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Database: PDB
Entry: 3B9Z
LinkDB: 3B9Z
Original site: 3B9Z 
HEADER    TRANSPORT PROTEIN                       07-NOV-07   3B9Z              
TITLE     CRYSTAL STRUCTURE OF THE NITROSOMONAS EUROPAEA RH PROTEIN COMPLEXED   
TITLE    2 WITH CARBON DIOXIDE                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AMMONIUM TRANSPORTER FAMILY RH-LIKE PROTEIN;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 31-418;                                           
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NITROSOMONAS EUROPAEA ATCC 19718;               
SOURCE   3 ORGANISM_TAXID: 228410;                                              
SOURCE   4 STRAIN: IFO 14298;                                                   
SOURCE   5 GENE: RH50, NE0448;                                                  
SOURCE   6 EXPRESSION_SYSTEM: METHYLOCOCCUS CAPSULATUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 414                                         
KEYWDS    CARBON DIOXIDE, CHANNEL, RH PROTEIN, CO2, TRANSPORT PROTEIN           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.LI,S.JAYACHANDRAN,H.-H.T.NGUYEN,M.K.CHAN                            
REVDAT   5   29-JUL-20 3B9Z    1       COMPND REMARK HETNAM SITE                
REVDAT   4   24-JAN-18 3B9Z    1       AUTHOR                                   
REVDAT   3   25-OCT-17 3B9Z    1       REMARK                                   
REVDAT   2   24-FEB-09 3B9Z    1       VERSN                                    
REVDAT   1   18-DEC-07 3B9Z    0                                                
JRNL        AUTH   X.LI,S.JAYACHANDRAN,H.H.NGUYEN,M.K.CHAN                      
JRNL        TITL   STRUCTURE OF THE NITROSOMONAS EUROPAEA RH PROTEIN.           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 104 19279 2007              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18040042                                                     
JRNL        DOI    10.1073/PNAS.0709710104                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 45092                          
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) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.179                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2275                            
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) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3117                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 192                          
REMARK   3   BIN FREE R VALUE                    : 0.2400                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2876                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
REMARK   3   SOLVENT ATOMS            : 321                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.52000                                              
REMARK   3    B22 (A**2) : 0.52000                                              
REMARK   3    B33 (A**2) : -0.78000                                             
REMARK   3    B12 (A**2) : 0.26000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.105         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.094         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.057         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.845         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3060 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4183 ; 1.002 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   412 ; 4.287 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   105 ;32.708 ;23.714       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   477 ;12.550 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ; 9.729 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   518 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2226 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1680 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2202 ; 0.298 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   312 ; 0.076 ; 0.200       
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):    85 ; 0.132 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    34 ; 0.080 ; 0.200       
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):  2019 ; 0.352 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3128 ; 0.626 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1189 ; 0.626 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1042 ; 0.958 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3B9Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045264.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAY-07                          
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               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91837                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM, DENZO                      
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, SCALA                   
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45094                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.631                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.42500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3B9Y                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14.5% PEG 2000 MME, 1 MM EDTA, 0.1 M     
REMARK 280  MES BUFFER, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.21700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       28.99280            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       47.82233            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       50.21700            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       28.99280            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       47.82233            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       50.21700            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       28.99280            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       47.82233            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.98560            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       95.64467            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       57.98560            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       95.64467            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       57.98560            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       95.64467            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14200 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 448  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 669  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 729  LIES ON A SPECIAL POSITION.                          
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    VAL A 149      -62.31    -92.37                                   
REMARK 500    ASP A 162       65.16   -160.61                                   
REMARK 500    ARG A 413      -41.23   -157.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3B9Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE NITROSOMONAS EUROPAEA RH PROTEIN            
DBREF  3B9Z A   31   418  UNP    Q82X47   Q82X47_NITEU    31    418             
SEQRES   1 A  388  GLU ILE ASN GLU ALA ARG LEU VAL ALA GLN TYR ASN TYR          
SEQRES   2 A  388  SER ILE ASN ILE LEU ALA MET LEU LEU VAL GLY PHE GLY          
SEQRES   3 A  388  PHE LEU MET VAL PHE VAL ARG ARG TYR GLY PHE SER ALA          
SEQRES   4 A  388  THR THR GLY THR TYR LEU VAL VAL ALA THR GLY LEU PRO          
SEQRES   5 A  388  LEU TYR ILE LEU LEU ARG ALA ASN GLY ILE PHE GLY HIS          
SEQRES   6 A  388  ALA LEU THR PRO HIS SER VAL ASP ALA VAL ILE TYR ALA          
SEQRES   7 A  388  GLU PHE ALA VAL ALA THR GLY LEU ILE ALA MET GLY ALA          
SEQRES   8 A  388  VAL LEU GLY ARG LEU ARG VAL PHE GLN TYR ALA LEU LEU          
SEQRES   9 A  388  ALA LEU PHE ILE VAL PRO VAL TYR LEU LEU ASN GLU TRP          
SEQRES  10 A  388  LEU VAL LEU ASP ASN ALA SER GLY LEU THR GLU GLY PHE          
SEQRES  11 A  388  GLN ASP SER ALA GLY SER ILE ALA ILE HIS ALA PHE GLY          
SEQRES  12 A  388  ALA TYR PHE GLY LEU GLY VAL SER ILE ALA LEU THR THR          
SEQRES  13 A  388  ALA ALA GLN ARG ALA GLN PRO ILE GLU SER ASP ALA THR          
SEQRES  14 A  388  SER ASP ARG PHE SER MET LEU GLY SER MET VAL LEU TRP          
SEQRES  15 A  388  LEU PHE TRP PRO SER PHE ALA THR ALA ILE VAL PRO PHE          
SEQRES  16 A  388  GLU GLN MET PRO GLN THR ILE VAL ASN THR LEU LEU ALA          
SEQRES  17 A  388  LEU CYS GLY ALA THR LEU ALA THR TYR PHE LEU SER ALA          
SEQRES  18 A  388  LEU PHE HIS LYS GLY LYS ALA SER ILE VAL ASP MET ALA          
SEQRES  19 A  388  ASN ALA ALA LEU ALA GLY GLY VAL ALA ILE GLY SER VAL          
SEQRES  20 A  388  CYS ASN ILE VAL GLY PRO VAL GLY ALA PHE VAL ILE GLY          
SEQRES  21 A  388  LEU LEU GLY GLY ALA ILE SER VAL VAL GLY PHE VAL PHE          
SEQRES  22 A  388  ILE GLN PRO MET LEU GLU SER LYS ALA LYS THR ILE ASP          
SEQRES  23 A  388  THR CYS GLY VAL HIS ASN LEU HIS GLY LEU PRO GLY LEU          
SEQRES  24 A  388  LEU GLY GLY PHE SER ALA ILE LEU ILE VAL PRO GLY ILE          
SEQRES  25 A  388  ALA VAL ALA GLN LEU THR GLY ILE GLY ILE THR LEU ALA          
SEQRES  26 A  388  LEU ALA LEU ILE GLY GLY VAL ILE ALA GLY ALA LEU ILE          
SEQRES  27 A  388  LYS LEU THR GLY THR THR LYS GLN ALA TYR GLU ASP SER          
SEQRES  28 A  388  HIS GLU PHE ILE HIS LEU ALA GLY PRO GLU ASP GLU HIS          
SEQRES  29 A  388  LYS ALA GLU ARG LEU VAL LEU GLU ALA LYS THR GLU ILE          
SEQRES  30 A  388  GLN GLY LEU LYS ASN ARG ILE ASP ALA ALA VAL                  
HET    BOG  A   1      20                                                       
HET    BOG  A 419      20                                                       
HET    CO2  A 420       3                                                       
HET    UNL  A 421       4                                                       
HETNAM     BOG OCTYL BETA-D-GLUCOPYRANOSIDE                                     
HETNAM     CO2 CARBON DIOXIDE                                                   
HETNAM     UNL UNKNOWN LIGAND                                                   
FORMUL   2  BOG    2(C14 H28 O6)                                                
FORMUL   4  CO2    C O2                                                         
FORMUL   6  HOH   *321(H2 O)                                                    
HELIX    1   1 ASN A   33  MET A   59  1                                  27    
HELIX    2   2 VAL A   60  VAL A   62  5                                   3    
HELIX    3   3 TYR A   65  ASN A   90  1                                  26    
HELIX    4   4 SER A  101  LEU A  123  1                                  23    
HELIX    5   5 ARG A  127  LEU A  150  1                                  24    
HELIX    6   6 ILE A  169  THR A  185  1                                  17    
HELIX    7   7 THR A  186  ALA A  191  1                                   6    
HELIX    8   8 ASP A  197  ALA A  221  1                                  25    
HELIX    9   9 PRO A  224  GLU A  226  5                                   3    
HELIX   10  10 GLN A  227  HIS A  254  1                                  28    
HELIX   11  11 SER A  259  ALA A  267  1                                   9    
HELIX   12  12 LEU A  268  GLY A  275  1                                   8    
HELIX   13  13 GLY A  282  PHE A  303  1                                  22    
HELIX   14  14 PHE A  303  ALA A  312  1                                  10    
HELIX   15  15 GLY A  319  HIS A  324  1                                   6    
HELIX   16  16 HIS A  324  VAL A  339  1                                  16    
HELIX   17  17 ILE A  342  LEU A  370  1                                  29    
HELIX   18  18 GLU A  379  GLU A  383  5                                   5    
HELIX   19  19 GLY A  389  GLU A  393  5                                   5    
HELIX   20  20 HIS A  394  ASN A  412  1                                  19    
HELIX   21  21 ARG A  413  VAL A  418  1                                   6    
CRYST1  100.434  100.434  143.467  90.00  90.00 120.00 H 3           9          
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      0.009957  0.005749  0.000000        0.00000                         
SCALE2      0.000000  0.011497  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006970        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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