USER MOD reduce.3.24.130724 H: found=0, std=0, add=0, rem=0, adj=0 USER MOD reduce.3.24.130724 removed 0 hydrogens (0 hets) HEADER MEMBRANE PROTEIN 03-AUG-01 1JQ1 TITLE POTASSIUM CHANNEL (KCSA) OPEN GATE MODEL COMPND MOL_ID: 1; COMPND 2 MOLECULE: VOLTAGE-GATED POTASSIUM CHANNEL; COMPND 3 CHAIN: A, B, C, D; COMPND 4 FRAGMENT: INNER TRANSMEMBRANE SEGMENT (RESIDUES 86-119); COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS; SOURCE 3 ORGANISM_TAXID: 1916; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: XL-2 BLUE; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE32 KEYWDS POTASSIUM CHANNEL, INTEGRAL MEMBRANE PROTEIN, OPEN STATE EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE; CA ATOMS ONLY, CHAIN A, B, C, D AUTHOR Y.-S.LIU,P.SOMPORNPISUT,E.PEROZO REVDAT 3 24-FEB-09 1JQ1 1 VERSN REVDAT 2 01-APR-03 1JQ1 1 JRNL REVDAT 1 03-OCT-01 1JQ1 0 JRNL AUTH Y.S.LIU,P.SOMPORNPISUT,E.PEROZO JRNL TITL STRUCTURE OF THE KCSA CHANNEL INTRACELLULAR GATE JRNL TITL 2 IN THE OPEN STATE. JRNL REF NAT.STRUCT.BIOL. V. 8 883 2001 JRNL REFN ISSN 1072-8368 JRNL PMID 11573095 JRNL DOI 10.1038/NSB1001-883 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH P.SOMPORNPISUT,Y.-S.LIU,E.PEROZO REMARK 1 TITL CALCULATION OF RIGID BODY CONFORMATIONAL CHANGES REMARK 1 TITL 2 USING RESTRAINT-DRIVEN CARTESIAN TRANSFORMATIONS REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH E.PEROZO,D.M.CORTES,L.G.CUELLO REMARK 1 TITL STRUCTURAL REARRANGEMENTS UNDERLYING K+-CHANNEL REMARK 1 TITL 2 ACTIVATION GATING REMARK 1 REF SCIENCE V. 285 73 1999 REMARK 1 REFN ISSN 0036-8075 REMARK 1 DOI 10.1126/SCIENCE.285.5424.73 REMARK 1 REFERENCE 3 REMARK 1 AUTH D.A.DOYLE,J.MORAIS CABRAL,R.A.PFUETZNER,A.KUO, REMARK 1 AUTH 2 J.M.GULBIS,S.L.COHEN,B.T.CHAIT,R.MACKINNON REMARK 1 TITL THE STRUCTURE OF THE POTASSIUM CHANNEL: MOLECULAR REMARK 1 TITL 2 BASIS OF K+ CONDUCTION AND SELECTIVITY REMARK 1 REF SCIENCE V. 280 69 1998 REMARK 1 REFN ISSN 0036-8075 REMARK 1 DOI 10.1126/SCIENCE.280.5360.69 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER 6.0 REMARK 3 AUTHORS : D.A.CASE ET.AL. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE ARE BASED ON: 1) TEN REMARK 3 PAIRS OF INTER-SUBUNIT DISTANCES FOR THE KCSA INNER HELICAL REMARK 3 BUNDLE IN THE CLOSED AND THE OPEN STATES AND 2) THE USE OF THE REMARK 3 CRYSTAL STRUCTURE AS THE CHANNEL IN THE CLOSED STATE, AND AS REMARK 3 THE REFERENCE STRUCTURE. THE COMPUTER PROGRAM REDCAT SEARCHES REMARK 3 (RESTRAINT-DRIVEN CARTESIAN TRANSFORMATION) BASED ON THE REMARK 3 EXHAUSTIVE SAMPLING OF RIGID-BODY MOVEMENT IN CARTESIAN SPACE REMARK 3 FOR THE TM2 INNER BUNDLE IN THE OPEN STATE WERE ALLOWED TO REMARK 3 CONVERGE TO A MINIMAL PENALTY VALUE. THE ENSEMBLE OF THE 50 REMARK 3 LOWEST PENALTY CONFORMERS WAS SUBJECTED TO MOLECULAR MECHANIC REMARK 3 ENERGY MINIMIZATION. FINAL REFINEMENT WAS PERFORMED ON THE REMARK 3 AVERAGE OPEN HELICAL BUNDLE BY ENERGY MINIMIZATION. REMARK 4 REMARK 4 1JQ1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 99 REMARK 99 THE STRUCTURE CONTAINS ONLY ALPHA-CARBONS BECAUSE REMARK 99 THE EXPERIMENTAL DATA USED TO CALCULATE THE STRUCTURES REMARK 99 ARE GOOD ENOUGH ONLY TO THE BACKBONE LEVEL. REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-01. REMARK 100 THE RCSB ID CODE IS RCSB014053. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 150.0; 150.0 REMARK 210 PH : 7.0; 4.0 REMARK 210 IONIC STRENGTH : 20 MM CITRATE PHOSPHATE; 20 REMARK 210 MM CITRATE PHOSPHATE REMARK 210 PRESSURE : 1 ATM; 1 ATM REMARK 210 SAMPLE CONTENTS : 1.0 MG/ML MIXED WITH REMARK 210 METHANETHIOSULFONATE SPIN LABEL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : CONTINUOUS WAVE EPR REMARK 210 SPECTROMETER FIELD STRENGTH : 3400 MHZ REMARK 210 SPECTROMETER MODEL : EMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : EPR AQUISIT 2.32, REDCAT REMARK 210 METHOD USED : FOURIER DECONVOLUTION, REMARK 210 CONFORMATIONAL GRID SEARCH A REMARK 210 CARTESAIN REPRESENTATION REMARK 210 MOLECULAR MECHANIC ENERGY REMARK 210 MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NULL REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1JQ2 RELATED DB: PDB REMARK 900 1JQ2 CONTAINS THE ENSEMBLE DBREF 1JQ1 A 86 119 UNP P0A334 KCSA_STRLI 86 119 DBREF 1JQ1 B 86 119 UNP P0A334 KCSA_STRLI 86 119 DBREF 1JQ1 C 86 119 UNP P0A334 KCSA_STRLI 86 119 DBREF 1JQ1 D 86 119 UNP P0A334 KCSA_STRLI 86 119 SEQADV 1JQ1 CYS A 90 UNP P0A334 LEU 90 ENGINEERED SEQADV 1JQ1 CYS B 90 UNP P0A334 LEU 90 ENGINEERED SEQADV 1JQ1 CYS C 90 UNP P0A334 LEU 90 ENGINEERED SEQADV 1JQ1 CYS D 90 UNP P0A334 LEU 90 ENGINEERED SEQRES 1 A 34 LEU TRP GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA SEQRES 2 A 34 GLY ILE THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA SEQRES 3 A 34 THR TRP PHE VAL GLY ARG GLU GLN SEQRES 1 B 34 LEU TRP GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA SEQRES 2 B 34 GLY ILE THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA SEQRES 3 B 34 THR TRP PHE VAL GLY ARG GLU GLN SEQRES 1 C 34 LEU TRP GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA SEQRES 2 C 34 GLY ILE THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA SEQRES 3 C 34 THR TRP PHE VAL GLY ARG GLU GLN SEQRES 1 D 34 LEU TRP GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA SEQRES 2 D 34 GLY ILE THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA SEQRES 3 D 34 THR TRP PHE VAL GLY ARG GLU GLN CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 ATOM 1 CA LEU A 86 -21.540 0.672 -19.368 1.00 0.00 C ATOM 2 CA TRP A 87 -21.488 0.068 -15.552 1.00 0.00 C ATOM 3 CA GLY A 88 -20.164 -3.580 -15.532 1.00 0.00 C ATOM 4 CA ARG A 89 -16.600 -2.188 -16.120 1.00 0.00 C ATOM 5 CA CYS A 90 -17.128 0.260 -13.196 1.00 0.00 C ATOM 6 CA VAL A 91 -18.056 -2.760 -10.972 1.00 0.00 C ATOM 7 CA ALA A 92 -14.888 -4.464 -12.344 1.00 0.00 C ATOM 8 CA VAL A 93 -12.748 -1.408 -11.280 1.00 0.00 C ATOM 9 CA VAL A 94 -14.460 -1.456 -7.800 1.00 0.00 C ATOM 10 CA VAL A 95 -13.752 -5.200 -7.164 1.00 0.00 C ATOM 11 CA MET A 96 -10.196 -4.760 -8.620 1.00 0.00 C ATOM 12 CA VAL A 97 -9.304 -1.884 -6.208 1.00 0.00 C ATOM 13 CA ALA A 98 -11.108 -3.732 -3.344 1.00 0.00 C ATOM 14 CA GLY A 99 -9.012 -6.880 -4.140 1.00 0.00 C ATOM 15 CA ILE A 100 -5.716 -4.876 -4.256 1.00 0.00 C ATOM 16 CA THR A 101 -6.896 -3.224 -0.972 1.00 0.00 C ATOM 17 CA SER A 102 -7.796 -6.604 0.680 1.00 0.00 C ATOM 18 CA PHE A 103 -4.400 -8.228 -0.020 1.00 0.00 C ATOM 19 CA GLY A 104 -2.632 -4.904 0.908 1.00 0.00 C ATOM 20 CA LEU A 105 -4.676 -5.152 4.180 1.00 0.00 C ATOM 21 CA VAL A 106 -3.564 -8.752 5.076 1.00 0.00 C ATOM 22 CA THR A 107 -0.080 -7.420 4.140 1.00 0.00 C ATOM 23 CA ALA A 108 -0.060 -4.232 6.344 1.00 0.00 C ATOM 24 CA ALA A 109 -0.204 -5.876 9.832 1.00 0.00 C ATOM 25 CA LEU A 110 2.616 -8.484 9.444 1.00 0.00 C ATOM 26 CA ALA A 111 5.452 -5.832 9.488 1.00 0.00 C ATOM 27 CA THR A 112 4.160 -3.840 12.504 1.00 0.00 C ATOM 28 CA TRP A 113 4.056 -7.368 14.044 1.00 0.00 C ATOM 29 CA PHE A 114 7.708 -7.972 12.840 1.00 0.00 C ATOM 30 CA VAL A 115 8.844 -4.492 14.156 1.00 0.00 C ATOM 31 CA GLY A 116 7.536 -5.956 17.472 1.00 0.00 C ATOM 32 CA ARG A 117 11.132 -7.480 17.424 1.00 0.00 C ATOM 33 CA GLU A 118 12.964 -4.196 18.076 1.00 0.00 C ATOM 34 CA GLN A 119 12.984 -6.252 21.392 1.00 0.00 C TER 35 GLN A 119 ATOM 36 CA LEU B 86 -0.628 -21.592 -19.096 1.00 0.00 C ATOM 37 CA TRP B 87 -0.028 -21.508 -15.280 1.00 0.00 C ATOM 38 CA GLY B 88 3.620 -20.180 -15.272 1.00 0.00 C ATOM 39 CA ARG B 89 2.220 -16.624 -15.896 1.00 0.00 C ATOM 40 CA CYS B 90 -0.228 -17.128 -12.964 1.00 0.00 C ATOM 41 CA VAL B 91 2.796 -18.028 -10.732 1.00 0.00 C ATOM 42 CA ALA B 92 4.492 -14.868 -12.140 1.00 0.00 C ATOM 43 CA VAL B 93 1.436 -12.720 -11.092 1.00 0.00 C ATOM 44 CA VAL B 94 1.492 -14.396 -7.600 1.00 0.00 C ATOM 45 CA VAL B 95 5.240 -13.680 -6.980 1.00 0.00 C ATOM 46 CA MET B 96 4.788 -10.136 -8.460 1.00 0.00 C ATOM 47 CA VAL B 97 1.924 -9.228 -6.040 1.00 0.00 C ATOM 48 CA ALA B 98 3.792 -11.016 -3.176 1.00 0.00 C ATOM 49 CA GLY B 99 6.928 -8.904 -3.996 1.00 0.00 C ATOM 50 CA ILE B 100 4.888 -5.628 -4.080 1.00 0.00 C ATOM 51 CA THR B 101 3.280 -6.816 -0.776 1.00 0.00 C ATOM 52 CA SER B 102 6.688 -7.680 0.824 1.00 0.00 C ATOM 53 CA PHE B 103 8.264 -4.272 0.084 1.00 0.00 C ATOM 54 CA GLY B 104 4.932 -2.524 1.032 1.00 0.00 C ATOM 55 CA LEU B 105 5.236 -4.504 4.340 1.00 0.00 C ATOM 56 CA VAL B 106 8.872 -3.420 5.140 1.00 0.00 C ATOM 57 CA THR B 107 7.516 0.048 4.216 1.00 0.00 C ATOM 58 CA ALA B 108 4.308 0.160 6.388 1.00 0.00 C ATOM 59 CA ALA B 109 5.852 0.052 9.924 1.00 0.00 C ATOM 60 CA LEU B 110 8.404 2.916 9.500 1.00 0.00 C ATOM 61 CA ALA B 111 5.732 5.732 9.548 1.00 0.00 C ATOM 62 CA THR B 112 3.780 4.404 12.568 1.00 0.00 C ATOM 63 CA TRP B 113 7.312 4.352 14.100 1.00 0.00 C ATOM 64 CA PHE B 114 7.888 8.000 12.860 1.00 0.00 C ATOM 65 CA VAL B 115 4.396 9.128 14.140 1.00 0.00 C ATOM 66 CA GLY B 116 5.856 7.848 17.472 1.00 0.00 C ATOM 67 CA ARG B 117 7.392 11.432 17.400 1.00 0.00 C ATOM 68 CA GLU B 118 4.104 13.256 18.052 1.00 0.00 C ATOM 69 CA GLN B 119 6.176 13.356 21.360 1.00 0.00 C TER 70 GLN B 119 ATOM 71 CA LEU C 86 21.608 -0.668 -18.976 1.00 0.00 C ATOM 72 CA TRP C 87 21.508 -0.060 -15.164 1.00 0.00 C ATOM 73 CA GLY C 88 20.200 3.592 -15.164 1.00 0.00 C ATOM 74 CA ARG C 89 16.640 2.216 -15.796 1.00 0.00 C ATOM 75 CA CYS C 90 17.116 -0.228 -12.856 1.00 0.00 C ATOM 76 CA VAL C 91 18.028 2.792 -10.628 1.00 0.00 C ATOM 77 CA ALA C 92 14.888 4.508 -12.048 1.00 0.00 C ATOM 78 CA VAL C 93 12.720 1.464 -11.004 1.00 0.00 C ATOM 79 CA VAL C 94 14.376 1.516 -7.500 1.00 0.00 C ATOM 80 CA VAL C 95 13.684 5.268 -6.884 1.00 0.00 C ATOM 81 CA MET C 96 10.148 4.840 -8.392 1.00 0.00 C ATOM 82 CA VAL C 97 9.200 1.972 -5.992 1.00 0.00 C ATOM 83 CA ALA C 98 10.944 3.840 -3.100 1.00 0.00 C ATOM 84 CA GLY C 99 8.892 7.004 -3.944 1.00 0.00 C ATOM 85 CA ILE C 100 5.600 5.000 -4.120 1.00 0.00 C ATOM 86 CA THR C 101 6.692 3.340 -0.808 1.00 0.00 C ATOM 87 CA SER C 102 7.472 6.744 0.844 1.00 0.00 C ATOM 88 CA PHE C 103 4.116 8.364 -0.052 1.00 0.00 C ATOM 89 CA GLY C 104 2.336 5.080 0.984 1.00 0.00 C ATOM 90 CA LEU C 105 4.348 5.300 4.284 1.00 0.00 C ATOM 91 CA VAL C 106 3.380 8.936 5.240 1.00 0.00 C ATOM 92 CA THR C 107 -0.140 7.708 4.316 1.00 0.00 C ATOM 93 CA ALA C 108 -0.292 4.468 6.436 1.00 0.00 C ATOM 94 CA ALA C 109 -0.120 6.032 9.956 1.00 0.00 C ATOM 95 CA LEU C 110 -2.936 8.632 9.492 1.00 0.00 C ATOM 96 CA ALA C 111 -5.752 5.968 9.448 1.00 0.00 C ATOM 97 CA THR C 112 -4.492 4.016 12.504 1.00 0.00 C ATOM 98 CA TRP C 113 -4.408 7.536 14.064 1.00 0.00 C ATOM 99 CA PHE C 114 -8.040 8.144 12.808 1.00 0.00 C ATOM 100 CA VAL C 115 -9.184 4.656 14.092 1.00 0.00 C ATOM 101 CA GLY C 116 -7.896 6.116 17.424 1.00 0.00 C ATOM 102 CA ARG C 117 -11.472 7.672 17.344 1.00 0.00 C ATOM 103 CA GLU C 118 -13.320 4.396 17.984 1.00 0.00 C ATOM 104 CA GLN C 119 -13.428 6.460 21.296 1.00 0.00 C TER 105 GLN C 119 ATOM 106 CA LEU D 86 0.728 21.584 -19.248 1.00 0.00 C ATOM 107 CA TRP D 87 0.088 21.516 -15.440 1.00 0.00 C ATOM 108 CA GLY D 88 -3.560 20.196 -15.456 1.00 0.00 C ATOM 109 CA ARG D 89 -2.164 16.632 -16.048 1.00 0.00 C ATOM 110 CA CYS D 90 0.256 17.148 -13.096 1.00 0.00 C ATOM 111 CA VAL D 91 -2.784 18.068 -10.896 1.00 0.00 C ATOM 112 CA ALA D 92 -4.476 14.904 -12.296 1.00 0.00 C ATOM 113 CA VAL D 93 -1.428 12.764 -11.216 1.00 0.00 C ATOM 114 CA VAL D 94 -1.508 14.456 -7.728 1.00 0.00 C ATOM 115 CA VAL D 95 -5.256 13.740 -7.128 1.00 0.00 C ATOM 116 CA MET D 96 -4.800 10.192 -8.604 1.00 0.00 C ATOM 117 CA VAL D 97 -1.940 9.288 -6.176 1.00 0.00 C ATOM 118 CA ALA D 98 -3.820 11.068 -3.308 1.00 0.00 C ATOM 119 CA GLY D 99 -6.952 8.964 -4.160 1.00 0.00 C ATOM 120 CA ILE D 100 -4.936 5.672 -4.264 1.00 0.00 C ATOM 121 CA THR D 101 -3.308 6.852 -0.968 1.00 0.00 C ATOM 122 CA SER D 102 -6.720 7.680 0.660 1.00 0.00 C ATOM 123 CA PHE D 103 -8.328 4.296 -0.152 1.00 0.00 C ATOM 124 CA GLY D 104 -5.040 2.548 0.924 1.00 0.00 C ATOM 125 CA LEU D 105 -5.312 4.640 4.164 1.00 0.00 C ATOM 126 CA VAL D 106 -8.908 3.552 5.108 1.00 0.00 C ATOM 127 CA THR D 107 -7.628 0.044 4.196 1.00 0.00 C ATOM 128 CA ALA D 108 -4.444 0.004 6.400 1.00 0.00 C ATOM 129 CA ALA D 109 -6.128 0.116 9.868 1.00 0.00 C ATOM 130 CA LEU D 110 -8.712 -2.716 9.400 1.00 0.00 C ATOM 131 CA ALA D 111 -6.048 -5.536 9.400 1.00 0.00 C ATOM 132 CA THR D 112 -4.080 -4.244 12.436 1.00 0.00 C ATOM 133 CA TRP D 113 -7.596 -4.164 14.004 1.00 0.00 C ATOM 134 CA PHE D 114 -8.176 -7.804 12.756 1.00 0.00 C ATOM 135 CA VAL D 115 -4.692 -8.932 14.056 1.00 0.00 C ATOM 136 CA GLY D 116 -6.160 -7.612 17.372 1.00 0.00 C ATOM 137 CA ARG D 117 -7.748 -11.172 17.320 1.00 0.00 C ATOM 138 CA GLU D 118 -4.496 -13.040 18.012 1.00 0.00 C ATOM 139 CA GLN D 119 -6.608 -13.148 21.296 1.00 0.00 C TER 140 GLN D 119 END