HEADER PROTEIN BINDING 17-APR-08 SMS20022 TITLE 1H CHEMICAL SHIFT ASSIGNMENTS FOR METASTIN ANALOG, S5A COMPND MOL_ID: 1; COMPND 2 MOLECULE: KISSPEPTIN-10; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 112-121; COMPND 5 SYNONYM: METASTASIS-SUPPRESSOR KISS-1; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: GPCR LIGAND, METASTIN ANALOG SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 4 ORGANISM_COMMON: HUMAN; SOURCE 5 ORGANISM_TAXID: 9606; SOURCE 6 OTHER_DETAILS: SOLID PHASE PEPTIDE SYNTHESIS USING FMOC CHEMISTRY KEYWDS PROTEIN BINDING EXPDTA SOLUTION NMR AUTHOR J.I.KIM JRNL AUTH J.Y.LEE,J.S.MOON,Y.-J.EU,C.W.LEE,S.-T.YANG,S.K.LEE,H.H.JUNG, JRNL AUTH 2 H.H.KIM,H.RHIM,J.Y.SEONG,J.I.KIM JRNL TITL MOLECULAR INTERACTION BETWEEN KISSPEPTIN DECAPEPTIDE ANALOGS JRNL TITL 2 AND A LIPID MEMBRANE JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 485 109 2009 JRNL REFN ISSN 0003-9861 JRNL PMID 19275876 JRNL DOI 10.1016/J.ABB.2009.03.002 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE, REMARK 3 JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 NULL COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-SEP-10. REMARK 100 THE BMRB ID CODE IS SMS20022. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 3.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 100MM [U-100% 2H] DPC; 90% H2O/ REMARK 210 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-1H NOESY; 2D 1H-1H TOCSY; REMARK 210 2D DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS REMARK 210 METHOD USED : DGSA-DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 2 -94.16 -79.69 REMARK 500 TRP A 3 19.40 -157.36 REMARK 500 ALA A 5 58.39 -160.41 REMARK 500 PHE A 6 -73.92 -160.59 REMARK 500 LEU A 8 -60.77 -109.88 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 9 0.32 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 20022 RELATED DB: BMRB DBREF A 1 10 UNP Q15726 KISS1_HUMAN 112 121 SEQADV ALA A 5 UNP Q15726 SER 116 ENGINEERED MUTATION SEQRES 1 A 10 TYR ASN TRP ASN ALA PHE GLY LEU ARG PHE 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 N TYR A 1 -0.132 6.072 2.854 1.00 0.00 N ATOM 2 CA TYR A 1 0.532 5.244 3.902 1.00 0.00 C ATOM 3 C TYR A 1 2.039 5.227 3.700 1.00 0.00 C ATOM 4 O TYR A 1 2.627 6.133 3.143 1.00 0.00 O ATOM 5 CB TYR A 1 -0.021 3.832 3.720 1.00 0.00 C ATOM 6 CG TYR A 1 -1.530 3.879 3.670 1.00 0.00 C ATOM 7 CD1 TYR A 1 -2.255 4.316 4.786 1.00 0.00 C ATOM 8 CD2 TYR A 1 -2.204 3.486 2.508 1.00 0.00 C ATOM 9 CE1 TYR A 1 -3.654 4.358 4.740 1.00 0.00 C ATOM 10 CE2 TYR A 1 -3.603 3.529 2.462 1.00 0.00 C ATOM 11 CZ TYR A 1 -4.328 3.965 3.578 1.00 0.00 C ATOM 12 OH TYR A 1 -5.708 4.006 3.532 1.00 0.00 O ATOM 13 H1 TYR A 1 -0.133 5.554 1.952 1.00 0.00 H ATOM 14 H2 TYR A 1 0.386 6.967 2.740 1.00 0.00 H ATOM 15 H3 TYR A 1 -1.111 6.271 3.138 1.00 0.00 H ATOM 16 HA TYR A 1 0.292 5.604 4.886 1.00 0.00 H ATOM 17 HB2 TYR A 1 0.363 3.414 2.801 1.00 0.00 H ATOM 18 HB3 TYR A 1 0.295 3.216 4.552 1.00 0.00 H ATOM 19 HD1 TYR A 1 -1.736 4.619 5.683 1.00 0.00 H ATOM 20 HD2 TYR A 1 -1.645 3.150 1.647 1.00 0.00 H ATOM 21 HE1 TYR A 1 -4.214 4.694 5.601 1.00 0.00 H ATOM 22 HE2 TYR A 1 -4.123 3.225 1.565 1.00 0.00 H ATOM 23 HH TYR A 1 -5.985 3.723 2.658 1.00 0.00 H ATOM 24 N ASN A 2 2.657 4.186 4.160 1.00 0.00 N ATOM 25 CA ASN A 2 4.130 4.053 4.026 1.00 0.00 C ATOM 26 C ASN A 2 4.496 3.581 2.614 1.00 0.00 C ATOM 27 O ASN A 2 4.634 4.372 1.702 1.00 0.00 O ATOM 28 CB ASN A 2 4.497 2.996 5.063 1.00 0.00 C ATOM 29 CG ASN A 2 4.277 3.560 6.467 1.00 0.00 C ATOM 30 OD1 ASN A 2 5.176 4.128 7.054 1.00 0.00 O ATOM 31 ND2 ASN A 2 3.109 3.427 7.033 1.00 0.00 N ATOM 32 H ASN A 2 2.143 3.483 4.606 1.00 0.00 H ATOM 33 HA ASN A 2 4.620 4.985 4.257 1.00 0.00 H ATOM 34 HB2 ASN A 2 3.867 2.128 4.922 1.00 0.00 H ATOM 35 HB3 ASN A 2 5.530 2.717 4.943 1.00 0.00 H ATOM 36 HD21 ASN A 2 2.383 2.969 6.558 1.00 0.00 H ATOM 37 HD22 ASN A 2 2.956 3.783 7.933 1.00 0.00 H ATOM 38 N TRP A 3 4.655 2.298 2.425 1.00 0.00 N ATOM 39 CA TRP A 3 5.010 1.780 1.073 1.00 0.00 C ATOM 40 C TRP A 3 4.602 0.310 0.947 1.00 0.00 C ATOM 41 O TRP A 3 5.085 -0.408 0.094 1.00 0.00 O ATOM 42 CB TRP A 3 6.529 1.925 0.981 1.00 0.00 C ATOM 43 CG TRP A 3 6.862 3.106 0.128 1.00 0.00 C ATOM 44 CD1 TRP A 3 7.005 4.374 0.578 1.00 0.00 C ATOM 45 CD2 TRP A 3 7.091 3.152 -1.309 1.00 0.00 C ATOM 46 NE1 TRP A 3 7.312 5.195 -0.494 1.00 0.00 N ATOM 47 CE2 TRP A 3 7.375 4.487 -1.678 1.00 0.00 C ATOM 48 CE3 TRP A 3 7.080 2.172 -2.318 1.00 0.00 C ATOM 49 CZ2 TRP A 3 7.641 4.839 -3.003 1.00 0.00 C ATOM 50 CZ3 TRP A 3 7.346 2.522 -3.651 1.00 0.00 C ATOM 51 CH2 TRP A 3 7.626 3.853 -3.993 1.00 0.00 C ATOM 52 H TRP A 3 4.539 1.674 3.171 1.00 0.00 H ATOM 53 HA TRP A 3 4.537 2.372 0.306 1.00 0.00 H ATOM 54 HB2 TRP A 3 6.939 2.066 1.971 1.00 0.00 H ATOM 55 HB3 TRP A 3 6.950 1.033 0.541 1.00 0.00 H ATOM 56 HD1 TRP A 3 6.898 4.693 1.605 1.00 0.00 H ATOM 57 HE1 TRP A 3 7.467 6.161 -0.439 1.00 0.00 H ATOM 58 HE3 TRP A 3 6.865 1.145 -2.065 1.00 0.00 H ATOM 59 HZ2 TRP A 3 7.856 5.866 -3.260 1.00 0.00 H ATOM 60 HZ3 TRP A 3 7.335 1.762 -4.418 1.00 0.00 H ATOM 61 HH2 TRP A 3 7.829 4.116 -5.021 1.00 0.00 H ATOM 62 N ASN A 4 3.712 -0.141 1.789 1.00 0.00 N ATOM 63 CA ASN A 4 3.269 -1.552 1.723 1.00 0.00 C ATOM 64 C ASN A 4 1.753 -1.618 1.520 1.00 0.00 C ATOM 65 O ASN A 4 1.112 -2.594 1.857 1.00 0.00 O ATOM 66 CB ASN A 4 3.668 -2.161 3.071 1.00 0.00 C ATOM 67 CG ASN A 4 2.681 -1.713 4.153 1.00 0.00 C ATOM 68 OD1 ASN A 4 2.429 -0.536 4.312 1.00 0.00 O ATOM 69 ND2 ASN A 4 2.108 -2.611 4.908 1.00 0.00 N ATOM 70 H ASN A 4 3.337 0.446 2.460 1.00 0.00 H ATOM 71 HA ASN A 4 3.778 -2.053 0.929 1.00 0.00 H ATOM 72 HB2 ASN A 4 3.655 -3.238 2.996 1.00 0.00 H ATOM 73 HB3 ASN A 4 4.661 -1.830 3.335 1.00 0.00 H ATOM 74 HD21 ASN A 4 2.311 -3.561 4.780 1.00 0.00 H ATOM 75 HD22 ASN A 4 1.474 -2.335 5.603 1.00 0.00 H ATOM 76 N ALA A 5 1.176 -0.583 0.971 1.00 0.00 N ATOM 77 CA ALA A 5 -0.289 -0.578 0.746 1.00 0.00 C ATOM 78 C ALA A 5 -0.661 0.468 -0.309 1.00 0.00 C ATOM 79 O ALA A 5 -1.438 1.367 -0.057 1.00 0.00 O ATOM 80 CB ALA A 5 -0.897 -0.218 2.102 1.00 0.00 C ATOM 81 H ALA A 5 1.706 0.186 0.706 1.00 0.00 H ATOM 82 HA ALA A 5 -0.614 -1.551 0.442 1.00 0.00 H ATOM 83 HB1 ALA A 5 -0.241 -0.554 2.892 1.00 0.00 H ATOM 84 HB2 ALA A 5 -1.859 -0.697 2.205 1.00 0.00 H ATOM 85 HB3 ALA A 5 -1.019 0.854 2.169 1.00 0.00 H ATOM 86 N PHE A 6 -0.117 0.356 -1.491 1.00 0.00 N ATOM 87 CA PHE A 6 -0.443 1.338 -2.554 1.00 0.00 C ATOM 88 C PHE A 6 -0.102 0.768 -3.933 1.00 0.00 C ATOM 89 O PHE A 6 -0.973 0.398 -4.696 1.00 0.00 O ATOM 90 CB PHE A 6 0.418 2.565 -2.246 1.00 0.00 C ATOM 91 CG PHE A 6 -0.423 3.813 -2.366 1.00 0.00 C ATOM 92 CD1 PHE A 6 -1.207 4.022 -3.507 1.00 0.00 C ATOM 93 CD2 PHE A 6 -0.419 4.761 -1.336 1.00 0.00 C ATOM 94 CE1 PHE A 6 -1.987 5.179 -3.618 1.00 0.00 C ATOM 95 CE2 PHE A 6 -1.199 5.918 -1.447 1.00 0.00 C ATOM 96 CZ PHE A 6 -1.983 6.127 -2.588 1.00 0.00 C ATOM 97 H PHE A 6 0.498 -0.371 -1.679 1.00 0.00 H ATOM 98 HA PHE A 6 -1.477 1.594 -2.505 1.00 0.00 H ATOM 99 HB2 PHE A 6 0.807 2.487 -1.241 1.00 0.00 H ATOM 100 HB3 PHE A 6 1.237 2.616 -2.947 1.00 0.00 H ATOM 101 HD1 PHE A 6 -1.210 3.290 -4.302 1.00 0.00 H ATOM 102 HD2 PHE A 6 0.187 4.599 -0.456 1.00 0.00 H ATOM 103 HE1 PHE A 6 -2.592 5.340 -4.497 1.00 0.00 H ATOM 104 HE2 PHE A 6 -1.195 6.650 -0.652 1.00 0.00 H ATOM 105 HZ PHE A 6 -2.585 7.020 -2.673 1.00 0.00 H ATOM 106 N GLY A 7 1.157 0.698 -4.258 1.00 0.00 N ATOM 107 CA GLY A 7 1.556 0.155 -5.588 1.00 0.00 C ATOM 108 C GLY A 7 1.827 -1.345 -5.472 1.00 0.00 C ATOM 109 O GLY A 7 2.109 -2.012 -6.448 1.00 0.00 O ATOM 110 H GLY A 7 1.841 1.003 -3.628 1.00 0.00 H ATOM 111 HA2 GLY A 7 0.759 0.325 -6.298 1.00 0.00 H ATOM 112 HA3 GLY A 7 2.451 0.654 -5.926 1.00 0.00 H ATOM 113 N LEU A 8 1.748 -1.883 -4.285 1.00 0.00 N ATOM 114 CA LEU A 8 2.003 -3.333 -4.106 1.00 0.00 C ATOM 115 C LEU A 8 0.701 -4.062 -3.766 1.00 0.00 C ATOM 116 O LEU A 8 0.264 -4.941 -4.481 1.00 0.00 O ATOM 117 CB LEU A 8 2.993 -3.443 -2.939 1.00 0.00 C ATOM 118 CG LEU A 8 3.996 -2.289 -2.991 1.00 0.00 C ATOM 119 CD1 LEU A 8 5.064 -2.491 -1.915 1.00 0.00 C ATOM 120 CD2 LEU A 8 4.661 -2.253 -4.369 1.00 0.00 C ATOM 121 H LEU A 8 1.526 -1.338 -3.517 1.00 0.00 H ATOM 122 HA LEU A 8 2.438 -3.735 -4.994 1.00 0.00 H ATOM 123 HB2 LEU A 8 2.451 -3.406 -2.005 1.00 0.00 H ATOM 124 HB3 LEU A 8 3.524 -4.380 -3.008 1.00 0.00 H ATOM 125 HG LEU A 8 3.479 -1.357 -2.814 1.00 0.00 H ATOM 126 HD11 LEU A 8 5.739 -1.648 -1.915 1.00 0.00 H ATOM 127 HD12 LEU A 8 5.618 -3.395 -2.123 1.00 0.00 H ATOM 128 HD13 LEU A 8 4.590 -2.574 -0.949 1.00 0.00 H ATOM 129 HD21 LEU A 8 5.703 -2.518 -4.273 1.00 0.00 H ATOM 130 HD22 LEU A 8 4.579 -1.259 -4.783 1.00 0.00 H ATOM 131 HD23 LEU A 8 4.169 -2.957 -5.024 1.00 0.00 H ATOM 132 N ARG A 9 0.082 -3.705 -2.674 1.00 0.00 N ATOM 133 CA ARG A 9 -1.182 -4.376 -2.281 1.00 0.00 C ATOM 134 C ARG A 9 -2.356 -3.815 -3.087 1.00 0.00 C ATOM 135 O ARG A 9 -3.375 -4.457 -3.247 1.00 0.00 O ATOM 136 CB ARG A 9 -1.353 -4.062 -0.794 1.00 0.00 C ATOM 137 CG ARG A 9 -0.762 -5.200 0.042 1.00 0.00 C ATOM 138 CD ARG A 9 -0.516 -4.709 1.470 1.00 0.00 C ATOM 139 NE ARG A 9 -1.317 -5.622 2.332 1.00 0.00 N ATOM 140 CZ ARG A 9 -1.011 -5.767 3.592 1.00 0.00 C ATOM 141 NH1 ARG A 9 -1.529 -4.969 4.486 1.00 0.00 N ATOM 142 NH2 ARG A 9 -0.188 -6.711 3.959 1.00 0.00 N ATOM 143 H ARG A 9 0.451 -3.005 -2.110 1.00 0.00 H ATOM 144 HA ARG A 9 -1.094 -5.434 -2.424 1.00 0.00 H ATOM 145 HB2 ARG A 9 -0.841 -3.139 -0.560 1.00 0.00 H ATOM 146 HB3 ARG A 9 -2.403 -3.959 -0.566 1.00 0.00 H ATOM 147 HG2 ARG A 9 -1.453 -6.030 0.059 1.00 0.00 H ATOM 148 HG3 ARG A 9 0.173 -5.518 -0.394 1.00 0.00 H ATOM 149 HD2 ARG A 9 0.535 -4.781 1.716 1.00 0.00 H ATOM 150 HD3 ARG A 9 -0.861 -3.694 1.585 1.00 0.00 H ATOM 151 HE ARG A 9 -2.074 -6.115 1.952 1.00 0.00 H ATOM 152 HH11 ARG A 9 -2.161 -4.247 4.205 1.00 0.00 H ATOM 153 HH12 ARG A 9 -1.295 -5.081 5.452 1.00 0.00 H ATOM 154 HH21 ARG A 9 0.208 -7.323 3.275 1.00 0.00 H ATOM 155 HH22 ARG A 9 0.046 -6.822 4.925 1.00 0.00 H ATOM 156 N PHE A 10 -2.222 -2.621 -3.595 1.00 0.00 N ATOM 157 CA PHE A 10 -3.331 -2.020 -4.391 1.00 0.00 C ATOM 158 C PHE A 10 -2.873 -1.767 -5.830 1.00 0.00 C ATOM 159 O PHE A 10 -1.707 -1.995 -6.109 1.00 0.00 O ATOM 160 CB PHE A 10 -3.652 -0.700 -3.688 1.00 0.00 C ATOM 161 CG PHE A 10 -4.560 -0.965 -2.510 1.00 0.00 C ATOM 162 CD1 PHE A 10 -4.065 -1.623 -1.377 1.00 0.00 C ATOM 163 CD2 PHE A 10 -5.897 -0.553 -2.552 1.00 0.00 C ATOM 164 CE1 PHE A 10 -4.909 -1.870 -0.287 1.00 0.00 C ATOM 165 CE2 PHE A 10 -6.740 -0.799 -1.462 1.00 0.00 C ATOM 166 CZ PHE A 10 -6.246 -1.458 -0.329 1.00 0.00 C ATOM 167 OXT PHE A 10 -3.696 -1.351 -6.629 1.00 0.00 O ATOM 168 H PHE A 10 -1.392 -2.119 -3.455 1.00 0.00 H ATOM 169 HA PHE A 10 -4.196 -2.664 -4.378 1.00 0.00 H ATOM 170 HB2 PHE A 10 -2.735 -0.244 -3.341 1.00 0.00 H ATOM 171 HB3 PHE A 10 -4.146 -0.034 -4.380 1.00 0.00 H ATOM 172 HD1 PHE A 10 -3.034 -1.941 -1.345 1.00 0.00 H ATOM 173 HD2 PHE A 10 -6.278 -0.045 -3.425 1.00 0.00 H ATOM 174 HE1 PHE A 10 -4.527 -2.378 0.586 1.00 0.00 H ATOM 175 HE2 PHE A 10 -7.771 -0.481 -1.494 1.00 0.00 H ATOM 176 HZ PHE A 10 -6.896 -1.648 0.511 1.00 0.00 H TER 177 PHE A 10 MASTER 108 0 0 0 0 0 0 6 93 1 0 1 END