HEADER TRANSPORT PROTEIN 19-NOV-15 5EUS
TITLE RAT PRESTIN STAS DOMAIN IN COMPLEX WITH BROMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRESTIN,RAT PRESTIN STAS DOMAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: STAS DOMAIN,STAS DOMAIN;
COMPND 5 SYNONYM: SOLUTE CARRIER FAMILY 26 MEMBER 5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
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, SLC26A5;
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 5EUS 1 REMARK
REVDAT 3 20-JUL-16 5EUS 1 JRNL
REVDAT 2 17-FEB-16 5EUS 1 JRNL
REVDAT 1 16-DEC-15 5EUS 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. 1.83 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) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 24555
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.330
REMARK 3 FREE R VALUE TEST SET COUNT : 1308
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 41.5233 - 3.8120 1.00 2619 122 0.1395 0.1704
REMARK 3 2 3.8120 - 3.0260 1.00 2542 184 0.1477 0.1883
REMARK 3 3 3.0260 - 2.6435 1.00 2636 122 0.1555 0.2231
REMARK 3 4 2.6435 - 2.4019 1.00 2585 126 0.1482 0.1928
REMARK 3 5 2.4019 - 2.2297 1.00 2607 136 0.1453 0.2175
REMARK 3 6 2.2297 - 2.0983 1.00 2597 136 0.1500 0.1722
REMARK 3 7 2.0983 - 1.9932 1.00 2564 168 0.1719 0.2388
REMARK 3 8 1.9932 - 1.9064 1.00 2571 144 0.2223 0.2914
REMARK 3 9 1.9064 - 1.8330 0.98 2526 170 0.2604 0.2661
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.26
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 : 0.011 1059
REMARK 3 ANGLE : 1.219 1430
REMARK 3 CHIRALITY : 0.055 164
REMARK 3 PLANARITY : 0.006 182
REMARK 3 DIHEDRAL : 15.395 380
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 505 THROUGH 539 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0381 -2.8275 -1.8433
REMARK 3 T TENSOR
REMARK 3 T11: 0.3054 T22: 0.2873
REMARK 3 T33: 0.3459 T12: -0.0235
REMARK 3 T13: 0.0446 T23: 0.0387
REMARK 3 L TENSOR
REMARK 3 L11: 0.5159 L22: 0.3821
REMARK 3 L33: 0.3718 L12: -0.2064
REMARK 3 L13: -0.2243 L23: -0.2097
REMARK 3 S TENSOR
REMARK 3 S11: 0.1924 S12: -0.1031 S13: 0.1187
REMARK 3 S21: 0.0019 S22: 0.0324 S23: 0.2154
REMARK 3 S31: -0.0530 S32: -0.2770 S33: 0.0003
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 540 THROUGH 552 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3124 0.9060 11.4293
REMARK 3 T TENSOR
REMARK 3 T11: 0.5053 T22: 0.3590
REMARK 3 T33: 0.4037 T12: -0.0683
REMARK 3 T13: 0.0774 T23: -0.0922
REMARK 3 L TENSOR
REMARK 3 L11: 0.1035 L22: 0.0284
REMARK 3 L33: 0.0910 L12: -0.0558
REMARK 3 L13: -0.0766 L23: 0.0293
REMARK 3 S TENSOR
REMARK 3 S11: 0.0212 S12: -0.5414 S13: 0.3075
REMARK 3 S21: 0.3864 S22: -0.2536 S23: 0.3794
REMARK 3 S31: -0.4775 S32: 0.3021 S33: -0.0024
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 638 THROUGH 718)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6206 -11.1613 3.6414
REMARK 3 T TENSOR
REMARK 3 T11: 0.3389 T22: 0.2443
REMARK 3 T33: 0.2453 T12: -0.0281
REMARK 3 T13: 0.0111 T23: 0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 1.2489 L22: 1.4547
REMARK 3 L33: 0.6972 L12: -0.1505
REMARK 3 L13: 0.2893 L23: -0.3667
REMARK 3 S TENSOR
REMARK 3 S11: 0.0361 S12: -0.1099 S13: -0.0604
REMARK 3 S21: 0.1867 S22: 0.0236 S23: -0.0612
REMARK 3 S31: 0.1212 S32: 0.0914 S33: 0.0000
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 5EUS 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_1000215485.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-10
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) : 0.91
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 : 13128
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 41.513
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 19.50
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.08200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 17.90
REMARK 200 R MERGE FOR SHELL (I) : 1.99800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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 (%): 46.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 1.8 M AMMONIUM
REMARK 280 SULPHATE, 126 MM POTASSIUM BROMIDE, 5% (W/V) PEG400, 0.1% (W/V)
REMARK 280 OCTYL-BETA-D-GLUCOPYRANOSIDE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 22.13867
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 44.27733
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 44.27733
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 22.13867
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 11.0 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 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 522 120.11 -39.45
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 BR A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO 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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LLO RELATED DB: PDB
REMARK 900 3LLO CONTAINS THE SAME PROTEIN IN APO FORM.
DBREF 5EUS A 505 563 UNP Q9EPH0 S26A5_RAT 505 563
DBREF 5EUS A 637 718 UNP Q9EPH0 S26A5_RAT 637 718
SEQADV 5EUS GLY A 635 UNP Q9EPH0 LINKER
SEQADV 5EUS 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 BR A 801 1
HET EDO A 802 10
HET EDO A 803 10
HET EDO A 804 10
HET EDO A 805 10
HET PG4 A 806 31
HETNAM BR BROMIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 BR BR 1-
FORMUL 3 EDO 4(C2 H6 O2)
FORMUL 7 PG4 C8 H18 O5
FORMUL 8 HOH *69(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 GLN A 714 1 10
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 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 2 GLY A 656 GLN A 714
SITE 1 AC2 2 GLN A 513 VAL A 710
SITE 1 AC3 2 TYR A 508 LYS A 536
SITE 1 AC4 3 ASP A 518 HOH A 901 HOH A 941
SITE 1 AC5 2 THR A 688 LYS A 699
SITE 1 AC6 6 GLY A 668 TYR A 673 ALA A 697 HIS A 704
SITE 2 AC6 6 ALA A 718 HOH A 911
CRYST1 61.408 61.408 66.416 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 0.016285 0.009402 0.000000 0.00000
SCALE2 0.000000 0.018804 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015057 0.00000
(ATOM LINES ARE NOT SHOWN.)
END