HEADER PERIPLASMIC BINDING PROTEIN 10-APR-89 2LIV 2LIV 3 COMPND LEUCINE(SLASH)*ISOLEUCINE(SLASH)*VALINE-BINDING PROTEIN 2LIV 4 COMPND 2 (/LIVBP$) 2LIV 5 SOURCE (ESCHERICHIA $COLI) 2LIV 6 AUTHOR J.S.SACK,M.A.SAPER,F.A.QUIOCHO 2LIV 7 REVDAT 1 12-JUL-89 2LIV 0 2LIV 8 REMARK 1 2LIV 9 REMARK 1 REFERENCE 1 2LIV 10 REMARK 1 AUTH J.S.SACK,M.A.SAPER,F.A.QUIOCHO 2LIV 11 REMARK 1 TITL PERIPLASMIC BINDING PROTEIN STRUCTURE AND FUNCTION. 2LIV 12 REMARK 1 TITL 2 REFINED X-RAY STRUCTURES OF THE 2LIV 13 REMARK 1 TITL 3 LEUCINE(SLASH)*ISOLEUCINE(SLASH)*VALINE-BINDING 2LIV 14 REMARK 1 TITL 4 PROTEIN AND ITS COMPLEX WITH LEUCINE 2LIV 15 REMARK 1 REF J.MOL.BIOL. V. 206 171 1989 2LIV 16 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2LIV 17 REMARK 1 REFERENCE 2 2LIV 18 REMARK 1 AUTH J.S.SACK,S.D.TRAKHANOV,I.H.TSIGANNIK,F.A.QUIOCHO 2LIV 19 REMARK 1 TITL STRUCTURE OF THE L-*LEUCINE-BINDING PROTEIN REFINED 2LIV 20 REMARK 1 TITL 2 AT 2.4 ANGSTROMS RESOLUTION AND COMPARISON WITH 2LIV 21 REMARK 1 TITL 3 THE LEU(SLASH)*ILE(SLASH)*VAL-BINDING PROTEIN 2LIV 22 REMARK 1 TITL 4 STRUCTURE 2LIV 23 REMARK 1 REF J.MOL.BIOL. V. 206 193 1989 2LIV 24 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2LIV 25 REMARK 1 REFERENCE 2 2LIV 26 REMARK 1 AUTH M.A.SAPER,F.A.QUIOCHO 2LIV 27 REMARK 1 TITL LEUCINE, ISOLEUCINE, VALINE-BINDING PROTEIN FROM 2LIV 28 REMARK 1 TITL 2 ESCHERICHIA $COLI 2LIV 29 REMARK 1 REF J.BIOL.CHEM. V. 258 11057 1983 2LIV 30 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 2LIV 31 REMARK 2 2LIV 32 REMARK 2 RESOLUTION. 2.4 ANGSTROMS. 2LIV 33 REMARK 3 2LIV 34 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST SQUARES PROCEDURE OF J. 2LIV 35 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*). THE R 2LIV 36 REMARK 3 VALUE IS 0.179 FOR 11817 REFLECTIONS IN THE RESOLUTION 2LIV 37 REMARK 3 RANGE 10.0 TO 2.4 ANGSTROMS. 2LIV 38 REMARK 3 2LIV 39 REMARK 3 NUMBER OF PROTEIN ATOMS 2589 2LIV 40 REMARK 3 NUMBER OF SOLVENT ATOMS 121 2LIV 41 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 2LIV 42 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 2LIV 43 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 2LIV 44 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 2LIV 45 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 2LIV 46 REMARK 3 BOND DISTANCE 0.020(0.020) 2LIV 47 REMARK 3 ANGLE DISTANCE 0.046(0.030) 2LIV 48 REMARK 3 PLANAR 1-4 DISTANCE 0.063(0.050) 2LIV 49 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.016(0.020) 2LIV 50 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.212(0.150) 2LIV 51 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 2LIV 52 REMARK 3 SINGLE TORSION CONTACT 0.216(0.500) 2LIV 53 REMARK 3 MULTIPLE TORSION CONTACT 0.319(0.500) 2LIV 54 REMARK 3 POSSIBLE HYDROGEN BOND 0.259(0.500) 2LIV 55 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 2LIV 56 REMARK 3 PLANAR (OMEGA) 4.9(3.0) 2LIV 57 REMARK 3 CHI 24.8(15.0) 2LIV 58 REMARK 3 AROMATIC 22.8(15.0) 2LIV 59 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 2LIV 60 REMARK 3 MAIN-CHAIN BOND .764(1.000) 2LIV 61 REMARK 3 MAIN-CHAIN ANGLE 1.295(1.500) 2LIV 62 REMARK 3 SIDE-CHAIN BOND 1.347(1.500) 2LIV 63 REMARK 3 SIDE-CHAIN ANGLE 2.111(2.000) 2LIV 64 REMARK 4 2LIV 65 REMARK 4 SITE *LBS* COMPRISES THOSE RESIDUES FORMING THE LEUCINE 2LIV 66 REMARK 4 BINDING SITE. 2LIV 67 SEQRES 1 344 GLU ASP ILE LYS VAL ALA VAL VAL GLY ALA MET SER GLY 2LIV 68 SEQRES 2 344 PRO VAL ALA GLN TYR GLY ASP GLN GLU PHE THR GLY ALA 2LIV 69 SEQRES 3 344 GLU GLN ALA VAL ALA ASP ILE ASN ALA LYS GLY GLY ILE 2LIV 70 SEQRES 4 344 LYS GLY ASN LYS LEU GLN ILE ALA LYS TYR ASP ASP ALA 2LIV 71 SEQRES 5 344 CYS ASP PRO LYS GLN ALA VAL ALA VAL ALA ASN LYS VAL 2LIV 72 SEQRES 6 344 VAL ASN ASP GLY ILE LYS TYR VAL ILE GLY HIS LEU CYS 2LIV 73 SEQRES 7 344 SER SER SER THR GLN PRO ALA SER ASP ILE TYR GLU ASP 2LIV 74 SEQRES 8 344 GLU GLY ILE LEU MET ILE THR PRO ALA ALA THR ALA PRO 2LIV 75 SEQRES 9 344 GLU LEU THR ALA ARG GLY TYR GLN LEU ILE LEU ARG THR 2LIV 76 SEQRES 10 344 THR GLY LEU ASP SER ASP GLN GLY PRO THR ALA ALA LYS 2LIV 77 SEQRES 11 344 TYR ILE LEU GLU LYS VAL LYS PRO GLN ARG ILE ALA ILE 2LIV 78 SEQRES 12 344 VAL HIS ASP LYS GLN GLN TYR GLY GLU GLY LEU ALA ARG 2LIV 79 SEQRES 13 344 ALA VAL GLN ASP GLY LEU LYS LYS GLY ASN ALA ASN VAL 2LIV 80 SEQRES 14 344 VAL PHE PHE ASP GLY ILE THR ALA GLY GLU LYS ASP PHE 2LIV 81 SEQRES 15 344 SER THR LEU VAL ALA ARG LEU LYS LYS GLU ASN ILE ASP 2LIV 82 SEQRES 16 344 PHE VAL TYR TYR GLY GLY TYR HIS PRO GLU MET GLY GLN 2LIV 83 SEQRES 17 344 ILE LEU ARG GLN ALA ARG ALA ALA GLY LEU LYS THR GLN 2LIV 84 SEQRES 18 344 PHE MET GLY PRO GLU GLY VAL ALA ASN VAL SER LEU SER 2LIV 85 SEQRES 19 344 ASN ILE ALA GLY GLU SER ALA GLU GLY LEU LEU VAL THR 2LIV 86 SEQRES 20 344 LYS PRO LYS ASN TYR ASP GLN VAL PRO ALA ASN LYS PRO 2LIV 87 SEQRES 21 344 ILE VAL ASP ALA ILE LYS ALA LYS LYS GLN ASP PRO SER 2LIV 88 SEQRES 22 344 GLY ALA PHE VAL TRP THR THR TYR ALA ALA LEU GLN SER 2LIV 89 SEQRES 23 344 LEU GLN ALA GLY LEU ASN GLN SER ASP ASP PRO ALA GLU 2LIV 90 SEQRES 24 344 ILE ALA LYS TYR LEU LYS ALA ASN SER VAL ASP THR VAL 2LIV 91 SEQRES 25 344 MET GLY PRO LEU THR TRP ASP GLU LYS GLY ASP LEU LYS 2LIV 92 SEQRES 26 344 GLY PHE GLU PHE GLY VAL PHE ASP TRP HIS ALA ASN GLY 2LIV 93 SEQRES 27 344 THR ALA THR ASP ALA LYS 2LIV 94 FORMUL 2 HOH *121(H2 O1) 2LIV 95 HELIX 1 A TYR 18 GLY 37 1 2LIV 96 HELIX 2 B ASP 54 GLY 69 1 2LIV 97 HELIX 3 C ALA 85 GLY 93 1 2LIV 98 HELIX 4 D GLN 124 LYS 135 1 2LIV 99 HELIX 5 E GLN 148 LYS 164 1 2LIV 100 HELIX 6 F PHE 182 LYS 191 1 2LIV 101 HELIX 7 G TYR 202 ALA 216 1 2LIV 102 HELIX 8 H ASN 258 ALA 267 1 2LIV 103 HELIX 9 I ALA 275 SER 294 1 2LIV 104 HELIX 10 J ASP 296 ASN 307 1 2LIV 105 SHEET 1 I 7 LYS 43 ASP 51 0 2LIV 106 SHEET 2 I 7 ILE 3 GLY 9 1 N ILE 3 O LYS 43 2LIV 107 SHEET 3 I 7 LYS 71 LEU 77 1 O TYR 72 N ALA 6 2LIV 108 SHEET 4 I 7 LEU 95 ALA 101 1 N LEU 95 O LYS 71 2LIV 109 SHEET 5 I 7 LEU 113 THR 117 1 O LEU 113 N MET 96 2LIV 110 SHEET 6 I 7 GLY 322 LYS 325 1 O GLY 322 N ARG 116 2LIV 111 SHEET 7 I 7 THR 317 ASP 319 -1 O THR 317 N LYS 325 2LIV 112 SHEET 1 II 7 ASN 168 ILE 175 0 2LIV 113 SHEET 2 II 7 ARG 140 ASP 146 1 N ILE 141 O ASN 168 2LIV 114 SHEET 3 II 7 ASP 195 GLY 200 1 N PHE 196 O ARG 140 2LIV 115 SHEET 4 II 7 GLN 221 GLU 226 1 N GLN 221 O ASP 195 2LIV 116 SHEET 5 II 7 GLY 243 LYS 248 1 N LEU 245 O PHE 222 2LIV 117 SHEET 6 II 7 GLY 330 HIS 335 -1 N GLY 330 O LYS 248 2LIV 118 SHEET 7 II 7 THR 339 ALA 343 1 O THR 339 N HIS 335 2LIV 119 SSBOND 1 CYS 53 CYS 78 2LIV 120 SITE 1 LBS 3 SER 79 ALA 100 THR 102 2LIV 121 CRYST1 39.880 70.990 115.630 90.00 90.00 90.00 P 21 21 21 4 2LIV 122 ORIGX1 1.000000 0.000000 0.000000 0.00000 2LIV 123 ORIGX2 0.000000 1.000000 0.000000 0.00000 2LIV 124 ORIGX3 0.000000 0.000000 1.000000 0.00000 2LIV 125 SCALE1 0.025075 0.000000 0.000000 0.00000 2LIV 126 SCALE2 0.000000 0.014086 0.000000 0.00000 2LIV 127 SCALE3 0.000000 0.000000 0.008648 0.00000 2LIV 128