HEADER HYDROLASE 03-OCT-17 6B6Q
TITLE ORTHORHOMBIC TRYPSIN CRYOCOOLED TO 100 K WITH 50% XYLOSE AS
TITLE 2 CRYOPROTECTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATIONIC TRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-TRYPSIN;
COMPND 5 EC: 3.4.21.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: BOS TAURUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BOVINE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9913
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.JUERS
REVDAT 5 29-JUL-20 6B6Q 1 COMPND REMARK HETNAM SITE
REVDAT 5 2 1 ATOM
REVDAT 4 01-JAN-20 6B6Q 1 REMARK
REVDAT 3 19-SEP-18 6B6Q 1 JRNL
REVDAT 2 06-DEC-17 6B6Q 1 REMARK
REVDAT 1 01-NOV-17 6B6Q 0
JRNL AUTH D.H.JUERS,C.A.FARLEY,C.P.SAXBY,R.A.COTTER,J.K.B.CAHN,
JRNL AUTH 2 R.C.HOLTON-BURKE,K.HARRISON,Z.WU
JRNL TITL THE IMPACT OF CRYOSOLUTION THERMAL CONTRACTION ON PROTEINS
JRNL TITL 2 AND PROTEIN CRYSTALS: VOLUMES, CONFORMATION AND ORDER.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 74 922 2018
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 30198901
JRNL DOI 10.1107/S2059798318008793
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
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) : 13.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.368
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 14571
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.122
REMARK 3 R VALUE (WORKING SET) : 0.119
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.250
REMARK 3 FREE R VALUE TEST SET COUNT : 765
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 13.3292 - 3.4048 0.96 2774 175 0.1265 0.1487
REMARK 3 2 3.4048 - 2.7099 0.99 2801 131 0.1270 0.2001
REMARK 3 3 2.7099 - 2.3696 1.00 2742 168 0.1203 0.1765
REMARK 3 4 2.3696 - 2.1539 1.00 2749 145 0.1083 0.1664
REMARK 3 5 2.1539 - 2.0001 1.00 2740 146 0.1032 0.1783
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.132
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.311
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 1771
REMARK 3 ANGLE : 0.848 2423
REMARK 3 CHIRALITY : 0.057 275
REMARK 3 PLANARITY : 0.005 309
REMARK 3 DIHEDRAL : 10.224 1069
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6B6Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1000230066.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OXFORD DIFFRACTION NOVA
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD ONYX CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14616
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 13.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.7000
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) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 14.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: WELL: 25% PEG 8K, 0.2 M AMSO4, 0.1 M
REMARK 280 BENZAMIDINE HAL, 0.1 M TRIS BUFFER PH 8.0 PROTEIN: 40 MG/ML IN
REMARK 280 WATER, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 27.21300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.16050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.13650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.16050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.21300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.13650
REMARK 290 SMTRY3 4 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
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 IN SAME ASYMMETRIC UNIT
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 O HOH A 472 O HOH A 598 1.97
REMARK 500 O HOH A 408 O HOH A 626 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OH TYR A 59 OD1 ASP A 153 4545 2.08
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 ASP A 71 -78.35 -119.46
REMARK 500 SER A 214 -63.28 -122.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 93.4
REMARK 620 3 VAL A 75 O 167.3 79.7
REMARK 620 4 GLU A 80 OE2 103.4 157.8 86.2
REMARK 620 5 HOH A 409 O 85.9 90.1 104.7 76.9
REMARK 620 6 HOH A 462 O 79.5 102.8 91.5 94.6 161.0
REMARK 620 N 1 2 3 4 5
DBREF 6B6Q A 16 245 UNP P00760 TRY1_BOVIN 24 246
SEQRES 1 A 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 A 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 A 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 A 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 A 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 A 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 A 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 A 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER
SEQRES 9 A 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 A 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 A 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 A 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE
SEQRES 13 A 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 A 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 A 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 A 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 A 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 A 223 SER ASN
HET CA A 301 1
HET BEN A 302 16
HET SO4 A 303 5
HET SO4 A 304 5
HET XYP A 305 20
HET XYS A 306 18
HETNAM CA CALCIUM ION
HETNAM BEN BENZAMIDINE
HETNAM SO4 SULFATE ION
HETNAM XYP BETA-D-XYLOPYRANOSE
HETNAM XYS ALPHA-D-XYLOPYRANOSE
FORMUL 2 CA CA 2+
FORMUL 3 BEN C7 H8 N2
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 XYP C5 H10 O5
FORMUL 7 XYS C5 H10 O5
FORMUL 8 HOH *239(H2 O)
HELIX 1 AA1 ALA A 55 TYR A 59 5 5
HELIX 2 AA2 SER A 164 TYR A 172 1 9
HELIX 3 AA3 TYR A 234 ASN A 245 1 12
SHEET 1 AA1 7 TYR A 20 THR A 21 0
SHEET 2 AA1 7 LYS A 156 PRO A 161 -1 O CYS A 157 N TYR A 20
SHEET 3 AA1 7 GLN A 135 GLY A 140 -1 N ILE A 138 O LEU A 158
SHEET 4 AA1 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 137
SHEET 5 AA1 7 LYS A 204 TRP A 215 -1 O LYS A 204 N CYS A 201
SHEET 6 AA1 7 GLY A 226 LYS A 230 -1 O VAL A 227 N TRP A 215
SHEET 7 AA1 7 MET A 180 ALA A 183 -1 N PHE A 181 O TYR A 228
SHEET 1 AA2 7 GLN A 30 ASN A 34 0
SHEET 2 AA2 7 HIS A 40 ASN A 48 -1 O CYS A 42 N LEU A 33
SHEET 3 AA2 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45
SHEET 4 AA2 7 MET A 104 LEU A 108 -1 O ILE A 106 N VAL A 52
SHEET 5 AA2 7 GLN A 81 VAL A 90 -1 N ILE A 89 O LEU A 105
SHEET 6 AA2 7 GLN A 64 LEU A 67 -1 N LEU A 67 O GLN A 81
SHEET 7 AA2 7 GLN A 30 ASN A 34 -1 N ASN A 34 O GLN A 64
SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.01
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.04
SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.04
SSBOND 4 CYS A 136 CYS A 201 1555 1555 2.03
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.02
LINK OE1 GLU A 70 CA CA A 301 1555 1555 2.22
LINK O ASN A 72 CA CA A 301 1555 1555 2.35
LINK O VAL A 75 CA CA A 301 1555 1555 2.26
LINK OE2 GLU A 80 CA CA A 301 1555 1555 2.29
LINK CA CA A 301 O HOH A 409 1555 1555 2.48
LINK CA CA A 301 O HOH A 462 1555 1555 2.41
CRYST1 54.426 58.273 66.321 90.00 90.00 90.00 P 21 21 21 4
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 0.018374 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017161 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015078 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
