HEADER BINDING PROTEIN 19-JUL-93 1SBP COMPND SULFATE-BINDING PROTEIN SOURCE (SALMONELLA TYPHIMURIUM) AUTHOR J.S.SACK,F.A.QUIOCHO REVDAT 1 31-OCT-93 1SBP 0 JRNL AUTH J.S.SACK,F.A.QUIOCHO JRNL TITL 1.7 ANGSTROMS REFINED STRUCTURE OF JRNL TITL 2 SULFATE-BINDING PROTEIN INVOLVED IN ACTIVE JRNL TITL 3 TRANSPORT AND NOVEL MODE OF SULFATE BINDING JRNL REF TO BE PUBLISHED JRNL REFN 353 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.L.JACOBSON,J.J.HE,P.S.VERMERSCH,D.D.LEMON, REMARK 1 AUTH 2 F.A.QUIOCHO REMARK 1 TITL ENGINEERED INTERDOMAIN DISULFIDE IN THE PERIPLASMIC REMARK 1 TITL 2 RECEPTOR FOR SULFATE TRANSPORT REDUCES FLEXIBILITY. REMARK 1 TITL 3 SITE-DIRECTED MUTAGENESIS AND LIGAND-BINDING REMARK 1 TITL 4 STUDIES REMARK 1 REF J.BIOL.CHEM. V. 266 5220 1991 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.W.PFLUGRATH,F.A.QUIOCHO REMARK 1 TITL THE 2 ANGSTROMS RESOLUTION STRUCTURE OF THE REMARK 1 TITL 2 SULFATE-BINDING PROTEIN INVOLVED IN ACTIVE REMARK 1 TITL 3 TRANSPORT IN SALMONELLA TYPHIMURIUM REMARK 1 REF J.MOL.BIOL. V. 200 163 1988 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 3 REMARK 1 AUTH B.L.JACOBSON,F.A.QUIOCHO REMARK 1 TITL SULFATE-BINDING PROTEIN DISLIKES PROTONATED REMARK 1 TITL 2 OXYACIDS. A MOLECULAR EXPLANATION REMARK 1 REF J.MOL.BIOL. V. 204 783 1988 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 4 REMARK 1 AUTH J.W.PFLUGRATH,F.A.QUIOCHO REMARK 1 TITL SULPHATE SEQUESTERED IN THE SULPHATE-BINDING REMARK 1 TITL 2 PROTEIN OF SALMONELLA TYPHIMURIUM IS BOUND SOLELY REMARK 1 TITL 3 BY HYDROGEN BONDS REMARK 1 REF NATURE V. 314 257 1985 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 REMARK 1 REFERENCE 5 REMARK 1 AUTH H.ISIHARA,R.W.HOGG REMARK 1 TITL AMINO ACID SEQUENCE OF THE SULFATE-BINDING REMARK 1 TITL 2 PROTEIN FROM SALMONELLA TYPHIMURIUM LT2 REMARK 1 REF J.BIOL.CHEM. V. 255 4614 1980 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.7 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM PROLSQ REMARK 3 AUTHORS KONNERT,HENDRICKSON REMARK 3 R VALUE 0.178 REMARK 3 RMSD BOND DISTANCES 0.019 ANGSTROMS REMARK 3 RMSD BOND ANGLE DISTANCES 0.035 ANGSTROMS REMARK 3 REMARK 3 NUMBER OF SOLVENT ATOMS 138 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) REMARK 3 BOND DISTANCE 0.019(0.020) REMARK 3 ANGLE DISTANCE 0.035(0.030) REMARK 3 PLANAR 1-4 DISTANCE 0.048(0.050) REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.017(0.020) REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.216(0.150) REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) REMARK 3 SINGLE TORSION CONTACT 0.177(0.500) REMARK 3 MULTIPLE TORSION CONTACT 0.188(0.500) REMARK 3 POSSIBLE HYDROGEN BOND 0.177(0.500) REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) REMARK 3 PLANAR 3.200(3.000) REMARK 3 STAGGERED 18.30(15.00) REMARK 3 ORTHONORMAL 21.10(20.00) REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) REMARK 3 MAIN-CHAIN BOND 1.040(1.000) REMARK 3 MAIN-CHAIN ANGLE 1.589(1.500) REMARK 3 SIDE-CHAIN BOND 1.467(1.000) REMARK 3 SIDE-CHAIN ANGLE 2.379(1.500) REMARK 4 REMARK 4 THE SEQUENCE IS BASED ON THAT GIVEN IN THE JRNL REFERENCE REMARK 4 AND IN REFERENCE 1. REMARK 5 REMARK 5 THE SIDE-CHAIN OF RESIDUE LYS 309 CAN NOT BE SEEN IN THE REMARK 5 ELECTRON DENSITY AND IS NOT INCLUDED IN THE COORDINATES. SEQRES 1 310 LYS ASP ILE GLN LEU LEU ASN VAL SER TYR ASP PRO THR SEQRES 2 310 ARG GLU LEU TYR GLU GLN TYR ASN LYS ALA PHE SER ALA SEQRES 3 310 HIS TRP LYS GLN GLU THR GLY ASP ASN VAL VAL ILE ASP SEQRES 4 310 GLN SER HIS GLY GLY SER GLY LYS GLN ALA THR SER VAL SEQRES 5 310 ILE ASN GLY ILE GLU ALA ASP THR VAL THR LEU ALA LEU SEQRES 6 310 ALA TYR ASP VAL ASN ALA ILE ALA GLU ARG GLY ARG ILE SEQRES 7 310 ASP LYS ASN TRP ILE LYS ARG LEU PRO ASP ASP SER ALA SEQRES 8 310 PRO TYR THR SER THR ILE VAL PHE LEU VAL ARG LYS GLY SEQRES 9 310 ASN PRO LYS GLN ILE HIS ASP TRP ASN ASP LEU ILE LYS SEQRES 10 310 PRO GLY VAL SER VAL ILE THR PRO ASN PRO LYS SER SER SEQRES 11 310 GLY GLY ALA ARG TRP ASN TYR LEU ALA ALA TRP GLY TYR SEQRES 12 310 ALA LEU HIS HIS ASN ASN ASN ASP GLN ALA LYS ALA GLU SEQRES 13 310 ASP PHE VAL LYS ALA LEU PHE LYS ASN VAL GLU VAL LEU SEQRES 14 310 ASP SER GLY ALA ARG GLY SER THR ASN THR PHE VAL GLU SEQRES 15 310 ARG GLY ILE GLY ASP VAL LEU ILE ALA TRP GLU ASN GLU SEQRES 16 310 ALA LEU LEU ALA THR ASN GLU LEU GLY LYS ASP LYS PHE SEQRES 17 310 GLU ILE VAL THR PRO SER GLU SER ILE LEU ALA GLU PRO SEQRES 18 310 THR VAL SER VAL VAL ASP LYS VAL VAL GLU LYS LYS ASP SEQRES 19 310 THR LYS ALA VAL ALA GLU ALA TYR LEU LYS TYR LEU TYR SEQRES 20 310 SER PRO GLU GLY GLN GLU ILE ALA ALA LYS ASN PHE TYR SEQRES 21 310 ARG PRO ARG ASP ALA ASP VAL ALA LYS LYS TYR ASP ASP SEQRES 22 310 ALA PHE PRO LYS LEU LYS LEU PHE THR ILE ASP GLU VAL SEQRES 23 310 PHE GLY GLY TRP ALA LYS ALA GLN LYS ASP HIS PHE ALA SEQRES 24 310 ASP GLY GLY THR PHE ASP GLN ILE SER LYS ARG HET SO4 310 5 SULFATE FORMUL 2 SO4 O4 S1 FORMUL 3 HOH *138(H2 O1) HELIX 1 1 ARG 14 GLY 33 1 N-DOMAIN HELIX 2 2 GLY 44 ASN 54 1 N-DOMAIN HELIX 3 3 ALA 66 GLU 74 1 N-DOMAIN HELIX 4 4 GLY 131 HIS 147 1 C-DOMAIN HELIX 5 5 GLN 152 LYS 164 1 C-DOMAIN HELIX 6 6 ALA 173 GLU 182 1 C-DOMAIN HELIX 7 7 GLU 193 THR 200 1 C-DOMAIN HELIX 8 8 ASP 227 ASP 234 1 N-DOMAIN HELIX 9 9 LYS 236 TYR 245 1 N-DOMAIN HELIX 10 10 PRO 249 ASN 258 1 N-DOMAIN HELIX 11 11 ALA 265 TYR 271 1 N-DOMAIN HELIX 12 12 TRP 290 PHE 298 1 C-DOMAIN SHEET 1 S1 4 ASN 35 SER 41 0 SHEET 2 S1 4 LYS 1 SER 9 1 O LYS 1 N ASN 35 SHEET 3 S1 4 ASP 59 LEU 63 1 N THR 60 O LEU 6 SHEET 4 S1 4 THR 222 VAL 226 -1 N THR 222 O LEU 63 SHEET 1 S2 5 ASN 165 GLU 167 0 SHEET 2 S2 5 SER 121 ILE 123 1 N VAL 122 O ASN 165 SHEET 3 S2 5 VAL 188 GLU 193 1 O VAL 188 N SER 121 SHEET 4 S2 5 THR 96 LYS 103 -1 O THR 96 N GLU 193 SHEET 5 S2 5 LYS 207 VAL 211 -1 O LYS 207 N LYS 103 SHEET 1 S3 2 SER 216 LEU 218 0 SHEET 2 S3 2 LYS 279 PHE 281 1 O LYS 279 N SER 216 CRYST1 40.770 49.370 141.030 90.00 90.00 90.00 P 21 21 21 4 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 0.024528 0.000000 0.000000 0.00000 SCALE2 0.000000 0.020255 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007091 0.00000