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HEADER PEPTIDE ANTIBIOTIC 18-OCT-93 1GRM
COMPND GRAMICIDIN A (NMR, 5 STRUCTURES)
SOURCE (BACILLUS BREVIS)
EXPDTA NMR
AUTHOR A.S.ARSENIEV,I.L.BARSUKOV,A.L.LOMIZE,V.Y.OREKHOV,V.F.BYSTROV
REVDAT 1 31-JAN-94 1GRM 0
JRNL AUTH A.L.LOMIZE, V.YU.OREKHOV, A.S.ARSENIEV
JRNL TITL REFINEMENT OF THE SPATIAL STRUCTURE
JRNL TITL 2 OF THE GRAMICIDIN A TRANSMEMBRANE ION-CHANNEL
JRNL TITL 3 (RUSSIAN)
JRNL REF BIOL.MEMBR.(USSR) V. 18 182 1992
JRNL REFN ASTM BIMEE9 SU ISSN 0233-4755 2018
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.S.ARSENIEV,I.L.BARSUKOV,V.F.BYSTROV,A.L.LOMIZE,
REMARK 1 AUTH 2 YU.A.OVCHINNIKOV
REMARK 1 TITL 1H-NMR STUDY OF GRAMICIDIN A TRANSMEMBRANE ION
REMARK 1 TITL 2 CHANNEL
REMARK 1 REF /FEBS$ LETT. V. 186 168 1985
REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.S.ARSENIEV,A.L.LOMIZE,I.L.BARSUKOV,V.F.BYSTROV
REMARK 1 TITL GRAMICIDIN A TRANSMEMBRANE ION-CHANNEL.
REMARK 1 TITL 2 THREE-DIMENSIONAL STRUCTURE RECONSTRUCTION BASED ON
REMARK 1 TITL 3 NMR SPECTROSCOPY AND ENERGY REFINEMENT (RUSSIAN)
REMARK 1 REF BIOL.MEMBR.(USSR) V. 3 1077 1986
REMARK 1 REFN ASTM BIMEE9 SU ISSN 0233-4755 2018
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.S.ARSENIEV,I.L.BARSUKOV,V.F.BYSTROV,
REMARK 1 AUTH 2 YU.A.OVCHINNIKOV
REMARK 1 TITL SPATIAL STRUCTURE OF GRAMICIDIN A TRANSMEMBRANE
REMARK 1 TITL 2 ION CHANNEL - NMR ANALYSIS IN MICELLES (RUSSIAN)
REMARK 1 REF BIOL.MEMBR.(USSR) V. 3 437 1986
REMARK 1 REFN ASTM BIMEE9 SU ISSN 0233-4755 2018
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE. SEE REMARK 4.
REMARK 3
REMARK 3 REFINEMENT. NONE.
REMARK 4
REMARK 4 THESE COORDINATES WERE GENERATED FROM SOLUTION NMR DATA.
REMARK 4 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT *CRYST1* AND
REMARK 4 *SCALE* RECORDS BE INCLUDED, BUT THE VALUES ON THESE
REMARK 4 RECORDS ARE MEANINGLESS.
REMARK 5
REMARK 5 GRAMICIDIN-A IS A LINEAR PENTADECAPEPTIDE ANTIBIOTIC
REMARK 5 ISOLATED FROM BACILLUS BREVIS. THE MOLECULAR DIMER FORMS
REMARK 5 TRANS-MEMBRANE ION CHANNELS WHICH TRANSPORT K+ IONS INTO
REMARK 5 THE MITOCHONDRIA OF GRAM-POSITIVE BACTERIA AND KILL THE
REMARK 5 CELL BY OVERLOADING THE K-ATPASE PUMP.
REMARK 6
REMARK 6 ENERGY REFINED THREE-DIMENSIONAL STRUCTURE OF GRAMICIDIN A
REMARK 6 TRANSMEMBRANE ION-CHANNEL WAS RECONSTRUCTED BASING ON
REMARK 6 1H-NMR SPECTRAL PARAMETERS OF GRAMICIDIN A INCORPORATED
REMARK 6 INTO SODIUM DODECYLSULFATE MICELLES. IT IS THE N-TERMINAL
REMARK 6 (HEAD-TO-HEAD) DIMER FORMED BY TWO RIGHT-HANDED
REMARK 6 SINGLE-STRANDED BETA-HELIXES WITH 6.3 RESIDUES PER TURN.
REMARK 7
REMARK 7 EXPERIMENTAL DATA SET: 541 NOE CROSS-PEAK VOLUMES (MIXING
REMARK 7 TIME WAS 100 AND 200 MS); 34 VICINAL COUPLING CONSTANTS
REMARK 7 OF H-N-CA-H AND H-CA-CB-H PROTONS; 32 SOLVENT
REMARK 7 ACCESSIBILITIES OF NH PROTONS.
REMARK 8
REMARK 8 METHOD OF STRUCTURE COMPUTATION:
REMARK 8 1. MODEL BUILDING AND ENERGY MINIMIZATION (ECEPP/2 FORCE
REMARK 8 FIELD) OF THE GRAMICIDIN A DIMER (TWO RIGHT-HANDED
REMARK 8 BETA-HELICES WITH 6,3 RESIDUES PER TURN) USING C2 SYMMETRY
REMARK 8 CONDITION.
REMARK 8 2. SYSTEMATIC SEARCH FOR ALLOWED SIDE CHAIN ROTAMERS
REMARK 8 (INCLUDING C-TERMINAL ETHANOLAMINE GROUP) WHICH ARE
REMARK 8 CONSISTENT WITH NOE CROSS-PEAK VOLUMES AND VICINAL COUPLING
REMARK 8 CONSTANTS. ALL DIMER CONFORMATIONS WITH DIFFERENT SIDE
REMARK 8 CHAIN ORIENTATIONS WERE OPTIMIZED ENERGETICALLY WITHOUT
REMARK 8 EXPERIMENTAL CONSTRAINTS AND THE PENALTY FUNCTIONS WERE
REMARK 8 CALCULATED TO COMPARE THEORETICAL AND EXPERIMENTAL NOE
REMARK 8 CROSS-PEAK VOLUMES AND VICINAL COUPLING CONSTANTS.
REMARK 8 THEORETICAL NOE CROSS-PEAK VOLUMES WERE CALCULATED USING
REMARK 8 COMPLETE RELAXATION MATRIX APPROXIMATION. ROTATIONAL
REMARK 8 CORRELATION TIME (2.5+-0.2 NS) OF THE DIMER IN MICELLES
REMARK 8 WAS ESTIMATED EXPERIMENTALLY. THE SAME APPROACH HAS BEEN
REMARK 8 DESCRIBED FOR BACTERIORHODOPSIN ALPHA-HELICAL FRAGMENT
REMARK 8 INCORPORATED INTO SODIUM DODECYL SULFATE MICELLES
REMARK 8 (A.L.LOMIZE, K.V.PERVUSHIN, A.S.ARSENIEV. J.BIOMOL.NMR,
REMARK 8 1992, V.18,P.182-199).
REMARK 8 3. DYNAMIC AVERAGING OF DIFFERENT DIMER CONFORMATIONS TO
REMARK 8 REFINE THE SET OF CONFORMATIONS WHICH ARE IN EQUILIBRIUM
REMARK 8 IN MICELLES.
REMARK 9
REMARK 9 A SET OF 5 LOW-ENERGY CONFORMATIONS OF THE GRAMICIDIN A
REMARK 9 ION-CHANNEL (THIS FILE) REPRESENTS FLEXIBILITY OF
REMARK 9 GRAMICIDIN A IN DODECYL SULFATE MICELLES JUDGING FROM 1H
REMARK 9 NMR DATA. THESE CONFORMATIONS ARE DIFFER IN THE SIDE CHAIN
REMARK 9 TORSION ANGLES CHI1 VAL 7 AND CHI2 D-LEU 4 AND D-LEU 10
REMARK 9 AND THE ORIENTATION OF THE C-TERMINAL ETHANOLAMINE GROUP.
REMARK 9 ROOT MEAN SQUARE DIFFERENCES BETWEEN THE ATOMIC COORDINATES
REMARK 9 OF THE DIMER CONFORMATIONS ARE IN THE RANGE OF 0.3-0.8 A.
REMARK 10
REMARK 10 R-FACTOR (NOE PENALTY FUNCTION) WAS ESTIMATED AS ROOT MEAN
REMARK 10 SQUARE DIFFERENCE OF INTERPROTON DISTANCES IN THE SPATIAL
REMARK 10 STRUCTURE OF THE PEPTIDE WITH THE DISTANCES CALCULATED
REMARK 10 FROM THE MEASURED NOE CROSS-PEAK VOLUMES. FOR THE FINAL
REMARK 10 SET OF THE 5 REPRESENTATIVE GRAMICIDIN A CONFORMATIONS THIS
REMARK 10 FACTOR WAS 0.21-0.23 A (IT DEPENDS ALSO ON THE MIXING TIME)
REMARK 10 FOR CROSS-PEAKS OF NH PROTONS AND 0.40-0.47 A FOR
REMARK 10 CROSS-PEAKS OF SIDE CHAIN PROTONS IN THE NOESY SPECTRA.
SEQRES 1 A 17 FOR VAL GLY ALA LEU ALA VAL VAL VAL TRP LEU TRP LEU
SEQRES 2 A 17 TRP LEU TRP ETA
SEQRES 1 B 17 FOR VAL GLY ALA LEU ALA VAL VAL VAL TRP LEU TRP LEU
SEQRES 2 B 17 TRP LEU TRP ETA
FTNOTE 1
FTNOTE 1 RESIDUES LEU 4, VAL 6, VAL 8, LEU 10, LEU 12, AND LEU 14 IN
FTNOTE 1 EACH CHAIN EXHIBIT THE D CONFIGURATION OF THE AMINO ACID.
HET ETA A 16 4 ETHANOLAMINE
HET ETA B 16 4 ETHANOLAMINE
FORMUL 1 ETA C2 H7 N1 O1
FORMUL 2 ETA C2 H7 N1 O1
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
REMARK 500 Only use MODEL 1 for MDAnalysis test case; all other deleted.
REMARK 500 This is the same structure that is used as test case 01 in the
REMARK 500 original HOLE sources by Oliver S. Smart.
REMARK 500 (The original had '1GRM n' with n the linenumber at the end
REMARK 500 of each line but because this is not meaningful in the
REMARK 500 PDB Format v3.3 it was deleted.)
MODEL 1
ATOM 1 C FOR A 0 -1.409 0.501 0.859 1.00 1.00
ATOM 2 O FOR A 0 -1.445 1.720 0.692 1.00 1.00
ATOM 3 N VAL A 1 -2.330 -0.205 1.496 1.00 1.00
ATOM 4 CA VAL A 1 -3.501 0.435 2.070 1.00 1.00
ATOM 5 C VAL A 1 -3.595 0.079 3.555 1.00 1.00
ATOM 6 O VAL A 1 -3.911 -1.055 3.906 1.00 1.00
ATOM 7 CB VAL A 1 -4.752 0.042 1.281 1.00 1.00
ATOM 8 CG1 VAL A 1 -5.974 0.826 1.764 1.00 1.00
ATOM 9 CG2 VAL A 1 -4.535 0.232 -0.221 1.00 1.00
ATOM 10 N GLY A 2 -3.315 1.072 4.387 1.00 1.00
ATOM 11 CA GLY A 2 -3.364 0.879 5.826 1.00 1.00
ATOM 12 C GLY A 2 -2.503 1.917 6.549 1.00 1.00
ATOM 13 O GLY A 2 -3.009 2.947 6.992 1.00 1.00
ATOM 14 N ALA A 3 -1.218 1.610 6.645 1.00 1.00
ATOM 15 CA ALA A 3 -0.282 2.504 7.305 1.00 1.00
ATOM 16 C ALA A 3 1.118 2.286 6.729 1.00 1.00
ATOM 17 O ALA A 3 1.488 1.161 6.395 1.00 1.00
ATOM 18 CB ALA A 3 -0.333 2.271 8.817 1.00 1.00
ATOM 19 N LEU A 4 1.860 3.379 6.631 1.00 1.00 1
ATOM 20 CA LEU A 4 3.212 3.322 6.101 1.00 1.00 1
ATOM 21 C LEU A 4 3.344 4.316 4.945 1.00 1.00 1
ATOM 22 O LEU A 4 3.076 5.504 5.109 1.00 1.00 1
ATOM 23 CB LEU A 4 4.235 3.539 7.217 1.00 1.00 1
ATOM 24 CG LEU A 4 5.653 3.290 6.701 1.00 1.00 1
ATOM 25 CD1 LEU A 4 6.367 4.609 6.398 1.00 1.00 1
ATOM 26 CD2 LEU A 4 6.446 2.419 7.676 1.00 1.00 1
ATOM 27 N ALA A 5 3.758 3.791 3.801 1.00 1.00
ATOM 28 CA ALA A 5 3.929 4.617 2.617 1.00 1.00
ATOM 29 C ALA A 5 2.939 4.169 1.540 1.00 1.00
ATOM 30 O ALA A 5 2.972 3.022 1.100 1.00 1.00
ATOM 31 CB ALA A 5 5.381 4.534 2.143 1.00 1.00
ATOM 32 N VAL A 6 2.080 5.099 1.149 1.00 1.00 1
ATOM 33 CA VAL A 6 1.082 4.815 0.132 1.00 1.00 1
ATOM 34 C VAL A 6 -0.248 5.456 0.535 1.00 1.00 1
ATOM 35 O VAL A 6 -0.349 6.677 0.629 1.00 1.00 1
ATOM 36 CB VAL A 6 1.580 5.284 -1.237 1.00 1.00 1
ATOM 37 CG1 VAL A 6 2.863 4.551 -1.635 1.00 1.00 1
ATOM 38 CG2 VAL A 6 0.496 5.113 -2.303 1.00 1.00 1
ATOM 39 N VAL A 7 -1.235 4.601 0.764 1.00 1.00
ATOM 40 CA VAL A 7 -2.554 5.068 1.156 1.00 1.00
ATOM 41 C VAL A 7 -2.807 4.698 2.618 1.00 1.00
ATOM 42 O VAL A 7 -2.463 3.600 3.053 1.00 1.00
ATOM 43 CB VAL A 7 -3.612 4.505 0.205 1.00 1.00
ATOM 44 CG1 VAL A 7 -4.962 5.192 0.419 1.00 1.00
ATOM 45 CG2 VAL A 7 -3.159 4.625 -1.252 1.00 1.00
ATOM 46 N VAL A 8 -3.408 5.635 3.337 1.00 1.00 1
ATOM 47 CA VAL A 8 -3.713 5.421 4.742 1.00 1.00 1
ATOM 48 C VAL A 8 -3.197 6.608 5.557 1.00 1.00 1
ATOM 49 O VAL A 8 -3.535 7.756 5.271 1.00 1.00 1
ATOM 50 CB VAL A 8 -5.212 5.179 4.922 1.00 1.00 1
ATOM 51 CG1 VAL A 8 -5.618 3.813 4.366 1.00 1.00 1
ATOM 52 CG2 VAL A 8 -5.618 5.317 6.390 1.00 1.00 1
ATOM 53 N TRP A 9 -2.386 6.292 6.556 1.00 1.00
ATOM 54 CA TRP A 9 -1.820 7.318 7.415 1.00 1.00
ATOM 55 C TRP A 9 -0.305 7.108 7.467 1.00 1.00
ATOM 56 O TRP A 9 0.164 5.987 7.660 1.00 1.00
ATOM 57 CB TRP A 9 -2.475 7.298 8.797 1.00 1.00
ATOM 58 CG TRP A 9 -1.741 8.137 9.845 1.00 1.00
ATOM 59 CD1 TRP A 9 -1.921 9.432 10.140 1.00 1.00
ATOM 60 CD2 TRP A 9 -0.709 7.727 10.733 1.00 1.00
ATOM 61 NE1 TRP A 9 -1.073 9.845 11.147 1.00 1.00
ATOM 62 CE2 TRP A 9 -0.304 8.748 11.518 1.00 1.00
ATOM 63 CE3 TRP A 9 -0.119 6.453 10.860 1.00 1.00
ATOM 64 CZ2 TRP A 9 0.697 8.654 12.492 1.00 1.00
ATOM 65 CZ3 TRP A 9 0.882 6.358 11.833 1.00 1.00
ATOM 66 CH2 TRP A 9 1.299 7.409 12.641 1.00 1.00
ATOM 67 N LEU A 10 0.419 8.204 7.292 1.00 1.00 1
ATOM 68 CA LEU A 10 1.871 8.154 7.318 1.00 1.00 1
ATOM 69 C LEU A 10 2.428 9.145 6.292 1.00 1.00 1
ATOM 70 O LEU A 10 2.400 10.354 6.513 1.00 1.00 1
ATOM 71 CB LEU A 10 2.390 8.384 8.738 1.00 1.00 1
ATOM 72 CG LEU A 10 3.913 8.530 8.734 1.00 1.00 1
ATOM 73 CD1 LEU A 10 4.417 9.056 10.080 1.00 1.00 1
ATOM 74 CD2 LEU A 10 4.589 7.215 8.343 1.00 1.00 1
ATOM 75 N TRP A 11 2.921 8.593 5.193 1.00 1.00
ATOM 76 CA TRP A 11 3.484 9.412 4.133 1.00 1.00
ATOM 77 C TRP A 11 2.866 8.961 2.807 1.00 1.00
ATOM 78 O TRP A 11 2.395 7.830 2.692 1.00 1.00
ATOM 79 CB TRP A 11 5.013 9.339 4.136 1.00 1.00
ATOM 80 CG TRP A 11 5.658 9.862 5.421 1.00 1.00
ATOM 81 CD1 TRP A 11 5.406 11.012 6.061 1.00 1.00
ATOM 82 CD2 TRP A 11 6.662 9.244 6.214 1.00 1.00
ATOM 83 NE1 TRP A 11 6.186 11.143 7.192 1.00 1.00
ATOM 84 CE2 TRP A 11 6.985 10.008 7.279 1.00 1.00
ATOM 85 CE3 TRP A 11 7.302 8.004 6.006 1.00 1.00
ATOM 86 CZ2 TRP A 11 7.941 9.666 8.243 1.00 1.00
ATOM 87 CZ3 TRP A 11 8.258 7.662 6.969 1.00 1.00
ATOM 88 CH2 TRP A 11 8.590 8.449 8.066 1.00 1.00
ATOM 89 N LEU A 12 2.890 9.867 1.842 1.00 1.00 1
ATOM 90 CA LEU A 12 2.338 9.576 0.529 1.00 1.00 1
ATOM 91 C LEU A 12 1.067 10.402 0.320 1.00 1.00 1
ATOM 92 O LEU A 12 1.135 11.556 -0.100 1.00 1.00 1
ATOM 93 CB LEU A 12 3.395 9.791 -0.556 1.00 1.00 1
ATOM 94 CG LEU A 12 4.677 9.029 -0.214 1.00 1.00 1
ATOM 95 CD1 LEU A 12 4.492 7.525 -0.421 1.00 1.00 1
ATOM 96 CD2 LEU A 12 5.868 9.575 -1.005 1.00 1.00 1
ATOM 97 N TRP A 13 -0.062 9.778 0.623 1.00 1.00
ATOM 98 CA TRP A 13 -1.346 10.442 0.474 1.00 1.00
ATOM 99 C TRP A 13 -2.250 9.984 1.621 1.00 1.00
ATOM 100 O TRP A 13 -2.045 8.913 2.189 1.00 1.00
ATOM 101 CB TRP A 13 -1.947 10.169 -0.906 1.00 1.00
ATOM 102 CG TRP A 13 -1.155 10.783 -2.061 1.00 1.00
ATOM 103 CD1 TRP A 13 -1.276 12.011 -2.584 1.00 1.00
ATOM 104 CD2 TRP A 13 -0.120 10.186 -2.832 1.00 1.00
ATOM 105 NE1 TRP A 13 -0.387 12.210 -3.621 1.00 1.00
ATOM 106 CE2 TRP A 13 0.346 11.038 -3.770 1.00 1.00
ATOM 107 CE3 TRP A 13 0.421 8.889 -2.714 1.00 1.00
ATOM 108 CZ2 TRP A 13 1.365 10.737 -4.682 1.00 1.00
ATOM 109 CZ3 TRP A 13 1.441 8.589 -3.625 1.00 1.00
ATOM 110 CH2 TRP A 13 1.920 9.466 -4.591 1.00 1.00
ATOM 111 N LEU A 14 -3.233 10.819 1.926 1.00 1.00 1
ATOM 112 CA LEU A 14 -4.168 10.515 2.996 1.00 1.00 1
ATOM 113 C LEU A 14 -3.957 11.496 4.150 1.00 1.00 1
ATOM 114 O LEU A 14 -4.386 12.646 4.077 1.00 1.00 1
ATOM 115 CB LEU A 14 -5.603 10.493 2.462 1.00 1.00 1
ATOM 116 CG LEU A 14 -5.836 9.251 1.600 1.00 1.00 1
ATOM 117 CD1 LEU A 14 -6.394 8.100 2.440 1.00 1.00 1
ATOM 118 CD2 LEU A 14 -6.731 9.575 0.402 1.00 1.00 1
ATOM 119 N TRP A 15 -3.294 11.006 5.187 1.00 1.00
ATOM 120 CA TRP A 15 -3.020 11.827 6.354 1.00 1.00
ATOM 121 C TRP A 15 -1.606 11.501 6.840 1.00 1.00
ATOM 122 O TRP A 15 -1.000 10.529 6.391 1.00 1.00
ATOM 123 CB TRP A 15 -4.086 11.619 7.433 1.00 1.00
ATOM 124 CG TRP A 15 -5.514 11.885 6.956 1.00 1.00
ATOM 125 CD1 TRP A 15 -6.165 13.056 6.907 1.00 1.00
ATOM 126 CD2 TRP A 15 -6.463 10.949 6.459 1.00 1.00
ATOM 127 NE1 TRP A 15 -7.445 12.904 6.417 1.00 1.00
ATOM 128 CE2 TRP A 15 -7.624 11.555 6.134 1.00 1.00
ATOM 129 CE3 TRP A 15 -6.312 9.557 6.289 1.00 1.00
ATOM 130 CZ2 TRP A 15 -8.748 10.897 5.619 1.00 1.00
ATOM 131 CZ3 TRP A 15 -7.435 8.900 5.774 1.00 1.00
ATOM 132 CH2 TRP A 15 -8.631 9.524 5.439 1.00 1.00
HETATM 133 CA ETA A 16 0.210 12.145 8.302 1.00 1.00
HETATM 134 N ETA A 16 -1.122 12.332 7.751 1.00 1.00
HETATM 135 CB ETA A 16 1.207 13.019 7.538 1.00 1.00
HETATM 136 O ETA A 16 1.257 12.684 6.153 1.00 1.00
TER 137 ETA A 16
ATOM 138 C FOR B 0 1.351 -0.528 0.850 1.00 1.00
ATOM 139 O FOR B 0 1.386 -1.747 0.684 1.00 1.00
ATOM 140 N VAL B 1 2.276 0.179 1.481 1.00 1.00
ATOM 141 CA VAL B 1 3.451 -0.461 2.047 1.00 1.00
ATOM 142 C VAL B 1 3.555 -0.104 3.532 1.00 1.00
ATOM 143 O VAL B 1 3.873 1.031 3.880 1.00 1.00
ATOM 144 CB VAL B 1 4.697 -0.068 1.250 1.00 1.00
ATOM 145 CG1 VAL B 1 5.922 -0.852 1.725 1.00 1.00
ATOM 146 CG2 VAL B 1 4.470 -0.260 -0.250 1.00 1.00
ATOM 147 N GLY B 2 3.281 -1.096 4.366 1.00 1.00
ATOM 148 CA GLY B 2 3.339 -0.902 5.805 1.00 1.00
ATOM 149 C GLY B 2 2.482 -1.940 6.534 1.00 1.00
ATOM 150 O GLY B 2 2.991 -2.970 6.974 1.00 1.00
ATOM 151 N ALA B 3 1.198 -1.633 6.638 1.00 1.00
ATOM 152 CA ALA B 3 0.267 -2.527 7.305 1.00 1.00
ATOM 153 C ALA B 3 -1.138 -2.309 6.738 1.00 1.00
ATOM 154 O ALA B 3 -1.509 -1.185 6.406 1.00 1.00
ATOM 155 CB ALA B 3 0.327 -2.293 8.816 1.00 1.00
ATOM 156 N LEU B 4 -1.880 -3.402 6.645 1.00 1.00 1
ATOM 157 CA LEU B 4 -3.235 -3.345 6.124 1.00 1.00 1
ATOM 158 C LEU B 4 -3.375 -4.340 4.970 1.00 1.00 1
ATOM 159 O LEU B 4 -3.106 -5.528 5.133 1.00 1.00 1
ATOM 160 CB LEU B 4 -4.251 -3.562 7.247 1.00 1.00 1
ATOM 161 CG LEU B 4 -5.672 -3.313 6.740 1.00 1.00 1
ATOM 162 CD1 LEU B 4 -6.388 -4.632 6.443 1.00 1.00 1
ATOM 163 CD2 LEU B 4 -6.459 -2.441 7.720 1.00 1.00 1
ATOM 164 N ALA B 5 -3.796 -3.816 3.828 1.00 1.00
ATOM 165 CA ALA B 5 -3.975 -4.642 2.646 1.00 1.00
ATOM 166 C ALA B 5 -2.992 -4.195 1.562 1.00 1.00
ATOM 167 O ALA B 5 -3.028 -3.048 1.121 1.00 1.00
ATOM 168 CB ALA B 5 -5.431 -4.560 2.181 1.00 1.00
ATOM 169 N VAL B 6 -2.136 -5.126 1.166 1.00 1.00 1
ATOM 170 CA VAL B 6 -1.144 -4.842 0.142 1.00 1.00 1
ATOM 171 C VAL B 6 0.188 -5.482 0.537 1.00 1.00 1
ATOM 172 O VAL B 6 0.290 -6.704 0.631 1.00 1.00 1
ATOM 173 CB VAL B 6 -1.651 -5.312 -1.223 1.00 1.00 1
ATOM 174 CG1 VAL B 6 -2.937 -4.579 -1.613 1.00 1.00 1
ATOM 175 CG2 VAL B 6 -0.574 -5.141 -2.296 1.00 1.00 1
ATOM 176 N VAL B 7 1.176 -4.627 0.759 1.00 1.00
ATOM 177 CA VAL B 7 2.498 -5.094 1.143 1.00 1.00
ATOM 178 C VAL B 7 2.761 -4.723 2.603 1.00 1.00
ATOM 179 O VAL B 7 2.419 -3.626 3.039 1.00 1.00
ATOM 180 CB VAL B 7 3.550 -4.532 0.184 1.00 1.00
ATOM 181 CG1 VAL B 7 4.901 -5.219 0.390 1.00 1.00
ATOM 182 CG2 VAL B 7 3.088 -4.653 -1.269 1.00 1.00
ATOM 183 N VAL B 8 3.367 -5.660 3.318 1.00 1.00 1
ATOM 184 CA VAL B 8 3.680 -5.446 4.721 1.00 1.00 1
ATOM 185 C VAL B 8 3.170 -6.632 5.540 1.00 1.00 1
ATOM 186 O VAL B 8 3.506 -7.780 5.253 1.00 1.00 1
ATOM 187 CB VAL B 8 5.181 -5.203 4.891 1.00 1.00 1
ATOM 188 CG1 VAL B 8 5.583 -3.837 4.332 1.00 1.00 1
ATOM 189 CG2 VAL B 8 5.596 -5.340 6.357 1.00 1.00 1
ATOM 190 N TRP B 9 2.365 -6.315 6.544 1.00 1.00
ATOM 191 CA TRP B 9 1.805 -7.341 7.408 1.00 1.00
ATOM 192 C TRP B 9 0.290 -7.131 7.470 1.00 1.00
ATOM 193 O TRP B 9 -0.177 -6.010 7.665 1.00 1.00
ATOM 194 CB TRP B 9 2.469 -7.320 8.785 1.00 1.00
ATOM 195 CG TRP B 9 1.742 -8.158 9.839 1.00 1.00
ATOM 196 CD1 TRP B 9 1.924 -9.452 10.133 1.00 1.00
ATOM 197 CD2 TRP B 9 0.716 -7.748 10.733 1.00 1.00
ATOM 198 NE1 TRP B 9 1.083 -9.865 11.146 1.00 1.00
ATOM 199 CE2 TRP B 9 0.316 -8.768 11.521 1.00 1.00
ATOM 200 CE3 TRP B 9 0.127 -6.473 10.863 1.00 1.00
ATOM 201 CZ2 TRP B 9 -0.679 -8.673 12.502 1.00 1.00
ATOM 202 CZ3 TRP B 9 -0.868 -6.378 11.843 1.00 1.00
ATOM 203 CH2 TRP B 9 -1.280 -7.428 12.654 1.00 1.00
ATOM 204 N LEU B 10 -0.434 -8.227 7.300 1.00 1.00 1
ATOM 205 CA LEU B 10 -1.886 -8.177 7.335 1.00 1.00 1
ATOM 206 C LEU B 10 -2.450 -9.168 6.314 1.00 1.00 1
ATOM 207 O LEU B 10 -2.421 -10.377 6.535 1.00 1.00 1
ATOM 208 CB LEU B 10 -2.396 -8.406 8.759 1.00 1.00 1
ATOM 209 CG LEU B 10 -3.919 -8.552 8.765 1.00 1.00 1
ATOM 210 CD1 LEU B 10 -4.414 -9.077 10.115 1.00 1.00 1
ATOM 211 CD2 LEU B 10 -4.597 -7.237 8.378 1.00 1.00 1
ATOM 212 N TRP B 11 -2.950 -8.617 5.218 1.00 1.00
ATOM 213 CA TRP B 11 -3.520 -9.437 4.162 1.00 1.00
ATOM 214 C TRP B 11 -2.911 -8.986 2.832 1.00 1.00
ATOM 215 O TRP B 11 -2.441 -7.856 2.713 1.00 1.00
ATOM 216 CB TRP B 11 -5.049 -9.363 4.175 1.00 1.00
ATOM 217 CG TRP B 11 -5.685 -9.886 5.464 1.00 1.00
ATOM 218 CD1 TRP B 11 -5.430 -11.035 6.103 1.00 1.00
ATOM 219 CD2 TRP B 11 -6.685 -9.267 6.263 1.00 1.00
ATOM 220 NE1 TRP B 11 -6.203 -11.165 7.239 1.00 1.00
ATOM 221 CE2 TRP B 11 -7.000 -10.031 7.331 1.00 1.00
ATOM 222 CE3 TRP B 11 -7.326 -8.027 6.059 1.00 1.00
ATOM 223 CZ2 TRP B 11 -7.950 -9.688 8.301 1.00 1.00
ATOM 224 CZ3 TRP B 11 -8.276 -7.685 7.028 1.00 1.00
ATOM 225 CH2 TRP B 11 -8.600 -8.471 8.127 1.00 1.00
ATOM 226 N LEU B 12 -2.941 -9.893 1.867 1.00 1.00 1
ATOM 227 CA LEU B 12 -2.398 -9.603 0.550 1.00 1.00 1
ATOM 228 C LEU B 12 -1.128 -10.429 0.334 1.00 1.00 1
ATOM 229 O LEU B 12 -1.199 -11.583 -0.085 1.00 1.00 1
ATOM 230 CB LEU B 12 -3.462 -9.819 -0.527 1.00 1.00 1
ATOM 231 CG LEU B 12 -4.741 -9.056 -0.177 1.00 1.00 1
ATOM 232 CD1 LEU B 12 -4.559 -7.552 -0.386 1.00 1.00 1
ATOM 233 CD2 LEU B 12 -5.937 -9.603 -0.960 1.00 1.00 1
ATOM 234 N TRP B 13 0.002 -9.805 0.629 1.00 1.00
ATOM 235 CA TRP B 13 1.286 -10.468 0.472 1.00 1.00
ATOM 236 C TRP B 13 2.197 -10.010 1.613 1.00 1.00
ATOM 237 O TRP B 13 1.996 -8.939 2.181 1.00 1.00
ATOM 238 CB TRP B 13 1.878 -10.197 -0.912 1.00 1.00
ATOM 239 CG TRP B 13 1.078 -10.811 -2.062 1.00 1.00
ATOM 240 CD1 TRP B 13 1.196 -12.040 -2.585 1.00 1.00
ATOM 241 CD2 TRP B 13 0.038 -10.215 -2.826 1.00 1.00
ATOM 242 NE1 TRP B 13 0.300 -12.239 -3.616 1.00 1.00
ATOM 243 CE2 TRP B 13 -0.434 -11.068 -3.761 1.00 1.00
ATOM 244 CE3 TRP B 13 -0.502 -8.918 -2.705 1.00 1.00
ATOM 245 CZ2 TRP B 13 -1.459 -10.767 -4.666 1.00 1.00
ATOM 246 CZ3 TRP B 13 -1.528 -8.618 -3.610 1.00 1.00
ATOM 247 CH2 TRP B 13 -2.013 -9.496 -4.572 1.00 1.00
ATOM 248 N LEU B 14 3.182 -10.845 1.912 1.00 1.00 1
ATOM 249 CA LEU B 14 4.124 -10.540 2.975 1.00 1.00 1
ATOM 250 C LEU B 14 3.921 -11.521 4.131 1.00 1.00 1
ATOM 251 O LEU B 14 4.350 -12.671 4.056 1.00 1.00 1
ATOM 252 CB LEU B 14 5.555 -10.519 2.432 1.00 1.00 1
ATOM 253 CG LEU B 14 5.783 -9.277 1.568 1.00 1.00 1
ATOM 254 CD1 LEU B 14 6.347 -8.125 2.403 1.00 1.00 1
ATOM 255 CD2 LEU B 14 6.670 -9.602 0.364 1.00 1.00 1
ATOM 256 N TRP B 15 3.265 -11.030 5.172 1.00 1.00
ATOM 257 CA TRP B 15 2.998 -11.850 6.342 1.00 1.00
ATOM 258 C TRP B 15 1.587 -11.523 6.837 1.00 1.00
ATOM 259 O TRP B 15 0.979 -10.552 6.391 1.00 1.00
ATOM 260 CB TRP B 15 4.071 -11.642 7.414 1.00 1.00
ATOM 261 CG TRP B 15 5.496 -11.908 6.927 1.00 1.00
ATOM 262 CD1 TRP B 15 6.146 -13.079 6.875 1.00 1.00
ATOM 263 CD2 TRP B 15 6.441 -10.972 6.424 1.00 1.00
ATOM 264 NE1 TRP B 15 7.424 -12.927 6.376 1.00 1.00
ATOM 265 CE2 TRP B 15 7.601 -11.578 6.091 1.00 1.00
ATOM 266 CE3 TRP B 15 6.290 -9.580 6.254 1.00 1.00
ATOM 267 CZ2 TRP B 15 8.721 -10.921 5.568 1.00 1.00
ATOM 268 CZ3 TRP B 15 7.409 -8.923 5.731 1.00 1.00
ATOM 269 CH2 TRP B 15 8.603 -9.548 5.388 1.00 1.00
HETATM 270 CA ETA B 16 -0.219 -12.167 8.311 1.00 1.00
HETATM 271 N ETA B 16 1.109 -12.354 7.751 1.00 1.00
HETATM 272 CB ETA B 16 -1.221 -13.041 7.554 1.00 1.00
HETATM 273 O ETA B 16 -1.280 -12.708 6.169 1.00 1.00
TER 274 ETA B 16
ENDMDL
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