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Database: PDB
Entry: 5C5X
LinkDB: 5C5X
Original site: 5C5X 
HEADER    TRANSPORT PROTEIN                       22-JUN-15   5C5X              
TITLE     CRYSTAL STRUCTURE OF THE S156E MUTANT OF HUMAN AQUAPORIN 5            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AQUAPORIN-5;                                               
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
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 5C5X    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.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 94885                          
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) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4754                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6711                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 359                          
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14447                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 796                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.07000                                              
REMARK   3    B22 (A**2) : 1.07000                                              
REMARK   3    B33 (A**2) : -1.60000                                             
REMARK   3    B12 (A**2) : 0.53000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.374         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.252         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.168         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.868         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14850 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20291 ; 0.950 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1944 ; 4.307 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   479 ;30.310 ;22.860       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2174 ;12.972 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;13.234 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2460 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10966 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7786 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10824 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   752 ; 0.102 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    43 ; 0.190 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.184 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  9970 ; 0.313 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15486 ; 0.564 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5618 ; 0.603 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4805 ; 1.018 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5C5X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211074.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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) : 0.8726                             
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 94885                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.810                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.18000                            
REMARK 200  R SYM                      (I) : 0.15600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.67100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3D9S                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR SOLUTION (100MM TRIS-HCL       
REMARK 280  PH7.9, 100MM NACL, 21% PEG400) MIXED WITH EACH OF 1,6-HEXANEDIOL    
REMARK 280  (30%, V/V) AND 1,3-PROPANEDIOL (40%, V/V) AND MIXED WITH THE        
REMARK 280  TEMPERATURE 281K, VAPOR DIFFUSION, HANGING DROP                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       94.83550            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       94.83550            
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       94.83550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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: 34550 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -134.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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     MET B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     MET E     1                                                      
REMARK 465     MET F     1                                                      
REMARK 465     MET G     1                                                      
REMARK 465     MET H     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER B  37    OG                                                  
REMARK 470     ASN B 112    CG   OD1  ND2                                       
REMARK 470     GLU B 234    CG   CD   OE1  OE2                                  
REMARK 470     SER D  37    OG                                                  
REMARK 470     PHE D  88    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE D 179    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN D 228    CG   OD1  ND2                                       
REMARK 470     SER F  37    OG                                                  
REMARK 470     ASN F 125    CG   OD1  ND2                                       
REMARK 470     SER H   7    OG                                                  
REMARK 470     SER H  37    OG                                                  
REMARK 470     GLN H  58    CG   CD   OE1  NE2                                  
REMARK 470     ASN H 125    CG   OD1  ND2                                       
REMARK 470     SER H 152    OG                                                  
REMARK 470     ASN H 228    CG   OD1  ND2                                       
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    LYS A   3      115.44     66.64                                   
REMARK 500    ASN A  69      106.03   -174.89                                   
REMARK 500    CYS A 182      111.85     65.82                                   
REMARK 500    SER A 183      -72.51   -100.56                                   
REMARK 500    MET A 184        0.25     59.81                                   
REMARK 500    LYS B   3      108.53     64.71                                   
REMARK 500    ALA B  38      105.52   -171.34                                   
REMARK 500    ASN B  69      111.85   -168.87                                   
REMARK 500    CYS B 182      108.91     66.13                                   
REMARK 500    SER B 183      -73.32    -95.94                                   
REMARK 500    MET B 184        3.84     58.02                                   
REMARK 500    ASN B 185      102.93   -162.32                                   
REMARK 500    SER B 229      -96.95    -56.25                                   
REMARK 500    LEU B 230      119.05     49.76                                   
REMARK 500    LYS C   3      111.48     74.63                                   
REMARK 500    ALA C  38       93.86   -163.31                                   
REMARK 500    ASN C  69      110.77   -163.84                                   
REMARK 500    CYS C 182      110.94     72.76                                   
REMARK 500    SER C 183      -70.16    -98.27                                   
REMARK 500    MET C 184        1.96     55.31                                   
REMARK 500    ASN C 185      105.69   -164.04                                   
REMARK 500    LYS D   3       94.60     64.46                                   
REMARK 500    ILE D  68       19.35     54.59                                   
REMARK 500    ASN D  69      116.34   -163.75                                   
REMARK 500    CYS D 182      116.45     67.94                                   
REMARK 500    SER D 183      -70.36   -103.24                                   
REMARK 500    MET D 184        0.34     57.17                                   
REMARK 500    ASN D 185      101.28   -161.22                                   
REMARK 500    SER D 229      -97.52     70.65                                   
REMARK 500    LEU D 230      145.65     62.57                                   
REMARK 500    LYS E   3       99.71     62.27                                   
REMARK 500    ILE E  68       18.99     54.54                                   
REMARK 500    ASN E  69      113.61   -163.23                                   
REMARK 500    CYS E 182      104.82     73.23                                   
REMARK 500    SER E 183      -69.69    -92.22                                   
REMARK 500    MET E 184        4.27     55.76                                   
REMARK 500    ASN E 185      106.38   -166.82                                   
REMARK 500    TRP E 207      -61.91   -100.97                                   
REMARK 500    ASN E 228     -168.11   -117.28                                   
REMARK 500    SER E 229      140.97    175.54                                   
REMARK 500    LEU E 230       98.92     96.26                                   
REMARK 500    LYS F   3       95.20     64.84                                   
REMARK 500    ILE F  68       18.58     54.64                                   
REMARK 500    ASN F  69      108.38   -163.24                                   
REMARK 500    CYS F 182      103.71     69.04                                   
REMARK 500    MET F 184        2.60     54.29                                   
REMARK 500    ASN F 185      103.72   -163.75                                   
REMARK 500    LYS G   3      106.73     67.04                                   
REMARK 500    ALA G  38      102.21   -170.78                                   
REMARK 500    ILE G  68       16.47     56.67                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 498        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH D 499        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH F 397        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH F 398        DISTANCE =  6.88 ANGSTROMS                       
REMARK 525    HOH F 399        DISTANCE =  7.88 ANGSTROMS                       
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 D  301                                                       
REMARK 610     PS6 H  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 D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PS6 H 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3D9S   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE STRUCTURE OF HUMAN AQUAPORIN 5                             
DBREF  5C5X A    1   245  UNP    P55064   AQP5_HUMAN       1    245             
DBREF  5C5X B    1   245  UNP    P55064   AQP5_HUMAN       1    245             
DBREF  5C5X C    1   245  UNP    P55064   AQP5_HUMAN       1    245             
DBREF  5C5X D    1   245  UNP    P55064   AQP5_HUMAN       1    245             
DBREF  5C5X E    1   245  UNP    P55064   AQP5_HUMAN       1    245             
DBREF  5C5X F    1   245  UNP    P55064   AQP5_HUMAN       1    245             
DBREF  5C5X G    1   245  UNP    P55064   AQP5_HUMAN       1    245             
DBREF  5C5X H    1   245  UNP    P55064   AQP5_HUMAN       1    245             
SEQADV 5C5X GLU A  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQADV 5C5X GLU B  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQADV 5C5X GLU C  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQADV 5C5X GLU D  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQADV 5C5X GLU E  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQADV 5C5X GLU F  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQADV 5C5X GLU G  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQADV 5C5X GLU H  156  UNP  P55064    SER   156 ENGINEERED MUTATION            
SEQRES   1 A  245  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 A  245  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 A  245  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 A  245  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 A  245  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 A  245  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 A  245  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 A  245  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 A  245  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 A  245  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 A  245  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 A  245  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 A  245  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 A  245  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 A  245  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 A  245  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 A  245  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 A  245  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 A  245  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO                  
SEQRES   1 B  245  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 B  245  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 B  245  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 B  245  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 B  245  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 B  245  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 B  245  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 B  245  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 B  245  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 B  245  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 B  245  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 B  245  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 B  245  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 B  245  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 B  245  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 B  245  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 B  245  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 B  245  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 B  245  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO                  
SEQRES   1 C  245  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 C  245  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 C  245  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 C  245  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 C  245  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 C  245  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 C  245  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 C  245  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 C  245  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 C  245  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 C  245  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 C  245  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 C  245  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 C  245  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 C  245  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 C  245  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 C  245  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 C  245  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 C  245  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO                  
SEQRES   1 D  245  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 D  245  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 D  245  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 D  245  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 D  245  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 D  245  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 D  245  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 D  245  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 D  245  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 D  245  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 D  245  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 D  245  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 D  245  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 D  245  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 D  245  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 D  245  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 D  245  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 D  245  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 D  245  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO                  
SEQRES   1 E  245  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 E  245  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 E  245  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 E  245  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 E  245  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 E  245  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 E  245  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 E  245  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 E  245  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 E  245  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 E  245  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 E  245  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 E  245  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 E  245  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 E  245  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 E  245  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 E  245  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 E  245  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 E  245  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO                  
SEQRES   1 F  245  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 F  245  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 F  245  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 F  245  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 F  245  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 F  245  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 F  245  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 F  245  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 F  245  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 F  245  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 F  245  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 F  245  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 F  245  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 F  245  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 F  245  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 F  245  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 F  245  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 F  245  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 F  245  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO                  
SEQRES   1 G  245  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 G  245  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 G  245  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 G  245  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 G  245  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 G  245  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 G  245  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 G  245  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 G  245  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 G  245  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 G  245  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 G  245  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 G  245  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 G  245  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 G  245  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 G  245  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 G  245  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 G  245  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 G  245  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO                  
SEQRES   1 H  245  MET LYS LYS GLU VAL CYS SER VAL ALA PHE LEU LYS ALA          
SEQRES   2 H  245  VAL PHE ALA GLU PHE LEU ALA THR LEU ILE PHE VAL PHE          
SEQRES   3 H  245  PHE GLY LEU GLY SER ALA LEU LYS TRP PRO SER ALA LEU          
SEQRES   4 H  245  PRO THR ILE LEU GLN ILE ALA LEU ALA PHE GLY LEU ALA          
SEQRES   5 H  245  ILE GLY THR LEU ALA GLN ALA LEU GLY PRO VAL SER GLY          
SEQRES   6 H  245  GLY HIS ILE ASN PRO ALA ILE THR LEU ALA LEU LEU VAL          
SEQRES   7 H  245  GLY ASN GLN ILE SER LEU LEU ARG ALA PHE PHE TYR VAL          
SEQRES   8 H  245  ALA ALA GLN LEU VAL GLY ALA ILE ALA GLY ALA GLY ILE          
SEQRES   9 H  245  LEU TYR GLY VAL ALA PRO LEU ASN ALA ARG GLY ASN LEU          
SEQRES  10 H  245  ALA VAL ASN ALA LEU ASN ASN ASN THR THR GLN GLY GLN          
SEQRES  11 H  245  ALA MET VAL VAL GLU LEU ILE LEU THR PHE GLN LEU ALA          
SEQRES  12 H  245  LEU CYS ILE PHE ALA SER THR ASP SER ARG ARG THR GLU          
SEQRES  13 H  245  PRO VAL GLY SER PRO ALA LEU SER ILE GLY LEU SER VAL          
SEQRES  14 H  245  THR LEU GLY HIS LEU VAL GLY ILE TYR PHE THR GLY CYS          
SEQRES  15 H  245  SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL VAL          
SEQRES  16 H  245  MET ASN ARG PHE SER PRO ALA HIS TRP VAL PHE TRP VAL          
SEQRES  17 H  245  GLY PRO ILE VAL GLY ALA VAL LEU ALA ALA ILE LEU TYR          
SEQRES  18 H  245  PHE TYR LEU LEU PHE PRO ASN SER LEU SER LEU SER GLU          
SEQRES  19 H  245  ARG VAL ALA ILE ILE LYS GLY THR TYR GLU PRO                  
HET    PS6  D 301      28                                                       
HET    PS6  H 301      28                                                       
HETNAM     PS6 O-[(S)-{[(2S)-2-(HEXANOYLOXY)-3-(TETRADECANOYLOXY)               
HETNAM   2 PS6  PROPYL]OXY}(HYDROXY)PHOSPHORYL]-D-SERINE                        
FORMUL   9  PS6    2(C26 H50 N O10 P)                                           
FORMUL  11  HOH   *796(H2 O)                                                    
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  GLY A   79  1                                  11    
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  THR A  150  1                                  24    
HELIX    7 AA7 SER A  160  GLY A  181  1                                  22    
HELIX    8 AA8 ASN A  185  MET A  196  1                                  12    
HELIX    9 AA9 SER A  200  HIS A  203  5                                   4    
HELIX   10 AB1 TRP A  204  LEU A  224  1                                  21    
HELIX   11 AB2 SER A  231  LYS A  240  1                                  10    
HELIX   12 AB3 SER B    7  LEU B   33  1                                  27    
HELIX   13 AB4 THR B   41  GLY B   65  1                                  25    
HELIX   14 AB5 ASN B   69  GLY B   79  1                                  11    
HELIX   15 AB6 SER B   83  ALA B  109  1                                  27    
HELIX   16 AB7 PRO B  110  GLY B  115  1                                   6    
HELIX   17 AB8 THR B  127  THR B  150  1                                  24    
HELIX   18 AB9 SER B  160  GLY B  181  1                                  22    
HELIX   19 AC1 ASN B  185  MET B  196  1                                  12    
HELIX   20 AC2 SER B  200  HIS B  203  5                                   4    
HELIX   21 AC3 TRP B  204  LEU B  224  1                                  21    
HELIX   22 AC4 SER B  231  GLY B  241  1                                  11    
HELIX   23 AC5 LYS C    3  CYS C    6  5                                   4    
HELIX   24 AC6 SER C    7  LEU C   33  1                                  27    
HELIX   25 AC7 THR C   41  GLY C   65  1                                  25    
HELIX   26 AC8 ASN C   69  GLY C   79  1                                  11    
HELIX   27 AC9 SER C   83  ALA C  109  1                                  27    
HELIX   28 AD1 PRO C  110  GLY C  115  1                                   6    
HELIX   29 AD2 THR C  127  THR C  150  1                                  24    
HELIX   30 AD3 SER C  160  GLY C  181  1                                  22    
HELIX   31 AD4 ASN C  185  ASN C  197  1                                  13    
HELIX   32 AD5 TRP C  204  LEU C  224  1                                  21    
HELIX   33 AD6 SER C  231  GLY C  241  1                                  11    
HELIX   34 AD7 LYS D    3  CYS D    6  5                                   4    
HELIX   35 AD8 SER D    7  LEU D   33  1                                  27    
HELIX   36 AD9 THR D   41  GLY D   65  1                                  25    
HELIX   37 AE1 ASN D   69  GLY D   79  1                                  11    
HELIX   38 AE2 SER D   83  ALA D  109  1                                  27    
HELIX   39 AE3 PRO D  110  GLY D  115  1                                   6    
HELIX   40 AE4 THR D  127  THR D  150  1                                  24    
HELIX   41 AE5 SER D  160  GLY D  181  1                                  22    
HELIX   42 AE6 ASN D  185  MET D  196  1                                  12    
HELIX   43 AE7 SER D  200  HIS D  203  5                                   4    
HELIX   44 AE8 TRP D  204  LEU D  224  1                                  21    
HELIX   45 AE9 SER D  231  LYS D  240  1                                  10    
HELIX   46 AF1 LYS E    3  CYS E    6  5                                   4    
HELIX   47 AF2 SER E    7  LEU E   33  1                                  27    
HELIX   48 AF3 THR E   41  GLY E   65  1                                  25    
HELIX   49 AF4 ASN E   69  GLY E   79  1                                  11    
HELIX   50 AF5 SER E   83  ALA E  109  1                                  27    
HELIX   51 AF6 PRO E  110  GLY E  115  1                                   6    
HELIX   52 AF7 THR E  127  THR E  150  1                                  24    
HELIX   53 AF8 SER E  160  GLY E  181  1                                  22    
HELIX   54 AF9 ASN E  185  MET E  196  1                                  12    
HELIX   55 AG1 TRP E  204  LEU E  224  1                                  21    
HELIX   56 AG2 SER E  231  LYS E  240  1                                  10    
HELIX   57 AG3 LYS F    3  CYS F    6  5                                   4    
HELIX   58 AG4 SER F    7  LEU F   33  1                                  27    
HELIX   59 AG5 THR F   41  GLY F   65  1                                  25    
HELIX   60 AG6 ASN F   69  GLY F   79  1                                  11    
HELIX   61 AG7 SER F   83  ALA F  109  1                                  27    
HELIX   62 AG8 PRO F  110  GLY F  115  1                                   6    
HELIX   63 AG9 THR F  127  THR F  150  1                                  24    
HELIX   64 AH1 SER F  160  ILE F  177  1                                  18    
HELIX   65 AH2 ASN F  185  ASN F  197  1                                  13    
HELIX   66 AH3 TRP F  204  LEU F  224  1                                  21    
HELIX   67 AH4 SER F  231  LYS F  240  1                                  10    
HELIX   68 AH5 SER G    7  ALA G   32  1                                  26    
HELIX   69 AH6 THR G   41  GLY G   65  1                                  25    
HELIX   70 AH7 ASN G   69  GLY G   79  1                                  11    
HELIX   71 AH8 SER G   83  ALA G  109  1                                  27    
HELIX   72 AH9 PRO G  110  GLY G  115  1                                   6    
HELIX   73 AI1 THR G  127  THR G  150  1                                  24    
HELIX   74 AI2 SER G  160  GLY G  181  1                                  22    
HELIX   75 AI3 ASN G  185  MET G  196  1                                  12    
HELIX   76 AI4 SER G  200  HIS G  203  5                                   4    
HELIX   77 AI5 TRP G  204  LEU G  224  1                                  21    
HELIX   78 AI6 SER G  231  GLY G  241  1                                  11    
HELIX   79 AI7 LYS H    3  CYS H    6  5                                   4    
HELIX   80 AI8 SER H    7  SER H   31  1                                  25    
HELIX   81 AI9 THR H   41  GLY H   65  1                                  25    
HELIX   82 AJ1 ASN H   69  GLY H   79  1                                  11    
HELIX   83 AJ2 SER H   83  ALA H  109  1                                  27    
HELIX   84 AJ3 PRO H  110  GLY H  115  1                                   6    
HELIX   85 AJ4 THR H  127  THR H  150  1                                  24    
HELIX   86 AJ5 SER H  160  GLY H  181  1                                  22    
HELIX   87 AJ6 ASN H  185  MET H  196  1                                  12    
HELIX   88 AJ7 TRP H  204  LEU H  224  1                                  21    
HELIX   89 AJ8 SER H  231  LYS H  240  1                                  10    
CISPEP   1 SER E  229    LEU E  230          0       -20.50                     
SITE     1 AC1 16 VAL A 158  GLY A 159  SER A 160  GLY B 159                    
SITE     2 AC1 16 SER B 160  GLY C 159  SER C 160  LEU C 163                    
SITE     3 AC1 16 HOH C 305  PRO D 157  VAL D 158  GLY D 159                    
SITE     4 AC1 16 LEU D 163  HOH D 411  HOH D 432  HOH D 438                    
SITE     1 AC2 14 GLY E 159  SER E 160  GLY F 159  GLY G 159                    
SITE     2 AC2 14 SER G 160  LEU G 163  PRO H 157  VAL H 158                    
SITE     3 AC2 14 GLY H 159  SER H 160  HOH H 419  HOH H 423                    
SITE     4 AC2 14 HOH H 429  HOH H 464                                          
CRYST1  170.750  170.750  189.671  90.00  90.00 120.00 P 63         48          
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      0.005857  0.003381  0.000000        0.00000                         
SCALE2      0.000000  0.006763  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005272        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system