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Database: PDB
Entry: 5JHH
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Original site: 5JHH 
HEADER    SIGNALING PROTEIN/TRANSCRIPTION/INHIBITO21-APR-16   5JHH              
TITLE     CRYSTAL STRUCTURE OF THE TERNARY COMPLEX BETWEEN THE HUMAN RHOA, ITS  
TITLE    2 INHIBITOR AND THE DH/PH DOMAIN OF HUMAN ARHGEF11                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 11;                 
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 714-1081;                                     
COMPND   5 SYNONYM: PDZ-RHOGEF;                                                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TRANSFORMING PROTEIN RHOA;                                 
COMPND   9 CHAIN: B, F;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 1-181;                                        
COMPND  11 SYNONYM: RHO CDNA CLONE 12,H12;                                      
COMPND  12 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: ARHGEF11, KIAA0380;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: RHOA, ARH12, ARHA, RHO12;                                      
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    RHOA-INHIBITOR-ARHGEF11 TERNARY COMPLEX, TARGET-BASED PHARMACEUTICAL  
KEYWDS   2 DESIGN, SIGNALING PROTEIN-TRANSCRIPTION-INHIBITOR COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.LV,R.WANG,L.MA,Q.MIAO,J.WU,Z.YAN,J.LI,L.MIAO,F.WANG                 
REVDAT   1   26-APR-17 5JHH    0                                                
JRNL        AUTH   R.WANG,Z.YAN,Z.LV,L.MA,Q.MIAO,Q.CHEN,F.WANG,J.LI,L.MIAO      
JRNL        TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC       
JRNL        TITL 2 ANALYSIS OF A SMALL GTPASE RHOA BOUND WITH ITS INHIBITOR AND 
JRNL        TITL 3 PDZRHOGEF                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 82.44                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 69765                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3565                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4872                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 255                          
REMARK   3   BIN FREE R VALUE                    : 0.3110                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8673                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 478                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : -0.04000                                             
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.03000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.245         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.207         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.156         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.560         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9064 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8940 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12238 ; 1.619 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20600 ; 0.814 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1097 ; 6.850 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   437 ;37.496 ;23.959       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1755 ;19.478 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    85 ;22.638 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1366 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10121 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2022 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4358 ; 3.446 ; 3.822       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4357 ; 3.440 ; 3.821       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5465 ; 5.130 ; 5.711       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5466 ; 5.131 ; 5.712       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4706 ; 4.493 ; 4.376       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4707 ; 4.493 ; 4.377       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6774 ; 7.028 ; 6.344       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10838 ; 9.720 ;30.646       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10839 ; 9.720 ;30.654       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5JHH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220427.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.541782                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73383                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 82.440                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.2680                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% V/V TACSIMATE PH 5.0, 0.1M SODIUM     
REMARK 280  CITRATE TRIBASIC DIHYDRATE PH 5.6, 16% PEG 3350, VAPOR DIFFUSION,   
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
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       59.52450            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 3600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 3190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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     MET A   713                                                      
REMARK 465     SER A  1009                                                      
REMARK 465     LYS A  1010                                                      
REMARK 465     THR A  1011                                                      
REMARK 465     ALA A  1012                                                      
REMARK 465     VAL A  1013                                                      
REMARK 465     GLY A  1014                                                      
REMARK 465     SER A  1015                                                      
REMARK 465     SER A  1016                                                      
REMARK 465     ASP A  1017                                                      
REMARK 465     SER A  1018                                                      
REMARK 465     LYS A  1019                                                      
REMARK 465     GLN A  1020                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B   181                                                      
REMARK 465     MET E   713                                                      
REMARK 465     THR E  1011                                                      
REMARK 465     ALA E  1012                                                      
REMARK 465     VAL E  1013                                                      
REMARK 465     GLY E  1014                                                      
REMARK 465     SER E  1015                                                      
REMARK 465     SER E  1016                                                      
REMARK 465     ASP E  1017                                                      
REMARK 465     SER E  1018                                                      
REMARK 465     LYS E  1019                                                      
REMARK 465     GLN E  1020                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     ALA F   181                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CAT  RA0 F   201     O    HOH F   329              1.08            
REMARK 500   O    ARG A   868     NH2  ARG B     5              1.56            
REMARK 500   O    ARG E   868     NH1  ARG F     5              1.73            
REMARK 500   CAB  RA0 F   201     O    HOH F   321              1.75            
REMARK 500   OAW  RA0 F   201     O    HOH F   301              1.77            
REMARK 500   NH1  ARG A   772     O    HOH A  1201              1.83            
REMARK 500   NE2  HIS E   863     OE1  GLN E   865              1.85            
REMARK 500   CAR  RA0 F   201     O    HOH F   329              1.95            
REMARK 500   O    ASN A   715     CG2  THR A   719              1.95            
REMARK 500   NH2  ARG A   772     O    HOH A  1202              1.98            
REMARK 500   O    ASN E   715     CG2  THR E   719              2.00            
REMARK 500   CB   ASP A   979     O    HOH A  1301              2.06            
REMARK 500   O    HOH A  1310     O    HOH A  1322              2.07            
REMARK 500   NZ   LYS A   998     O    HOH A  1203              2.08            
REMARK 500   O    TRP A   716     O    HIS A   718              2.08            
REMARK 500   O    HOH B   362     O    HOH B   370              2.09            
REMARK 500   O    HIS A  1008     O    HOH A  1204              2.09            
REMARK 500   CAA  RA0 F   201     O    HOH F   321              2.11            
REMARK 500   NZ   LYS A   884     O    HOH A  1205              2.14            
REMARK 500   NH1  ARG A   964     OD2  ASP A   991              2.15            
REMARK 500   N    THR B    19     OAW  RA0 B   201              2.17            
REMARK 500   O    HOH A  1339     O    HOH A  1359              2.18            
REMARK 500   O    HOH A  1213     O    HOH A  1271              2.19            
REMARK 500   NH2  ARG B   129     O    HOH B   301              2.19            
REMARK 500   O    HOH A  1249     O    HOH B   375              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 816   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A 816   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG B  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 122   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B 122   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG B 176   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG F 122   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG F 122   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG F 176   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 715      128.00    151.77                                   
REMARK 500    THR A 719     -138.98     51.71                                   
REMARK 500    ASN A 781       46.68   -156.93                                   
REMARK 500    GLU A 802       39.54    -82.92                                   
REMARK 500    LYS A 807     -122.05    -92.52                                   
REMARK 500    ALA A 942       46.05   -105.75                                   
REMARK 500    ALA A 944       -4.50    -56.62                                   
REMARK 500    ARG A 947     -158.99    -87.77                                   
REMARK 500    SER A 949      -90.83   -110.64                                   
REMARK 500    ASP A1000     -115.21     56.98                                   
REMARK 500    GLU B  32      -72.60    -72.13                                   
REMARK 500    LYS B 135       36.81     74.36                                   
REMARK 500    ASN E 715      121.55    164.91                                   
REMARK 500    THR E 719      -88.36   -107.19                                   
REMARK 500    LYS E 722     -123.32   -175.41                                   
REMARK 500    ASP E 723       22.62    -75.45                                   
REMARK 500    ASN E 781       43.34   -153.79                                   
REMARK 500    LYS E 807     -123.15    -95.94                                   
REMARK 500    ALA E 944       12.45    -66.81                                   
REMARK 500    ASP E 979       -9.18     78.51                                   
REMARK 500    ASP E1000     -113.55     61.16                                   
REMARK 500    LEU E1051      -84.37    -98.24                                   
REMARK 500    ASP F  49       46.76     38.05                                   
REMARK 500    ASP F 120        3.00    -61.26                                   
REMARK 500    LYS F 133      -27.97    -39.67                                   
REMARK 500    LYS F 164       -4.85     78.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue RA0 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue RA0 F 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5JHG   RELATED DB: PDB                                   
DBREF  5JHH A  714  1081  UNP    O15085   ARHGB_HUMAN    714   1081             
DBREF  5JHH B    1   181  UNP    P61586   RHOA_HUMAN       1    181             
DBREF  5JHH E  714  1081  UNP    O15085   ARHGB_HUMAN    714   1081             
DBREF  5JHH F    1   181  UNP    P61586   RHOA_HUMAN       1    181             
SEQADV 5JHH MET A  713  UNP  O15085              EXPRESSION TAG                 
SEQADV 5JHH MET E  713  UNP  O15085              EXPRESSION TAG                 
SEQRES   1 A  369  MET GLN ASN TRP GLN HIS THR VAL GLY LYS ASP VAL VAL          
SEQRES   2 A  369  ALA GLY LEU THR GLN ARG GLU ILE ASP ARG GLN GLU VAL          
SEQRES   3 A  369  ILE ASN GLU LEU PHE VAL THR GLU ALA SER HIS LEU ARG          
SEQRES   4 A  369  THR LEU ARG VAL LEU ASP LEU ILE PHE TYR GLN ARG MET          
SEQRES   5 A  369  LYS LYS GLU ASN LEU MET PRO ARG GLU GLU LEU ALA ARG          
SEQRES   6 A  369  LEU PHE PRO ASN LEU PRO GLU LEU ILE GLU ILE HIS ASN          
SEQRES   7 A  369  SER TRP CYS GLU ALA MET LYS LYS LEU ARG GLU GLU GLY          
SEQRES   8 A  369  PRO ILE ILE LYS GLU ILE SER ASP LEU MET LEU ALA ARG          
SEQRES   9 A  369  PHE ASP GLY PRO ALA ARG GLU GLU LEU GLN GLN VAL ALA          
SEQRES  10 A  369  ALA GLN PHE CYS SER TYR GLN SER ILE ALA LEU GLU LEU          
SEQRES  11 A  369  ILE LYS THR LYS GLN ARG LYS GLU SER ARG PHE GLN LEU          
SEQRES  12 A  369  PHE MET GLN GLU ALA GLU SER HIS PRO GLN CYS ARG ARG          
SEQRES  13 A  369  LEU GLN LEU ARG ASP LEU ILE ILE SER GLU MET GLN ARG          
SEQRES  14 A  369  LEU THR LYS TYR PRO LEU LEU LEU GLU SER ILE ILE LYS          
SEQRES  15 A  369  HIS THR GLU GLY GLY THR SER GLU HIS GLU LYS LEU CYS          
SEQRES  16 A  369  ARG ALA ARG ASP GLN CYS ARG GLU ILE LEU LYS TYR VAL          
SEQRES  17 A  369  ASN GLU ALA VAL LYS GLN THR GLU ASN ARG HIS ARG LEU          
SEQRES  18 A  369  GLU GLY TYR GLN LYS ARG LEU ASP ALA THR ALA LEU GLU          
SEQRES  19 A  369  ARG ALA SER ASN PRO LEU ALA ALA GLU PHE LYS SER LEU          
SEQRES  20 A  369  ASP LEU THR THR ARG LYS MET ILE HIS GLU GLY PRO LEU          
SEQRES  21 A  369  THR TRP ARG ILE SER LYS ASP LYS THR LEU ASP LEU HIS          
SEQRES  22 A  369  VAL LEU LEU LEU GLU ASP LEU LEU VAL LEU LEU GLN LYS          
SEQRES  23 A  369  GLN ASP GLU LYS LEU LEU LEU LYS CYS HIS SER LYS THR          
SEQRES  24 A  369  ALA VAL GLY SER SER ASP SER LYS GLN THR PHE SER PRO          
SEQRES  25 A  369  VAL LEU LYS LEU ASN ALA VAL LEU ILE ARG SER VAL ALA          
SEQRES  26 A  369  THR ASP LYS ARG ALA PHE PHE ILE ILE CYS THR SER LYS          
SEQRES  27 A  369  LEU GLY PRO PRO GLN ILE TYR GLU LEU VAL ALA LEU THR          
SEQRES  28 A  369  SER SER ASP LYS ASN THR TRP MET GLU LEU LEU GLU GLU          
SEQRES  29 A  369  ALA VAL ARG ASN ALA                                          
SEQRES   1 B  181  MET ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY ASP          
SEQRES   2 B  181  GLY ALA CYS GLY LYS THR CYS LEU LEU ILE VAL PHE SER          
SEQRES   3 B  181  LYS ASP GLN PHE PRO GLU VAL TYR VAL PRO THR VAL PHE          
SEQRES   4 B  181  GLU ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS GLN          
SEQRES   5 B  181  VAL GLU LEU ALA LEU TRP ASP THR ALA GLY GLN GLU ASP          
SEQRES   6 B  181  TYR ASP ARG LEU ARG PRO LEU SER TYR PRO ASP THR ASP          
SEQRES   7 B  181  VAL ILE LEU MET CYS PHE SER ILE ASP SER PRO ASP SER          
SEQRES   8 B  181  LEU GLU ASN ILE PRO GLU LYS TRP THR PRO GLU VAL LYS          
SEQRES   9 B  181  HIS PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY ASN          
SEQRES  10 B  181  LYS LYS ASP LEU ARG ASN ASP GLU HIS THR ARG ARG GLU          
SEQRES  11 B  181  LEU ALA LYS MET LYS GLN GLU PRO VAL LYS PRO GLU GLU          
SEQRES  12 B  181  GLY ARG ASP MET ALA ASN ARG ILE GLY ALA PHE GLY TYR          
SEQRES  13 B  181  MET GLU CYS SER ALA LYS THR LYS ASP GLY VAL ARG GLU          
SEQRES  14 B  181  VAL PHE GLU MET ALA THR ARG ALA ALA LEU GLN ALA              
SEQRES   1 E  369  MET GLN ASN TRP GLN HIS THR VAL GLY LYS ASP VAL VAL          
SEQRES   2 E  369  ALA GLY LEU THR GLN ARG GLU ILE ASP ARG GLN GLU VAL          
SEQRES   3 E  369  ILE ASN GLU LEU PHE VAL THR GLU ALA SER HIS LEU ARG          
SEQRES   4 E  369  THR LEU ARG VAL LEU ASP LEU ILE PHE TYR GLN ARG MET          
SEQRES   5 E  369  LYS LYS GLU ASN LEU MET PRO ARG GLU GLU LEU ALA ARG          
SEQRES   6 E  369  LEU PHE PRO ASN LEU PRO GLU LEU ILE GLU ILE HIS ASN          
SEQRES   7 E  369  SER TRP CYS GLU ALA MET LYS LYS LEU ARG GLU GLU GLY          
SEQRES   8 E  369  PRO ILE ILE LYS GLU ILE SER ASP LEU MET LEU ALA ARG          
SEQRES   9 E  369  PHE ASP GLY PRO ALA ARG GLU GLU LEU GLN GLN VAL ALA          
SEQRES  10 E  369  ALA GLN PHE CYS SER TYR GLN SER ILE ALA LEU GLU LEU          
SEQRES  11 E  369  ILE LYS THR LYS GLN ARG LYS GLU SER ARG PHE GLN LEU          
SEQRES  12 E  369  PHE MET GLN GLU ALA GLU SER HIS PRO GLN CYS ARG ARG          
SEQRES  13 E  369  LEU GLN LEU ARG ASP LEU ILE ILE SER GLU MET GLN ARG          
SEQRES  14 E  369  LEU THR LYS TYR PRO LEU LEU LEU GLU SER ILE ILE LYS          
SEQRES  15 E  369  HIS THR GLU GLY GLY THR SER GLU HIS GLU LYS LEU CYS          
SEQRES  16 E  369  ARG ALA ARG ASP GLN CYS ARG GLU ILE LEU LYS TYR VAL          
SEQRES  17 E  369  ASN GLU ALA VAL LYS GLN THR GLU ASN ARG HIS ARG LEU          
SEQRES  18 E  369  GLU GLY TYR GLN LYS ARG LEU ASP ALA THR ALA LEU GLU          
SEQRES  19 E  369  ARG ALA SER ASN PRO LEU ALA ALA GLU PHE LYS SER LEU          
SEQRES  20 E  369  ASP LEU THR THR ARG LYS MET ILE HIS GLU GLY PRO LEU          
SEQRES  21 E  369  THR TRP ARG ILE SER LYS ASP LYS THR LEU ASP LEU HIS          
SEQRES  22 E  369  VAL LEU LEU LEU GLU ASP LEU LEU VAL LEU LEU GLN LYS          
SEQRES  23 E  369  GLN ASP GLU LYS LEU LEU LEU LYS CYS HIS SER LYS THR          
SEQRES  24 E  369  ALA VAL GLY SER SER ASP SER LYS GLN THR PHE SER PRO          
SEQRES  25 E  369  VAL LEU LYS LEU ASN ALA VAL LEU ILE ARG SER VAL ALA          
SEQRES  26 E  369  THR ASP LYS ARG ALA PHE PHE ILE ILE CYS THR SER LYS          
SEQRES  27 E  369  LEU GLY PRO PRO GLN ILE TYR GLU LEU VAL ALA LEU THR          
SEQRES  28 E  369  SER SER ASP LYS ASN THR TRP MET GLU LEU LEU GLU GLU          
SEQRES  29 E  369  ALA VAL ARG ASN ALA                                          
SEQRES   1 F  181  MET ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY ASP          
SEQRES   2 F  181  GLY ALA CYS GLY LYS THR CYS LEU LEU ILE VAL PHE SER          
SEQRES   3 F  181  LYS ASP GLN PHE PRO GLU VAL TYR VAL PRO THR VAL PHE          
SEQRES   4 F  181  GLU ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS GLN          
SEQRES   5 F  181  VAL GLU LEU ALA LEU TRP ASP THR ALA GLY GLN GLU ASP          
SEQRES   6 F  181  TYR ASP ARG LEU ARG PRO LEU SER TYR PRO ASP THR ASP          
SEQRES   7 F  181  VAL ILE LEU MET CYS PHE SER ILE ASP SER PRO ASP SER          
SEQRES   8 F  181  LEU GLU ASN ILE PRO GLU LYS TRP THR PRO GLU VAL LYS          
SEQRES   9 F  181  HIS PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY ASN          
SEQRES  10 F  181  LYS LYS ASP LEU ARG ASN ASP GLU HIS THR ARG ARG GLU          
SEQRES  11 F  181  LEU ALA LYS MET LYS GLN GLU PRO VAL LYS PRO GLU GLU          
SEQRES  12 F  181  GLY ARG ASP MET ALA ASN ARG ILE GLY ALA PHE GLY TYR          
SEQRES  13 F  181  MET GLU CYS SER ALA LYS THR LYS ASP GLY VAL ARG GLU          
SEQRES  14 F  181  VAL PHE GLU MET ALA THR ARG ALA ALA LEU GLN ALA              
HET    GOL  A1101       6                                                       
HET    GOL  A1102       6                                                       
HET    RA0  B 201      24                                                       
HET    GOL  E1101       6                                                       
HET    RA0  F 201      24                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     RA0 3-{3-[ETHYL(QUINOLIN-2-YL)AMINO]PHENYL}PROPANOIC ACID            
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    3(C3 H8 O3)                                                  
FORMUL   7  RA0    2(C20 H20 N2 O2)                                             
FORMUL  10  HOH   *478(H2 O)                                                    
HELIX    1 AA1 THR A  729  PHE A  760  1                                  32    
HELIX    2 AA2 PHE A  760  GLU A  767  1                                   8    
HELIX    3 AA3 PRO A  771  PHE A  779  1                                   9    
HELIX    4 AA4 ASN A  781  GLU A  802  1                                  22    
HELIX    5 AA5 ILE A  809  ASP A  818  1                                  10    
HELIX    6 AA6 ASP A  818  SER A  834  1                                  17    
HELIX    7 AA7 TYR A  835  GLU A  850  1                                  16    
HELIX    8 AA8 GLU A  850  HIS A  863  1                                  14    
HELIX    9 AA9 PRO A  864  ARG A  867  5                                   4    
HELIX   10 AB1 GLN A  870  ILE A  875  1                                   6    
HELIX   11 AB2 ILE A  876  HIS A  895  1                                  20    
HELIX   12 AB3 THR A  900  ARG A  939  1                                  40    
HELIX   13 AB4 ASN A  950  LYS A  957  5                                   8    
HELIX   14 AB5 ASP A  960  ARG A  964  5                                   5    
HELIX   15 AB6 THR A 1063  ALA A 1081  1                                  19    
HELIX   16 AB7 GLY B   17  ASP B   28  1                                  12    
HELIX   17 AB8 LEU B   69  TYR B   74  5                                   6    
HELIX   18 AB9 SER B   88  LYS B   98  1                                  11    
HELIX   19 AC1 LYS B   98  CYS B  107  1                                  10    
HELIX   20 AC2 LYS B  118  ARG B  122  5                                   5    
HELIX   21 AC3 ASP B  124  MET B  134  1                                  11    
HELIX   22 AC4 LYS B  140  GLY B  152  1                                  13    
HELIX   23 AC5 GLY B  166  GLN B  180  1                                  15    
HELIX   24 AC6 THR E  729  PHE E  760  1                                  32    
HELIX   25 AC7 PHE E  760  GLU E  767  1                                   8    
HELIX   26 AC8 PRO E  771  PHE E  779  1                                   9    
HELIX   27 AC9 ASN E  781  GLU E  802  1                                  22    
HELIX   28 AD1 ILE E  809  ASP E  818  1                                  10    
HELIX   29 AD2 ASP E  818  TYR E  835  1                                  18    
HELIX   30 AD3 TYR E  835  GLU E  850  1                                  16    
HELIX   31 AD4 GLU E  850  HIS E  863  1                                  14    
HELIX   32 AD5 PRO E  864  ARG E  867  5                                   4    
HELIX   33 AD6 GLN E  870  ILE E  875  1                                   6    
HELIX   34 AD7 ILE E  876  HIS E  895  1                                  20    
HELIX   35 AD8 THR E  900  ARG E  939  1                                  40    
HELIX   36 AD9 ALA E  942  GLU E  946  5                                   5    
HELIX   37 AE1 ASN E  950  GLU E  955  1                                   6    
HELIX   38 AE2 ASP E  960  ARG E  964  5                                   5    
HELIX   39 AE3 THR E 1063  ASN E 1080  1                                  18    
HELIX   40 AE4 GLY F   17  ASP F   28  1                                  12    
HELIX   41 AE5 LEU F   69  TYR F   74  5                                   6    
HELIX   42 AE6 SER F   88  LYS F   98  1                                  11    
HELIX   43 AE7 LYS F   98  CYS F  107  1                                  10    
HELIX   44 AE8 LYS F  118  ARG F  122  5                                   5    
HELIX   45 AE9 ASP F  124  LYS F  133  1                                  10    
HELIX   46 AF1 LYS F  140  ILE F  151  1                                  12    
HELIX   47 AF2 GLY F  166  GLN F  180  1                                  15    
SHEET    1 AA1 4 LEU A 940  ASP A 941  0                                        
SHEET    2 AA1 4 LYS A1002  LEU A1004  1  O  LEU A1003   N  ASP A 941           
SHEET    3 AA1 4 LEU A 992  GLN A 999 -1  N  GLN A 997   O  LEU A1004           
SHEET    4 AA1 4 VAL A1025  LYS A1027 -1  O  LEU A1026   N  LEU A 993           
SHEET    1 AA2 8 LEU A 940  ASP A 941  0                                        
SHEET    2 AA2 8 LYS A1002  LEU A1004  1  O  LEU A1003   N  ASP A 941           
SHEET    3 AA2 8 LEU A 992  GLN A 999 -1  N  GLN A 997   O  LEU A1004           
SHEET    4 AA2 8 THR A 981  LEU A 989 -1  N  HIS A 985   O  LEU A 996           
SHEET    5 AA2 8 MET A 966  ARG A 975 -1  N  TRP A 974   O  LEU A 982           
SHEET    6 AA2 8 TYR A1057  VAL A1060 -1  O  VAL A1060   N  THR A 973           
SHEET    7 AA2 8 ALA A1042  CYS A1047 -1  N  PHE A1043   O  LEU A1059           
SHEET    8 AA2 8 VAL A1031  SER A1035 -1  N  ARG A1034   O  PHE A1044           
SHEET    1 AA3 6 TYR B  42  VAL B  48  0                                        
SHEET    2 AA3 6 LYS B  51  TRP B  58 -1  O  LEU B  55   N  ALA B  44           
SHEET    3 AA3 6 ARG B   5  GLY B  12  1  N  LYS B   6   O  ALA B  56           
SHEET    4 AA3 6 VAL B  79  SER B  85  1  O  CYS B  83   N  VAL B  11           
SHEET    5 AA3 6 ILE B 112  ASN B 117  1  O  VAL B 115   N  MET B  82           
SHEET    6 AA3 6 GLY B 155  GLU B 158  1  O  MET B 157   N  GLY B 116           
SHEET    1 AA4 4 LEU E 940  ASP E 941  0                                        
SHEET    2 AA4 4 LYS E1002  LEU E1004  1  O  LEU E1003   N  ASP E 941           
SHEET    3 AA4 4 LEU E 992  GLN E 999 -1  N  GLN E 997   O  LEU E1004           
SHEET    4 AA4 4 VAL E1025  LYS E1027 -1  O  LEU E1026   N  LEU E 993           
SHEET    1 AA5 8 LEU E 940  ASP E 941  0                                        
SHEET    2 AA5 8 LYS E1002  LEU E1004  1  O  LEU E1003   N  ASP E 941           
SHEET    3 AA5 8 LEU E 992  GLN E 999 -1  N  GLN E 997   O  LEU E1004           
SHEET    4 AA5 8 LYS E 980  LEU E 989 -1  N  LEU E 987   O  VAL E 994           
SHEET    5 AA5 8 MET E 966  SER E 977 -1  N  ILE E 967   O  LEU E 988           
SHEET    6 AA5 8 GLN E1055  VAL E1060 -1  O  GLU E1058   N  ARG E 975           
SHEET    7 AA5 8 ALA E1042  CYS E1047 -1  N  CYS E1047   O  GLN E1055           
SHEET    8 AA5 8 VAL E1031  SER E1035 -1  N  ARG E1034   O  PHE E1044           
SHEET    1 AA6 6 TYR F  42  VAL F  48  0                                        
SHEET    2 AA6 6 LYS F  51  TRP F  58 -1  O  LEU F  55   N  ALA F  44           
SHEET    3 AA6 6 ILE F   4  GLY F  12  1  N  ILE F   4   O  GLU F  54           
SHEET    4 AA6 6 VAL F  79  SER F  85  1  O  CYS F  83   N  VAL F  11           
SHEET    5 AA6 6 ILE F 112  ASN F 117  1  O  ILE F 113   N  ILE F  80           
SHEET    6 AA6 6 GLY F 155  GLU F 158  1  O  MET F 157   N  GLY F 116           
SITE     1 AC1  7 ILE A 788  SER A 791  TRP A 792  ALA A 795                    
SITE     2 AC1  7 ALA A 815  ARG A 816  HOH A1312                               
SITE     1 AC2  5 HIS A 968  HOH A1230  HOH A1313  GLU B 102                    
SITE     2 AC2  5 HIS B 105                                                     
SITE     1 AC3 12 GLY B  14  ALA B  15  GLY B  17  LYS B  18                    
SITE     2 AC3 12 THR B  19  CYS B  20  LYS B 118  ASP B 120                    
SITE     3 AC3 12 ALA B 161  LYS B 162  HOH B 303  HOH B 377                    
SITE     1 AC4  6 SER E 791  TRP E 792  ALA E 795  ALA E 815                    
SITE     2 AC4  6 ARG E 816  HOH E1251                                          
SITE     1 AC5 17 GLY F  14  ALA F  15  GLY F  17  LYS F  18                    
SITE     2 AC5 17 THR F  19  CYS F  20  VAL F  35  ALA F  61                    
SITE     3 AC5 17 LYS F 118  ASP F 120  SER F 160  ALA F 161                    
SITE     4 AC5 17 LYS F 162  HOH F 301  HOH F 321  HOH F 329                    
SITE     5 AC5 17 HOH F 357                                                     
CRYST1   88.855  119.049   90.526  90.00 114.39  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      0.011254  0.000000  0.005104        0.00000                         
SCALE2      0.000000  0.008400  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012129        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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