HEADER TRANSPORT PROTEIN 19-NOV-15 5EUU
TITLE RAT PRESTIN STAS DOMAIN IN COMPLEX WITH CHLORIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRESTIN,PRESTIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: STAS DOMAIN,STAS DOMAIN,STAS DOMAIN,STAS DOMAIN;
COMPND 5 SYNONYM: SOLUTE CARRIER FAMILY 26 MEMBER 5,SOLUTE CARRIER FAMILY 26
COMPND 6 MEMBER 5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: RESIDUES 564-636 (VARIABLE LOOP) ARE DELETED, GLYSER
COMPND 10 ARE INSERTED BETWEEN POSITION 563 AND 637
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: SLC26A5, PRES;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET SUMO
KEYWDS ANION-BINDING SITE, PROTEIN-ANION COMPLEX, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.LOLLI,E.PASQUALETTO,E.COSTANZI,G.BONETTO,R.BATTISTUTTA
REVDAT 3 10-JAN-24 5EUU 1 REMARK
REVDAT 2 17-FEB-16 5EUU 1 JRNL
REVDAT 1 16-DEC-15 5EUU 0
JRNL AUTH G.LOLLI,E.PASQUALETTO,E.COSTANZI,G.BONETTO,R.BATTISTUTTA
JRNL TITL THE STAS DOMAIN OF MAMMALIAN SLC26A5 PRESTIN HARBOURS AN
JRNL TITL 2 ANION-BINDING SITE.
JRNL REF BIOCHEM.J. V. 473 365 2016
JRNL REFN ESSN 1470-8728
JRNL PMID 26635354
JRNL DOI 10.1042/BJ20151089
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.PASQUALETTO,R.AIELLO,L.GESIOT,G.BONETTO,M.BELLANDA,
REMARK 1 AUTH 2 R.BATTISTUTTA
REMARK 1 TITL STRUCTURE OF THE CYTOSOLIC PORTION OF THE MOTOR PROTEIN
REMARK 1 TITL 2 PRESTIN AND FUNCTIONAL ROLE OF THE STAS DOMAIN IN SLC26/SULP
REMARK 1 TITL 3 ANION TRANSPORTERS
REMARK 1 REF J.MOL.BIOL. V. 400 448 2010
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 20471983
REMARK 1 DOI 10.1016/J.JMB.2010.05.013
REMARK 2
REMARK 2 RESOLUTION. 1.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 23464
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.490
REMARK 3 FREE R VALUE TEST SET COUNT : 1288
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 31.0708 - 3.8877 1.00 2503 141 0.1555 0.1864
REMARK 3 2 3.8877 - 3.0867 1.00 2466 183 0.1432 0.1984
REMARK 3 3 3.0867 - 2.6968 1.00 2499 130 0.1595 0.1831
REMARK 3 4 2.6968 - 2.4503 1.00 2527 122 0.1552 0.1859
REMARK 3 5 2.4503 - 2.2747 1.00 2471 153 0.1419 0.1866
REMARK 3 6 2.2747 - 2.1407 1.00 2469 164 0.1437 0.2046
REMARK 3 7 2.1407 - 2.0335 1.00 2535 144 0.1677 0.1980
REMARK 3 8 2.0335 - 1.9450 1.00 2496 112 0.1822 0.1942
REMARK 3 9 1.9450 - 1.8701 0.88 2210 139 0.2789 0.3373
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 1065
REMARK 3 ANGLE : 0.764 1436
REMARK 3 CHIRALITY : 0.031 164
REMARK 3 PLANARITY : 0.003 182
REMARK 3 DIHEDRAL : 14.107 384
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 505 THROUGH 539 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8338 14.0232 -12.9306
REMARK 3 T TENSOR
REMARK 3 T11: 0.2021 T22: 0.2148
REMARK 3 T33: 0.2826 T12: -0.0002
REMARK 3 T13: -0.0587 T23: 0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 0.1369 L22: 0.4025
REMARK 3 L33: 0.2688 L12: 0.0485
REMARK 3 L13: 0.0555 L23: -0.1524
REMARK 3 S TENSOR
REMARK 3 S11: -0.0492 S12: -0.1718 S13: -0.3016
REMARK 3 S21: 0.0884 S22: 0.0897 S23: 0.0419
REMARK 3 S31: 0.3412 S32: 0.0706 S33: -0.0018
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 540 THROUGH 552)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1283 22.7623 0.6108
REMARK 3 T TENSOR
REMARK 3 T11: 0.2370 T22: 0.3402
REMARK 3 T33: 0.2312 T12: -0.1391
REMARK 3 T13: 0.0253 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 0.1045 L22: 0.1754
REMARK 3 L33: 1.1889 L12: -0.1658
REMARK 3 L13: -0.2238 L23: 0.3130
REMARK 3 S TENSOR
REMARK 3 S11: 0.4048 S12: -0.3765 S13: -0.2211
REMARK 3 S21: 0.3733 S22: -0.0718 S23: 0.0653
REMARK 3 S31: -0.3238 S32: -0.4335 S33: 0.1091
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 638 THROUGH 657 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0165 27.3197 -6.8376
REMARK 3 T TENSOR
REMARK 3 T11: 0.1643 T22: 0.2693
REMARK 3 T33: 0.2066 T12: -0.0258
REMARK 3 T13: -0.0096 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.2169 L22: 0.3142
REMARK 3 L33: -0.0159 L12: 0.2651
REMARK 3 L13: 0.0236 L23: 0.0499
REMARK 3 S TENSOR
REMARK 3 S11: 0.1365 S12: -0.2848 S13: -0.1736
REMARK 3 S21: 0.2531 S22: -0.1451 S23: 0.0555
REMARK 3 S31: 0.0176 S32: -0.1444 S33: -0.0006
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 658 THROUGH 671 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4480 30.6695 2.1346
REMARK 3 T TENSOR
REMARK 3 T11: 0.2795 T22: 0.3757
REMARK 3 T33: 0.1728 T12: -0.1101
REMARK 3 T13: -0.0495 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 0.2001 L22: 0.4258
REMARK 3 L33: -0.0026 L12: 0.2819
REMARK 3 L13: -0.0513 L23: -0.0328
REMARK 3 S TENSOR
REMARK 3 S11: 0.2752 S12: -0.6224 S13: -0.2070
REMARK 3 S21: 0.6422 S22: -0.3412 S23: -0.1368
REMARK 3 S31: -0.1562 S32: -0.0330 S33: -0.0371
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 672 THROUGH 698 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3405 36.6665 -7.5454
REMARK 3 T TENSOR
REMARK 3 T11: 0.2165 T22: 0.2331
REMARK 3 T33: 0.2476 T12: -0.0271
REMARK 3 T13: -0.0204 T23: -0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 0.1651 L22: 0.1201
REMARK 3 L33: 0.0785 L12: 0.0940
REMARK 3 L13: 0.0934 L23: 0.0281
REMARK 3 S TENSOR
REMARK 3 S11: 0.0843 S12: -0.1617 S13: 0.2129
REMARK 3 S21: 0.1042 S22: -0.1184 S23: -0.0048
REMARK 3 S31: -0.1530 S32: 0.0318 S33: 0.0005
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 699 THROUGH 718 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7405 29.7920 -13.6513
REMARK 3 T TENSOR
REMARK 3 T11: 0.1855 T22: 0.2872
REMARK 3 T33: 0.2233 T12: -0.0268
REMARK 3 T13: -0.0211 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.0984 L22: 0.1544
REMARK 3 L33: 0.2229 L12: -0.0200
REMARK 3 L13: -0.1401 L23: -0.0059
REMARK 3 S TENSOR
REMARK 3 S11: 0.0379 S12: 0.1164 S13: 0.0822
REMARK 3 S21: -0.0851 S22: 0.1248 S23: -0.1090
REMARK 3 S31: -0.1671 S32: 0.2707 S33: 0.0004
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5EUU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215548.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 2.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12555
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
REMARK 200 RESOLUTION RANGE LOW (A) : 41.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 15.60
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : 0.07500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.74900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3LLO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 1.8 M AMMONIUM
REMARK 280 SULPHATE, 5% (W/V) PEG400, 0.1% (W/V) OCTYL-BETA-D-
REMARK 280 GLUCOPYRANOSIDE. CRYSTALS WERE SOAKED WITH PRECIPITANT SOLUTION
REMARK 280 SUPPLEMENTED WITH 1 M AMMONIUM CHLORIDE, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 22.19567
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 44.39133
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 44.39133
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 22.19567
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SER A 553
REMARK 465 SER A 554
REMARK 465 ALA A 555
REMARK 465 LEU A 556
REMARK 465 LYS A 557
REMARK 465 ARG A 558
REMARK 465 LYS A 559
REMARK 465 THR A 560
REMARK 465 GLY A 561
REMARK 465 VAL A 562
REMARK 465 ASN A 563
REMARK 465 GLY A 635
REMARK 465 SER A 636
REMARK 465 GLU A 637
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 807
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LLO RELATED DB: PDB
REMARK 900 3LLO CONTAINS THE SAME PROTEIN IN THE APO FORM
REMARK 900 RELATED ID: 5EUS RELATED DB: PDB
REMARK 900 5EUS CONTAINS THE SAME PROTEIN IN COMPLEX WITH BROMIDE
DBREF 5EUU A 505 563 UNP Q9EPH0 S26A5_RAT 505 563
DBREF 5EUU A 637 718 UNP Q9EPH0 S26A5_RAT 637 718
SEQADV 5EUU GLY A 635 UNP Q9EPH0 LINKER
SEQADV 5EUU SER A 636 UNP Q9EPH0 LINKER
SEQRES 1 A 143 SER PRO SER TYR THR VAL LEU GLY GLN LEU PRO ASP THR
SEQRES 2 A 143 ASP VAL TYR ILE ASP ILE ASP ALA TYR GLU GLU VAL LYS
SEQRES 3 A 143 GLU ILE PRO GLY ILE LYS ILE PHE GLN ILE ASN ALA PRO
SEQRES 4 A 143 ILE TYR TYR ALA ASN SER ASP LEU TYR SER SER ALA LEU
SEQRES 5 A 143 LYS ARG LYS THR GLY VAL ASN GLY SER GLU ASN ILE HIS
SEQRES 6 A 143 THR VAL ILE LEU ASP PHE THR GLN VAL ASN PHE MET ASP
SEQRES 7 A 143 SER VAL GLY VAL LYS THR LEU ALA GLY ILE VAL LYS GLU
SEQRES 8 A 143 TYR GLY ASP VAL GLY ILE TYR VAL TYR LEU ALA GLY CYS
SEQRES 9 A 143 SER ALA GLN VAL VAL ASN ASP LEU THR SER ASN ARG PHE
SEQRES 10 A 143 PHE GLU ASN PRO ALA LEU LYS GLU LEU LEU PHE HIS SER
SEQRES 11 A 143 ILE HIS ASP ALA VAL LEU GLY SER GLN VAL ARG GLU ALA
HET CL A 801 1
HET CL A 802 1
HET EDO A 803 10
HET EDO A 804 10
HET EDO A 805 10
HET PG4 A 806 31
HET PGE A 807 24
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CL 2(CL 1-)
FORMUL 4 EDO 3(C2 H6 O2)
FORMUL 7 PG4 C8 H18 O5
FORMUL 8 PGE C6 H14 O4
FORMUL 9 HOH *87(H2 O)
HELIX 1 AA1 PRO A 543 TYR A 552 1 10
HELIX 2 AA2 ASP A 653 ASP A 669 1 17
HELIX 3 AA3 SER A 680 ASN A 690 1 11
HELIX 4 AA4 ASN A 695 GLU A 700 5 6
HELIX 5 AA5 SER A 705 SER A 713 1 9
SHEET 1 AA1 6 TYR A 520 ASP A 522 0
SHEET 2 AA1 6 TYR A 508 GLN A 513 -1 N GLY A 512 O ILE A 521
SHEET 3 AA1 6 ILE A 535 ILE A 540 -1 O GLN A 539 N THR A 509
SHEET 4 AA1 6 THR A 641 ASP A 645 1 O ASP A 645 N PHE A 538
SHEET 5 AA1 6 TYR A 673 ALA A 677 1 O TYR A 675 N LEU A 644
SHEET 6 AA1 6 LEU A 702 PHE A 703 1 O PHE A 703 N LEU A 676
SITE 1 AC1 6 MET A 652 ASP A 653 GLY A 656 GLN A 714
SITE 2 AC1 6 HOH A 929 HOH A 949
SITE 1 AC2 1 ILE A 706
SITE 1 AC3 1 GLN A 513
SITE 1 AC4 4 VAL A 684 THR A 688 LYS A 699 HOH A 919
SITE 1 AC5 1 GLU A 666
SITE 1 AC6 8 GLY A 668 TYR A 673 ALA A 697 GLU A 700
SITE 2 AC6 8 LEU A 701 HIS A 704 ALA A 718 HOH A 901
SITE 1 AC7 3 PRO A 506 ALA A 542 ASN A 695
CRYST1 62.133 62.133 66.587 90.00 90.00 120.00 P 31 2 1 6
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 0.016095 0.009292 0.000000 0.00000
SCALE2 0.000000 0.018584 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015018 0.00000
(ATOM LINES ARE NOT SHOWN.)
END