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Database: PDB
Entry: 3QFW
LinkDB: 3QFW
Original site: 3QFW 
HEADER    LYASE                                   23-JAN-11   3QFW              
TITLE     CRYSTAL STRUCTURE OF RUBISCO-LIKE PROTEIN FROM RHODOPSEUDOMONAS       
TITLE    2 PALUSTRIS                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE LARGE      
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: RUBISCO-LIKE PROTEIN;                                       
COMPND   6 EC: 4.1.1.39;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;                     
SOURCE   3 ORGANISM_TAXID: 316056;                                              
SOURCE   4 STRAIN: BISB18;                                                      
SOURCE   5 GENE: RPC_2184;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, NEW YORK    
KEYWDS   2 SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS, NYSGXRC, RLP FOLD,      
KEYWDS   3 LYASE                                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.FEDOROV,E.V.FEDOROV,J.A.GERLT,S.K.BURLEY,S.C.ALMO,NEW YORK SGX    
AUTHOR   2 RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)                    
REVDAT   1   09-FEB-11 3QFW    0                                                
JRNL        AUTH   A.A.FEDOROV,E.V.FEDOROV,J.A.GERLT,S.K.BURLEY,S.C.ALMO        
JRNL        TITL   CRYSTAL STRUCTURE OF RUBISCO-LIKE PROTEIN FROM               
JRNL        TITL 2 RHODOPSEUDOMONAS PALUSTRIS                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 71923                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.246                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3639                            
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 27.9246 -  5.2887    0.93     2634   137  0.2600 0.2932        
REMARK   3     2  5.2887 -  4.2024    0.92     2608   120  0.2167 0.2334        
REMARK   3     3  4.2024 -  3.6725    0.94     2617   162  0.2262 0.2854        
REMARK   3     4  3.6725 -  3.3373    0.98     2725   138  0.2430 0.2944        
REMARK   3     5  3.3373 -  3.0985    0.99     2749   162  0.2601 0.2848        
REMARK   3     6  3.0985 -  2.9160    0.99     2753   143  0.2512 0.2945        
REMARK   3     7  2.9160 -  2.7701    0.99     2792   133  0.2434 0.2475        
REMARK   3     8  2.7701 -  2.6496    0.99     2746   163  0.2493 0.2815        
REMARK   3     9  2.6496 -  2.5477    0.99     2787   120  0.2552 0.2832        
REMARK   3    10  2.5477 -  2.4598    0.98     2757   130  0.2344 0.2758        
REMARK   3    11  2.4598 -  2.3829    0.99     2716   137  0.2261 0.2794        
REMARK   3    12  2.3829 -  2.3149    0.98     2736   161  0.2266 0.2679        
REMARK   3    13  2.3149 -  2.2539    0.98     2754   146  0.2303 0.2814        
REMARK   3    14  2.2539 -  2.1990    0.98     2696   157  0.2468 0.3290        
REMARK   3    15  2.1990 -  2.1490    0.98     2707   167  0.2406 0.2784        
REMARK   3    16  2.1490 -  2.1033    0.98     2701   163  0.2380 0.3153        
REMARK   3    17  2.1033 -  2.0612    0.98     2711   142  0.2540 0.3004        
REMARK   3    18  2.0612 -  2.0223    0.98     2724   146  0.2508 0.3054        
REMARK   3    19  2.0223 -  1.9862    0.97     2727   129  0.2469 0.3349        
REMARK   3    20  1.9862 -  1.9526    0.97     2719   142  0.2485 0.2704        
REMARK   3    21  1.9526 -  1.9211    0.97     2683   151  0.2654 0.3101        
REMARK   3    22  1.9211 -  1.8915    0.97     2725   149  0.2766 0.3388        
REMARK   3    23  1.8915 -  1.8637    0.95     2619   160  0.2948 0.3350        
REMARK   3    24  1.8637 -  1.8375    0.81     2291   118  0.2934 0.3237        
REMARK   3    25  1.8375 -  1.8127    0.73     2027    92  0.2979 0.3405        
REMARK   3    26  1.8127 -  1.7891    0.56     1580    71  0.3167 0.3104        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.41                                          
REMARK   3   B_SOL              : 60.93                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.850           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.12                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 14.77480                                             
REMARK   3    B22 (A**2) : 2.57320                                              
REMARK   3    B33 (A**2) : -17.34810                                            
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -1.56990                                             
REMARK   3    B23 (A**2) : -0.00000                                             
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      :  0.007           5293                                  
REMARK   3   ANGLE     :  1.042           7188                                  
REMARK   3   CHIRALITY :  0.067            835                                  
REMARK   3   PLANARITY :  0.005            948                                  
REMARK   3   DIHEDRAL  : 13.662           1920                                  
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 3QFW COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063593.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97915                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71923                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.789                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.921                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
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   (%): 52.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0,1M BIS-TRIS, 0.2M        
REMARK 280  LITHIUM SULFATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 293.0K                                                  
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       59.60850            
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: 5590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     GLY A    42                                                      
REMARK 465     ASP A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     ALA A    45                                                      
REMARK 465     ILE A    46                                                      
REMARK 465     VAL A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     GLY A   259                                                      
REMARK 465     ALA A   260                                                      
REMARK 465     ALA A   261                                                      
REMARK 465     GLY A   288                                                      
REMARK 465     ARG A   289                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     GLY A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     LEU A   346                                                      
REMARK 465     LEU A   347                                                      
REMARK 465     ALA A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     ARG A   350                                                      
REMARK 465     GLU A   351                                                      
REMARK 465     GLY A   372                                                      
REMARK 465     HIS A   373                                                      
REMARK 465     HIS A   374                                                      
REMARK 465     HIS A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     HIS A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     GLY B    42                                                      
REMARK 465     ASP B    43                                                      
REMARK 465     PRO B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     ILE B    46                                                      
REMARK 465     VAL B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     GLY B   343                                                      
REMARK 465     GLY B   344                                                      
REMARK 465     SER B   345                                                      
REMARK 465     LEU B   346                                                      
REMARK 465     LEU B   347                                                      
REMARK 465     ALA B   348                                                      
REMARK 465     SER B   349                                                      
REMARK 465     ARG B   350                                                      
REMARK 465     GLU B   351                                                      
REMARK 465     GLY B   372                                                      
REMARK 465     HIS B   373                                                      
REMARK 465     HIS B   374                                                      
REMARK 465     HIS B   375                                                      
REMARK 465     HIS B   376                                                      
REMARK 465     HIS B   377                                                      
REMARK 465     HIS B   378                                                      
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     THR A  11    O                                                   
REMARK 470     THR B  11    O                                                   
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    SER A  33     -107.46   -131.04                                   
REMARK 500    PHE A  88       11.72   -157.80                                   
REMARK 500    ALA A 170     -104.51   -131.88                                   
REMARK 500    SER A 175       71.96   -169.96                                   
REMARK 500    SER B  33     -104.91   -133.99                                   
REMARK 500    PHE B  88        9.22   -151.90                                   
REMARK 500    ALA B 170     -102.76   -133.25                                   
REMARK 500    SER B 175       76.73   -171.27                                   
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 SO4 A 379                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 380                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 381                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 379                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 380                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 381                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-9490A   RELATED DB: TARGETDB                     
DBREF  3QFW A    4   370  UNP    Q216E8   Q216E8_RHOPB     2    368             
DBREF  3QFW B    4   370  UNP    Q216E8   Q216E8_RHOPB     2    368             
SEQADV 3QFW MET A    1  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW SER A    2  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW LEU A    3  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW GLU A  371  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW GLY A  372  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS A  373  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS A  374  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS A  375  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS A  376  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS A  377  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS A  378  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW MET B    1  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW SER B    2  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW LEU B    3  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW GLU B  371  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW GLY B  372  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS B  373  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS B  374  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS B  375  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS B  376  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS B  377  UNP  Q216E8              EXPRESSION TAG                 
SEQADV 3QFW HIS B  378  UNP  Q216E8              EXPRESSION TAG                 
SEQRES   1 A  378  MET SER LEU THR GLU PRO ARG ILE VAL ALA THR TYR HIS          
SEQRES   2 A  378  ILE ALA SER ASP ALA GLU ARG ILE GLU GLN ARG ALA LEU          
SEQRES   3 A  378  ALA LEU ALA ILE GLU GLN SER VAL GLU CYS PRO LEU GLU          
SEQRES   4 A  378  ALA ILE GLY ASP PRO ALA ILE VAL ALA ASN ILE VAL GLY          
SEQRES   5 A  378  ARG VAL GLU ASP VAL ALA GLU LEU GLN PRO GLY ARG TYR          
SEQRES   6 A  378  ALA VAL ARG ILE GLY LEU ALA ALA ALA THR ALA PRO ALA          
SEQRES   7 A  378  GLU PRO GLY GLN LEU LEU ASN MET LEU PHE GLY ASN SER          
SEQRES   8 A  378  SER ILE GLN PRO ASP ILE ALA LEU ALA ASP VAL GLU LEU          
SEQRES   9 A  378  PRO ALA HIS TYR LEU THR ALA PHE GLY GLY PRO ARG VAL          
SEQRES  10 A  378  GLY LEU ALA GLY ILE ARG THR LEU THR GLY ALA GLN SER          
SEQRES  11 A  378  ARG ALA LEU THR ALA SER ALA LEU LYS PRO GLN GLY LEU          
SEQRES  12 A  378  SER PRO ALA ALA LEU ALA SER ILE ALA HIS GLN LEU ALA          
SEQRES  13 A  378  LEU GLY GLY VAL ASP LEU ILE LYS ASP ASP HIS GLY LEU          
SEQRES  14 A  378  ALA ASP GLN ALA PHE SER PRO PHE ALA GLU ARG ALA ALA          
SEQRES  15 A  378  ALA VAL GLY LYS ALA VAL ARG GLU ALA ASN ALA ALA ARG          
SEQRES  16 A  378  GLY GLY ARG THR LEU TYR ALA PRO ASN ILE SER GLY THR          
SEQRES  17 A  378  LEU ASP ASP MET ARG ARG GLN LEU GLY VAL ILE ARG ASP          
SEQRES  18 A  378  GLU GLY ILE GLY ALA VAL LEU VAL ALA PRO MET ILE VAL          
SEQRES  19 A  378  GLY VAL SER ASN PHE HIS ALA ILE VAL LYS GLU ALA ALA          
SEQRES  20 A  378  GLY LEU VAL VAL VAL ALA HIS PRO ALA MET ALA GLY ALA          
SEQRES  21 A  378  ALA LYS ILE ALA ALA PRO LEU LEU LEU GLY ARG LEU PHE          
SEQRES  22 A  378  ARG LEU PHE GLY ALA ASP ALA THR VAL PHE PRO ASN TYR          
SEQRES  23 A  378  GLY GLY ARG PHE ALA TYR SER THR ALA SER CYS LEU ALA          
SEQRES  24 A  378  LEU ALA GLN ALA ALA ARG ASP PRO PHE GLY LYS LEU ASN          
SEQRES  25 A  378  ALA CYS ILE PRO THR PRO ALA GLY GLY ILE MET LEU GLN          
SEQRES  26 A  378  ARG VAL ASN GLU LEU LEU ARG PHE TYR GLY GLN ASP VAL          
SEQRES  27 A  378  MET LEU LEU ILE GLY GLY SER LEU LEU ALA SER ARG GLU          
SEQRES  28 A  378  ARG LEU THR GLU GLN ALA SER ARG PHE VAL ASN LYS VAL          
SEQRES  29 A  378  ALA ASP TYR GLY GLN ARG GLU GLY HIS HIS HIS HIS HIS          
SEQRES  30 A  378  HIS                                                          
SEQRES   1 B  378  MET SER LEU THR GLU PRO ARG ILE VAL ALA THR TYR HIS          
SEQRES   2 B  378  ILE ALA SER ASP ALA GLU ARG ILE GLU GLN ARG ALA LEU          
SEQRES   3 B  378  ALA LEU ALA ILE GLU GLN SER VAL GLU CYS PRO LEU GLU          
SEQRES   4 B  378  ALA ILE GLY ASP PRO ALA ILE VAL ALA ASN ILE VAL GLY          
SEQRES   5 B  378  ARG VAL GLU ASP VAL ALA GLU LEU GLN PRO GLY ARG TYR          
SEQRES   6 B  378  ALA VAL ARG ILE GLY LEU ALA ALA ALA THR ALA PRO ALA          
SEQRES   7 B  378  GLU PRO GLY GLN LEU LEU ASN MET LEU PHE GLY ASN SER          
SEQRES   8 B  378  SER ILE GLN PRO ASP ILE ALA LEU ALA ASP VAL GLU LEU          
SEQRES   9 B  378  PRO ALA HIS TYR LEU THR ALA PHE GLY GLY PRO ARG VAL          
SEQRES  10 B  378  GLY LEU ALA GLY ILE ARG THR LEU THR GLY ALA GLN SER          
SEQRES  11 B  378  ARG ALA LEU THR ALA SER ALA LEU LYS PRO GLN GLY LEU          
SEQRES  12 B  378  SER PRO ALA ALA LEU ALA SER ILE ALA HIS GLN LEU ALA          
SEQRES  13 B  378  LEU GLY GLY VAL ASP LEU ILE LYS ASP ASP HIS GLY LEU          
SEQRES  14 B  378  ALA ASP GLN ALA PHE SER PRO PHE ALA GLU ARG ALA ALA          
SEQRES  15 B  378  ALA VAL GLY LYS ALA VAL ARG GLU ALA ASN ALA ALA ARG          
SEQRES  16 B  378  GLY GLY ARG THR LEU TYR ALA PRO ASN ILE SER GLY THR          
SEQRES  17 B  378  LEU ASP ASP MET ARG ARG GLN LEU GLY VAL ILE ARG ASP          
SEQRES  18 B  378  GLU GLY ILE GLY ALA VAL LEU VAL ALA PRO MET ILE VAL          
SEQRES  19 B  378  GLY VAL SER ASN PHE HIS ALA ILE VAL LYS GLU ALA ALA          
SEQRES  20 B  378  GLY LEU VAL VAL VAL ALA HIS PRO ALA MET ALA GLY ALA          
SEQRES  21 B  378  ALA LYS ILE ALA ALA PRO LEU LEU LEU GLY ARG LEU PHE          
SEQRES  22 B  378  ARG LEU PHE GLY ALA ASP ALA THR VAL PHE PRO ASN TYR          
SEQRES  23 B  378  GLY GLY ARG PHE ALA TYR SER THR ALA SER CYS LEU ALA          
SEQRES  24 B  378  LEU ALA GLN ALA ALA ARG ASP PRO PHE GLY LYS LEU ASN          
SEQRES  25 B  378  ALA CYS ILE PRO THR PRO ALA GLY GLY ILE MET LEU GLN          
SEQRES  26 B  378  ARG VAL ASN GLU LEU LEU ARG PHE TYR GLY GLN ASP VAL          
SEQRES  27 B  378  MET LEU LEU ILE GLY GLY SER LEU LEU ALA SER ARG GLU          
SEQRES  28 B  378  ARG LEU THR GLU GLN ALA SER ARG PHE VAL ASN LYS VAL          
SEQRES  29 B  378  ALA ASP TYR GLY GLN ARG GLU GLY HIS HIS HIS HIS HIS          
SEQRES  30 B  378  HIS                                                          
HET    SO4  A 379       5                                                       
HET    SO4  A 380       5                                                       
HET    SO4  A 381       5                                                       
HET    SO4  B 379       5                                                       
HET    SO4  B 380       5                                                       
HET    SO4  B 381       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   9  HOH   *212(H2 O)                                                    
HELIX    1   1 ASP A   17  GLN A   32  1                                  16    
HELIX    2   2 PRO A   37  ILE A   41  5                                   5    
HELIX    3   3 ALA A   72  ALA A   76  5                                   5    
HELIX    4   4 GLU A   79  GLY A   89  1                                  11    
HELIX    5   5 ASN A   90  GLN A   94  5                                   5    
HELIX    6   6 PRO A  105  GLY A  113  1                                   9    
HELIX    7   7 VAL A  117  GLY A  127  1                                  11    
HELIX    8   8 SER A  144  GLY A  158  1                                  15    
HELIX    9   9 PRO A  176  GLY A  196  1                                  21    
HELIX   10  10 THR A  208  GLY A  223  1                                  16    
HELIX   11  11 ALA A  230  GLY A  235  1                                   6    
HELIX   12  12 GLY A  235  LYS A  244  1                                  10    
HELIX   13  13 ALA A  264  GLY A  270  1                                   7    
HELIX   14  14 GLY A  270  GLY A  277  1                                   8    
HELIX   15  15 SER A  293  ASP A  306  1                                  14    
HELIX   16  16 MET A  323  GLN A  325  5                                   3    
HELIX   17  17 ARG A  326  GLY A  335  1                                  10    
HELIX   18  18 ARG A  352  TYR A  367  1                                  16    
HELIX   19  19 ASP B   17  GLN B   32  1                                  16    
HELIX   20  20 PRO B   37  ILE B   41  5                                   5    
HELIX   21  21 ALA B   72  ALA B   76  5                                   5    
HELIX   22  22 GLU B   79  GLY B   89  1                                  11    
HELIX   23  23 ASN B   90  GLN B   94  5                                   5    
HELIX   24  24 PRO B  105  GLY B  113  1                                   9    
HELIX   25  25 VAL B  117  GLY B  127  1                                  11    
HELIX   26  26 SER B  144  GLY B  158  1                                  15    
HELIX   27  27 PRO B  176  GLY B  196  1                                  21    
HELIX   28  28 THR B  208  GLY B  223  1                                  16    
HELIX   29  29 ALA B  230  GLY B  235  1                                   6    
HELIX   30  30 GLY B  235  LYS B  244  1                                  10    
HELIX   31  31 ALA B  264  GLY B  270  1                                   7    
HELIX   32  32 GLY B  270  GLY B  277  1                                   8    
HELIX   33  33 SER B  293  ASP B  306  1                                  14    
HELIX   34  34 ARG B  326  GLY B  335  1                                  10    
HELIX   35  35 ARG B  352  TYR B  367  1                                  16    
SHEET    1   A 4 ARG A  53  GLN A  61  0                                        
SHEET    2   A 4 ARG A  64  LEU A  71 -1  O  GLY A  70   N  ARG A  53           
SHEET    3   A 4 HIS A  13  ALA A  15 -1  N  ILE A  14   O  TYR A  65           
SHEET    4   A 4 ILE A  97  ALA A  98 -1  O  ALA A  98   N  HIS A  13           
SHEET    1   B 4 ARG A  53  GLN A  61  0                                        
SHEET    2   B 4 ARG A  64  LEU A  71 -1  O  GLY A  70   N  ARG A  53           
SHEET    3   B 4 ILE A   8  ALA A  10 -1  N  ILE A   8   O  LEU A  71           
SHEET    4   B 4 VAL A 102  GLU A 103 -1  O  GLU A 103   N  VAL A   9           
SHEET    1   C 4 LEU A 200  ALA A 202  0                                        
SHEET    2   C 4 LEU A 162  ASP A 165  1  N  ILE A 163   O  LEU A 200           
SHEET    3   C 4 LEU A 133  LEU A 138  1  N  SER A 136   O  LYS A 164           
SHEET    4   C 4 MET A 339  LEU A 341  1  O  LEU A 340   N  ALA A 135           
SHEET    1   D 4 ALA A 226  VAL A 229  0                                        
SHEET    2   D 4 VAL A 250  ALA A 253  1  O  VAL A 252   N  VAL A 227           
SHEET    3   D 4 ALA A 280  PRO A 284  1  O  ALA A 280   N  ALA A 253           
SHEET    4   D 4 ILE A 315  ALA A 319  1  O  THR A 317   N  THR A 281           
SHEET    1   E 4 ARG B  53  GLN B  61  0                                        
SHEET    2   E 4 ARG B  64  LEU B  71 -1  O  GLY B  70   N  ARG B  53           
SHEET    3   E 4 HIS B  13  ALA B  15 -1  N  ILE B  14   O  TYR B  65           
SHEET    4   E 4 ILE B  97  ALA B  98 -1  O  ALA B  98   N  HIS B  13           
SHEET    1   F 4 ARG B  53  GLN B  61  0                                        
SHEET    2   F 4 ARG B  64  LEU B  71 -1  O  GLY B  70   N  ARG B  53           
SHEET    3   F 4 ILE B   8  ALA B  10 -1  N  ILE B   8   O  LEU B  71           
SHEET    4   F 4 VAL B 102  GLU B 103 -1  O  GLU B 103   N  VAL B   9           
SHEET    1   G 4 LEU B 200  ALA B 202  0                                        
SHEET    2   G 4 LEU B 162  ASP B 165  1  N  ILE B 163   O  ALA B 202           
SHEET    3   G 4 LEU B 133  LEU B 138  1  N  SER B 136   O  LYS B 164           
SHEET    4   G 4 MET B 339  LEU B 341  1  O  LEU B 340   N  ALA B 135           
SHEET    1   H 4 ALA B 226  VAL B 229  0                                        
SHEET    2   H 4 VAL B 250  ALA B 253  1  O  VAL B 252   N  VAL B 227           
SHEET    3   H 4 ALA B 280  PRO B 284  1  O  ALA B 280   N  ALA B 253           
SHEET    4   H 4 ILE B 315  ALA B 319  1  O  THR B 317   N  THR B 281           
CISPEP   1 LYS A  139    PRO A  140          0        -1.88                     
CISPEP   2 LYS B  139    PRO B  140          0         1.34                     
SITE     1 AC1  5 ASN A 328  ARG A 332  HOH A 457  ASN B 312                    
SITE     2 AC1  5 HOH B 394                                                     
SITE     1 AC2  3 SER A 293  THR A 294  GLN B 129                               
SITE     1 AC3  4 GLY A 127  GLN A 129  SER A 130  ARG A 131                    
SITE     1 AC4  4 GLN A 129  SER B 293  THR B 294  HOH B 477                    
SITE     1 AC5  3 ASN B 328  ARG B 332  HOH B 438                               
SITE     1 AC6  4 GLY B 127  GLN B 129  SER B 130  ARG B 131                    
CRYST1   57.440  119.217   66.856  90.00 115.46  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      0.017409  0.000000  0.008289        0.00000                         
SCALE2      0.000000  0.008388  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016566        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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