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
