HEADER TRANSPORT PROTEIN 19-NOV-15 5EUX
TITLE RAT PRESTIN STAS DOMAIN IN COMPLEX WITH THIOCYANATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRESTIN,PRESTIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 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: NORWAY 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 4 10-JAN-24 5EUX 1 REMARK
REVDAT 3 20-DEC-17 5EUX 1 JRNL
REVDAT 2 17-FEB-16 5EUX 1 JRNL
REVDAT 1 16-DEC-15 5EUX 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 ESSN 1089-8638
REMARK 1 PMID 20471983
REMARK 1 DOI 10.1016/J.JMB.2010.05.013
REMARK 2
REMARK 2 RESOLUTION. 2.04 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) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 9652
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.280
REMARK 3 FREE R VALUE TEST SET COUNT : 951
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 41.9969 - 3.8970 1.00 2521 137 0.1388 0.1531
REMARK 3 2 3.8970 - 3.0934 1.00 2526 126 0.1548 0.2030
REMARK 3 3 3.0934 - 2.7025 0.99 2459 170 0.1760 0.2228
REMARK 3 4 2.7025 - 2.4554 0.98 2479 145 0.1931 0.2297
REMARK 3 5 2.4554 - 2.2795 0.96 2412 130 0.1957 0.2130
REMARK 3 6 2.2795 - 2.1451 0.95 2432 89 0.2012 0.2870
REMARK 3 7 2.1451 - 2.0376 0.89 2240 154 0.2293 0.2896
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) : 20.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.88
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 : 0.016 1064
REMARK 3 ANGLE : 1.259 1433
REMARK 3 CHIRALITY : 0.055 164
REMARK 3 PLANARITY : 0.006 181
REMARK 3 DIHEDRAL : 14.997 383
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 506 THROUGH 530 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7450 12.8425 -14.8143
REMARK 3 T TENSOR
REMARK 3 T11: 0.3910 T22: 0.4148
REMARK 3 T33: 0.4988 T12: 0.0055
REMARK 3 T13: -0.0340 T23: 0.0465
REMARK 3 L TENSOR
REMARK 3 L11: 0.6177 L22: 0.9215
REMARK 3 L33: 0.7913 L12: 0.5044
REMARK 3 L13: 0.7147 L23: 0.1937
REMARK 3 S TENSOR
REMARK 3 S11: -0.0037 S12: -0.0465 S13: -0.5209
REMARK 3 S21: 0.0588 S22: 0.1761 S23: -0.1818
REMARK 3 S31: 0.4695 S32: 0.1469 S33: 0.0005
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 531 THROUGH 550 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.3535 20.8578 -4.4246
REMARK 3 T TENSOR
REMARK 3 T11: 0.3242 T22: 0.5160
REMARK 3 T33: 0.4149 T12: -0.1009
REMARK 3 T13: -0.0152 T23: 0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 0.2340 L22: 0.8179
REMARK 3 L33: 0.1190 L12: -0.1313
REMARK 3 L13: 0.2700 L23: -0.3893
REMARK 3 S TENSOR
REMARK 3 S11: 0.2829 S12: -0.3838 S13: -0.0597
REMARK 3 S21: 0.4268 S22: -0.2229 S23: 0.0255
REMARK 3 S31: 0.2959 S32: -0.2244 S33: -0.0005
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 551 THROUGH 553 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5631 19.5158 6.6089
REMARK 3 T TENSOR
REMARK 3 T11: 0.5930 T22: 1.2339
REMARK 3 T33: 1.2173 T12: 0.0350
REMARK 3 T13: 0.0253 T23: 0.1510
REMARK 3 L TENSOR
REMARK 3 L11: 0.0119 L22: 0.0127
REMARK 3 L33: 0.1296 L12: -0.0265
REMARK 3 L13: 0.0130 L23: 0.0146
REMARK 3 S TENSOR
REMARK 3 S11: 0.5736 S12: 0.1243 S13: 0.6961
REMARK 3 S21: 1.0688 S22: 0.2211 S23: -0.7123
REMARK 3 S31: -0.0797 S32: -0.0960 S33: -0.0015
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 638 THROUGH 666 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2037 28.7308 -4.2067
REMARK 3 T TENSOR
REMARK 3 T11: 0.2665 T22: 0.4862
REMARK 3 T33: 0.2817 T12: -0.0714
REMARK 3 T13: -0.0158 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.7271 L22: 1.0839
REMARK 3 L33: 0.3551 L12: -0.1576
REMARK 3 L13: -0.2159 L23: 0.1870
REMARK 3 S TENSOR
REMARK 3 S11: 0.3218 S12: -0.4323 S13: -0.0747
REMARK 3 S21: 0.3373 S22: -0.2669 S23: -0.0365
REMARK 3 S31: 0.0932 S32: -0.1060 S33: -0.0001
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 667 THROUGH 692 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6429 34.1444 -6.2538
REMARK 3 T TENSOR
REMARK 3 T11: 0.2825 T22: 0.4667
REMARK 3 T33: 0.3207 T12: -0.0251
REMARK 3 T13: -0.0202 T23: -0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 0.6843 L22: 1.4253
REMARK 3 L33: -0.0716 L12: 0.5283
REMARK 3 L13: 0.2490 L23: 0.3109
REMARK 3 S TENSOR
REMARK 3 S11: 0.1959 S12: -0.2659 S13: 0.1661
REMARK 3 S21: 0.2404 S22: -0.1798 S23: 0.0438
REMARK 3 S31: -0.0793 S32: -0.0750 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 693 THROUGH 701 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0351 40.4049 -6.8132
REMARK 3 T TENSOR
REMARK 3 T11: 0.3922 T22: 0.4924
REMARK 3 T33: 0.3897 T12: -0.0488
REMARK 3 T13: -0.0641 T23: -0.1390
REMARK 3 L TENSOR
REMARK 3 L11: 0.2535 L22: 1.0416
REMARK 3 L33: 0.7561 L12: 0.1465
REMARK 3 L13: -0.2066 L23: -0.6988
REMARK 3 S TENSOR
REMARK 3 S11: -0.1989 S12: -1.0442 S13: 0.5165
REMARK 3 S21: -0.6027 S22: 0.1556 S23: -0.4997
REMARK 3 S31: -0.3773 S32: 0.4678 S33: -0.0745
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 702 THROUGH 718 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1685 28.6093 -14.3546
REMARK 3 T TENSOR
REMARK 3 T11: 0.2301 T22: 0.4287
REMARK 3 T33: 0.2962 T12: -0.0293
REMARK 3 T13: -0.0148 T23: -0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 0.3196 L22: 0.4806
REMARK 3 L33: 0.1160 L12: 0.2018
REMARK 3 L13: -0.4867 L23: -0.2210
REMARK 3 S TENSOR
REMARK 3 S11: 0.0039 S12: -0.0054 S13: -0.0671
REMARK 3 S21: -0.0367 S22: 0.2806 S23: 0.0688
REMARK 3 S31: -0.0998 S32: 0.1785 S33: 0.0012
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 5EUX 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_1000215554.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAY-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 : 9671
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.038
REMARK 200 RESOLUTION RANGE LOW (A) : 41.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 17.40
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.3
REMARK 200 DATA REDUNDANCY IN SHELL : 14.20
REMARK 200 R MERGE FOR SHELL (I) : 1.13800
REMARK 200 R SYM FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 3LLO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 1.8 M AMMONIUM
REMARK 280 SULPHATE, 250 MM NASCN, 5% (W/V) PEG400, 0.1% (W/V) OCTYL-BETA-D-
REMARK 280 GLUCOPYRANOSIDE, VAPOR DIFFUSION, 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 22.25167
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 44.50333
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 44.50333
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 22.25167
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: 1320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 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 505
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HG1 THR A 641 HH22 ARG A 716 1.21
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 ASP A 522 122.97 -33.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 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 EDO A 806
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
REMARK 900 RELATED ID: 5EUU RELATED DB: PDB
REMARK 900 5EUU CONTAINS THE SAME PROTEIN IN COMPLEX WITH CHLORIDE
REMARK 900 RELATED ID: 5EUW RELATED DB: PDB
REMARK 900 5EUW CONTAINS THE SAME PROTEIN IN COMPLEX WITH NITRATE
DBREF 5EUX A 505 563 UNP Q9EPH0 S26A5_RAT 505 563
DBREF 5EUX A 637 718 UNP Q9EPH0 S26A5_RAT 637 718
SEQADV 5EUX GLY A 635 UNP Q9EPH0 LINKER
SEQADV 5EUX 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 SCN A 801 3
HET PEG A 802 17
HET PG4 A 803 31
HET EDO A 804 10
HET EDO A 805 10
HET EDO A 806 10
HETNAM SCN THIOCYANATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 SCN C N S 1-
FORMUL 3 PEG C4 H10 O3
FORMUL 4 PG4 C8 H18 O5
FORMUL 5 EDO 3(C2 H6 O2)
FORMUL 8 HOH *42(H2 O)
HELIX 1 AA1 PRO A 543 SER A 553 1 11
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 ILE A 643 N LYS A 536
SHEET 5 AA1 6 TYR A 673 ALA A 677 1 O TYR A 673 N VAL A 642
SHEET 6 AA1 6 LEU A 702 PHE A 703 1 O PHE A 703 N LEU A 676
SITE 1 AC1 5 ILE A 544 MET A 652 ASP A 653 GLY A 656
SITE 2 AC1 5 GLN A 714
SITE 1 AC2 2 TYR A 552 LYS A 699
SITE 1 AC3 6 GLY A 668 TYR A 673 ALA A 697 HIS A 704
SITE 2 AC3 6 ALA A 718 HOH A 919
SITE 1 AC4 2 GLN A 513 VAL A 710
SITE 1 AC5 2 TYR A 508 LYS A 536
SITE 1 AC6 4 THR A 517 ASP A 518 ALA A 525 HOH A 920
CRYST1 62.365 62.365 66.755 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 0.016035 0.009258 0.000000 0.00000
SCALE2 0.000000 0.018515 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014980 0.00000
(ATOM LINES ARE NOT SHOWN.)
END