HEADER IMMUNE SYSTEM 14-APR-24 9EZV TITLE STRUCTURE OF THE SINGLE-DOMAIN ANTIBODY VHH_H2 IN COMPLEX WITH HUMAN TITLE 2 VSIG4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: V-SET AND IMMUNOGLOBULIN DOMAIN-CONTAINING PROTEIN 4; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PROTEIN Z39IG; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: IMMUNOGLOBULIN V-SET DOMAIN; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: SINGLE-DOMAIN ANTIBODY VHH_H2; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 OTHER_DETAILS: SINGLE-DOMAIN ANTIBODY SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: VSIG4, CRIG, Z39IG, UNQ317/PRO362; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS VHH, NANOBODY, IN SILICO, ANTIBODY, COMPLEX, SINGLE-DOMAIN, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR I.MARKOVIC,S.N.SAVVIDES REVDAT 1 29-OCT-25 9EZV 0 JRNL AUTH I.MARKOVIC,S.N.SAVVIDES JRNL TITL STRUCTURE OF THE SINGLE-DOMAIN ANTIBODY VHH_H1 IN COMPLEX JRNL TITL 2 WITH HUMAN VSIG4 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.45 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 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) : 1.45 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.76 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 43871 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.176 REMARK 3 R VALUE (WORKING SET) : 0.174 REMARK 3 FREE R VALUE : 0.215 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.560 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 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 33.7600 - 3.4900 1.00 3193 146 0.1706 0.2036 REMARK 3 2 3.4900 - 2.7700 1.00 3052 148 0.1725 0.1826 REMARK 3 3 2.7700 - 2.4200 1.00 3028 146 0.1729 0.2382 REMARK 3 4 2.4200 - 2.2000 1.00 2993 140 0.1644 0.2038 REMARK 3 5 2.2000 - 2.0400 1.00 2992 146 0.1559 0.2189 REMARK 3 6 2.0400 - 1.9200 1.00 2983 144 0.1437 0.2009 REMARK 3 7 1.9200 - 1.8300 1.00 2968 142 0.1549 0.1851 REMARK 3 8 1.8300 - 1.7500 1.00 2971 144 0.1709 0.2257 REMARK 3 9 1.7500 - 1.6800 1.00 2964 144 0.1834 0.2432 REMARK 3 10 1.6800 - 1.6200 0.99 2932 137 0.2124 0.3140 REMARK 3 11 1.6200 - 1.5700 1.00 2956 138 0.2144 0.2563 REMARK 3 12 1.5700 - 1.5300 1.00 2935 142 0.2242 0.3034 REMARK 3 13 1.5300 - 1.4900 1.00 2948 146 0.2474 0.3080 REMARK 3 14 1.4900 - 1.4500 1.00 2956 137 0.2976 0.3433 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL 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) : 0.185 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.079 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.07 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.74 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 : 0.002 2026 REMARK 3 ANGLE : 0.619 2741 REMARK 3 CHIRALITY : 0.070 285 REMARK 3 PLANARITY : 0.004 363 REMARK 3 DIHEDRAL : 5.894 287 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 9EZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-APR-24. REMARK 100 THE DEPOSITION ID IS D_1292137921. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-OCT-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY REMARK 200 BEAMLINE : P13 (MX1) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762 REMARK 200 MONOCHROMATOR : M 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 : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43885 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450 REMARK 200 RESOLUTION RANGE LOW (A) : 53.070 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 13.30 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.7700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54 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 FOR SHELL : NULL 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 (%): 40.72 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0,1M NA-CITRATE PH 5,6 20% 2-PROPANOL REMARK 280 21% PEG 4000, PH 5.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 287K 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 26.14550 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.76550 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.53450 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.76550 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.14550 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.53450 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 ALA A 119 REMARK 465 ALA A 120 REMARK 465 ALA A 121 REMARK 465 HIS A 122 REMARK 465 HIS A 123 REMARK 465 HIS A 124 REMARK 465 HIS A 125 REMARK 465 HIS A 126 REMARK 465 HIS A 127 REMARK 465 GLN B 0 REMARK 465 ALA B 125 REMARK 465 ALA B 126 REMARK 465 ALA B 127 REMARK 465 HIS B 128 REMARK 465 HIS B 129 REMARK 465 HIS B 130 REMARK 465 HIS B 131 REMARK 465 HIS B 132 REMARK 465 HIS B 133 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 HIS A 71 -9.34 -150.23 REMARK 500 PHE B 53 -107.92 61.41 REMARK 500 REMARK 500 REMARK: NULL DBREF 9EZV A 1 118 UNP Q9Y279 VSIG4_HUMAN 20 137 DBREF 9EZV B 0 133 PDB 9EZV 9EZV 0 133 SEQADV 9EZV ALA A 119 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZV ALA A 120 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZV ALA A 121 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZV HIS A 122 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZV HIS A 123 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZV HIS A 124 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZV HIS A 125 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZV HIS A 126 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZV HIS A 127 UNP Q9Y279 EXPRESSION TAG SEQRES 1 A 127 ARG PRO ILE LEU GLU VAL PRO GLU SER VAL THR GLY PRO SEQRES 2 A 127 TRP LYS GLY ASP VAL ASN LEU PRO CYS THR TYR ASP PRO SEQRES 3 A 127 LEU GLN GLY TYR THR GLN VAL LEU VAL LYS TRP LEU VAL SEQRES 4 A 127 GLN ARG GLY SER ASP PRO VAL THR ILE PHE LEU ARG ASP SEQRES 5 A 127 SER SER GLY ASP HIS ILE GLN GLN ALA LYS TYR GLN GLY SEQRES 6 A 127 ARG LEU HIS VAL SER HIS LYS VAL PRO GLY ASP VAL SER SEQRES 7 A 127 LEU GLN LEU SER THR LEU GLU MET ASP ASP ARG SER HIS SEQRES 8 A 127 TYR THR CYS GLU VAL THR TRP GLN THR PRO ASP GLY ASN SEQRES 9 A 127 GLN VAL VAL ARG ASP LYS ILE THR GLU LEU ARG VAL GLN SEQRES 10 A 127 LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 1 B 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 134 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 134 ARG THR PHE SER SER TYR GLY MET GLY TRP PHE ARG GLN SEQRES 4 B 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5 B 134 PRO PHE GLY GLY ASN THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 B 134 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 B 134 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 B 134 ALA VAL TYR TYR CYS ALA ALA GLY ARG TRP ASN ARG TYR SEQRES 9 B 134 GLY PHE GLU ASP GLN ASP ASN PHE ASP TYR TRP GLY GLN SEQRES 10 B 134 GLY THR GLN VAL THR VAL SER SER ALA ALA ALA HIS HIS SEQRES 11 B 134 HIS HIS HIS HIS HET EDO A 201 4 HET EDO A 202 4 HET EDO A 203 4 HET IPA A 204 4 HET EDO A 205 4 HET EDO A 206 4 HET EDO B 201 4 HET EDO B 202 4 HET EDO B 203 4 HETNAM EDO 1,2-ETHANEDIOL HETNAM IPA ISOPROPYL ALCOHOL HETSYN EDO ETHYLENE GLYCOL HETSYN IPA 2-PROPANOL FORMUL 3 EDO 8(C2 H6 O2) FORMUL 6 IPA C3 H8 O FORMUL 12 HOH *178(H2 O) HELIX 1 AA1 GLN A 60 GLN A 64 5 5 HELIX 2 AA2 GLU A 85 ARG A 89 5 5 HELIX 3 AA3 THR B 27 TYR B 31 5 5 HELIX 4 AA4 ASP B 61 LYS B 64 5 4 HELIX 5 AA5 ASN B 73 LYS B 75 5 3 HELIX 6 AA6 LYS B 86 THR B 90 5 5 HELIX 7 AA7 ASP B 107 PHE B 111 5 5 SHEET 1 AA1 6 SER A 9 PRO A 13 0 SHEET 2 AA1 6 GLN A 105 GLN A 117 1 O GLN A 117 N GLY A 12 SHEET 3 AA1 6 SER A 90 GLN A 99 -1 N TYR A 92 O THR A 112 SHEET 4 AA1 6 THR A 31 ARG A 41 -1 N LYS A 36 O GLU A 95 SHEET 5 AA1 6 ASP A 44 ASP A 52 -1 O ARG A 51 N VAL A 35 SHEET 6 AA1 6 GLY A 55 ILE A 58 -1 O HIS A 57 N LEU A 50 SHEET 1 AA2 3 VAL A 18 LEU A 20 0 SHEET 2 AA2 3 LEU A 79 LEU A 81 -1 O LEU A 79 N LEU A 20 SHEET 3 AA2 3 LEU A 67 VAL A 69 -1 N HIS A 68 O GLN A 80 SHEET 1 AA3 4 LEU B 3 SER B 6 0 SHEET 2 AA3 4 LEU B 17 ALA B 23 -1 O SER B 20 N SER B 6 SHEET 3 AA3 4 THR B 77 MET B 82 -1 O LEU B 80 N LEU B 19 SHEET 4 AA3 4 PHE B 67 ASP B 72 -1 N SER B 70 O TYR B 79 SHEET 1 AA4 6 GLY B 9 GLN B 12 0 SHEET 2 AA4 6 THR B 118 SER B 123 1 O SER B 123 N VAL B 11 SHEET 3 AA4 6 ALA B 91 GLY B 98 -1 N TYR B 93 O THR B 118 SHEET 4 AA4 6 GLY B 32 GLN B 38 -1 N PHE B 36 O TYR B 94 SHEET 5 AA4 6 GLU B 45 ILE B 50 -1 O ALA B 48 N TRP B 35 SHEET 6 AA4 6 THR B 57 TYR B 59 -1 O TYR B 58 N ALA B 49 SHEET 1 AA5 4 GLY B 9 GLN B 12 0 SHEET 2 AA5 4 THR B 118 SER B 123 1 O SER B 123 N VAL B 11 SHEET 3 AA5 4 ALA B 91 GLY B 98 -1 N TYR B 93 O THR B 118 SHEET 4 AA5 4 TYR B 113 TRP B 114 -1 O TYR B 113 N ALA B 97 SSBOND 1 CYS A 22 CYS A 94 1555 1555 2.03 SSBOND 2 CYS B 21 CYS B 95 1555 1555 2.04 CISPEP 1 ARG A 1 PRO A 2 0 -2.98 CRYST1 52.291 53.069 87.531 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 0.019124 0.000000 0.000000 0.00000 SCALE2 0.000000 0.018843 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011425 0.00000