HEADER MOTOR PROTEIN 26-AUG-09 3A69
TITLE ATOMIC MODEL OF THE BACTERIAL FLAGELLAR HOOK BASED ON
TITLE 2 DOCKING AN X-RAY DERIVED STRUCTURE AND TERMINAL TWO ALPHA-
TITLE 3 HELICES INTO AN 7.1 ANGSTROM RESOLUTION CRYOEM MAP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAGELLAR HOOK PROTEIN FLGE;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA
SOURCE 3 SEROVAR TYPHIMURIUM;
SOURCE 4 ORGANISM_TAXID: 90371;
SOURCE 5 STRAIN: SJW880
KEYWDS THE BACTERIAL FLAGELLAR MOTOR, UNIVERSAL JOINT, BACTERIAL
KEYWDS 2 FLAGELLUM, MOTOR PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR T.FUJII,T.KATO,K.NAMBA
REVDAT 1 15-DEC-09 3A69 0
JRNL AUTH T.FUJII,T.KATO,K.NAMBA
JRNL TITL SPECIFIC ARRANGEMENT OF ALPHA-HELICAL COILED COILS
JRNL TITL 2 IN THE CORE DOMAIN OF THE BACTERIAL FLAGELLAR HOOK
JRNL TITL 3 FOR THE UNIVERSAL JOINT FUNCTION
JRNL REF STRUCTURE V. 17 1485 2009
JRNL REFN ISSN 0969-2126
JRNL PMID 19913483
JRNL DOI 10.1016/J.STR.2009.08.017
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 7.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : IHRSR
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : 1.680
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 7.100
REMARK 3 NUMBER OF PARTICLES : NULL
REMARK 3 CTF CORRECTION METHOD : EACH IMAGES
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: TMV IMAGES
REMARK 3
REMARK 3 OTHER DETAILS: A MODIFIED VERSION OF SPIDER PROGRAM WAS USED
REMARK 3 FOR THE RECONSTRUCTION
REMARK 4
REMARK 4 3A69 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB028863.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : HELICAL
REMARK 245 SPECIMEN TYPE : VITREOUS ICE (CRYO EM)
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : FILAMENT
REMARK 245 PARTICLE TYPE : NULL
REMARK 245 NAME OF SAMPLE : BACTERIAL FLAGELLAR HOOK
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : 20MM TRIS-HCL, 100MM NACL
REMARK 245 PH : 7.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 20-FEB-08
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 50.00
REMARK 245 MICROSCOPE MODEL : OTHER
REMARK 245 DETECTOR TYPE : 16 MEGAPIXELS SLOW-SCAN
REMARK 245 CCD CAMERA, TEMCAM-F415MP
REMARK 245 MINIMUM DEFOCUS (NM) : 500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 1.60
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 20.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 50000
REMARK 245 CALIBRATED MAGNIFICATION : 89285
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
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
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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR
REMARK 300 HELICAL SYMMETRY WITH THE FOLLOWING PARAMETERS:
REMARK 300 ROTATION PER SUBUNIT (TWIST) = 64.79 DEGREES
REMARK 300 RISE PER SUBUNIT (HEIGHT) = 4.12 ANGSTROMS
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 0.808298 -0.588773 0.000000 0.00000
REMARK 350 BIOMT2 1 0.588773 0.808298 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 -20.61500
REMARK 350 BIOMT1 2 -0.188341 -0.982104 0.000000 0.00000
REMARK 350 BIOMT2 2 0.982104 -0.188341 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -16.49200
REMARK 350 BIOMT1 3 -0.968765 -0.247980 0.000000 0.00000
REMARK 350 BIOMT2 3 0.247980 -0.968765 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 -12.36900
REMARK 350 BIOMT1 4 -0.637047 0.770825 0.000000 0.00000
REMARK 350 BIOMT2 4 -0.770825 -0.637047 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 -8.24600
REMARK 350 BIOMT1 5 0.426000 0.904723 0.000000 0.00000
REMARK 350 BIOMT2 5 -0.904723 0.426000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 -4.12300
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 7 0.426000 -0.904723 0.000000 0.00000
REMARK 350 BIOMT2 7 0.904723 0.426000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 1.000000 4.12300
REMARK 350 BIOMT1 8 -0.637047 -0.770825 0.000000 0.00000
REMARK 350 BIOMT2 8 0.770825 -0.637047 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 0.000000 1.000000 8.24600
REMARK 350 BIOMT1 9 -0.968765 0.247980 0.000000 0.00000
REMARK 350 BIOMT2 9 -0.247980 -0.968765 0.000000 0.00000
REMARK 350 BIOMT3 9 0.000000 0.000000 1.000000 12.36900
REMARK 350 BIOMT1 10 -0.188341 0.982104 0.000000 0.00000
REMARK 350 BIOMT2 10 -0.982104 -0.188341 0.000000 0.00000
REMARK 350 BIOMT3 10 0.000000 0.000000 1.000000 16.49200
REMARK 350 BIOMT1 11 0.808298 0.588773 0.000000 0.00000
REMARK 350 BIOMT2 11 -0.588773 0.808298 0.000000 0.00000
REMARK 350 BIOMT3 11 0.000000 0.000000 1.000000 20.61500
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASN A 25
REMARK 465 SER A 26
REMARK 465 ALA A 27
REMARK 465 THR A 28
REMARK 465 TYR A 29
REMARK 465 GLY A 30
REMARK 465 PHE A 31
REMARK 465 LYS A 32
REMARK 465 SER A 33
REMARK 465 GLY A 34
REMARK 465 THR A 35
REMARK 465 ALA A 36
REMARK 465 SER A 37
REMARK 465 PHE A 38
REMARK 465 ALA A 39
REMARK 465 ASP A 40
REMARK 465 MET A 41
REMARK 465 PHE A 42
REMARK 465 ALA A 43
REMARK 465 GLY A 44
REMARK 465 SER A 45
REMARK 465 LYS A 46
REMARK 465 VAL A 47
REMARK 465 GLY A 48
REMARK 465 LEU A 49
REMARK 465 GLY A 50
REMARK 465 VAL A 51
REMARK 465 LYS A 52
REMARK 465 VAL A 53
REMARK 465 ALA A 54
REMARK 465 GLY A 55
REMARK 465 ILE A 56
REMARK 465 THR A 57
REMARK 465 GLN A 58
REMARK 465 ASP A 59
REMARK 465 PHE A 60
REMARK 465 THR A 61
REMARK 465 ASP A 62
REMARK 465 GLY A 63
REMARK 465 THR A 64
REMARK 465 THR A 65
REMARK 465 THR A 66
REMARK 465 ASN A 67
REMARK 465 THR A 68
REMARK 465 GLY A 69
REMARK 465 ARG A 70
REMARK 465 GLY A 358
REMARK 465 ALA A 359
REMARK 465 LEU A 360
REMARK 465 GLU A 361
REMARK 465 ALA A 362
REMARK 465 SER A 363
REMARK 465 ASN A 364
REMARK 465 VAL A 365
REMARK 465 ASP A 366
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 105 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
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 ASN A 264 -0.53 80.24
REMARK 500 PRO A 285 160.78 -40.68
REMARK 500 ASP A 330 -143.99 48.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-1647 RELATED DB: EMDB
REMARK 900 7.1 ANGSTROM REOLUTION CRYOEM MAP OF THE BACTERIAL
REMARK 900 FLAGELLAR HOOK
DBREF 3A69 A 1 402 UNP P0A1J1 FLGE_SALTY 2 403
SEQRES 1 A 402 SER PHE SER GLN ALA VAL SER GLY LEU ASN ALA ALA ALA
SEQRES 2 A 402 THR ASN LEU ASP VAL ILE GLY ASN ASN ILE ALA ASN SER
SEQRES 3 A 402 ALA THR TYR GLY PHE LYS SER GLY THR ALA SER PHE ALA
SEQRES 4 A 402 ASP MET PHE ALA GLY SER LYS VAL GLY LEU GLY VAL LYS
SEQRES 5 A 402 VAL ALA GLY ILE THR GLN ASP PHE THR ASP GLY THR THR
SEQRES 6 A 402 THR ASN THR GLY ARG GLY LEU ASP VAL ALA ILE SER GLN
SEQRES 7 A 402 ASN GLY PHE PHE ARG LEU VAL ASP SER ASN GLY SER VAL
SEQRES 8 A 402 PHE TYR SER ARG ASN GLY GLN PHE LYS LEU ASP GLU ASN
SEQRES 9 A 402 ARG ASN LEU VAL ASN MET GLN GLY MET GLN LEU THR GLY
SEQRES 10 A 402 TYR PRO ALA THR GLY THR PRO PRO THR ILE GLN GLN GLY
SEQRES 11 A 402 ALA ASN PRO ALA PRO ILE THR ILE PRO ASN THR LEU MET
SEQRES 12 A 402 ALA ALA LYS SER THR THR THR ALA SER MET GLN ILE ASN
SEQRES 13 A 402 LEU ASN SER THR ASP PRO VAL PRO SER LYS THR PRO PHE
SEQRES 14 A 402 SER VAL SER ASP ALA ASP SER TYR ASN LYS LYS GLY THR
SEQRES 15 A 402 VAL THR VAL TYR ASP SER GLN GLY ASN ALA HIS ASP MET
SEQRES 16 A 402 ASN VAL TYR PHE VAL LYS THR LYS ASP ASN GLU TRP ALA
SEQRES 17 A 402 VAL TYR THR HIS ASP SER SER ASP PRO ALA ALA THR ALA
SEQRES 18 A 402 PRO THR THR ALA SER THR THR LEU LYS PHE ASN GLU ASN
SEQRES 19 A 402 GLY ILE LEU GLU SER GLY GLY THR VAL ASN ILE THR THR
SEQRES 20 A 402 GLY THR ILE ASN GLY ALA THR ALA ALA THR PHE SER LEU
SEQRES 21 A 402 SER PHE LEU ASN SER MET GLN GLN ASN THR GLY ALA ASN
SEQRES 22 A 402 ASN ILE VAL ALA THR ASN GLN ASN GLY TYR LYS PRO GLY
SEQRES 23 A 402 ASP LEU VAL SER TYR GLN ILE ASN ASN ASP GLY THR VAL
SEQRES 24 A 402 VAL GLY ASN TYR SER ASN GLU GLN GLU GLN VAL LEU GLY
SEQRES 25 A 402 GLN ILE VAL LEU ALA ASN PHE ALA ASN ASN GLU GLY LEU
SEQRES 26 A 402 ALA SER GLN GLY ASP ASN VAL TRP ALA ALA THR GLN ALA
SEQRES 27 A 402 SER GLY VAL ALA LEU LEU GLY THR ALA GLY SER GLY ASN
SEQRES 28 A 402 PHE GLY LYS LEU THR ASN GLY ALA LEU GLU ALA SER ASN
SEQRES 29 A 402 VAL ASP LEU SER LYS GLU LEU VAL ASN MET ILE VAL ALA
SEQRES 30 A 402 GLN ARG ASN TYR GLN SER ASN ALA GLN THR ILE LYS THR
SEQRES 31 A 402 GLN ASP GLN ILE LEU ASN THR LEU VAL ASN LEU ARG
HELIX 1 1 SER A 1 ALA A 24 1 24
HELIX 2 2 ASN A 321 LEU A 325 5 5
HELIX 3 3 LEU A 367 LEU A 401 1 35
SHEET 1 A 3 LEU A 72 ASP A 73 0
SHEET 2 A 3 GLN A 98 LEU A 101 -1 O PHE A 99 N LEU A 72
SHEET 3 A 3 LEU A 107 VAL A 108 -1 O VAL A 108 N LYS A 100
SHEET 1 B 6 VAL A 91 SER A 94 0
SHEET 2 B 6 PHE A 81 VAL A 85 -1 N LEU A 84 O PHE A 92
SHEET 3 B 6 GLN A 114 PRO A 119 -1 O GLN A 114 N VAL A 85
SHEET 4 B 6 GLU A 308 ILE A 314 -1 O GLN A 313 N TYR A 118
SHEET 5 B 6 THR A 298 TYR A 303 -1 N VAL A 299 O LEU A 311
SHEET 6 B 6 LEU A 288 ILE A 293 -1 N VAL A 289 O ASN A 302
SHEET 1 C 5 ALA A 134 PRO A 135 0
SHEET 2 C 5 GLN A 114 PRO A 119 -1 N GLY A 117 O ALA A 134
SHEET 3 C 5 PHE A 81 VAL A 85 -1 N VAL A 85 O GLN A 114
SHEET 4 C 5 LEU A 316 ASN A 318 -1 O ALA A 317 N PHE A 81
SHEET 5 C 5 LEU A 343 GLY A 345 -1 O GLY A 345 N LEU A 316
SHEET 1 D 4 THR A 242 THR A 246 0
SHEET 2 D 4 THR A 257 SER A 261 -1 O PHE A 258 N ILE A 245
SHEET 3 D 4 THR A 150 ASN A 158 1 N ALA A 151 O SER A 259
SHEET 4 D 4 MET A 266 GLN A 268 1 O MET A 266 N LEU A 157
SHEET 1 E 4 THR A 242 THR A 246 0
SHEET 2 E 4 THR A 257 SER A 261 -1 O PHE A 258 N ILE A 245
SHEET 3 E 4 THR A 150 ASN A 158 1 N ALA A 151 O SER A 259
SHEET 4 E 4 ASN A 274 GLN A 280 -1 O ALA A 277 N GLN A 154
SHEET 1 F 5 LYS A 179 TYR A 186 0
SHEET 2 F 5 ALA A 192 LYS A 203 -1 O HIS A 193 N VAL A 185
SHEET 3 F 5 GLU A 206 ASP A 213 -1 O ALA A 208 N VAL A 200
SHEET 4 F 5 THR A 227 PHE A 231 -1 O LEU A 229 N TRP A 207
SHEET 5 F 5 LEU A 237 SER A 239 -1 O GLU A 238 N LYS A 230
SHEET 1 G 2 ALA A 326 SER A 327 0
SHEET 2 G 2 TRP A 333 ALA A 334 -1 O ALA A 334 N ALA A 326
CISPEP 1 THR A 123 PRO A 124 0 3.44
CISPEP 2 THR A 167 PRO A 168 0 -8.23
CISPEP 3 PRO A 285 GLY A 286 0 -0.02
CRYST1 336.000 336.000 336.000 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 0.002976 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002976 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002976 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
