HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 11-MAY-04 1WD5
TITLE CRYSTAL STRUCTURE OF TT1426 FROM THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN TT1426;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS STRUCTURAL GENOMICS, HYPOTHETICAL PROTEIN, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SHIBATA,M.KUKIMOTO-NIINO,K.MURAYAMA,M.SHIROUZU,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 24-FEB-09 1WD5 1 VERSN
REVDAT 2 08-MAR-05 1WD5 1 AUTHOR JRNL KEYWDS REMARK
REVDAT 1 11-NOV-04 1WD5 0
JRNL AUTH M.KUKIMOTO-NIINO,R.SHIBATA,K.MURAYAMA,H.HAMANA,
JRNL AUTH 2 M.NISHIMOTO,Y.BESSHO,T.TERADA,M.SHIROUZU,
JRNL AUTH 3 S.KURAMITSU,S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF A PREDICTED
JRNL TITL 2 PHOSPHORIBOSYLTRANSFERASE (TT1426) FROM THERMUS
JRNL TITL 3 THERMOPHILUS HB8 AT 2.01 A RESOLUTION
JRNL REF PROTEIN SCI. V. 14 823 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 15689504
JRNL DOI 10.1110/PS.041229405
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 219596.220
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.1
REMARK 3 NUMBER OF REFLECTIONS : 18107
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1530
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 44.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2561
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 113
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1578
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 224
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 6.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.50000
REMARK 3 B22 (A**2) : 4.50000
REMARK 3 B33 (A**2) : -8.99000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.20
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.74
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.220 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.890 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.370 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.460 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 57.80
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : MES.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : MES.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WD5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAY-04.
REMARK 100 THE RCSB ID CODE IS RCSB023449.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97910, 0.97938, 0.97400
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31382
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 7.380
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.30300
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.64350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 51.98500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 51.98500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 12.82175
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 51.98500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 51.98500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 38.46525
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 51.98500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.98500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 12.82175
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 51.98500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.98500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 38.46525
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 25.64350
REMARK 290
REMARK 290 REMARK: NULL
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 ALA A 24 61.08 36.46
REMARK 500 ALA A 182 -85.46 -95.63
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 MES A 2955
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003001426 RELATED DB: TARGETDB
DBREF 1WD5 A 1 208 UNP Q5SIB2 Q5SIB2_THET8 1 208
SEQRES 1 A 208 MSE ARG PHE ARG ASP ARG ARG HIS ALA GLY ALA LEU LEU
SEQRES 2 A 208 ALA GLU ALA LEU ALA PRO LEU GLY LEU GLU ALA PRO VAL
SEQRES 3 A 208 VAL LEU GLY LEU PRO ARG GLY GLY VAL VAL VAL ALA ASP
SEQRES 4 A 208 GLU VAL ALA ARG ARG LEU GLY GLY GLU LEU ASP VAL VAL
SEQRES 5 A 208 LEU VAL ARG LYS VAL GLY ALA PRO GLY ASN PRO GLU PHE
SEQRES 6 A 208 ALA LEU GLY ALA VAL GLY GLU GLY GLY GLU LEU VAL LEU
SEQRES 7 A 208 MSE PRO TYR ALA LEU ARG TYR ALA ASP GLN SER TYR LEU
SEQRES 8 A 208 GLU ARG GLU ALA ALA ARG GLN ARG ASP VAL LEU ARG LYS
SEQRES 9 A 208 ARG ALA GLU ARG TYR ARG ARG VAL ARG PRO LYS ALA ALA
SEQRES 10 A 208 ARG LYS GLY ARG ASP VAL VAL LEU VAL ASP ASP GLY VAL
SEQRES 11 A 208 ALA THR GLY ALA SER MSE GLU ALA ALA LEU SER VAL VAL
SEQRES 12 A 208 PHE GLN GLU GLY PRO ARG ARG VAL VAL VAL ALA VAL PRO
SEQRES 13 A 208 VAL ALA SER PRO GLU ALA VAL GLU ARG LEU LYS ALA ARG
SEQRES 14 A 208 ALA GLU VAL VAL ALA LEU SER VAL PRO GLN ASP PHE ALA
SEQRES 15 A 208 ALA VAL GLY ALA TYR TYR LEU ASP PHE GLY GLU VAL THR
SEQRES 16 A 208 ASP GLU ASP VAL GLU ALA ILE LEU LEU GLU TRP ALA GLY
MODRES 1WD5 MSE A 1 MET SELENOMETHIONINE
MODRES 1WD5 MSE A 79 MET SELENOMETHIONINE
MODRES 1WD5 MSE A 136 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 79 8
HET MSE A 136 8
HET MES A2955 12
HETNAM MSE SELENOMETHIONINE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 2 MES C6 H13 N O4 S
FORMUL 3 HOH *224(H2 O)
HELIX 1 1 ASP A 5 ALA A 18 1 14
HELIX 2 2 PRO A 19 GLY A 21 5 3
HELIX 3 3 ARG A 32 GLY A 46 1 15
HELIX 4 4 TYR A 81 ALA A 86 1 6
HELIX 5 5 ASP A 87 ARG A 113 1 27
HELIX 6 6 GLY A 133 GLN A 145 1 13
HELIX 7 7 SER A 159 ALA A 168 1 10
HELIX 8 8 ALA A 183 TYR A 188 5 6
HELIX 9 9 THR A 195 GLU A 205 1 11
SHEET 1 A 5 GLU A 48 VAL A 51 0
SHEET 2 A 5 VAL A 26 GLY A 29 1 N VAL A 27 O GLU A 48
SHEET 3 A 5 ASP A 122 VAL A 126 1 O VAL A 124 N LEU A 28
SHEET 4 A 5 ARG A 150 VAL A 157 1 O ALA A 154 N LEU A 125
SHEET 5 A 5 GLU A 171 SER A 176 1 O VAL A 173 N VAL A 153
SHEET 1 B 3 VAL A 54 ALA A 59 0
SHEET 2 B 3 ASN A 62 GLY A 71 -1 O LEU A 67 N VAL A 57
SHEET 3 B 3 LEU A 76 LEU A 78 -1 O VAL A 77 N ALA A 69
LINK C MSE A 1 N ARG A 2 1555 1555 1.33
LINK C LEU A 78 N MSE A 79 1555 1555 1.33
LINK C MSE A 79 N PRO A 80 1555 1555 1.34
LINK C SER A 135 N MSE A 136 1555 1555 1.33
LINK C MSE A 136 N GLU A 137 1555 1555 1.33
CISPEP 1 PRO A 31 ARG A 32 0 -1.06
SITE 1 AC1 6 LEU A 12 GLU A 15 TYR A 90 ARG A 93
SITE 2 AC1 6 ARG A 97 HOH A1170
CRYST1 103.970 103.970 51.287 90.00 90.00 90.00 P 41 21 2 8
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 0.009618 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019498 0.00000
HETATM 1 N MSE A 1 23.887 40.551 -19.527 1.00 48.72 N
HETATM 2 CA MSE A 1 22.889 40.951 -20.563 1.00 48.52 C
HETATM 3 C MSE A 1 22.377 42.358 -20.247 1.00 45.86 C
HETATM 4 O MSE A 1 22.996 43.085 -19.468 1.00 45.36 O
HETATM 5 CB MSE A 1 21.731 39.945 -20.577 1.00 53.21 C
HETATM 6 CG MSE A 1 20.871 39.984 -21.831 1.00 59.07 C
HETATM 7 SE MSE A 1 19.896 38.474 -22.046 1.00 72.29 SE
HETATM 8 CE MSE A 1 20.997 37.481 -23.070 1.00 64.87 C
(ATOM LINES ARE NOT SHOWN.)
END
