HEADER IMMUNE SYSTEM 07-APR-25 9UDP TITLE SINGLE-CHAIN FV ANTIBODY OF B2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SINGLE-CHAIN FV ANTIBODY OF B2; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIGEN BINDING, AFFINITY MATURATION, SOMATIC HYPERMUTATION, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.YOSHIDA,Y.HANAZONO,N.NUMOTO,N.ITO,M.ODA REVDAT 1 05-NOV-25 9UDP 0 JRNL AUTH M.YOSHIDA,Y.HANAZONO,N.NUMOTO,S.YABUNO,N.ITO,T.AZUMA,M.ODA JRNL TITL STRUCTURAL BASIS OF ANTI-(4-HYDROXY-3-NITROPHENYL)ACETYL JRNL TITL 2 ANTIBODIES DURING AFFINITY MATURATION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.48 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.99 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 39623 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.157 REMARK 3 R VALUE (WORKING SET) : 0.156 REMARK 3 FREE R VALUE : 0.174 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1982 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 31.9900 - 3.5700 1.00 2876 152 0.1612 0.1773 REMARK 3 2 3.5700 - 2.8300 1.00 2738 144 0.1453 0.1503 REMARK 3 3 2.8300 - 2.4700 1.00 2730 143 0.1473 0.1747 REMARK 3 4 2.4700 - 2.2500 1.00 2715 143 0.1479 0.1610 REMARK 3 5 2.2500 - 2.0900 1.00 2682 142 0.1420 0.1589 REMARK 3 6 2.0900 - 1.9600 1.00 2668 141 0.1346 0.1473 REMARK 3 7 1.9600 - 1.8600 1.00 2680 140 0.1399 0.1702 REMARK 3 8 1.8600 - 1.7800 1.00 2664 140 0.1485 0.2096 REMARK 3 9 1.7800 - 1.7100 1.00 2658 140 0.1600 0.1731 REMARK 3 10 1.7100 - 1.6600 1.00 2653 141 0.1716 0.2055 REMARK 3 11 1.6600 - 1.6000 1.00 2646 138 0.1821 0.2103 REMARK 3 12 1.6000 - 1.5600 1.00 2664 141 0.1931 0.2104 REMARK 3 13 1.5600 - 1.5200 1.00 2658 139 0.2074 0.2396 REMARK 3 14 1.5200 - 1.4800 1.00 2609 138 0.2278 0.2379 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.114 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.145 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 14.29 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.58 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 : 0.008 1991 REMARK 3 ANGLE : 1.072 2726 REMARK 3 CHIRALITY : 0.099 300 REMARK 3 PLANARITY : 0.008 348 REMARK 3 DIHEDRAL : 14.293 731 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.8565 9.0314 23.9292 REMARK 3 T TENSOR REMARK 3 T11: 0.1127 T22: 0.1010 REMARK 3 T33: 0.1037 T12: 0.0090 REMARK 3 T13: -0.0075 T23: -0.0047 REMARK 3 L TENSOR REMARK 3 L11: 0.5239 L22: 0.4773 REMARK 3 L33: 0.6893 L12: 0.1994 REMARK 3 L13: 0.0147 L23: 0.3906 REMARK 3 S TENSOR REMARK 3 S11: 0.0358 S12: 0.0344 S13: -0.0302 REMARK 3 S21: -0.0622 S22: -0.0108 S23: 0.0093 REMARK 3 S31: -0.0290 S32: 0.0090 S33: 0.0002 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 128 THROUGH 245 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.7986 -6.8148 10.4268 REMARK 3 T TENSOR REMARK 3 T11: 0.0967 T22: 0.1077 REMARK 3 T33: 0.1015 T12: -0.0099 REMARK 3 T13: 0.0093 T23: -0.0089 REMARK 3 L TENSOR REMARK 3 L11: 0.4936 L22: 0.9612 REMARK 3 L33: 0.8333 L12: -0.2260 REMARK 3 L13: 0.0703 L23: 0.2365 REMARK 3 S TENSOR REMARK 3 S11: -0.0329 S12: -0.0238 S13: 0.0043 REMARK 3 S21: 0.0197 S22: -0.0148 S23: 0.0098 REMARK 3 S31: 0.0268 S32: -0.0220 S33: -0.0026 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 9UDP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-APR-25. REMARK 100 THE DEPOSITION ID IS D_1300058282. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-DEC-23 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 : PHOTON FACTORY REMARK 200 BEAMLINE : BL-17A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39699 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : 0.08500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.70 REMARK 200 R MERGE FOR SHELL (I) : 0.97400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.300 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.41 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 4.0 M SODIUM FORMATE, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K 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 19.88100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.64450 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.97800 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.64450 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.88100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.97800 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: 180 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10280 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 GLY A 1 REMARK 465 GLY A 113 REMARK 465 GLY A 114 REMARK 465 GLY A 115 REMARK 465 GLY A 116 REMARK 465 SER A 117 REMARK 465 GLY A 118 REMARK 465 GLY A 119 REMARK 465 GLY A 120 REMARK 465 GLY A 121 REMARK 465 SER A 122 REMARK 465 GLY A 123 REMARK 465 GLY A 124 REMARK 465 GLY A 125 REMARK 465 GLY A 126 REMARK 465 SER A 127 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 THR A 55 -54.03 73.41 REMARK 500 ASN A 56 16.24 -142.15 REMARK 500 SER A 97 -46.60 70.88 REMARK 500 ASN A 98 16.97 -150.54 REMARK 500 ALA A 230 -105.62 -110.11 REMARK 500 REMARK 500 REMARK: NULL DBREF 9UDP A 1 245 PDB 9UDP 9UDP 1 245 SEQRES 1 A 245 GLY SER GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR SEQRES 2 A 245 THR SER PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SEQRES 3 A 245 SER THR GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP SEQRES 4 A 245 VAL GLN GLU LYS PRO ASP HIS LEU PHE THR GLY LEU ILE SEQRES 5 A 245 GLY GLY THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG SEQRES 6 A 245 PHE SER GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR SEQRES 7 A 245 ILE THR GLY ALA GLN THR GLU ASP GLU ALA ILE TYR PHE SEQRES 8 A 245 CYS ALA LEU TRP TYR SER ASN HIS TRP VAL PHE GLY GLY SEQRES 9 A 245 GLY THR LYS LEU THR VAL LEU GLY GLY GLY GLY GLY SER SEQRES 10 A 245 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLN VAL GLN SEQRES 11 A 245 LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS PRO GLY ALA SEQRES 12 A 245 SER VAL LYS LEU SER CYS LYS ALA SER GLY TYR THR PHE SEQRES 13 A 245 THR SER TYR LEU MET HIS TRP VAL LYS GLN ARG PRO GLY SEQRES 14 A 245 ARG GLY LEU GLU TRP ILE GLY ARG ILE ASP PRO ASN SER SEQRES 15 A 245 GLY GLY THR LYS TYR SER GLU LYS PHE LYS SER LYS ALA SEQRES 16 A 245 THR LEU THR VAL ASP LYS PRO SER SER THR ALA TYR MET SEQRES 17 A 245 GLN PHE SER SER LEU THR SER GLU ASP SER ALA VAL TYR SEQRES 18 A 245 TYR CYS ALA ARG TYR TYR TYR GLY ALA TYR PHE ASP TYR SEQRES 19 A 245 TRP GLY GLN GLY THR THR LEU THR VAL SER SER HET FMT A 301 6 HET FMT A 302 6 HET FMT A 303 6 HET GOL A 304 6 HET GOL A 305 6 HET GOL A 306 6 HETNAM FMT FORMIC ACID HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 2 FMT 3(C H2 O2) FORMUL 5 GOL 3(C3 H8 O3) FORMUL 8 HOH *223(H2 O) HELIX 1 AA1 THR A 32 TYR A 36 5 5 HELIX 2 AA2 GLN A 83 GLU A 87 5 5 HELIX 3 AA3 THR A 155 TYR A 159 5 5 HELIX 4 AA4 THR A 214 SER A 218 5 5 SHEET 1 AA1 4 VAL A 6 GLN A 8 0 SHEET 2 AA1 4 THR A 19 SER A 26 -1 O ARG A 25 N THR A 7 SHEET 3 AA1 4 LYS A 74 THR A 80 -1 O ILE A 79 N VAL A 20 SHEET 4 AA1 4 PHE A 66 ILE A 71 -1 N SER A 67 O THR A 78 SHEET 1 AA2 6 ALA A 11 THR A 14 0 SHEET 2 AA2 6 THR A 106 VAL A 110 1 O THR A 109 N THR A 14 SHEET 3 AA2 6 ALA A 88 TRP A 95 -1 N ALA A 88 O LEU A 108 SHEET 4 AA2 6 ASN A 38 LYS A 43 -1 N GLU A 42 O ILE A 89 SHEET 5 AA2 6 LEU A 47 GLY A 53 -1 O LEU A 47 N LYS A 43 SHEET 6 AA2 6 ASN A 57 ARG A 58 -1 O ASN A 57 N GLY A 53 SHEET 1 AA3 4 ALA A 11 THR A 14 0 SHEET 2 AA3 4 THR A 106 VAL A 110 1 O THR A 109 N THR A 14 SHEET 3 AA3 4 ALA A 88 TRP A 95 -1 N ALA A 88 O LEU A 108 SHEET 4 AA3 4 TRP A 100 PHE A 102 -1 O VAL A 101 N LEU A 94 SHEET 1 AA4 4 GLN A 130 GLN A 132 0 SHEET 2 AA4 4 VAL A 145 SER A 152 -1 O LYS A 150 N GLN A 132 SHEET 3 AA4 4 THR A 205 PHE A 210 -1 O MET A 208 N LEU A 147 SHEET 4 AA4 4 THR A 196 ASP A 200 -1 N THR A 198 O TYR A 207 SHEET 1 AA5 6 ALA A 136 VAL A 139 0 SHEET 2 AA5 6 THR A 239 VAL A 243 1 O THR A 242 N GLU A 137 SHEET 3 AA5 6 ALA A 219 TYR A 226 -1 N ALA A 219 O LEU A 241 SHEET 4 AA5 6 LEU A 160 GLN A 166 -1 N HIS A 162 O ALA A 224 SHEET 5 AA5 6 LEU A 172 ILE A 178 -1 O GLU A 173 N LYS A 165 SHEET 6 AA5 6 THR A 185 TYR A 187 -1 O LYS A 186 N ARG A 177 SSBOND 1 CYS A 24 CYS A 92 1555 1555 2.08 SSBOND 2 CYS A 149 CYS A 223 1555 1555 2.05 CRYST1 39.762 71.956 81.289 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 0.025150 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013897 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012302 0.00000