HEADER CALCIUM-BINDING PROTEIN 29-SEP-92 1CLL 1CLL 2 COMPND CALMODULIN (VERTEBRATE) 1CLL 3 SOURCE HUMAN (HOMO SAPIENS) RECOMBINANT FORM 1CLL 4 AUTHOR R.CHATTOPADHYAYA,F.A.QUIOCHO 1CLL 5 REVDAT 1 31-OCT-93 1CLL 0 1CLL 6 JRNL AUTH R.CHATTOPADHYAYA,W.E.MEADOR,A.R.MEANS,F.A.QUIOCHO 1CLL 7 JRNL TITL CALMODULIN STRUCTURE REFINED AT 1.7 ANGSTROMS 1CLL 8 JRNL TITL 2 RESOLUTION 1CLL 9 JRNL REF J.MOL.BIOL. V. 228 1177 1992 1CLL 10 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1CLL 11 REMARK 1 1CLL 12 REMARK 1 REFERENCE 1 1CLL 13 REMARK 1 AUTH W.E.MEADOR,A.R.MEANS,F.A.QUIOCHO 1CLL 14 REMARK 1 TITL TARGET ENZYME RECOGNITION BY CALMODULIN: 2.4 1CLL 15 REMARK 1 TITL 2 ANGSTROMS STRUCTURE OF A CALMODULIN-PEPTIDE 1CLL 16 REMARK 1 TITL 3 COMPLEX 1CLL 17 REMARK 1 REF SCIENCE V. 257 1251 1992 1CLL 18 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 038 1CLL 19 REMARK 1 REFERENCE 2 1CLL 20 REMARK 1 AUTH Y.S.BABU,C.E.BUGG,W.J.COOK 1CLL 21 REMARK 1 TITL STRUCTURE OF CALMODULIN REFINED AT 2.2 ANGSTROMS 1CLL 22 REMARK 1 TITL 2 RESOLUTION 1CLL 23 REMARK 1 REF J.MOL.BIOL. V. 204 191 1988 1CLL 24 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1CLL 25 REMARK 2 1CLL 26 REMARK 2 RESOLUTION. 1.7 ANGSTROMS. 1CLL 27 REMARK 3 1CLL 28 REMARK 3 REFINEMENT. 1CLL 29 REMARK 3 PROGRAM PROLSQ 1CLL 30 REMARK 3 AUTHORS KONNERT,HENDRICKSON 1CLL 31 REMARK 3 R VALUE 0.216 1CLL 32 REMARK 3 1CLL 33 REMARK 3 NUMBER OF REFLECTIONS 14469 1CLL 34 REMARK 3 RESOLUTION RANGE 10.0 - 1.7 ANGSTROMS 1CLL 35 REMARK 3 DATA CUTOFF 0.5 SIGMA(F) 1CLL 36 REMARK 3 1CLL 37 REMARK 3 NUMBER OF PROTEIN ATOMS 126 1CLL 38 REMARK 3 NUMBER OF SOLVENT ATOMS 125 1CLL 39 REMARK 3 1CLL 40 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 1CLL 41 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 1CLL 42 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 1CLL 43 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 1CLL 44 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 1CLL 45 REMARK 3 BOND DISTANCE 0.009(0.020) 1CLL 46 REMARK 3 ANGLE DISTANCE 0.032(0.040) 1CLL 47 REMARK 3 PLANAR 1-4 DISTANCE 0.040(0.060) 1CLL 48 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.007(0.020) 1CLL 49 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.152(0.150) 1CLL 50 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 1CLL 51 REMARK 3 SINGLE TORSION CONTACT 0.199(0.500) 1CLL 52 REMARK 3 MULTIPLE TORSION CONTACT 0.304(0.500) 1CLL 53 REMARK 3 POSSIBLE HYDROGEN BOND 0.281(0.500) 1CLL 54 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 1CLL 55 REMARK 3 PLANAR 1.6(3.0) 1CLL 56 REMARK 3 STAGGERED 21.4(15.0) 1CLL 57 REMARK 3 ORTHONORMAL 26.6(20.0) 1CLL 58 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 1CLL 59 REMARK 3 MAIN-CHAIN BOND 2.0(4.0) 1CLL 60 REMARK 3 MAIN-CHAIN ANGLE 2.5(5.0) 1CLL 61 REMARK 3 SIDE-CHAIN BOND 3.0(5.0) 1CLL 62 REMARK 3 SIDE-CHAIN ANGLE 4.2(6.0) 1CLL 63 REMARK 3 1CLL 64 REMARK 3 THE 2.2A MODEL OF BABU ET AL.(1988) WAS USED. ALTHOUGH THE 1CLL 65 REMARK 3 CELL CONSTANTS ARE ALMOST IDENTICAL BETWEEN THE TWO STUDIES 1CLL 66 REMARK 3 AND THE SPACE GROUP ALSO IS THE SAME, A SMALL ROTATION OF 1CLL 67 REMARK 3 LESS THAN 5 DEGREES WAS NEEDED TO APPROPRIATELY ORIENT THE 1CLL 68 REMARK 3 MODEL IN THE PRESENT UNIT CELL. THE ANGLE WAS FOUND FROM 1CLL 69 REMARK 3 THE CROWTHER ROTATION FUNCTION AS IMPLEMENTED IN MERLOT. 1CLL 70 REMARK 3 RIGID REFINEMENT WITHIN MERLOT REDUCED THE R VALUE TO 0.329 1CLL 71 REMARK 3 USING ALL DATA TO 2.5A, WITH AN OVERALL TEMPERATURE FACTOR 1CLL 72 REMARK 3 OF 25A**2. THEREAFTER, PROLSQ WAS USED FOR FURTHER 1CLL 73 REMARK 3 REFINEMENT. A TOTAL OF 14,469 REFLECTIONS WITH 1CLL 74 REMARK 3 F>0.5SIGMA(F) WAS USED OUT OF 15,417 UNIQUE MEASURED 1CLL 75 REMARK 3 REFLECTIONS. THE R VALUE FOR ALL REFLECTIONS IS 0.225. 1CLL 76 REMARK 4 1CLL 77 REMARK 4 THE CALMODULIN STRUCTURE IN THIS STUDY IS VERY SIMILAR TO 1CLL 78 REMARK 4 THE EARLIER STRUCTURE OF BABU ET AL., WITH A RMS DEVIATION 1CLL 79 REMARK 4 OF 0.36 ANGSTROMS. CALMODULIN REMAINS A DUMBBELL SHAPED 1CLL 80 REMARK 4 MOLECULE, WITH SIMILAR LOBES AND CONNECTED BY A CENTRAL 1CLL 81 REMARK 4 ALPHA HELIX. EACH LOBE CONTAINS THREE ALPHA HELICES, TWO 1CLL 82 REMARK 4 CALCIUM ION BINDING EF HAND LOOPS, WITH A SHORT 1CLL 83 REMARK 4 ANTI-PARALLEL BETA SHEET BETWEEN ADJACENT EF HAND LOOPS 1CLL 84 REMARK 4 AND ONE NON-EF HAND LOOP. THE LARGEST DIFFERENCES BETWEEN 1CLL 85 REMARK 4 THE TWO CALMODULIN STRUCTURES WERE IN THE CENTRAL HELIX, 1CLL 86 REMARK 4 WITH THE PRESENT STUDY INDICATING A MORE IDEAL ALPHA HELIX 1CLL 87 REMARK 4 CONNECTING THE TWO LOBES COMPARED TO WHAT BABU ET AL. 1CLL 88 REMARK 4 (1988) HAD FOUND. ASP 118 IS FOUND TO BE IN DOUBLE 1CLL 89 REMARK 4 CONFORMATION. ELECTRON DENSITIES FOR RESIDUES 1 - 4 AND 1CLL 90 REMARK 4 148, AT THE TWO TERMINI OF THE MOLECULE, ARE POOR AND NOT 1CLL 91 REMARK 4 INCLUDED IN THE MODEL EXCEPT FOR MAIN CHAIN ATOMS OF 1CLL 92 REMARK 4 RESIDUE 4. 1CLL 93 REMARK 5 1CLL 94 REMARK 5 CRYSTAL PACKING IS EXTENSIVELY STUDIED IN THE 1CLL 95 REMARK 5 CHATTOPADHYAYA ET AL. PAPER ON CALMODULIN, AND FACILE 1CLL 96 REMARK 5 CRYSTAL GROWTH ALONG THE Z-DIRECTION EXPLAINED. THE 1CLL 97 REMARK 5 AUTHORS ALSO HAVE REPORTED IN DETAIL ABOUT THE HYDROGEN 1CLL 98 REMARK 5 BONDING WITHIN VARIOUS STRUCTURAL ELEMENTS IN THAT 1CLL 99 REMARK 5 PUBLICATION. HYDRATION IS ALSO DESCRIBED. THESE ARE AREAS 1CLL 100 REMARK 5 WHICH WERE NOT DEALT WITH IN THE BABU ET AL. (1988) 1CLL 101 REMARK 5 PUBLICATION. 1CLL 102 REMARK 6 1CLL 103 REMARK 6 THE MEAN AND STANDARD DEVIATION OF PHI IS -62.6, 8.2. THE 1CLL 104 REMARK 6 MEAN AND STANDARD DEVIATION OF PSI IS -42.0, 10.1. 1CLL 105 REMARK 7 1CLL 106 REMARK 7 THE ANTI-PARALLEL BETA SHEETS ARE EXTREMELY SHORT IN THIS 1CLL 107 REMARK 7 STRUCTURE. THERE IS ADDITIONAL CONNECTIVITY VIA WATERS 1CLL 108 REMARK 7 BETWEEN THE TWO STRANDS OF EACH SHEET. 1CLL 109 SEQRES 1 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS 1CLL 110 SEQRES 2 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR 1CLL 111 SEQRES 3 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU 1CLL 112 SEQRES 4 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE 1CLL 113 SEQRES 5 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE 1CLL 114 SEQRES 6 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP 1CLL 115 SEQRES 7 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL 1CLL 116 SEQRES 8 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU 1CLL 117 SEQRES 9 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR 1CLL 118 SEQRES 10 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE 1CLL 119 SEQRES 11 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN 1CLL 120 SEQRES 12 148 MET MET THR ALA LYS 1CLL 121 HET CA 148 1 CALCIUM +2 COUNTER ION 1CLL 122 HET CA 149 1 CALCIUM +2 COUNTER ION 1CLL 123 HET CA 150 1 CALCIUM +2 COUNTER ION 1CLL 124 HET CA 151 1 CALCIUM +2 COUNTER ION 1CLL 125 HET EOH 1 3 ETHANOL 1CLL 126 FORMUL 2 CA 4(CA1) 1CLL 127 FORMUL 3 EOH C2 H6 O1 1CLL 128 FORMUL 4 HOH *139(H2 O1) 1CLL 129 HELIX 1 I THR 5 PHE 19 1 1CLL 130 HELIX 2 II THR 29 ARG 37 1 1CLL 131 HELIX 3 III GLU 45 VAL 55 1 1CLL 132 HELIX 4 IV PHE 65 PHE 92 1 SEE REMARK 6 1CLL 133 HELIX 5 V ALA 102 ASN 111 1 1CLL 134 HELIX 6 VI ASP 118 ALA 128 1 1CLL 135 HELIX 7 VII TYR 138 THR 146 1 1CLL 136 SHEET 1 S1 2 ILE 27 THR 29 0 1CLL 137 SHEET 2 S1 2 ILE 63 PHE 65 -1 N ILE 63 O ILE 27 1CLL 138 SHEET 1 S2 2 ILE 100 ALA 102 0 1CLL 139 SHEET 2 S2 2 VAL 136 TYR 138 -1 N VAL 136 O ILE 100 1CLL 140 CRYST1 30.170 53.600 25.140 93.62 97.30 89.17 P 1 1 1CLL 141 ORIGX1 0.033146 -0.000480 0.004224 0.00000 1CLL 142 ORIGX2 0.000000 0.018659 0.001155 0.00000 1CLL 143 ORIGX3 0.000000 0.000000 0.040179 0.00000 1CLL 144 SCALE1 0.033146 -0.000480 0.004224 0.00000 1CLL 145 SCALE2 0.000000 0.018659 0.001155 0.00000 1CLL 146 SCALE3 0.000000 0.000000 0.040179 0.00000 1CLL 147 (ATOM LINES ARE NOT SHOWN.) END