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Database: PDB
Entry: 3D9S
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Original site: 3D9S 
HEADER    MEMBRANE PROTEIN                        27-MAY-08   3D9S              
TITLE     HUMAN AQUAPORIN 5 (AQP5) - HIGH RESOLUTION X-RAY STRUCTURE            
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                                                      
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: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: X33;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPICZB;                                   
SOURCE  11 OTHER_DETAILS: EASYSELECT PICHIA EXPRESSION KIT                      
SOURCE  12 (INVITROGEN)                                                         
KEYWDS    AQUAPORIN, AQP, AQUAGLYCEROPORIN, MEMBRANE PROTEIN, WATER             
KEYWDS   2 TRANSPORT, X-RAY DIFFRACTION, LIPID, PHOSPHATIDYLSERINE,             
KEYWDS   3 PSF, NPA, AR/R, WATER CHANNEL, GLYCOPROTEIN, MEMBRANE,               
KEYWDS   4 TRANSMEMBRANE, TRANSPORT                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.HORSEFIELD,K.NORDEN,M.FELLERT,A.BACKMARK,S.TORNROTH-                
AUTHOR   2 HORSEFIELD,A.C.TERWISSCHA VAN SCHELTINGA,J.KVASSMAN,                 
AUTHOR   3 P.KJELLBOM,U.JOHANSON,R.NEUTZE                                       
REVDAT   4   24-FEB-09 3D9S    1       VERSN                                    
REVDAT   3   23-SEP-08 3D9S    1       JRNL   REMARK                            
REVDAT   2   09-SEP-08 3D9S    1       TITLE                                    
REVDAT   1   26-AUG-08 3D9S    0                                                
JRNL        AUTH   R.HORSEFIELD,K.NORDEN,M.FELLERT,A.BACKMARK,                  
JRNL        AUTH 2 S.TORNROTH-HORSEFIELD,                                       
JRNL        AUTH 3 A.C.TERWISSCHA VAN SCHELTINGA,J.KVASSMAN,                    
JRNL        AUTH 4 P.KJELLBOM,U.JOHANSON,R.NEUTZE                               
JRNL        TITL   HIGH-RESOLUTION X-RAY STRUCTURE OF HUMAN AQUAPORIN           
JRNL        TITL 2 5                                                            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105 13327 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18768791                                                     
JRNL        DOI    10.1073/PNAS.0801466105                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 78.0                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : THIN RESOLUTION SHELLS         
REMARK   3                                       (RANDOMLY) TO ACCOUNT FOR      
REMARK   3                                       TWINNING; TWIN RELATED         
REMARK   3                                       REFLECTIONS ALWAYS IN THE      
REMARK   3                                       SAME SET (WORK OR TEST         
REMARK   3                                       SET) NOT DIVIDED BETWEEN       
REMARK   3                                       THEM.                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.162                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.193                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 4174                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 84751                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.153                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 66554                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 7241                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 38                                            
REMARK   3   SOLVENT ATOMS      : 111                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 7386.58                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 29577                   
REMARK   3   NUMBER OF RESTRAINTS                     : 30558                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.006                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.024                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.024                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.033                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.035                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.013                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.103                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: FIRSTLY, A HOMOLOGY MODEL FOR AQP5        
REMARK   3  WAS GENERATED USING THE SWISS-MODEL WEB SERVER WITH THE BOVINE      
REMARK   3  AQP1 STRUCTURE (PDB 1J4N) AS A TEMPLATE. THE HOMOLOGY MODEL         
REMARK   3  WAS THEN USED AS SEARCH MODEL IN MOLECULAR REPLACEMENT              
REMARK   3  CALCULATIONS. SEE PRIMARY CITATION FOR ADDITIONAL DETAILS.;         
REMARK   3  THIS DATA IS MEROHEDRALLY TWINNED; THE TWINNING OPERATOR IS         
REMARK   3  (H,K,L) -> (K, H, -L) AND THE TWINNING FRACTION IS 0.463.           
REMARK   3  DIFFRACTION DATA WAS FROM A CRYSTAL WITH NEAR-PERFECT PSEUDO-       
REMARK   3  MEROHEDRAL TWINNING WITH THE TWIN OPERATOR(010 100 00-1)            
REMARK   3  SWAPPING THE A AND B AXES. THEREFORE, CONVENTIONAL PROGRAMS/        
REMARK   3  MAPS ARE NOT RECOMMENDED WHEN ANALYSING THIS PDB AND STRUCTURE      
REMARK   3  FACTORS. SHELX (WITH BASF AND TWIN VALUES SET) IS USEFUL FOR        
REMARK   3  MAP CALCULATION BUT THE TWINNING COMPATIBLE SCRIPTS ARE BEST        
REMARK   3  FOR RELIABLE OMIT MAPS (SEE SUPPORTING INFORMATION OF PRIMARY       
REMARK   3  CITATION).                                                          
REMARK   4                                                                      
REMARK   4 3D9S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB047771.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 170.0                              
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
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   : 84751                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.560                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.9                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO                    
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1J4N                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% POLYETHYLENE GLYCOL 400, 0.1M        
REMARK 280  TRIS HCL PH 7.6, 0.1M NACL, 6% V/V 1,6-HEXANEDIOL, 3% V/V 1,4-      
REMARK 280  BUTANEDIOL OR 3% V/V 1,3-PROPANEDIOL, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 281K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       45.23850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       92.19750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.32200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       92.19750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.23850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.32200            
REMARK 290   SMTRY3   4  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: 13190 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -132.0 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     0                                                      
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     0                                                      
REMARK 465     ASP B   246                                                      
REMARK 465     GLU B   247                                                      
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     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     LYS C     2                                                      
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     0                                                      
REMARK 465     ASP D   246                                                      
REMARK 465     GLU D   247                                                      
REMARK 465     ASP D   248                                                      
REMARK 465     TRP D   249                                                      
REMARK 465     GLU D   250                                                      
REMARK 465     GLU D   251                                                      
REMARK 465     GLN D   252                                                      
REMARK 465     ARG D   253                                                      
REMARK 465     GLU D   254                                                      
REMARK 465     GLU D   255                                                      
REMARK 465     ARG D   256                                                      
REMARK 465     LYS D   257                                                      
REMARK 465     LYS D   258                                                      
REMARK 465     THR D   259                                                      
REMARK 465     MET D   260                                                      
REMARK 465     GLU D   261                                                      
REMARK 465     LEU D   262                                                      
REMARK 465     THR D   263                                                      
REMARK 465     THR D   264                                                      
REMARK 465     ARG D   265                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASN A 116   C   -  N   -  CA  ANGL. DEV. =  27.8 DEGREES          
REMARK 500    LEU B  22   CA  -  CB  -  CG  ANGL. DEV. =  24.7 DEGREES          
REMARK 500    LEU B 230   CA  -  CB  -  CG  ANGL. DEV. =  16.4 DEGREES          
REMARK 500    ARG C  86   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ASN C 116   C   -  N   -  CA  ANGL. DEV. =  19.7 DEGREES          
REMARK 500    LEU C 117   C   -  N   -  CA  ANGL. DEV. =  25.3 DEGREES          
REMARK 500    LEU C 144   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    TYR C 223   CB  -  CG  -  CD1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    LEU C 230   C   -  N   -  CA  ANGL. DEV. =  18.6 DEGREES          
REMARK 500    ASN D 112   C   -  N   -  CA  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    TYR D 178   CB  -  CG  -  CD2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG D 188   CD  -  NE  -  CZ  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ARG D 188   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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  33      152.32    -48.36                                   
REMARK 500    TRP A  35      104.09     57.27                                   
REMARK 500    ALA A  38      100.34   -162.66                                   
REMARK 500    ILE A  68       23.95     48.89                                   
REMARK 500    ASN A  69      110.99   -163.93                                   
REMARK 500    ASN A  80      167.81     62.89                                   
REMARK 500    GLN A  81        4.94    102.74                                   
REMARK 500    ASN A 116      -49.48    105.68                                   
REMARK 500    PHE A 179      -62.51   -107.70                                   
REMARK 500    CYS A 182      106.68     68.34                                   
REMARK 500    SER A 183      -86.45    -90.83                                   
REMARK 500    ASN A 185       98.71   -169.24                                   
REMARK 500    SER A 200      142.72    -39.39                                   
REMARK 500    SER A 231      137.21     57.50                                   
REMARK 500    LEU A 232     -119.01    -89.45                                   
REMARK 500    SER A 233       16.48    -40.77                                   
REMARK 500    LYS B  34       69.31    -69.07                                   
REMARK 500    ALA B  38      101.15   -174.00                                   
REMARK 500    ASN B  69      114.79   -177.20                                   
REMARK 500    ALA B 121      103.76    178.75                                   
REMARK 500    ARG B 154      126.22    -20.92                                   
REMARK 500    THR B 180       -6.34   -141.68                                   
REMARK 500    CYS B 182      104.83     54.49                                   
REMARK 500    SER B 183      -80.09    -93.40                                   
REMARK 500    ASN B 185      110.58   -175.79                                   
REMARK 500    ARG B 198       58.27   -146.08                                   
REMARK 500    SER B 200      163.27     78.38                                   
REMARK 500    ALA B 202       -5.82     73.97                                   
REMARK 500    GLU C   4     -106.33    -82.42                                   
REMARK 500    VAL C   5      -69.92     14.56                                   
REMARK 500    LEU C  22      -72.30    -43.40                                   
REMARK 500    ALA C  38       91.69   -168.76                                   
REMARK 500    ASN C  69      103.45   -169.90                                   
REMARK 500    ASN C 116      -86.12    -28.91                                   
REMARK 500    LEU C 117       72.68   -105.58                                   
REMARK 500    ASN C 123        6.25    -56.95                                   
REMARK 500    ASN C 124      -51.40     66.79                                   
REMARK 500    THR C 180       -7.30   -142.42                                   
REMARK 500    CYS C 182      100.59     67.20                                   
REMARK 500    SER C 183      -64.61    -93.15                                   
REMARK 500    MET C 184       -3.10     66.09                                   
REMARK 500    ASN C 185      101.40   -160.71                                   
REMARK 500    ASN C 197      -91.91     49.98                                   
REMARK 500    ARG C 198       77.58      2.81                                   
REMARK 500    LEU C 230       -0.79     -7.17                                   
REMARK 500    SER C 231      136.26     56.20                                   
REMARK 500    GLU C 244      -76.39    -84.69                                   
REMARK 500    CYS D   6       41.80   -106.97                                   
REMARK 500    SER D  37      -74.59    -15.90                                   
REMARK 500    SER D  64      -21.10   -142.21                                   
REMARK 500    ILE D  68       23.93     49.98                                   
REMARK 500    ASN D  69      110.60   -167.05                                   
REMARK 500    ASN D 124      -53.49     75.31                                   
REMARK 500    CYS D 182      111.11     76.64                                   
REMARK 500    SER D 183      -76.94   -101.47                                   
REMARK 500    ASN D 185      100.73   -179.15                                   
REMARK 500    VAL D 194     -174.14    -67.22                                   
REMARK 500    VAL D 195      -85.50     61.47                                   
REMARK 500    ASN D 197       64.52   -119.49                                   
REMARK 500    GLU D 244      159.59    161.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 PS6 IS A MODIFIED FORM OF PHOSPHATIDYLSERINE (PSF).                  
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PS6 D 266                 
DBREF  3D9S A    2   265  UNP    P55064   AQP5_HUMAN       2    265             
DBREF  3D9S B    2   265  UNP    P55064   AQP5_HUMAN       2    265             
DBREF  3D9S C    2   265  UNP    P55064   AQP5_HUMAN       2    265             
DBREF  3D9S D    2   265  UNP    P55064   AQP5_HUMAN       2    265             
SEQADV 3D9S MET A    0  UNP  P55064              INITIATING METHIONINE          
SEQADV 3D9S SER A    1  UNP  P55064              EXPRESSION TAG                 
SEQADV 3D9S MET B    0  UNP  P55064              INITIATING METHIONINE          
SEQADV 3D9S SER B    1  UNP  P55064              EXPRESSION TAG                 
SEQADV 3D9S MET C    0  UNP  P55064              INITIATING METHIONINE          
SEQADV 3D9S SER C    1  UNP  P55064              EXPRESSION TAG                 
SEQADV 3D9S MET D    0  UNP  P55064              INITIATING METHIONINE          
SEQADV 3D9S SER D    1  UNP  P55064              EXPRESSION TAG                 
SEQRES   1 A  266  MET SER LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS          
SEQRES   2 A  266  ALA VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL          
SEQRES   3 A  266  PHE PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA          
SEQRES   4 A  266  LEU PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU          
SEQRES   5 A  266  ALA ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER          
SEQRES   6 A  266  GLY GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU          
SEQRES   7 A  266  VAL GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR          
SEQRES   8 A  266  VAL ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY          
SEQRES   9 A  266  ILE LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN          
SEQRES  10 A  266  LEU ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY          
SEQRES  11 A  266  GLN ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU          
SEQRES  12 A  266  ALA LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR          
SEQRES  13 A  266  SER PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER          
SEQRES  14 A  266  VAL THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY          
SEQRES  15 A  266  CYS SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL          
SEQRES  16 A  266  VAL MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP          
SEQRES  17 A  266  VAL GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU          
SEQRES  18 A  266  TYR PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER          
SEQRES  19 A  266  GLU ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO ASP          
SEQRES  20 A  266  GLU ASP TRP GLU GLU GLN ARG GLU GLU ARG LYS LYS THR          
SEQRES  21 A  266  MET GLU LEU THR THR ARG                                      
SEQRES   1 B  266  MET SER LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS          
SEQRES   2 B  266  ALA VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL          
SEQRES   3 B  266  PHE PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA          
SEQRES   4 B  266  LEU PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU          
SEQRES   5 B  266  ALA ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER          
SEQRES   6 B  266  GLY GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU          
SEQRES   7 B  266  VAL GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR          
SEQRES   8 B  266  VAL ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY          
SEQRES   9 B  266  ILE LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN          
SEQRES  10 B  266  LEU ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY          
SEQRES  11 B  266  GLN ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU          
SEQRES  12 B  266  ALA LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR          
SEQRES  13 B  266  SER PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER          
SEQRES  14 B  266  VAL THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY          
SEQRES  15 B  266  CYS SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL          
SEQRES  16 B  266  VAL MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP          
SEQRES  17 B  266  VAL GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU          
SEQRES  18 B  266  TYR PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER          
SEQRES  19 B  266  GLU ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO ASP          
SEQRES  20 B  266  GLU ASP TRP GLU GLU GLN ARG GLU GLU ARG LYS LYS THR          
SEQRES  21 B  266  MET GLU LEU THR THR ARG                                      
SEQRES   1 C  266  MET SER LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS          
SEQRES   2 C  266  ALA VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL          
SEQRES   3 C  266  PHE PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA          
SEQRES   4 C  266  LEU PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU          
SEQRES   5 C  266  ALA ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER          
SEQRES   6 C  266  GLY GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU          
SEQRES   7 C  266  VAL GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR          
SEQRES   8 C  266  VAL ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY          
SEQRES   9 C  266  ILE LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN          
SEQRES  10 C  266  LEU ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY          
SEQRES  11 C  266  GLN ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU          
SEQRES  12 C  266  ALA LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR          
SEQRES  13 C  266  SER PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER          
SEQRES  14 C  266  VAL THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY          
SEQRES  15 C  266  CYS SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL          
SEQRES  16 C  266  VAL MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP          
SEQRES  17 C  266  VAL GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU          
SEQRES  18 C  266  TYR PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER          
SEQRES  19 C  266  GLU ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO ASP          
SEQRES  20 C  266  GLU ASP TRP GLU GLU GLN ARG GLU GLU ARG LYS LYS THR          
SEQRES  21 C  266  MET GLU LEU THR THR ARG                                      
SEQRES   1 D  266  MET SER LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS          
SEQRES   2 D  266  ALA VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL          
SEQRES   3 D  266  PHE PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA          
SEQRES   4 D  266  LEU PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU          
SEQRES   5 D  266  ALA ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER          
SEQRES   6 D  266  GLY GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU          
SEQRES   7 D  266  VAL GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR          
SEQRES   8 D  266  VAL ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY          
SEQRES   9 D  266  ILE LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN          
SEQRES  10 D  266  LEU ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY          
SEQRES  11 D  266  GLN ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU          
SEQRES  12 D  266  ALA LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR          
SEQRES  13 D  266  SER PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER          
SEQRES  14 D  266  VAL THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY          
SEQRES  15 D  266  CYS SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL          
SEQRES  16 D  266  VAL MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP          
SEQRES  17 D  266  VAL GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU          
SEQRES  18 D  266  TYR PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER          
SEQRES  19 D  266  GLU ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO ASP          
SEQRES  20 D  266  GLU ASP TRP GLU GLU GLN ARG GLU GLU ARG LYS LYS THR          
SEQRES  21 D  266  MET GLU LEU THR THR ARG                                      
HET    PS6  D 266      38                                                       
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                                              
FORMUL   6  HOH   *111(H2 O)                                                    
HELIX    1   1 SER A    1  CYS A    6  1                                   6    
HELIX    2   2 SER A    7  LEU A   33  1                                  27    
HELIX    3   3 THR A   41  GLY A   65  1                                  25    
HELIX    4   4 ASN A   69  GLY A   79  1                                  11    
HELIX    5   5 SER A   83  ALA A  109  1                                  27    
HELIX    6   6 PRO A  110  GLY A  115  1                                   6    
HELIX    7   7 THR A  127  ASP A  151  1                                  25    
HELIX    8   8 SER A  160  GLY A  181  1                                  22    
HELIX    9   9 ASN A  185  ASN A  197  1                                  13    
HELIX   10  10 ALA A  202  LEU A  224  1                                  23    
HELIX   11  11 ARG A  235  LYS A  240  1                                   6    
HELIX   12  12 SER B    1  CYS B    6  1                                   6    
HELIX   13  13 SER B    7  SER B   31  1                                  25    
HELIX   14  14 THR B   41  GLY B   65  1                                  25    
HELIX   15  15 ASN B   69  GLY B   79  1                                  11    
HELIX   16  16 SER B   83  ALA B  109  1                                  27    
HELIX   17  17 PRO B  110  GLY B  115  1                                   6    
HELIX   18  18 THR B  127  THR B  150  1                                  24    
HELIX   19  19 SER B  160  GLY B  181  1                                  22    
HELIX   20  20 ASN B  185  MET B  196  1                                  12    
HELIX   21  21 TRP B  204  TYR B  223  1                                  20    
HELIX   22  22 SER B  231  GLY B  241  1                                  11    
HELIX   23  23 SER C    7  LEU C   33  1                                  27    
HELIX   24  24 THR C   41  GLY C   65  1                                  25    
HELIX   25  25 ASN C   69  GLY C   79  1                                  11    
HELIX   26  26 SER C   83  GLY C  107  1                                  25    
HELIX   27  27 PRO C  110  GLY C  115  1                                   6    
HELIX   28  28 THR C  127  THR C  150  1                                  24    
HELIX   29  29 SER C  160  ILE C  177  1                                  18    
HELIX   30  30 ASN C  185  MET C  196  1                                  12    
HELIX   31  31 TRP C  204  TYR C  223  1                                  20    
HELIX   32  32 SER C  231  LYS C  240  1                                  10    
HELIX   33  33 SER D    1  CYS D    6  1                                   6    
HELIX   34  34 SER D    7  LEU D   33  1                                  27    
HELIX   35  35 THR D   41  GLY D   65  1                                  25    
HELIX   36  36 ASN D   69  GLY D   79  1                                  11    
HELIX   37  37 SER D   83  ALA D  109  1                                  27    
HELIX   38  38 PRO D  110  GLY D  115  1                                   6    
HELIX   39  39 THR D  127  ASP D  151  1                                  25    
HELIX   40  40 SER D  160  GLY D  181  1                                  22    
HELIX   41  41 ASN D  185  VAL D  194  1                                  10    
HELIX   42  42 TRP D  204  LEU D  224  1                                  21    
HELIX   43  43 SER D  231  GLY D  241  1                                  11    
CISPEP   1 GLY A  115    ASN A  116          0         4.49                     
CISPEP   2 LEU A  230    SER A  231          0         6.36                     
CISPEP   3 SER A  231    LEU A  232          0        -3.31                     
CISPEP   4 ASN C  116    LEU C  117          0        22.91                     
CISPEP   5 GLU C  244    PRO C  245          0        -0.99                     
SITE     1 AC1 16 LEU A  47  GLY A 159  LEU A 163  LEU B  47                    
SITE     2 AC1 16 GLY B 159  PRO C 157  VAL C 158  GLY C 159                    
SITE     3 AC1 16 SER C 160  LEU C 163  SER D 156  PRO D 157                    
SITE     4 AC1 16 VAL D 158  GLY D 159  SER D 160  LEU D 163                    
CRYST1   90.477   90.644  184.395  90.00  90.00  90.00 P 21 21 21   16          
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      0.011053  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011032  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005423        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system