GenomeNet

Database: PDB
Entry: 3B9W
LinkDB: 3B9W
Original site: 3B9W 
HEADER    TRANSPORT PROTEIN                       07-NOV-07   3B9W              
TITLE     THE 1.3 A RESOLUTION STRUCTURE OF NITROSOMONAS EUROPAEA RH50 AND      
TITLE    2 MECHANISTIC IMPLICATIONS FOR NH3 TRANSPORT BY RHESUS FAMILY PROTEINS 
CAVEAT     3B9W    BOG A 408 HAS WRONG CHIRALITY AT ATOM C2 BOG A 408 HAS WRONG 
CAVEAT   2 3B9W    CHIRALITY AT ATOM C3                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AMMONIUM TRANSPORTER FAMILY;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 25-425;                                           
COMPND   5 SYNONYM: RHESUS PROTEIN, RH-LIKE PROTEIN;                            
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NITROSOMONAS EUROPAEA;                          
SOURCE   3 ORGANISM_TAXID: 915;                                                 
SOURCE   4 GENE: RH50;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: GT1000;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PAD7                                      
KEYWDS    MEMBRANE PROTEIN, AMMONIA TRANSPORT, RHESUS PROTEIN, TRANSPORT        
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.LUPO,F.K.WINKLER                                                    
REVDAT   6   29-JUL-20 3B9W    1       CAVEAT COMPND REMARK SEQADV              
REVDAT   6 2                   1       HETNAM SITE                              
REVDAT   5   25-OCT-17 3B9W    1       REMARK                                   
REVDAT   4   13-JUL-11 3B9W    1       VERSN                                    
REVDAT   3   24-FEB-09 3B9W    1       VERSN                                    
REVDAT   2   04-DEC-07 3B9W    1       JRNL                                     
REVDAT   1   20-NOV-07 3B9W    0                                                
JRNL        AUTH   D.LUPO,X.D.LI,A.DURAND,T.TOMIZAKI,B.CHERIF-ZAHAR,G.MATASSI,  
JRNL        AUTH 2 M.MERRICK,F.K.WINKLER                                        
JRNL        TITL   THE 1.3-A RESOLUTION STRUCTURE OF NITROSOMONAS EUROPAEA RH50 
JRNL        TITL 2 AND MECHANISTIC IMPLICATIONS FOR NH3 TRANSPORT BY RHESUS     
JRNL        TITL 3 FAMILY PROTEINS.                                             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 104 19303 2007              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18032606                                                     
JRNL        DOI    10.1073/PNAS.0706563104                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 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) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 125231                         
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) : 0.148                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.171                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6637                            
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) : 1.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.33                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9283                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 503                          
REMARK   3   BIN FREE R VALUE                    : 0.3160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2671                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 372                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.15000                                              
REMARK   3    B22 (A**2) : 0.15000                                              
REMARK   3    B33 (A**2) : -0.23000                                             
REMARK   3    B12 (A**2) : 0.08000                                              
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): 0.035         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.036         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.024         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.364         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.977                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.972                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2779 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3793 ; 1.005 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   369 ; 4.598 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    94 ;32.435 ;23.617       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   417 ;11.261 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;10.411 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   464 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2036 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1514 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2019 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   329 ; 0.084 ; 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):    67 ; 0.134 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    36 ; 0.081 ; 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):  1853 ; 2.848 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2865 ; 3.493 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1066 ; 4.712 ; 4.500       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   924 ; 6.147 ; 6.000       
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):  2919 ; 2.625 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   372 ;10.532 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2718 ; 6.045 ; 3.000       
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   : 1.00                                          
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 3B9W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045261.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07209                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 131874                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.7100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.68200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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 ENTRTY 2NUU                                      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MM TRIS/HCL PH=8.5, 0.2M NACL, 24%     
REMARK 280  PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, PH 8.5    
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       50.03050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       28.88512            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       47.94267            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       50.03050            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       28.88512            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       47.94267            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       50.03050            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       28.88512            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       47.94267            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.77025            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       95.88533            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       57.77025            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       95.88533            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       57.77025            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       95.88533            
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: 14590 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 719  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 720  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 721  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     SER A     1                                                      
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     HIS A   370                                                      
REMARK 465     LYS A   371                                                      
REMARK 465     ALA A   372                                                      
REMARK 465     GLU A   373                                                      
REMARK 465     ARG A   374                                                      
REMARK 465     LEU A   375                                                      
REMARK 465     VAL A   376                                                      
REMARK 465     LEU A   377                                                      
REMARK 465     GLU A   378                                                      
REMARK 465     ALA A   379                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     THR A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     ILE A   383                                                      
REMARK 465     GLN A   384                                                      
REMARK 465     GLY A   385                                                      
REMARK 465     LEU A   386                                                      
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     HIS A   402                                                      
REMARK 465     HIS A   403                                                      
REMARK 465     HIS A   404                                                      
REMARK 465     HIS A   405                                                      
REMARK 465     HIS A   406                                                      
REMARK 465     HIS 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    VAL A 125      -61.40    -94.76                                   
REMARK 500    ASP A 138       65.18   -160.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XQF   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE AMMONIUM TRANSPORTER AMTB FROM ESCHERICHIA COLI            
REMARK 900 RELATED ID: 1U7G   RELATED DB: PDB                                   
REMARK 900 TRIPLE MUTANT OF THE AMMONIUM TRANSPORTER AMTB FROM ESCHERICHIA COLI 
REMARK 900 RELATED ID: 2B2F   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE AMMONIUM TRANSPORTER AMT1 FROM ARCHAEOGLOBUS FULGIDUS      
DBREF  3B9W A    1   401  UNP    Q82X47   Q82X47_NITEU    25    425             
SEQADV 3B9W HIS A  402  UNP  Q82X47              EXPRESSION TAG                 
SEQADV 3B9W HIS A  403  UNP  Q82X47              EXPRESSION TAG                 
SEQADV 3B9W HIS A  404  UNP  Q82X47              EXPRESSION TAG                 
SEQADV 3B9W HIS A  405  UNP  Q82X47              EXPRESSION TAG                 
SEQADV 3B9W HIS A  406  UNP  Q82X47              EXPRESSION TAG                 
SEQADV 3B9W HIS A  407  UNP  Q82X47              EXPRESSION TAG                 
SEQRES   1 A  407  SER ALA VAL ALA PRO ALA GLU ILE ASN GLU ALA ARG LEU          
SEQRES   2 A  407  VAL ALA GLN TYR ASN TYR SER ILE ASN ILE LEU ALA MET          
SEQRES   3 A  407  LEU LEU VAL GLY PHE GLY PHE LEU MET VAL PHE VAL ARG          
SEQRES   4 A  407  ARG TYR GLY PHE SER ALA THR THR GLY THR TYR LEU VAL          
SEQRES   5 A  407  VAL ALA THR GLY LEU PRO LEU TYR ILE LEU LEU ARG ALA          
SEQRES   6 A  407  ASN GLY ILE PHE GLY HIS ALA LEU THR PRO HIS SER VAL          
SEQRES   7 A  407  ASP ALA VAL ILE TYR ALA GLU PHE ALA VAL ALA THR GLY          
SEQRES   8 A  407  LEU ILE ALA MET GLY ALA VAL LEU GLY ARG LEU ARG VAL          
SEQRES   9 A  407  PHE GLN TYR ALA LEU LEU ALA LEU PHE ILE VAL PRO VAL          
SEQRES  10 A  407  TYR LEU LEU ASN GLU TRP LEU VAL LEU ASP ASN ALA SER          
SEQRES  11 A  407  GLY LEU THR GLU GLY PHE GLN ASP SER ALA GLY SER ILE          
SEQRES  12 A  407  ALA ILE HIS ALA PHE GLY ALA TYR PHE GLY LEU GLY VAL          
SEQRES  13 A  407  SER ILE ALA LEU THR THR ALA ALA GLN ARG ALA GLN PRO          
SEQRES  14 A  407  ILE GLU SER ASP ALA THR SER ASP ARG PHE SER MET LEU          
SEQRES  15 A  407  GLY SER MET VAL LEU TRP LEU PHE TRP PRO SER PHE ALA          
SEQRES  16 A  407  THR ALA ILE VAL PRO PHE GLU GLN MET PRO GLN THR ILE          
SEQRES  17 A  407  VAL ASN THR LEU LEU ALA LEU CYS GLY ALA THR LEU ALA          
SEQRES  18 A  407  THR TYR PHE LEU SER ALA LEU PHE HIS LYS GLY LYS ALA          
SEQRES  19 A  407  SER ILE VAL ASP MET ALA ASN ALA ALA LEU ALA GLY GLY          
SEQRES  20 A  407  VAL ALA ILE GLY SER VAL CYS ASN ILE VAL GLY PRO VAL          
SEQRES  21 A  407  GLY ALA PHE VAL ILE GLY LEU LEU GLY GLY ALA ILE SER          
SEQRES  22 A  407  VAL VAL GLY PHE VAL PHE ILE GLN PRO MET LEU GLU SER          
SEQRES  23 A  407  LYS ALA LYS THR ILE ASP THR CYS GLY VAL HIS ASN LEU          
SEQRES  24 A  407  HIS GLY LEU PRO GLY LEU LEU GLY GLY PHE SER ALA ILE          
SEQRES  25 A  407  LEU ILE VAL PRO GLY ILE ALA VAL ALA GLN LEU THR GLY          
SEQRES  26 A  407  ILE GLY ILE THR LEU ALA LEU ALA LEU ILE GLY GLY VAL          
SEQRES  27 A  407  ILE ALA GLY ALA LEU ILE LYS LEU THR GLY THR THR LYS          
SEQRES  28 A  407  GLN ALA TYR GLU ASP SER HIS GLU PHE ILE HIS LEU ALA          
SEQRES  29 A  407  GLY PRO GLU ASP GLU HIS LYS ALA GLU ARG LEU VAL LEU          
SEQRES  30 A  407  GLU ALA LYS THR GLU ILE GLN GLY LEU LYS ASN ARG ILE          
SEQRES  31 A  407  ASP ALA ALA VAL LEU SER ALA LYS SER GLU GLY HIS HIS          
SEQRES  32 A  407  HIS HIS HIS HIS                                              
HET    BOG  A 408      20                                                       
HET    GOL  A 409       6                                                       
HETNAM     BOG OCTYL BETA-D-GLUCOPYRANOSIDE                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  BOG    C14 H28 O6                                                   
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  HOH   *372(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 GLY A  301  VAL A  315  1                                  15    
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    
CRYST1  100.061  100.061  143.828  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      0.009994  0.005770  0.000000        0.00000                         
SCALE2      0.000000  0.011540  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006953        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system