HEADER TRANSPORT PROTEIN 12-JAN-10 2KSQ
TITLE THE MYRISTOYLATED YEAST ARF1 IN A GTP AND BICELLE BOUND CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-RIBOSYLATION FACTOR 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: ARF1, YDL192W, D1244;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET20(B)
KEYWDS ARF, MYRISTOYLATED, MYRISTOYL, GTP, BICELLE, ER-GOLGI TRANSPORT,
KEYWDS 2 GOLGI APPARATUS, GTP-BINDING, LIPOPROTEIN, MYRISTATE, NUCLEOTIDE-
KEYWDS 3 BINDING, PROTEIN TRANSPORT, TRANSPORT, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.LIU,R.KAHN,J.PRESTEGARD
REVDAT 5 27-JUL-11 2KSQ 1 REMARK REVDAT
REVDAT 4 13-JUL-11 2KSQ 1 VERSN
REVDAT 3 18-MAY-11 2KSQ 1 HETNAM
REVDAT 2 21-JUL-10 2KSQ 1 JRNL
REVDAT 1 07-JUL-10 2KSQ 0
JRNL AUTH Y.LIU,R.A.KAHN,J.H.PRESTEGARD
JRNL TITL DYNAMIC STRUCTURE OF MEMBRANE-ANCHORED ARF*GTP.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 876 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20601958
JRNL DOI 10.1038/NSMB.1853
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR_NIH
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KSQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-10.
REMARK 100 THE RCSB ID CODE IS RCSB101527.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8 MM [U-13C; U-15N; U-2H]
REMARK 210 PROTEIN, 95% H2O/5% D2O; 0.8 MM
REMARK 210 [VI(D1)L-METHYL-1H,13C; U-15N; U-
REMARK 210 2H] PROTEIN, 95% H2O/5% D2O; 0.8
REMARK 210 MM [PHE-1H,13C; U-15N; U-2H]
REMARK 210 PROTEIN, 95% H2O/5% D2O; 0.8 MM
REMARK 210 [U-100% 13C; U-100% 15N; U-70%
REMARK 210 2H] PROTEIN, 95% H2O/5% D2O; 0.3
REMARK 210 MM [U-15N; 70%-2H] PROTEIN, 95%
REMARK 210 H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HNCA; 3D HN(CA)CB; 3D HN(CO)
REMARK 210 CA; 3D C-EXCITED C-CMHM TOCSY; 3D
REMARK 210 NOESY-CH-HMQC; 3D NOESY-NH-TROSY;
REMARK 210 3D NOESY-AROMCH-CT-TROSY; 3D HCCH
REMARK 210 -TOCSY; 2D HSQC-TROSY; 2D JMOD-
REMARK 210 NC'; 2D JMOD-NH; 2D 1H-15N FAST
REMARK 210 HSQC; 2D 1H-R1 HSQC; 2D AROM-CT-
REMARK 210 TROSY 1H IPAP
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMRJ, NMRPIPE, SPARKY, X-PLOR_
REMARK 210 NIH
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 280
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H GLY A 29 O1B GTP A 187 1.57
REMARK 500
REMARK 500 REMARK: NULL
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 1 ILE A 49 70.69 -103.00
REMARK 500 1 ASN A 60 -0.18 75.13
REMARK 500 1 TYR A 82 25.00 81.95
REMARK 500 1 CYS A 83 101.81 38.27
REMARK 500 1 ASN A 84 -28.37 -179.59
REMARK 500 1 ASP A 96 78.63 -111.04
REMARK 500 1 PRO A 152 97.07 -67.72
REMARK 500 1 ASN A 179 -65.75 67.34
REMARK 500 2 LEU A 25 -164.51 -122.08
REMARK 500 2 CYS A 83 -70.77 67.19
REMARK 500 2 ASN A 84 62.40 -168.43
REMARK 500 2 ASP A 96 79.90 -113.40
REMARK 500 2 ASN A 179 30.29 -90.07
REMARK 500 3 LYS A 16 -81.98 -119.32
REMARK 500 3 LEU A 25 -164.25 -56.74
REMARK 500 3 ASN A 60 -1.70 76.35
REMARK 500 3 GLN A 71 -87.84 -143.15
REMARK 500 3 CYS A 83 -80.20 62.56
REMARK 500 3 ASN A 84 62.93 -156.20
REMARK 500 3 ASP A 96 79.39 -115.41
REMARK 500 3 PRO A 152 95.53 -67.88
REMARK 500 3 ASN A 179 61.39 35.07
REMARK 500 3 SER A 180 104.65 61.46
REMARK 500 4 LYS A 16 41.89 177.50
REMARK 500 4 HIS A 80 -40.36 -130.21
REMARK 500 4 ASP A 96 78.53 -108.91
REMARK 500 4 PRO A 152 95.87 -67.21
REMARK 500 4 SER A 180 -47.66 -154.46
REMARK 500 5 PRO A 47 108.46 -57.43
REMARK 500 5 ASN A 60 -0.58 75.30
REMARK 500 5 HIS A 80 17.69 -150.23
REMARK 500 5 TYR A 82 -73.18 -127.21
REMARK 500 5 ASN A 84 29.25 -162.76
REMARK 500 5 ASP A 96 76.69 -109.71
REMARK 500 5 PRO A 152 95.50 -67.43
REMARK 500 5 LEU A 177 -61.84 -95.03
REMARK 500 5 ASN A 179 62.82 34.67
REMARK 500 5 SER A 180 168.11 59.37
REMARK 500 6 ASN A 15 113.65 61.43
REMARK 500 6 LYS A 16 104.73 -51.87
REMARK 500 6 ASN A 60 -2.74 76.30
REMARK 500 6 GLN A 71 -126.01 73.20
REMARK 500 6 HIS A 80 26.97 -158.40
REMARK 500 6 TYR A 82 -67.06 -155.51
REMARK 500 6 ASN A 84 25.59 -149.48
REMARK 500 6 ASP A 96 79.48 -110.48
REMARK 500 6 PRO A 152 99.77 -67.34
REMARK 500 7 ASN A 15 -87.10 55.85
REMARK 500 7 LYS A 16 62.43 -115.89
REMARK 500 7 ASN A 60 -0.73 75.59
REMARK 500
REMARK 500 THIS ENTRY HAS 183 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTN A 182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTN A 183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTN A 184
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTN A 185
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTN A 186
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 187
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A MYRISTOYL GROUP (DERIVED FROM MYRISTIC ACID) IS COVALENTLY
REMARK 999 ATTACHED TO THE N-TERMINUS VIA AN AMIDE BOND. FURTHERMORE, WILD-
REMARK 999 TYPE PROTEIN WAS USED FOR ALL EXPERIMENTS (NOESY AND RDC) EXCEPT
REMARK 999 FOR THE PRE EXPERIMENTS WHICH REQUIRES A X-TO-CYS MUTATION. THE CYS
REMARK 999 MUTATIONS ARE NOT SIMULTANEOUSLY PRESENT BUT ONE AT A TIME. HOWEVER
REMARK 999 THE PRE DATA WERE COMBINED DURING CALCULATION AND THEREFORE IT
REMARK 999 APPEARS ALL THESE RESIDUES ARE REPLACED BY CYS IN THE FINAL PDB.
DBREF 2KSQ A 2 181 UNP P11076 ARF1_YEAST 2 181
SEQADV 2KSQ MYR A 1 UNP P11076 SEE REMARK 999
SEQADV 2KSQ CYS A 55 UNP P11076 THR 55 SEE REMARK 999
SEQADV 2KSQ CYS A 59 UNP P11076 LYS 59 SEE REMARK 999
SEQADV 2KSQ CYS A 83 UNP P11076 ARG 83 SEE REMARK 999
SEQADV 2KSQ CYS A 117 UNP P11076 ARG 117 SEE REMARK 999
SEQADV 2KSQ CYS A 176 UNP P11076 SER 176 SEE REMARK 999
SEQRES 1 A 181 MYR GLY LEU PHE ALA SER LYS LEU PHE SER ASN LEU PHE
SEQRES 2 A 181 GLY ASN LYS GLU MET ARG ILE LEU MET VAL GLY LEU ASP
SEQRES 3 A 181 GLY ALA GLY LYS THR THR VAL LEU TYR LYS LEU LYS LEU
SEQRES 4 A 181 GLY GLU VAL ILE THR THR ILE PRO THR ILE GLY PHE ASN
SEQRES 5 A 181 VAL GLU CYS VAL GLN TYR CYS ASN ILE SER PHE THR VAL
SEQRES 6 A 181 TRP ASP VAL GLY GLY GLN ASP ARG ILE ARG SER LEU TRP
SEQRES 7 A 181 ARG HIS TYR TYR CYS ASN THR GLU GLY VAL ILE PHE VAL
SEQRES 8 A 181 VAL ASP SER ASN ASP ARG SER ARG ILE GLY GLU ALA ARG
SEQRES 9 A 181 GLU VAL MET GLN ARG MET LEU ASN GLU ASP GLU LEU CYS
SEQRES 10 A 181 ASN ALA ALA TRP LEU VAL PHE ALA ASN LYS GLN ASP LEU
SEQRES 11 A 181 PRO GLU ALA MET SER ALA ALA GLU ILE THR GLU LYS LEU
SEQRES 12 A 181 GLY LEU HIS SER ILE ARG ASN ARG PRO TRP PHE ILE GLN
SEQRES 13 A 181 ALA THR CYS ALA THR SER GLY GLU GLY LEU TYR GLU GLY
SEQRES 14 A 181 LEU GLU TRP LEU SER ASN CYS LEU LYS ASN SER THR
HET MYR A 1 42
HET MTN A 182 81
HET MTN A 183 81
HET MTN A 184 81
HET MTN A 185 81
HET MTN A 186 81
HET GTP A 187 43
HETNAM MYR MYRISTIC ACID
HETNAM MTN S-[(1-OXYL-2,2,5,5-TETRAMETHYL-2,5-DIHYDRO-1H-PYRROL-3-
HETNAM 2 MTN YL)METHYL] METHANESULFONOTHIOATE
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETSYN MTN MTSL
FORMUL 1 MYR C14 H28 O2
FORMUL 2 MTN 5(C10 H18 N O3 S2)
FORMUL 7 GTP C10 H16 N5 O14 P3
HELIX 1 1 GLY A 2 ASN A 11 1 10
HELIX 2 2 LEU A 12 GLY A 14 5 3
HELIX 3 3 GLY A 29 GLY A 40 1 12
HELIX 4 4 GLN A 71 SER A 76 1 6
HELIX 5 5 LEU A 77 TYR A 81 5 5
HELIX 6 6 ARG A 99 ASN A 112 1 14
HELIX 7 7 GLU A 113 CYS A 117 5 5
HELIX 8 8 SER A 135 LEU A 143 1 9
HELIX 9 9 GLY A 165 LYS A 178 1 14
SHEET 1 A 3 PHE A 51 ASN A 52 0
SHEET 2 A 3 ILE A 61 VAL A 68 -1 O ASP A 67 N ASN A 52
SHEET 3 A 3 CYS A 55 TYR A 58 -1 N TYR A 58 O ILE A 61
SHEET 1 B 6 PHE A 51 ASN A 52 0
SHEET 2 B 6 ILE A 61 VAL A 68 -1 O ASP A 67 N ASN A 52
SHEET 3 B 6 GLU A 17 GLY A 24 1 N MET A 22 O TRP A 66
SHEET 4 B 6 GLY A 87 ASP A 93 1 O ILE A 89 N LEU A 21
SHEET 5 B 6 TRP A 121 ASN A 126 1 O LEU A 122 N VAL A 88
SHEET 6 B 6 TRP A 153 ALA A 157 1 O PHE A 154 N VAL A 123
LINK C1 MYR A 1 N GLY A 2 1555 1555 1.33
LINK SG CYS A 55 S1 AMTN A 182 1555 1555 2.03
LINK SG CYS A 55 S1 BMTN A 182 1555 1555 2.03
LINK SG CYS A 55 S1 CMTN A 182 1555 1555 2.03
LINK SG CYS A 59 S1 AMTN A 183 1555 1555 2.03
LINK SG CYS A 59 S1 BMTN A 183 1555 1555 2.03
LINK SG CYS A 59 S1 CMTN A 183 1555 1555 2.03
LINK SG CYS A 83 S1 AMTN A 184 1555 1555 2.03
LINK SG CYS A 83 S1 BMTN A 184 1555 1555 2.03
LINK SG CYS A 83 S1 CMTN A 184 1555 1555 2.03
LINK SG CYS A 117 S1 AMTN A 185 1555 1555 2.03
LINK SG CYS A 117 S1 BMTN A 185 1555 1555 2.03
LINK SG CYS A 117 S1 CMTN A 185 1555 1555 2.03
LINK SG CYS A 176 S1 AMTN A 186 1555 1555 2.03
LINK SG CYS A 176 S1 BMTN A 186 1555 1555 2.03
LINK SG CYS A 176 S1 CMTN A 186 1555 1555 2.03
SITE 1 AC1 1 CYS A 55
SITE 1 AC2 1 CYS A 59
SITE 1 AC3 2 HIS A 80 CYS A 83
SITE 1 AC4 5 ASN A 112 GLU A 113 ASP A 114 CYS A 117
SITE 2 AC4 5 ARG A 151
SITE 1 AC5 3 ASN A 175 CYS A 176 LYS A 178
SITE 1 AC6 16 ASP A 26 GLY A 27 ALA A 28 GLY A 29
SITE 2 AC6 16 LYS A 30 THR A 31 THR A 32 THR A 45
SITE 3 AC6 16 ILE A 46 THR A 48 GLY A 69 GLY A 70
SITE 4 AC6 16 ASN A 126 ASP A 129 ALA A 160 THR A 161
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
MODEL 1
HETATM 1 C1 MYR A 1 -8.173 -35.221 8.275 1.00 0.00 C
HETATM 2 O1 MYR A 1 -9.137 -34.513 8.570 1.00 0.00 O
HETATM 3 C2 MYR A 1 -8.201 -36.100 7.040 1.00 0.00 C
HETATM 4 C3 MYR A 1 -7.982 -35.315 5.757 1.00 0.00 C
HETATM 5 C4 MYR A 1 -9.285 -34.727 5.236 1.00 0.00 C
HETATM 6 C5 MYR A 1 -9.106 -34.116 3.856 1.00 0.00 C
HETATM 7 C6 MYR A 1 -10.392 -34.178 3.048 1.00 0.00 C
HETATM 8 C7 MYR A 1 -11.202 -32.900 3.191 1.00 0.00 C
HETATM 9 C8 MYR A 1 -11.609 -32.656 4.636 1.00 0.00 C
HETATM 10 C9 MYR A 1 -12.943 -31.934 4.724 1.00 0.00 C
HETATM 11 C10 MYR A 1 -13.477 -31.922 6.147 1.00 0.00 C
HETATM 12 C11 MYR A 1 -14.989 -31.764 6.174 1.00 0.00 C
HETATM 13 C12 MYR A 1 -15.558 -32.072 7.549 1.00 0.00 C
HETATM 14 C13 MYR A 1 -17.046 -32.370 7.482 1.00 0.00 C
HETATM 15 C14 MYR A 1 -17.922 -31.151 7.686 1.00 0.00 C
HETATM 16 H21 MYR A 1 -9.161 -36.589 6.987 1.00 0.00 H
HETATM 17 H22 MYR A 1 -7.422 -36.845 7.129 1.00 0.00 H
HETATM 18 H31 MYR A 1 -7.571 -35.976 5.009 1.00 0.00 H
HETATM 19 H32 MYR A 1 -7.289 -34.510 5.952 1.00 0.00 H
HETATM 20 H41 MYR A 1 -9.621 -33.963 5.920 1.00 0.00 H
HETATM 21 H42 MYR A 1 -10.024 -35.512 5.178 1.00 0.00 H
HETATM 22 H51 MYR A 1 -8.334 -34.657 3.330 1.00 0.00 H
HETATM 23 H52 MYR A 1 -8.812 -33.083 3.967 1.00 0.00 H
HETATM 24 H61 MYR A 1 -10.985 -35.010 3.398 1.00 0.00 H
HETATM 25 H62 MYR A 1 -10.145 -34.322 2.007 1.00 0.00 H
HETATM 26 H71 MYR A 1 -12.093 -32.980 2.584 1.00 0.00 H
HETATM 27 H72 MYR A 1 -10.606 -32.068 2.851 1.00 0.00 H
HETATM 28 H81 MYR A 1 -10.851 -32.055 5.117 1.00 0.00 H
HETATM 29 H82 MYR A 1 -11.692 -33.607 5.141 1.00 0.00 H
HETATM 30 H91 MYR A 1 -13.656 -32.434 4.086 1.00 0.00 H
HETATM 31 H92 MYR A 1 -12.813 -30.914 4.392 1.00 0.00 H
HETATM 32 H101 MYR A 1 -13.028 -31.100 6.684 1.00 0.00 H
HETATM 33 H102 MYR A 1 -13.216 -32.853 6.627 1.00 0.00 H
HETATM 34 H111 MYR A 1 -15.425 -32.439 5.453 1.00 0.00 H
HETATM 35 H112 MYR A 1 -15.238 -30.745 5.913 1.00 0.00 H
HETATM 36 H121 MYR A 1 -15.398 -31.219 8.193 1.00 0.00 H
HETATM 37 H122 MYR A 1 -15.047 -32.932 7.954 1.00 0.00 H
HETATM 38 H131 MYR A 1 -17.291 -33.091 8.248 1.00 0.00 H
HETATM 39 H132 MYR A 1 -17.274 -32.785 6.512 1.00 0.00 H
HETATM 40 H141 MYR A 1 -17.464 -30.498 8.413 1.00 0.00 H
HETATM 41 H142 MYR A 1 -18.892 -31.462 8.041 1.00 0.00 H
HETATM 42 H143 MYR A 1 -18.032 -30.626 6.749 1.00 0.00 H
(ATOM LINES ARE NOT SHOWN.)
END
