HEADER BINDING PROTEIN 03-JAN-94 1HSL 1HSL 2 COMPND HISTIDINE-BINDING PROTEIN COMPLEXED WITH L-HISTIDINE 1HSL 3 SOURCE (ESCHERICHIA COLI, STRAIN K-12) 1HSL 4 AUTHOR N.YAO,S.TRAKHANOV,F.A.QUIOCHO 1HSL 5 REVDAT 2 31-JUL-94 1HSLA 3 JRNL REMARK ATOM 1HSLA 1 REVDAT 1 31-MAY-94 1HSL 0 1HSL 6 JRNL AUTH N.YAO,S.TRAKHANOV,F.A.QUIOCHO 1HSL 7 JRNL TITL REFINED 1.89 ANGSTROMS STRUCTURE OF THE 1HSL 8 JRNL TITL 2 HISTIDINE-BINDING PROTEIN COMPLEXED WITH 1HSL 9 JRNL TITL 3 HISTIDINE AND ITS RELATIONSHIP WITH MANY OTHER 1HSLA 2 JRNL TITL 5 ACTIVE TRANSPORT(SLASH)CHEMOSENSORY RECEPTORS 1HSLA 3 JRNL REF BIOCHEMISTRY V. 33 4769 1994 1HSLA 4 JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033 1HSLA 5 REMARK 1 1HSL 15 REMARK 1 REFERENCE 1 1HSL 16 REMARK 1 AUTH C.-H.KANG,S.-H.KIM,K.NIKAIDO,S.GOKCEN,G.F.-L.AMES 1HSL 17 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF 1HSL 18 REMARK 1 TITL 2 HISJ AND LAO PERIPLASMIC PROTEINS FROM SALMONELLA 1HSL 19 REMARK 1 TITL 3 TYPHIMURIUM 1HSL 20 REMARK 1 REF J.MOL.BIOL. V. 207 643 1989 1HSL 21 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1HSL 22 REMARK 1 REFERENCE 2 1HSL 23 REMARK 1 AUTH S.D.TRAKHANOV,N.Y.CHIRGADZE,E.F.YUSIFOV 1HSL 24 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY 1HSL 25 REMARK 1 TITL 2 CRYSTALLOGRAPHIC DATA OF A HISTIDINE-BINDING 1HSL 26 REMARK 1 TITL 3 PROTEIN FROM ESCHERICHIA COLI 1HSL 27 REMARK 1 REF J.MOL.BIOL. V. 207 847 1989 1HSL 28 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1HSL 29 REMARK 2 1HSL 30 REMARK 2 RESOLUTION. 1.89 ANGSTROMS. 1HSLA 6 REMARK 3 1HSL 32 REMARK 3 REFINEMENT. 1HSL 33 REMARK 3 PROGRAM X-PLOR 1HSL 34 REMARK 3 AUTHORS BRUNGER 1HSL 35 REMARK 3 R VALUE 0.199 1HSL 36 REMARK 3 RMSD BOND DISTANCES 0.020 ANGSTROMS 1HSL 37 REMARK 3 RMSD BOND ANGLES 3.772 DEGREES 1HSL 38 REMARK 3 1HSL 39 REMARK 3 NUMBER OF REFLECTIONS 28331 1HSL 40 REMARK 3 RESOLUTION RANGE 8. - 1.89 ANGSTROMS 1HSLA 7 REMARK 3 DATA CUTOFF 2.0 SIGMA(F) 1HSLA 8 REMARK 3 PERCENT COMPLETION 70. 1HSLA 9 REMARK 3 1HSL 43 REMARK 3 NUMBER OF PROTEIN ATOMS 3686 1HSL 44 REMARK 3 NUMBER OF SOLVENT ATOMS 286 1HSL 45 REMARK 4 1HSL 46 REMARK 4 THE SEQUENCE OF THE ESCHERICHIA COLI HISTIDINE BINDING 1HSL 47 REMARK 4 PROTEIN IS NOT KNOWN, THE SEQUENCE PRESENTED IN THIS ENTRY 1HSL 48 REMARK 4 IS THAT OF THE SALMONELLA TYPHIMURIUM PROTEIN WHICH THE 1HSL 49 REMARK 4 AUTHORS BELIEVE TO BE VERY SIMILAR. SEE THE *JRNL* ARTICLE 1HSL 50 REMARK 4 FOR MORE DETAILS. 1HSL 51 REMARK 5 1HSLA 10 REMARK 5 BY REQUEST OF THE DEPOSITOR, THE PROTEIN DATA BANK HAS NOT 1HSLA 11 REMARK 5 APPLIED THE IUPAC-IUB RECOMMENDATIONS REGARDING THE 1HSLA 12 REMARK 5 DESIGNATION OF BRANCHES 1 AND 2 OF SIDE-CHAIN ATOMS IN 1HSLA 13 REMARK 5 RESIDUES ARG, ASP, GLU, LEU, PHE, TYR, AND VAL TO THIS 1HSLA 14 REMARK 5 ENTRY. 1HSLA 15 REMARK 6 1HSLA 16 REMARK 6 CORRECTION. UPDATE JRNL REFERENCE TO REFLECT PUBLICATION. 1HSLA 17 REMARK 6 CHANGE RESOLUTION FROM 1.9 TP 1.89. REVISE SIGMA AND 1HSLA 18 REMARK 6 PERCENT COMPLETION IN REMARK 3. MAKE APPROPIATE CHANGES 1HSLA 19 REMARK 6 TO ATOM RECORD SO THAT THE ATOM NAMING IS THAT USED BY 1HSLA 20 REMARK 6 THE DEPOSITOR IN THE ORIGINAL DEPOSITION. ADD REMARK 5 TO 1HSLA 21 REMARK 6 DESCRIBE THIS. 31-JUL-94. 1HSLA 22 SEQRES 1 A 238 ALA ILE PRO GLN LYS ILE ARG ILE GLY THR ASP PRO THR 1HSL 52 SEQRES 2 A 238 TYR ALA PRO PHE GLU SER LYS ASN ALA GLN GLY GLU LEU 1HSL 53 SEQRES 3 A 238 VAL GLY PHE ASP ILE ASP LEU ALA LYS GLU LEU CYS LYS 1HSL 54 SEQRES 4 A 238 ARG ILE ASN THR GLN CYS THR PHE VAL GLU ASN PRO LEU 1HSL 55 SEQRES 5 A 238 ASP ALA LEU ILE PRO SER LEU LYS ALA LYS LYS ILE ASP 1HSL 56 SEQRES 6 A 238 ALA ILE MET SER SER LEU SER ILE THR GLU LYS ARG GLN 1HSL 57 SEQRES 7 A 238 GLN GLU ILE ALA PHE THR ASP LYS LEU TYR ALA ALA ASP 1HSL 58 SEQRES 8 A 238 SER ARG LEU VAL VAL ALA LYS ASN SER ASP ILE GLN PRO 1HSL 59 SEQRES 9 A 238 THR VAL ALA SER LEU LYS GLY LYS ARG VAL GLY VAL LEU 1HSL 60 SEQRES 10 A 238 GLN GLY THR THR GLN GLU THR PHE GLY ASN GLU HIS TRP 1HSL 61 SEQRES 11 A 238 ALA PRO LYS GLY ILE GLU ILE VAL SER TYR GLN GLY GLN 1HSL 62 SEQRES 12 A 238 ASP ASN ILE TYR SER ASP LEU THR ALA GLY ARG ILE ASP 1HSL 63 SEQRES 13 A 238 ALA ALA PHE GLN ASP GLU VAL ALA ALA SER GLU GLY PHE 1HSL 64 SEQRES 14 A 238 LEU LYS GLN PRO VAL GLY LYS ASP TYR LYS PHE GLY GLY 1HSL 65 SEQRES 15 A 238 PRO ALA VAL LYS ASP GLU LYS LEU PHE GLY VAL GLY THR 1HSL 66 SEQRES 16 A 238 GLY MET GLY LEU ARG LYS GLU ASP ASN GLU LEU ARG GLU 1HSL 67 SEQRES 17 A 238 ALA LEU ASN LYS ALA PHE ALA GLU MET ARG ALA ASP GLY 1HSL 68 SEQRES 18 A 238 THR TYR GLU LYS LEU ALA LYS LYS TYR PHE ASP PHE ASP 1HSL 69 SEQRES 19 A 238 VAL TYR GLY GLY 1HSL 70 SEQRES 1 C 1 HIS 1HSL 71 SEQRES 1 B 238 ALA ILE PRO GLN LYS ILE ARG ILE GLY THR ASP PRO THR 1HSL 72 SEQRES 2 B 238 TYR ALA PRO PHE GLU SER LYS ASN ALA GLN GLY GLU LEU 1HSL 73 SEQRES 3 B 238 VAL GLY PHE ASP ILE ASP LEU ALA LYS GLU LEU CYS LYS 1HSL 74 SEQRES 4 B 238 ARG ILE ASN THR GLN CYS THR PHE VAL GLU ASN PRO LEU 1HSL 75 SEQRES 5 B 238 ASP ALA LEU ILE PRO SER LEU LYS ALA LYS LYS ILE ASP 1HSL 76 SEQRES 6 B 238 ALA ILE MET SER SER LEU SER ILE THR GLU LYS ARG GLN 1HSL 77 SEQRES 7 B 238 GLN GLU ILE ALA PHE THR ASP LYS LEU TYR ALA ALA ASP 1HSL 78 SEQRES 8 B 238 SER ARG LEU VAL VAL ALA LYS ASN SER ASP ILE GLN PRO 1HSL 79 SEQRES 9 B 238 THR VAL ALA SER LEU LYS GLY LYS ARG VAL GLY VAL LEU 1HSL 80 SEQRES 10 B 238 GLN GLY THR THR GLN GLU THR PHE GLY ASN GLU HIS TRP 1HSL 81 SEQRES 11 B 238 ALA PRO LYS GLY ILE GLU ILE VAL SER TYR GLN GLY GLN 1HSL 82 SEQRES 12 B 238 ASP ASN ILE TYR SER ASP LEU THR ALA GLY ARG ILE ASP 1HSL 83 SEQRES 13 B 238 ALA ALA PHE GLN ASP GLU VAL ALA ALA SER GLU GLY PHE 1HSL 84 SEQRES 14 B 238 LEU LYS GLN PRO VAL GLY LYS ASP TYR LYS PHE GLY GLY 1HSL 85 SEQRES 15 B 238 PRO ALA VAL LYS ASP GLU LYS LEU PHE GLY VAL GLY THR 1HSL 86 SEQRES 16 B 238 GLY MET GLY LEU ARG LYS GLU ASP ASN GLU LEU ARG GLU 1HSL 87 SEQRES 17 B 238 ALA LEU ASN LYS ALA PHE ALA GLU MET ARG ALA ASP GLY 1HSL 88 SEQRES 18 B 238 THR TYR GLU LYS LEU ALA LYS LYS TYR PHE ASP PHE ASP 1HSL 89 SEQRES 19 B 238 VAL TYR GLY GLY 1HSL 90 SEQRES 1 D 1 HIS 1HSL 91 FTNOTE 1 1HSL 92 FTNOTE 1 CIS PROLINE - PRO A 16 1HSL 93 FTNOTE 2 1HSL 94 FTNOTE 2 CIS PROLINE - PRO B 16 1HSL 95 HET CD 750 1 CADMIUM ATOM 1HSL 96 HET CD 751 1 CADMIUM ATOM 1HSL 97 HET CD 752 1 CADMIUM ATOM 1HSL 98 HET CD 753 1 CADMIUM ATOM 1HSL 99 HET CD 754 1 CADMIUM ATOM 1HSL 100 HET CD 755 1 CADMIUM ATOM 1HSL 101 HET CD 756 1 CADMIUM ATOM 1HSL 102 FORMUL 5 CD 7(CD1) 1HSL 103 FORMUL 6 HOH *286(H2 O1) 1HSL 104 SSBOND 1 CYS A 38 CYS A 45 1HSL 105 SSBOND 2 CYS B 38 CYS B 45 1HSL 106 CRYST1 39.160 102.520 64.980 90.00 93.56 90.00 P 21 4 1HSL 107 ORIGX1 1.000000 0.000000 0.000000 0.00000 1HSL 108 ORIGX2 0.000000 1.000000 0.000000 0.00000 1HSL 109 ORIGX3 0.000000 0.000000 1.000000 0.00000 1HSL 110 SCALE1 0.025536 0.000000 0.001589 0.00000 1HSL 111 SCALE2 0.000000 0.009754 0.000000 0.00000 1HSL 112 SCALE3 0.000000 0.000000 0.015419 0.00000 1HSL 113