SER A   872                                                      
REMARK 465     GLN A   873                                                      
REMARK 465     GLY A   874                                                      
REMARK 465     ILE A   875                                                      
REMARK 465     ASN A   876                                                      
REMARK 465     GLU A   877                                                      
REMARK 465     HIS A   878                                                      
REMARK 465     HIS A   879                                                      
REMARK 465     HIS A   880                                                      
REMARK 465     HIS A   881                                                      
REMARK 465     HIS A   882                                                      
REMARK 465     HIS A   883                                                      
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     VAL B 206    CG1  CG2                                            
REMARK 470     ASN B 683    CG   OD1  ND2                                       
REMARK 470     MET B 860    CG   SD   CE                                        
REMARK 470     MET A   1    CG   SD   CE                                        
REMARK 470     THR A 437    OG1  CG2                                            
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   OH   TYR B   590     OD2  ASP A   451     1554     2.14            
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    ARG B  15      -47.86     75.27                                   
REMARK 500    PHE B  39       40.10   -159.72                                   
REMARK 500    ALA B 199      102.28   -168.50                                   
REMARK 500    ASP B 248      -40.43     61.93                                   
REMARK 500    LEU B 296       59.06   -110.54                                   
REMARK 500    ARG B 297       83.78    -49.97                                   
REMARK 500    MET B 323       -2.67   -140.78                                   
REMARK 500    ALA B 333       31.24    -90.10                                   
REMARK 500    TYR B 397       68.00   -150.60                                   
REMARK 500    ALA B 430      130.15     66.46                                   
REMARK 500    ASN B 507       55.81   -116.90                                   
REMARK 500    ALA B 544     -145.15     61.18                                   
REMARK 500    GLN B 546       61.23   -119.44                                   
REMARK 500    ALA B 615       69.16   -150.86                                   
REMARK 500    ALA B 616      -62.91   -147.00                                   
REMARK 500    GLN B 646     -168.15     65.90                                   
REMARK 500    TRP B 661      -47.07   -144.58                                   
REMARK 500    VAL B 680      -92.39   -131.85                                   
REMARK 500    ASP B 685        9.12    -68.16                                   
REMARK 500    ARG B 741      127.05     92.82                                   
REMARK 500    ASN B 771     -148.88   -108.86                                   
REMARK 500    ALA B 811      -21.73     81.43                                   
REMARK 500    PHE B 855       40.75    -81.93                                   
REMARK 500    ARG A  16       74.93   -117.21                                   
REMARK 500    PHE A  39       90.77    -65.05                                   
REMARK 500    VAL A 206      -90.05   -143.74                                   
REMARK 500    ALA A 211       54.07   -106.95                                   
REMARK 500    GLN A 235     -172.80     62.55                                   
REMARK 500    ALA A 295      -84.42    -66.41                                   
REMARK 500    SER A 298      113.09   -160.28                                   
REMARK 500    ILE A 363     -131.32     51.07                                   
REMARK 500    PRO A 394       30.87    -77.58                                   
REMARK 500    PRO A 438      -70.47    -57.51                                   
REMARK 500    LEU A 475       89.85    -62.55                                   
REMARK 500    ASP A 486       97.57     63.50                                   
REMARK 500    ALA A 505       62.11    -64.22                                   
REMARK 500    ALA A 544      -78.96    -68.17                                   
REMARK 500    THR A 565       58.89   -112.81                                   
REMARK 500    PRO A 568     -177.91    -66.27                                   
REMARK 500    PRO A 571       94.95    -61.46                                   
REMARK 500    ALA A 616      -79.38   -105.31                                   
REMARK 500    ASP A 617     -166.23   -169.33                                   
REMARK 500    PHE A 628      -45.16   -136.93                                   
REMARK 500    PRO A 664       73.04    -53.97                                   
REMARK 500    ASP A 665     -128.14   -177.93                                   
REMARK 500    LYS A 675      120.96    -18.65                                   
REMARK 500    VAL A 676       70.04   -110.81                                   
REMARK 500    ASP A 685       23.15    -74.38                                   
REMARK 500    THR A 686      -74.48    -71.87                                   
REMARK 500    ALA A 698      -74.60    -71.44                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5KHS   RELATED DB: PDB                                   
DBREF1 5KHN B    1   877  UNP                  A0A1B4TSD3_9BURK                 
DBREF2 5KHN B     A0A1B4TSD3                          1         877             
DBREF1 5KHN A    1   877  UNP                  A0A1B4TSD3_9BURK                 
DBREF2 5KHN A     A0A1B4TSD3                          1         877             
SEQADV 5KHN GLY B  360  UNP  A0A1B4TSD ASP   360 ENGINEERED MUTATION            
SEQADV 5KHN ALA B  362  UNP  A0A1B4TSD ARG   362 ENGINEERED MUTATION            
SEQADV 5KHN ALA B  365  UNP  A0A1B4TSD HIS   365 ENGINEERED MUTATION            
SEQADV 5KHN HIS B  878  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQADV 5KHN HIS B  879  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQADV 5KHN HIS B  880  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQADV 5KHN HIS B  881  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQADV 5KHN HIS B  882  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQADV 5KHN HIS B  883  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQADV 5KHN GLY A  360  UNP  A0A1B4TSD ASP   360 ENGINEERED MUTATION            
SEQADV 5KHN ALA A  362  UNP  A0A1B4TSD ARG   362 ENGINEERED MUTATION            
SEQADV 5KHN ALA A  365  UNP  A0A1B4TSD HIS   365 ENGINEERED MUTATION            
SEQADV 5KHN HIS A  878  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQADV 5KHN HIS A  879  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQADV 5KHN HIS A  880  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQADV 5KHN HIS A  881  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQADV 5KHN HIS A  882  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQADV 5KHN HIS A  883  UNP  A0A1B4TSD           EXPRESSION TAG                 
SEQRES   1 B  883  MET VAL THR SER LEU ILE VAL ARG LEU VAL ALA TRP SER          
SEQRES   2 B  883  VAL ARG ARG PRO VAL TRP VAL VAL VAL LEU SER LEU LEU          
SEQRES   3 B  883  ILE ALA ALA PHE SER GLY VAL TYR VAL ALA ARG HIS PHE          
SEQRES   4 B  883  LYS ILE ASN THR ASP ILE SER LYS LEU VAL ASP ALA GLU          
SEQRES   5 B  883  PRO GLN TRP ALA ALA LEU SER GLN ALA VAL ASP ARG ALA          
SEQRES   6 B  883  PHE PRO GLN ARG ASN GLY THR ILE LEU ALA VAL VAL GLU          
SEQRES   7 B  883  ALA PRO ALA PRO GLU PHE ALA THR ALA ALA ALA HIS ALA          
SEQRES   8 B  883  LEU THR GLU SER LEU GLN LYS GLN ALA ALA ALA GLY ARG          
SEQRES   9 B  883  ILE GLY PRO VAL ALA GLU PRO GLY GLY GLY PRO PHE PHE          
SEQRES  10 B  883  GLU HIS ASN GLY LEU LEU PHE LEU SER PRO GLN GLN VAL          
SEQRES  11 B  883  ALA ASP THR THR SER GLN LEU ALA SER ALA ARG PRO LEU          
SEQRES  12 B  883  VAL ASN GLU LEU ALA LYS ASN PRO SER LEU THR GLY LEU          
SEQRES  13 B  883  ALA THR THR LEU SER THR THR LEU GLY GLN PRO LEU LEU          
SEQRES  14 B  883  THR GLY GLN VAL LYS LEU PRO SER MET ALA LYS LEU LEU          
SEQRES  15 B  883  SER ARG SER ALA ALA THR VAL ASP ASP VAL LEU ALA GLY          
SEQRES  16 B  883  LYS PRO ALA ALA PHE SER TRP ARG ALA LEU VAL ASP ASN          
SEQRES  17 B  883  ASP ALA ALA ARG GLN PRO ALA ARG ALA PHE VAL THR VAL          
SEQRES  18 B  883  GLN PRO VAL VAL ASN TYR GLY ALA LEU LYS ALA GLY ALA          
SEQRES  19 B  883  GLN THR SER ASP VAL ILE ARG GLU THR ALA ARG ALA LEU          
SEQRES  20 B  883  ASP LEU GLU LYS ARG TYR GLY ALA VAL VAL ARG LEU THR          
SEQRES  21 B  883  GLY GLU GLN PRO LEU ALA ASP ASP GLU PHE SER SER VAL          
SEQRES  22 B  883  GLU ASP GLY ALA ALA LEU ASN GLY VAL VAL THR LEU LEU          
SEQRES  23 B  883  VAL VAL PHE VAL ILE LEU TRP LEU ALA LEU ARG SER LYS          
SEQRES  24 B  883  ARG MET ILE ALA SER VAL LEU VAL THR LEU PHE VAL GLY          
SEQRES  25 B  883  LEU VAL VAL THR ALA ALA LEU GLY LEU ALA MET VAL GLY          
SEQRES  26 B  883  SER LEU ASN MET ILE SER VAL ALA PHE MET VAL LEU PHE          
SEQRES  27 B  883  VAL GLY LEU GLY VAL ASP PHE SER ILE GLN TYR GLY VAL          
SEQRES  28 B  883  LYS TYR ARG GLU GLU ARG PHE ARG GLY GLU ALA ILE ASP          
SEQRES  29 B  883  ALA ALA LEU ILE GLY ALA ALA HIS SER MET GLY MET PRO          
SEQRES  30 B  883  LEU ALA LEU ALA THR THR ALA VAL ALA ALA SER PHE PHE          
SEQRES  31 B  883  SER PHE ILE PRO THR ALA TYR ARG GLY VAL SER GLU LEU          
SEQRES  32 B  883  GLY LEU ILE ALA GLY VAL GLY MET PHE VAL ALA LEU LEU          
SEQRES  33 B  883  THR THR LEU THR LEU LEU PRO ALA LEU LEU ARG LEU PHE          
SEQRES  34 B  883  ALA PRO PRO GLY GLU SER LYS THR PRO GLY PHE PRO TRP          
SEQRES  35 B  883  LEU ALA PRO VAL ASP ASP TYR LEU ASP ARG HIS ARG LYS          
SEQRES  36 B  883  PRO ILE LEU ILE GLY THR LEU ALA VAL VAL ILE GLY ALA          
SEQRES  37 B  883  LEU PRO LEU LEU ALA PHE LEU HIS PHE ASP PHE ASN PRO          
SEQRES  38 B  883  LEU HIS LEU LYS ASP PRO HIS SER GLU SER MET SER THR          
SEQRES  39 B  883  LEU LEU ALA LEU LYS ASP SER PRO GLU ALA ALA VAL ASN          
SEQRES  40 B  883  ASP VAL THR LEU LEU ALA PRO SER LEU ALA ASP ALA ASP          
SEQRES  41 B  883  ALA ALA ALA LYS ARG LEU ASP ALA LEU PRO GLU VAL GLY          
SEQRES  42 B  883  ARG THR THR THR LEU SER THR PHE ILE PRO ALA ASP GLN          
SEQRES  43 B  883  PRO GLU LYS ARG ALA ALA ILE ALA THR ALA ALA SER THR          
SEQRES  44 B  883  LEU LEU PRO ALA LEU THR GLN PRO PRO ALA PRO PRO ALA          
SEQRES  45 B  883  THR ASP ALA GLN ARG VAL ALA ALA LEU LYS ARG ALA SER          
SEQRES  46 B  883  ASP LEU LEU GLY TYR ALA ALA GLU ASP HIS PRO GLY PRO          
SEQRES  47 B  883  GLY ALA ALA ALA ALA GLN HIS LEU SER GLN SER LEU ALA          
SEQRES  48 B  883  LYS LEU ALA ALA ALA ASP SER ALA THR ARG ASP ARG ALA          
SEQRES  49 B  883  GLU ARG ALA PHE ALA ASP THR LEU ARG ILE ALA LEU ASN          
SEQRES  50 B  883  GLN LEU ALA ALA LEU LEU GLN PRO GLN GLU ILE THR ARG          
SEQRES  51 B  883  ASP THR LEU PRO PRO PRO LEU VAL ARG ASP TRP VAL ALA          
SEQRES  52 B  883  PRO ASP GLY LYS ALA LEU VAL GLN ILE SER PRO LYS VAL          
SEQRES  53 B  883  PRO LYS GLY VAL ASP PRO ASN ASP ASP THR MET LEU ARG          
SEQRES  54 B  883  HIS PHE ALA THR ALA VAL LYS ALA ALA GLU PRO GLY ALA          
SEQRES  55 B  883  ILE GLY GLY PRO ILE SER ILE LEU HIS SER ALA ASN THR          
SEQRES  56 B  883  ILE ILE SER ALA PHE LEU HIS ALA ALA LEU TRP SER ILE          
SEQRES  57 B  883  ILE SER ILE THR ILE LEU LEU TRP ILE THR LEU ARG ARG          
SEQRES  58 B  883  PHE GLY ASP VAL LEU ARG THR LEU VAL PRO LEU LEU VAL          
SEQRES  59 B  883  SER GLY ILE VAL THR LEU GLU MET CYS VAL VAL LEU GLY          
SEQRES  60 B  883  MET SER LEU ASN PHE ALA ASN ILE ILE ALA LEU PRO LEU          
SEQRES  61 B  883  MET LEU GLY VAL GLY VAL ALA PHE LYS VAL TYR PHE VAL          
SEQRES  62 B  883  MET ALA TRP ARG ALA GLY GLN THR GLY LEU LEU HIS SER          
SEQRES  63 B  883  SER LEU THR HIS ALA VAL LEU PHE SER ALA ALA THR THR          
SEQRES  64 B  883  ALA THR ALA PHE GLY SER LEU TRP LEU SER HIS HIS PRO          
SEQRES  65 B  883  GLY THR SER SER MET GLY LYS LEU LEU ALA LEU ALA LEU          
SEQRES  66 B  883  THR CYS THR LEU ILE GLY ALA VAL VAL PHE GLN PRO VAL          
SEQRES  67 B  883  LEU MET GLY LYS PRO ARG VAL LYS ARG ALA LYS ASN GLN          
SEQRES  68 B  883  SER GLN GLY ILE ASN GLU HIS HIS HIS HIS HIS HIS              
SEQRES   1 A  883  MET VAL THR SER LEU ILE VAL ARG LEU VAL ALA TRP SER          
SEQRES   2 A  883  VAL ARG ARG PRO VAL TRP VAL VAL VAL LEU SER LEU LEU          
SEQRES   3 A  883  ILE ALA ALA PHE SER GLY VAL TYR VAL ALA ARG HIS PHE          
SEQRES   4 A  883  LYS ILE ASN THR ASP ILE SER LYS LEU VAL ASP ALA GLU          
SEQRES   5 A  883  PRO GLN TRP ALA ALA LEU SER GLN ALA VAL ASP ARG ALA          
SEQRES   6 A  883  PHE PRO GLN ARG ASN GLY THR ILE LEU ALA VAL VAL GLU          
SEQRES   7 A  883  ALA PRO ALA PRO GLU PHE ALA THR ALA ALA ALA HIS ALA          
SEQRES   8 A  883  LEU THR GLU SER LEU GLN LYS GLN ALA ALA ALA GLY ARG          
SEQRES   9 A  883  ILE GLY PRO VAL ALA GLU PRO GLY GLY GLY PRO PHE PHE          
SEQRES  10 A  883  GLU HIS ASN GLY LEU LEU PHE LEU SER PRO GLN GLN VAL          
SEQRES  11 A  883  ALA ASP THR THR SER GLN LEU ALA SER ALA ARG PRO LEU          
SEQRES  12 A  883  VAL ASN GLU LEU ALA LYS ASN PRO SER LEU THR GLY LEU          
SEQRES  13 A  883  ALA THR THR LEU SER THR THR LEU GLY GLN PRO LEU LEU          
SEQRES  14 A  883  THR GLY GLN VAL LYS LEU PRO SER MET ALA LYS LEU LEU          
SEQRES  15 A  883  SER ARG SER ALA ALA THR VAL ASP ASP VAL LEU ALA GLY          
SEQRES  16 A  883  LYS PRO ALA ALA PHE SER TRP ARG ALA LEU VAL ASP ASN          
SEQRES  17 A  883  ASP ALA ALA ARG GLN PRO ALA ARG ALA PHE VAL THR VAL          
SEQRES  18 A  883  GLN PRO VAL VAL ASN TYR GLY ALA LEU LYS ALA GLY ALA          
SEQRES  19 A  883  GLN THR SER ASP VAL ILE ARG GLU THR ALA ARG ALA LEU          
SEQRES  20 A  883  ASP LEU GLU LYS ARG TYR GLY ALA VAL VAL ARG LEU THR          
SEQRES  21 A  883  GLY GLU GLN PRO LEU ALA ASP ASP GLU PHE SER SER VAL          
SEQRES  22 A  883  GLU ASP GLY ALA ALA LEU ASN GLY VAL VAL THR LEU LEU          
SEQRES  23 A  883  VAL VAL PHE VAL ILE LEU TRP LEU ALA LEU ARG SER LYS          
SEQRES  24 A  883  ARG MET ILE ALA SER VAL LEU VAL THR LEU PHE VAL GLY          
SEQRES  25 A  883  LEU VAL VAL THR ALA ALA LEU GLY LEU ALA MET VAL GLY          
SEQRES  26 A  883  SER LEU ASN MET ILE SER VAL ALA PHE MET VAL LEU PHE          
SEQRES  27 A  883  VAL GLY LEU GLY VAL ASP PHE SER ILE GLN TYR GLY VAL          
SEQRES  28 A  883  LYS TYR ARG GLU GLU ARG PHE ARG GLY GLU ALA ILE ASP          
SEQRES  29 A  883  ALA ALA LEU ILE GLY ALA ALA HIS SER MET GLY MET PRO          
SEQRES  30 A  883  LEU ALA LEU ALA THR THR ALA VAL ALA ALA SER PHE PHE          
SEQRES  31 A  883  SER PHE ILE PRO THR ALA TYR ARG GLY VAL SER GLU LEU          
SEQRES  32 A  883  GLY LEU ILE ALA GLY VAL GLY MET PHE VAL ALA LEU LEU          
SEQRES  33 A  883  THR THR LEU THR LEU LEU PRO ALA LEU LEU ARG LEU PHE          
SEQRES  34 A  883  ALA PRO PRO GLY GLU SER LYS THR PRO GLY PHE PRO TRP          
SEQRES  35 A  883  LEU ALA PRO VAL ASP ASP TYR LEU ASP ARG HIS ARG LYS          
SEQRES  36 A  883  PRO ILE LEU ILE GLY THR LEU ALA VAL VAL ILE GLY ALA          
SEQRES  37 A  883  LEU PRO LEU LEU ALA PHE LEU HIS PHE ASP PHE ASN PRO          
SEQRES  38 A  883  LEU HIS LEU LYS ASP PRO HIS SER GLU SER MET SER THR          
SEQRES  39 A  883  LEU LEU ALA LEU LYS ASP SER PRO GLU ALA ALA VAL ASN          
SEQRES  40 A  883  ASP VAL THR LEU LEU ALA PRO SER LEU ALA ASP ALA ASP          
SEQRES  41 A  883  ALA ALA ALA LYS ARG LEU ASP ALA LEU PRO GLU VAL GLY          
SEQRES  42 A  883  ARG THR THR THR LEU SER THR PHE ILE PRO ALA ASP GLN          
SEQRES  43 A  883  PRO GLU LYS ARG ALA ALA ILE ALA THR ALA ALA SER THR          
SEQRES  44 A  883  LEU LEU PRO ALA LEU THR GLN PRO PRO ALA PRO PRO ALA          
SEQRES  45 A  883  THR ASP ALA GLN ARG VAL ALA ALA LEU LYS ARG ALA SER          
SEQRES  46 A  883  ASP LEU LEU GLY TYR ALA ALA GLU ASP HIS PRO GLY PRO          
SEQRES  47 A  883  GLY ALA ALA ALA ALA GLN HIS LEU SER GLN SER LEU ALA          
SEQRES  48 A  883  LYS LEU ALA ALA ALA ASP SER ALA THR ARG ASP ARG ALA          
SEQRES  49 A  883  GLU ARG ALA PHE ALA ASP THR LEU ARG ILE ALA LEU ASN          
SEQRES  50 A  883  GLN LEU ALA ALA LEU LEU GLN PRO GLN GLU ILE THR ARG          
SEQRES  51 A  883  ASP THR LEU PRO PRO PRO LEU VAL ARG ASP TRP VAL ALA          
SEQRES  52 A  883  PRO ASP GLY LYS ALA LEU VAL GLN ILE SER PRO LYS VAL          
SEQRES  53 A  883  PRO LYS GLY VAL ASP PRO ASN ASP ASP THR MET LEU ARG          
SEQRES  54 A  883  HIS PHE ALA THR ALA VAL LYS ALA ALA GLU PRO GLY ALA          
SEQRES  55 A  883  ILE GLY GLY PRO ILE SER ILE LEU HIS SER ALA ASN THR          
SEQRES  56 A  883  ILE ILE SER ALA PHE LEU HIS ALA ALA LEU TRP SER ILE          
SEQRES  57 A  883  ILE SER ILE THR ILE LEU LEU TRP ILE THR LEU ARG ARG          
SEQRES  58 A  883  PHE GLY ASP VAL LEU ARG THR LEU VAL PRO LEU LEU VAL          
SEQRES  59 A  883  SER GLY ILE VAL THR LEU GLU MET CYS VAL VAL LEU GLY          
SEQRES  60 A  883  MET SER LEU ASN PHE ALA ASN ILE ILE ALA LEU PRO LEU          
SEQRES  61 A  883  MET LEU GLY VAL GLY VAL ALA PHE LYS VAL TYR PHE VAL          
SEQRES  62 A  883  MET ALA TRP ARG ALA GLY GLN THR GLY LEU LEU HIS SER          
SEQRES  63 A  883  SER LEU THR HIS ALA VAL LEU PHE SER ALA ALA THR THR          
SEQRES  64 A  883  ALA THR ALA PHE GLY SER LEU TRP LEU SER HIS HIS PRO          
SEQRES  65 A  883  GLY THR SER SER MET GLY LYS LEU LEU ALA LEU ALA LEU          
SEQRES  66 A  883  THR CYS THR LEU ILE GLY ALA VAL VAL PHE GLN PRO VAL          
SEQRES  67 A  883  LEU MET GLY LYS PRO ARG VAL LYS ARG ALA LYS ASN GLN          
SEQRES  68 A  883  SER GLN GLY ILE ASN GLU HIS HIS HIS HIS HIS HIS              
HELIX    1 AA1 MET B    1  VAL B   14  1                                  14    
HELIX    2 AA2 ARG B   16  HIS B   38  1                                  23    
HELIX    3 AA3 ASP B   44  LEU B   48  5                                   5    
HELIX    4 AA4 GLU B   52  PHE B   66  1                                  15    
HELIX    5 AA5 PRO B   67  ASN B   70  5                                   4    
HELIX    6 AA6 ALA B   81  ALA B  102  1                                  22    
HELIX    7 AA7 GLY B  114  ASN B  120  1                                   7    
HELIX    8 AA8 GLY B  121  LEU B  125  5                                   5    
HELIX    9 AA9 SER B  126  ALA B  140  1                                  15    
HELIX   10 AB1 ALA B  140  ASN B  150  1                                  11    
HELIX   11 AB2 SER B  152  GLN B  166  1                                  15    
HELIX   12 AB3 LEU B  175  SER B  177  5                                   3    
HELIX   13 AB4 MET B  178  GLY B  195  1                                  18    
HELIX   14 AB5 TRP B  202  ASP B  207  1                                   6    
HELIX   15 AB6 GLN B  235  LEU B  247  1                                  13    
HELIX   16 AB7 ASP B  248  GLY B  254  1                                   7    
HELIX   17 AB8 GLU B  262  GLU B  274  1                                  13    
HELIX   18 AB9 GLY B  276  LEU B  296  1                                  21    
HELIX   19 AC1 SER B  298  GLY B  325  1                                  28    
HELIX   20 AC2 SER B  331  ALA B  333  5                                   3    
HELIX   21 AC3 PHE B  334  ARG B  359  1                                  26    
HELIX   22 AC4 ALA B  362  SER B  373  1                                  12    
HELIX   23 AC5 MET B  374  SER B  391  1                                  18    
HELIX   24 AC6 TYR B  397  ALA B  430  1                                  34    
HELIX   25 AC7 TRP B  442  HIS B  453  1                                  12    
HELIX   26 AC8 HIS B  453  ALA B  468  1                                  16    
HELIX   27 AC9 LEU B  469  LEU B  475  5                                   7    
HELIX   28 AD1 SER B  489  LEU B  498  1                                  10    
HELIX   29 AD2 SER B  515  ASP B  527  1                                  13    
HELIX   30 AD3 LEU B  538  ILE B  542  5                                   5    
HELIX   31 AD4 PRO B  547  THR B  565  1                                  19    
HELIX   32 AD5 THR B  573  HIS B  595  1                                  23    
HELIX   33 AD6 GLY B  597  ALA B  614  1                                  18    
HELIX   34 AD7 SER B  618  LEU B  643  1                                  26    
HELIX   35 AD8 PRO B  654  ASP B  660  1                                   7    
HELIX   36 AD9 ASP B  684  GLU B  699  1                                  16    
HELIX   37 AE1 GLY B  705  THR B  738  1                                  34    
HELIX   38 AE2 ARG B  741  GLY B  767  1                                  27    
HELIX   39 AE3 ALA B  773  ILE B  775  5                                   3    
HELIX   40 AE4 ILE B  776  TRP B  796  1                                  21    
HELIX   41 AE5 GLY B  802  HIS B  810  1                                   9    
HELIX   42 AE6 ALA B  811  LEU B  828  1                                  18    
HELIX   43 AE7 HIS B  831  PHE B  855  1                                  25    
HELIX   44 AE8 GLN B  856  LEU B  859  5                                   4    
HELIX   45 AE9 VAL A    2  ARG A   16  1                                  15    
HELIX   46 AF1 ARG A   16  PHE A   39  1                                  24    
HELIX   47 AF2 ASP A   44  LEU A   48  5                                   5    
HELIX   48 AF3 GLU A   52  PHE A   66  1                                  15    
HELIX   49 AF4 ALA A   81  ALA A  102  1                                  22    
HELIX   50 AF5 GLY A  114  GLY A  121  1                                   8    
HELIX   51 AF6 LEU A  122  PHE A  124  5                                   3    
HELIX   52 AF7 SER A  126  ALA A  140  1                                  15    
HELIX   53 AF8 ALA A  140  ASN A  150  1                                  11    
HELIX   54 AF9 SER A  152  LEU A  164  1                                  13    
HELIX   55 AG1 GLN A  166  GLY A  171  1                                   6    
HELIX   56 AG2 LYS A  174  GLY A  195  1                                  22    
HELIX   57 AG3 GLN A  235  ASP A  248  1                                  14    
HELIX   58 AG4 ASP A  248  TYR A  253  1                                   6    
HELIX   59 AG5 GLU A  262  ASP A  275  1                                  14    
HELIX   60 AG6 GLY A  276  LEU A  296  1                                  21    
HELIX   61 AG7 SER A  298  GLY A  325  1                                  28    
HELIX   62 AG8 MET A  329  VAL A  332  5                                   4    
HELIX   63 AG9 ALA A  333  GLY A  360  1                                  28    
HELIX   64 AH1 ALA A  362  MET A  374  1                                  13    
HELIX   65 AH2 GLY A  375  SER A  391  1                                  17    
HELIX   66 AH3 TYR A  397  PHE A  429  1                                  33    
HELIX   67 AH4 LEU A  443  ALA A  468  1                                  26    
HELIX   68 AH5 LEU A  469  LEU A  475  5                                   7    
HELIX   69 AH6 ASN A  480  LYS A  485  5                                   6    
HELIX   70 AH7 SER A  489  LEU A  498  1                                  10    
HELIX   71 AH8 SER A  515  ALA A  528  1                                  14    
HELIX   72 AH9 LEU A  538  ILE A  542  5                                   5    
HELIX   73 AI1 ASP A  545  THR A  565  1                                  21    
HELIX   74 AI2 THR A  573  HIS A  595  1                                  23    
HELIX   75 AI3 GLY A  597  ALA A  615  1                                  19    
HELIX   76 AI4 SER A  618  ALA A  627  1                                  10    
HELIX   77 AI5 ALA A  629  LEU A  643  1                                  15    
HELIX   78 AI6 THR A  649  LEU A  653  5                                   5    
HELIX   79 AI7 PRO A  654  ASP A  660  1                                   7    
HELIX   80 AI8 THR A  686  GLU A  699  1                                  14    
HELIX   81 AI9 GLY A  705  LEU A  739  1                                  35    
HELIX   82 AJ1 ARG A  741  GLY A  767  1                                  27    
HELIX   83 AJ2 ALA A  773  ILE A  775  5                                   3    
HELIX   84 AJ3 ILE A  776  TRP A  796  1                                  21    
HELIX   85 AJ4 GLY A  802  HIS A  810  1                                   9    
HELIX   86 AJ5 VAL A  812  LEU A  828  1                                  17    
HELIX   87 AJ6 HIS A  831  PHE A  855  1                                  25    
HELIX   88 AJ7 PHE A  855  MET A  860  1                                   6    
SHEET    1 AA1 4 VAL B 108  ALA B 109  0                                        
SHEET    2 AA1 4 ALA B 215  VAL B 221 -1  O  THR B 220   N  ALA B 109           
SHEET    3 AA1 4 ILE B  73  ALA B  79 -1  N  VAL B  77   O  ALA B 217           
SHEET    4 AA1 4 VAL B 256  GLY B 261 -1  O  THR B 260   N  LEU B  74           
SHEET    1 AA2 4 ARG B 534  THR B 536  0                                        
SHEET    2 AA2 4 ALA B 668  SER B 673 -1  O  SER B 673   N  ARG B 534           
SHEET    3 AA2 4 VAL B 509  ALA B 513 -1  N  LEU B 511   O  VAL B 670           
SHEET    4 AA2 4 ILE B 703  GLY B 704 -1  O  ILE B 703   N  THR B 510           
SHEET    1 AA3 4 VAL A 108  ALA A 109  0                                        
SHEET    2 AA3 4 ARG A 216  VAL A 221 -1  O  THR A 220   N  ALA A 109           
SHEET    3 AA3 4 ILE A  73  GLU A  78 -1  N  VAL A  77   O  ALA A 217           
SHEET    4 AA3 4 VAL A 256  GLY A 261 -1  O  ARG A 258   N  VAL A  76           
SHEET    1 AA4 3 VAL A 509  ALA A 513  0                                        
SHEET    2 AA4 3 LYS A 667  PRO A 674 -1  O  VAL A 670   N  LEU A 511           
SHEET    3 AA4 3 GLY A 533  THR A 536 -1  N  THR A 536   O  GLN A 671           
SHEET    1 AA5 3 VAL A 509  ALA A 513  0                                        
SHEET    2 AA5 3 LYS A 667  PRO A 674 -1  O  VAL A 670   N  LEU A 511           
SHEET    3 AA5 3 VAL A 662  ALA A 663 -1  N  ALA A 663   O  LYS A 667           
CRYST1  111.914  129.546  111.728  90.00 114.04  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008935  0.000000  0.003986        0.00000                         
SCALE2      0.000000  0.007719  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009800        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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