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Database: PDB
Entry: 3BHS
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Original site: 3BHS 
HEADER    TRANSPORT PROTEIN                       29-NOV-07   3BHS              
TITLE     NITROSOMONAS EUROPAEA RH50 AND MECHANISM OF CONDUCTION BY RHESUS      
TITLE    2 PROTEIN FAMILY OF CHANNELS                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AMMONIUM TRANSPORTER FAMILY PROTEIN RH50;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 26-425;                                           
COMPND   5 SYNONYM: RH-LIKE PROTEIN;                                            
COMPND   6 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: 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 EXPRESSION_SYSTEM_PLASMID: PET52 3C/LIC                              
KEYWDS    AMMONIA, RHESUS, RH50, CHANNEL, AMT, NITROSOMONAS, RH50 AMMONIUM      
KEYWDS   2 TRANSPORTER FAMILY, RH50 AMMONIA TRANSPORTER, MEMBRANE PROTEIN,      
KEYWDS   3 STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, CENTER FOR 
KEYWDS   4 STRUCTURES OF MEMBRANE PROTEINS, CSMP, TRANSMEMBRANE, TRANSPORT      
KEYWDS   5 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.GRUSWITZ,C.-M.HO,M.C.DEL ROSARIO,C.M.WESTHOFF,R.M.STROUD,CENTER FOR 
AUTHOR   2 STRUCTURES OF MEMBRANE PROTEINS (CSMP)                               
REVDAT   3   24-JAN-18 3BHS    1       AUTHOR JRNL                              
REVDAT   2   24-FEB-09 3BHS    1       VERSN                                    
REVDAT   1   04-DEC-07 3BHS    0                                                
JRNL        AUTH   F.GRUSWITZ,C.-M.HO,M.C.DEL ROSARIO,C.M.WESTHOFF,R.M.STROUD   
JRNL        TITL   NITROSOMONAS EUROPAEA RH50 AND MECHANISM OF CONDUCTION BY    
JRNL        TITL 2 RHESUS PROTEIN FAMILY OF CHANNELS.                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 30705                          
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) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1646                            
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) : 1.99                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2180                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 112                          
REMARK   3   BIN FREE R VALUE                    : 0.3060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2806                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 154                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.92000                                              
REMARK   3    B22 (A**2) : 1.92000                                              
REMARK   3    B33 (A**2) : -2.88000                                             
REMARK   3    B12 (A**2) : 0.96000                                              
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): 0.158         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.150         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.951         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2865 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1820 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3904 ; 1.487 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4469 ; 0.929 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   378 ; 5.689 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    98 ;34.356 ;23.571       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   440 ;12.961 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;11.362 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   475 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3205 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   589 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   744 ; 0.245 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1962 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1536 ; 0.198 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1354 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   124 ; 0.167 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.068 ; 0.200       
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):     6 ; 0.091 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    37 ; 0.238 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.151 ; 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):  2377 ; 3.192 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   787 ; 0.986 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2974 ; 3.736 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1155 ; 2.681 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   930 ; 3.554 ; 3.000       
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   : 1.20                                          
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 3BHS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045537.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 78                                 
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11587                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32561                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.990                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.39500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2NS1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 MICROLITER DROP RATIO OF (PROTEIN    
REMARK 280  IN 0.02M HEPES PH 7.4, 0.1M NACL, 0.04M B-OCTYL GLUCOSIDE, 2MM      
REMARK 280  DITHIOTHREITOL) AND (100MM HEPES, 25% PEG 400). CRYOPROTECTED       
REMARK 280  WITH 10% GLYCEROL, PH 7.0, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 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       48.33750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       27.90767            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       45.87367            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       48.33750            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       27.90767            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       45.87367            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       48.33750            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       27.90767            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       45.87367            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       55.81534            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       91.74733            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       55.81534            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       91.74733            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       55.81534            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       91.74733            
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: 12800 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 579  LIES ON A SPECIAL POSITION.                          
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     ALA A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     ASN A   388                                                      
REMARK 465     ARG A   389                                                      
REMARK 465     ILE A   390                                                      
REMARK 465     ASP A   391                                                      
REMARK 465     ALA A   392                                                      
REMARK 465     ALA A   393                                                      
REMARK 465     VAL A   394                                                      
REMARK 465     LEU A   395                                                      
REMARK 465     SER A   396                                                      
REMARK 465     ALA A   397                                                      
REMARK 465     LYS A   398                                                      
REMARK 465     SER A   399                                                      
REMARK 465     GLU A   400                                                      
REMARK 465     GLY A   401                                                      
REMARK 465     ASN A   402                                                      
REMARK 465     ALA A   403                                                      
REMARK 465     LEU A   404                                                      
REMARK 465     VAL A   405                                                      
REMARK 465     PRO A   406                                                      
REMARK 465     ARG A   407                                                      
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    LEU A  28      -71.92    -79.68                                   
REMARK 500    ASP A 138       59.33   -161.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3B9W   RELATED DB: PDB                                   
REMARK 900 ALTERNATIVE CRYSTAL FORM                                             
REMARK 900 RELATED ID: 3B9X   RELATED DB: PDB                                   
REMARK 900 ALTERNATIVE CRYSTAL FORM                                             
REMARK 900 RELATED ID: 3B9Y   RELATED DB: PDB                                   
REMARK 900 ALTERNATIVE CRYSTAL FORM WITH CO2                                    
REMARK 900 RELATED ID: 1U7G   RELATED DB: PDB                                   
REMARK 900 AMMONIUM TRANSPORTER AMTB FROM ESCHERICHIA COLI WITH MUTATIONS       
REMARK 900 RELATED ID: 1XQF   RELATED DB: PDB                                   
REMARK 900 AMMONIUM TRANSPORTER AMTB FROM ESCHERICHIA COLI                      
REMARK 900 RELATED ID: 2NS1   RELATED DB: PDB                                   
REMARK 900 AMTB FROM ESCHERICHIA COLI IN REGULATORY COMPLEX                     
DBREF  3BHS A    2   401  UNP    Q82X47   Q82X47_NITEU    26    425             
SEQADV 3BHS ASN A  402  UNP  Q82X47              EXPRESSION TAG                 
SEQADV 3BHS ALA A  403  UNP  Q82X47              EXPRESSION TAG                 
SEQADV 3BHS LEU A  404  UNP  Q82X47              EXPRESSION TAG                 
SEQADV 3BHS VAL A  405  UNP  Q82X47              EXPRESSION TAG                 
SEQADV 3BHS PRO A  406  UNP  Q82X47              EXPRESSION TAG                 
SEQADV 3BHS ARG A  407  UNP  Q82X47              EXPRESSION TAG                 
SEQRES   1 A  406  ALA VAL ALA PRO ALA GLU ILE ASN GLU ALA ARG LEU VAL          
SEQRES   2 A  406  ALA GLN TYR ASN TYR SER ILE ASN ILE LEU ALA MET LEU          
SEQRES   3 A  406  LEU VAL GLY PHE GLY PHE LEU MET VAL PHE VAL ARG ARG          
SEQRES   4 A  406  TYR GLY PHE SER ALA THR THR GLY THR TYR LEU VAL VAL          
SEQRES   5 A  406  ALA THR GLY LEU PRO LEU TYR ILE LEU LEU ARG ALA ASN          
SEQRES   6 A  406  GLY ILE PHE GLY HIS ALA LEU THR PRO HIS SER VAL ASP          
SEQRES   7 A  406  ALA VAL ILE TYR ALA GLU PHE ALA VAL ALA THR GLY LEU          
SEQRES   8 A  406  ILE ALA MET GLY ALA VAL LEU GLY ARG LEU ARG VAL PHE          
SEQRES   9 A  406  GLN TYR ALA LEU LEU ALA LEU PHE ILE VAL PRO VAL TYR          
SEQRES  10 A  406  LEU LEU ASN GLU TRP LEU VAL LEU ASP ASN ALA SER GLY          
SEQRES  11 A  406  LEU THR GLU GLY PHE GLN ASP SER ALA GLY SER ILE ALA          
SEQRES  12 A  406  ILE HIS ALA PHE GLY ALA TYR PHE GLY LEU GLY VAL SER          
SEQRES  13 A  406  ILE ALA LEU THR THR ALA ALA GLN ARG ALA GLN PRO ILE          
SEQRES  14 A  406  GLU SER ASP ALA THR SER ASP ARG PHE SER MET LEU GLY          
SEQRES  15 A  406  SER MET VAL LEU TRP LEU PHE TRP PRO SER PHE ALA THR          
SEQRES  16 A  406  ALA ILE VAL PRO PHE GLU GLN MET PRO GLN THR ILE VAL          
SEQRES  17 A  406  ASN THR LEU LEU ALA LEU CYS GLY ALA THR LEU ALA THR          
SEQRES  18 A  406  TYR PHE LEU SER ALA LEU PHE HIS LYS GLY LYS ALA SER          
SEQRES  19 A  406  ILE VAL ASP MET ALA ASN ALA ALA LEU ALA GLY GLY VAL          
SEQRES  20 A  406  ALA ILE GLY SER VAL CYS ASN ILE VAL GLY PRO VAL GLY          
SEQRES  21 A  406  ALA PHE VAL ILE GLY LEU LEU GLY GLY ALA ILE SER VAL          
SEQRES  22 A  406  VAL GLY PHE VAL PHE ILE GLN PRO MET LEU GLU SER LYS          
SEQRES  23 A  406  ALA LYS THR ILE ASP THR CYS GLY VAL HIS ASN LEU HIS          
SEQRES  24 A  406  GLY LEU PRO GLY LEU LEU GLY GLY PHE SER ALA ILE LEU          
SEQRES  25 A  406  ILE VAL PRO GLY ILE ALA VAL ALA GLN LEU THR GLY ILE          
SEQRES  26 A  406  GLY ILE THR LEU ALA LEU ALA LEU ILE GLY GLY VAL ILE          
SEQRES  27 A  406  ALA GLY ALA LEU ILE LYS LEU THR GLY THR THR LYS GLN          
SEQRES  28 A  406  ALA TYR GLU ASP SER HIS GLU PHE ILE HIS LEU ALA GLY          
SEQRES  29 A  406  PRO GLU ASP GLU HIS LYS ALA GLU ARG LEU VAL LEU GLU          
SEQRES  30 A  406  ALA LYS THR GLU ILE GLN GLY LEU LYS ASN ARG ILE ASP          
SEQRES  31 A  406  ALA ALA VAL LEU SER ALA LYS SER GLU GLY ASN ALA LEU          
SEQRES  32 A  406  VAL PRO ARG                                                  
FORMUL   2  HOH   *154(H2 O)                                                    
HELIX    1   1 ASN A    9  MET A   35  1                                  27    
HELIX    2   2 VAL A   36  VAL A   38  5                                   3    
HELIX    3   3 TYR A   41  ASN A   66  1                                  26    
HELIX    4   4 SER A   77  LEU A   99  1                                  23    
HELIX    5   5 ARG A  103  LEU A  126  1                                  24    
HELIX    6   6 ILE A  145  THR A  161  1                                  17    
HELIX    7   7 THR A  162  ALA A  167  1                                   6    
HELIX    8   8 ASP A  173  ALA A  197  1                                  25    
HELIX    9   9 PRO A  200  GLU A  202  5                                   3    
HELIX   10  10 GLN A  203  HIS A  230  1                                  28    
HELIX   11  11 SER A  235  ALA A  243  1                                   9    
HELIX   12  12 LEU A  244  GLY A  251  1                                   8    
HELIX   13  13 GLY A  258  PHE A  279  1                                  22    
HELIX   14  14 PHE A  279  ALA A  288  1                                  10    
HELIX   15  15 GLY A  295  HIS A  300  1                                   6    
HELIX   16  16 HIS A  300  VAL A  315  1                                  16    
HELIX   17  17 ILE A  318  LEU A  346  1                                  29    
HELIX   18  18 GLU A  355  GLU A  359  5                                   5    
HELIX   19  19 GLY A  365  GLU A  369  5                                   5    
HELIX   20  20 HIS A  370  GLY A  385  1                                  16    
CRYST1   96.675   96.675  137.621  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      0.010344  0.005972  0.000000        0.00000                         
SCALE2      0.000000  0.011944  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007266        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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