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
