GenomeNet

Database: PDB
Entry: 5DYE
LinkDB: 5DYE
Original site: 5DYE 
HEADER    TRANSPORT PROTEIN                       24-SEP-15   5DYE              
TITLE     CRYSTAL STRUCTURE OF THE FULL LENGTH S156E MUTANT OF HUMAN AQUAPORIN 5
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AQUAPORIN-5;                                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: AQP-5;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AQP5;                                                          
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    TRANSPORT PROTEIN, MEMBRANE PROTEIN                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.KITCHEN,F.OEBERG,J.SJOEHAMN,K.HEDFALK,R.M.BILL,A.C.CONNER,          
AUTHOR   2 M.T.CONNER,S.TOERNROTH-HORSEFIELD                                    
REVDAT   1   02-DEC-15 5DYE    0                                                
JRNL        AUTH   P.KITCHEN,F.OBERG,J.SJOHAMN,K.HEDFALK,R.M.BILL,A.C.CONNER,   
JRNL        AUTH 2 M.T.CONNER,S.TORNROTH-HORSEFIELD                             
JRNL        TITL   PLASMA MEMBRANE ABUNDANCE OF HUMAN AQUAPORIN 5 IS            
JRNL        TITL 2 DYNAMICALLY REGULATED BY MULTIPLE PATHWAYS.                  
JRNL        REF    PLOS ONE                      V.  10 43027 2015              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   26569106                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0143027                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0131                                      
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) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 150.76                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 20774                          
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) : 0.280                           
REMARK   3   R VALUE            (WORKING SET) : 0.279                           
REMARK   3   FREE R VALUE                     : 0.311                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1115                            
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) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1525                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.3790                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7296                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 161.6                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.70000                                              
REMARK   3    B22 (A**2) : 4.70000                                              
REMARK   3    B33 (A**2) : -15.23000                                            
REMARK   3    B12 (A**2) : 2.35000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.661         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.754         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 57.103        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.889                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.883                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7510 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7458 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10257 ; 1.084 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17025 ; 0.892 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   977 ; 5.844 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   254 ;32.331 ;23.110       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1098 ;13.861 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;10.372 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1235 ; 0.052 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8489 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1752 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3923 ; 4.895 ;16.127       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3923 ; 4.895 ;16.127       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4895 ; 8.315 ;24.168       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  4896 ; 8.314 ;24.170       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3587 ; 3.581 ;16.550       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3588 ; 3.581 ;16.550       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  5363 ; 6.585 ;24.705       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  8650 ;11.994 ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  8651 ;11.994 ;  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 5DYE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214019.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAY-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22191                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 101.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG 400, 0.1M TRIS PH 7.9, 0.1 M     
REMARK 280  NACL, 3% 1,6 HEXANEDIOL AND 4% 1,3-PROPANEDIOL AS ADDITIVE TO       
REMARK 280  THE DROP ONLY, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 281K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 1 2                          
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   -Y,-X,-Z                                                
REMARK 290       5555   -X+Y,Y,-Z                                               
REMARK 290       6555   X,X-Y,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -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  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13470 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 35660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -131.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PRO A   245                                                      
REMARK 465     ASP A   246                                                      
REMARK 465     GLU A   247                                                      
REMARK 465     ASP A   248                                                      
REMARK 465     TRP A   249                                                      
REMARK 465     GLU A   250                                                      
REMARK 465     GLU A   251                                                      
REMARK 465     GLN A   252                                                      
REMARK 465     ARG A   253                                                      
REMARK 465     GLU A   254                                                      
REMARK 465     GLU A   255                                                      
REMARK 465     ARG A   256                                                      
REMARK 465     LYS A   257                                                      
REMARK 465     LYS A   258                                                      
REMARK 465     THR A   259                                                      
REMARK 465     MET A   260                                                      
REMARK 465     GLU A   261                                                      
REMARK 465     LEU A   262                                                      
REMARK 465     THR A   263                                                      
REMARK 465     THR A   264                                                      
REMARK 465     ARG A   265                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ASP B   248                                                      
REMARK 465     TRP B   249                                                      
REMARK 465     GLU B   250                                                      
REMARK 465     GLU B   251                                                      
REMARK 465     GLN B   252                                                      
REMARK 465     ARG B   253                                                      
REMARK 465     GLU B   254                                                      
REMARK 465     GLU B   255                                                      
REMARK 465     ARG B   256                                                      
REMARK 465     LYS B   257                                                      
REMARK 465     LYS B   258                                                      
REMARK 465     THR B   259                                                      
REMARK 465     MET B   260                                                      
REMARK 465     GLU B   261                                                      
REMARK 465     LEU B   262                                                      
REMARK 465     THR B   263                                                      
REMARK 465     THR B   264                                                      
REMARK 465     ARG B   265                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     ASP C   246                                                      
REMARK 465     GLU C   247                                                      
REMARK 465     ASP C   248                                                      
REMARK 465     TRP C   249                                                      
REMARK 465     GLU C   250                                                      
REMARK 465     GLU C   251                                                      
REMARK 465     GLN C   252                                                      
REMARK 465     ARG C   253                                                      
REMARK 465     GLU C   254                                                      
REMARK 465     GLU C   255                                                      
REMARK 465     ARG C   256                                                      
REMARK 465     LYS C   257                                                      
REMARK 465     LYS C   258                                                      
REMARK 465     THR C   259                                                      
REMARK 465     MET C   260                                                      
REMARK 465     GLU C   261                                                      
REMARK 465     LEU C   262                                                      
REMARK 465     THR C   263                                                      
REMARK 465     THR C   264                                                      
REMARK 465     ARG C   265                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASP D   247A                                                     
REMARK 465     ARG D   255                                                      
REMARK 465     LYS D   256                                                      
REMARK 465     LYS D   257                                                      
REMARK 465     THR D   258                                                      
REMARK 465     MET D   259                                                      
REMARK 465     GLU D   260                                                      
REMARK 465     LEU D   261                                                      
REMARK 465     THR D   262                                                      
REMARK 465     THR D   263                                                      
REMARK 465     ARG D   264                                                      
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    GLU A   4       10.42   -148.25                                   
REMARK 500    ALA A  38      105.44   -163.72                                   
REMARK 500    ASN A  69      124.62   -177.93                                   
REMARK 500    ASN A  80       37.83     74.37                                   
REMARK 500    PHE A 179      -73.26    -96.86                                   
REMARK 500    CYS A 182      101.93     70.45                                   
REMARK 500    SER A 183      -70.46    -85.89                                   
REMARK 500    MET A 184       24.26     47.64                                   
REMARK 500    ASN A 185      116.38    178.17                                   
REMARK 500    MET A 196      -97.96   -164.27                                   
REMARK 500    ASN A 197      -76.16   -169.12                                   
REMARK 500    ARG A 198     -169.09   -110.34                                   
REMARK 500    ALA A 202       56.10   -108.49                                   
REMARK 500    SER A 229       68.26     60.76                                   
REMARK 500    THR A 242       63.09   -107.25                                   
REMARK 500    ALA B  32       53.71   -118.97                                   
REMARK 500    ALA B  38      114.84   -166.76                                   
REMARK 500    ASN B  69       98.77   -170.84                                   
REMARK 500    ASN B  80       61.13     88.12                                   
REMARK 500    CYS B 182      113.85     55.13                                   
REMARK 500    SER B 183      -79.60   -104.54                                   
REMARK 500    MET B 184       19.23     54.73                                   
REMARK 500    ASN B 185       92.83   -164.32                                   
REMARK 500    SER B 229       69.35     69.29                                   
REMARK 500    GLU B 244       96.54   -164.22                                   
REMARK 500    ASP B 246     -165.24     60.25                                   
REMARK 500    ALA C  38      118.10   -164.89                                   
REMARK 500    ILE C  68       14.99     58.98                                   
REMARK 500    ARG C 114      -70.30    -34.34                                   
REMARK 500    CYS C 182      131.61     64.98                                   
REMARK 500    SER C 183      -82.19   -134.58                                   
REMARK 500    MET C 184      -35.03     64.20                                   
REMARK 500    ASN C 197       46.20     71.64                                   
REMARK 500    ALA C 202       44.94   -103.79                                   
REMARK 500    SER C 229       76.68     54.61                                   
REMARK 500    THR C 242       50.58   -151.76                                   
REMARK 500    GLU C 244      -71.11    -83.72                                   
REMARK 500    ALA D  38      114.55   -168.04                                   
REMARK 500    VAL D  63      -72.70    -69.23                                   
REMARK 500    ASN D  69      110.77   -168.01                                   
REMARK 500    CYS D 182       97.06     55.70                                   
REMARK 500    SER D 183      -72.57    -82.86                                   
REMARK 500    MET D 184       -8.22     56.13                                   
REMARK 500    ASN D 197       50.17     71.44                                   
REMARK 500    TRP D 248       71.55     43.15                                   
REMARK 500    GLU D 250     -173.44     68.69                                   
REMARK 500    GLN D 251     -172.29     73.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A    3     GLU A    4                  149.83                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PS6 B  301                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PS6 B 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5C5X   RELATED DB: PDB                                   
REMARK 900 5C5X CONTAINS THE SAME PROTEIN TRUNCATED AT THE C-TERMINUS.          
REMARK 900 RELATED ID: 3D9S   RELATED DB: PDB                                   
REMARK 900 3D9S CONTAINS THE WILD-TYPE PROTEIN.                                 
DBREF  5DYE A    1   265  UNP    P55064   AQP5_HUMAN       1    265             
DBREF  5DYE B    1   265  UNP    P55064   AQP5_HUMAN       1    265             
DBREF  5DYE C    1   265  UNP    P55064   AQP5_HUMAN       1    265             
DBREF  5DYE D    1   264  UNP    P55064   AQP5_HUMAN       1    265             
SEQADV 5DYE GLU A  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQADV 5DYE GLU B  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQADV 5DYE GLU C  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQADV 5DYE GLU D  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQRES   1 A  265  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 A  265  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 A  265  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 A  265  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 A  265  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 A  265  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 A  265  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 A  265  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 A  265  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 A  265  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 A  265  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 A  265  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 A  265  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 A  265  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 A  265  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 A  265  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 A  265  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 A  265  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 A  265  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO ASP GLU          
SEQRES  20 A  265  ASP TRP GLU GLU GLN ARG GLU GLU ARG LYS LYS THR MET          
SEQRES  21 A  265  GLU LEU THR THR ARG                                          
SEQRES   1 B  265  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 B  265  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 B  265  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 B  265  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 B  265  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 B  265  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 B  265  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 B  265  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 B  265  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 B  265  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 B  265  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 B  265  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 B  265  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 B  265  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 B  265  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 B  265  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 B  265  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 B  265  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 B  265  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO ASP GLU          
SEQRES  20 B  265  ASP TRP GLU GLU GLN ARG GLU GLU ARG LYS LYS THR MET          
SEQRES  21 B  265  GLU LEU THR THR ARG                                          
SEQRES   1 C  265  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 C  265  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 C  265  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 C  265  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 C  265  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 C  265  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 C  265  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 C  265  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 C  265  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 C  265  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 C  265  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 C  265  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 C  265  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 C  265  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 C  265  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 C  265  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 C  265  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 C  265  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 C  265  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO ASP GLU          
SEQRES  20 C  265  ASP TRP GLU GLU GLN ARG GLU GLU ARG LYS LYS THR MET          
SEQRES  21 C  265  GLU LEU THR THR ARG                                          
SEQRES   1 D  265  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 D  265  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 D  265  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 D  265  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 D  265  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 D  265  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 D  265  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 D  265  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 D  265  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 D  265  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 D  265  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 D  265  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 D  265  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 D  265  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 D  265  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 D  265  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 D  265  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 D  265  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 D  265  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO ASP GLU          
SEQRES  20 D  265  ASP TRP GLU GLU GLN ARG GLU GLU ARG LYS LYS THR MET          
SEQRES  21 D  265  GLU LEU THR THR ARG                                          
HET    PS6  B 301      29                                                       
HETNAM     PS6 O-[(S)-{[(2S)-2-(HEXANOYLOXY)-3-(TETRADECANOYLOXY)               
HETNAM   2 PS6  PROPYL]OXY}(HYDROXY)PHOSPHORYL]-D-SERINE                        
FORMUL   5  PS6    C26 H50 N O10 P                                              
HELIX    1 AA1 SER A    7  LEU A   33  1                                  27    
HELIX    2 AA2 THR A   41  GLY A   65  1                                  25    
HELIX    3 AA3 ASN A   69  VAL A   78  1                                  10    
HELIX    4 AA4 SER A   83  ALA A  109  1                                  27    
HELIX    5 AA5 PRO A  110  GLY A  115  1                                   6    
HELIX    6 AA6 THR A  127  ASP A  151  1                                  25    
HELIX    7 AA7 SER A  160  GLY A  181  1                                  22    
HELIX    8 AA8 ASN A  185  GLY A  191  1                                   7    
HELIX    9 AA9 TRP A  204  TYR A  221  1                                  18    
HELIX   10 AB1 SER A  231  GLY A  241  1                                  11    
HELIX   11 AB2 SER B    7  SER B   31  1                                  25    
HELIX   12 AB3 THR B   41  GLY B   65  1                                  25    
HELIX   13 AB4 ASN B   69  ASN B   80  1                                  12    
HELIX   14 AB5 SER B   83  ALA B  109  1                                  27    
HELIX   15 AB6 PRO B  110  GLY B  115  1                                   6    
HELIX   16 AB7 THR B  127  THR B  150  1                                  24    
HELIX   17 AB8 SER B  160  GLY B  181  1                                  22    
HELIX   18 AB9 ASN B  185  MET B  196  1                                  12    
HELIX   19 AC1 HIS B  203  TYR B  223  1                                  21    
HELIX   20 AC2 SER B  231  GLY B  241  1                                  11    
HELIX   21 AC3 SER C    7  ALA C   32  1                                  26    
HELIX   22 AC4 THR C   41  GLY C   61  1                                  21    
HELIX   23 AC5 ASN C   69  GLY C   79  1                                  11    
HELIX   24 AC6 SER C   83  ALA C  109  1                                  27    
HELIX   25 AC7 PRO C  110  GLY C  115  1                                   6    
HELIX   26 AC8 THR C  127  THR C  150  1                                  24    
HELIX   27 AC9 SER C  160  GLY C  181  1                                  22    
HELIX   28 AD1 ASN C  185  MET C  196  1                                  12    
HELIX   29 AD2 ALA C  202  LEU C  224  1                                  23    
HELIX   30 AD3 SER C  231  GLY C  241  1                                  11    
HELIX   31 AD4 LYS D    3  SER D    7  1                                   5    
HELIX   32 AD5 SER D    7  ALA D   32  1                                  26    
HELIX   33 AD6 THR D   41  LEU D   60  1                                  20    
HELIX   34 AD7 LEU D   60  GLY D   65  1                                   6    
HELIX   35 AD8 ASN D   69  GLY D   79  1                                  11    
HELIX   36 AD9 SER D   83  GLY D  107  1                                  25    
HELIX   37 AE1 PRO D  110  GLY D  115  1                                   6    
HELIX   38 AE2 THR D  127  ASP D  151  1                                  25    
HELIX   39 AE3 SER D  160  ILE D  177  1                                  18    
HELIX   40 AE4 ASN D  185  MET D  196  1                                  12    
HELIX   41 AE5 ALA D  202  LEU D  224  1                                  23    
HELIX   42 AE6 SER D  231  GLY D  241  1                                  11    
CISPEP   1 GLU C  244    PRO C  245          0         0.46                     
CISPEP   2 GLU D  244    PRO D  245          0         2.02                     
CISPEP   3 ARG D  252    GLU D  253          0         3.93                     
SITE     1 AC1 12 THR A 155  PRO A 157  GLY A 159  SER A 160                    
SITE     2 AC1 12 GLY B 159  SER B 160  LEU B 163  GLY C 159                    
SITE     3 AC1 12 SER C 160  LEU C 163  GLY D 159  SER D 160                    
CRYST1  174.286  174.286  100.858  90.00  90.00 120.00 P 3 1 2      24          
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      0.005738  0.003313  0.000000        0.00000                         
SCALE2      0.000000  0.006625  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009915        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system