HEADER IMMUNE SYSTEM 14-APR-24 9EZW TITLE STRUCTURE OF THE SINGLE-DOMAIN ANTIBODY VHH_H3 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, C, E, G; COMPND 4 SYNONYM: PROTEIN Z39IG; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: SINGLE-DOMAIN ANTIBODY VHH_H3; COMPND 8 CHAIN: B, D, F, H; COMPND 9 ENGINEERED: YES 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 9EZW 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. 1.90 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.97 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 89475 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.194 REMARK 3 R VALUE (WORKING SET) : 0.190 REMARK 3 FREE R VALUE : 0.228 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 8947 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 64.9700 - 5.9000 1.00 2947 328 0.1869 0.1965 REMARK 3 2 5.9000 - 4.6800 0.95 2661 295 0.1501 0.1669 REMARK 3 3 4.6800 - 4.0900 1.00 2789 310 0.1337 0.1595 REMARK 3 4 4.0900 - 3.7200 1.00 2783 309 0.1595 0.1959 REMARK 3 5 3.7200 - 3.4500 1.00 2757 307 0.1731 0.1951 REMARK 3 6 3.4500 - 3.2500 1.00 2749 305 0.1814 0.2079 REMARK 3 7 3.2500 - 3.0900 1.00 2738 305 0.1797 0.2210 REMARK 3 8 3.0900 - 2.9500 1.00 2718 302 0.1966 0.2466 REMARK 3 9 2.9500 - 2.8400 0.92 2521 279 0.1939 0.2435 REMARK 3 10 2.8400 - 2.7400 0.98 2664 297 0.1972 0.2374 REMARK 3 11 2.7400 - 2.6500 0.99 2681 297 0.1985 0.2626 REMARK 3 12 2.6500 - 2.5800 0.99 2721 303 0.2012 0.2595 REMARK 3 13 2.5800 - 2.5100 0.99 2692 299 0.1939 0.2496 REMARK 3 14 2.5100 - 2.4500 1.00 2695 300 0.1949 0.2429 REMARK 3 15 2.4500 - 2.3900 0.99 2712 301 0.2070 0.2747 REMARK 3 16 2.3900 - 2.3400 0.99 2652 294 0.2148 0.2861 REMARK 3 17 2.3400 - 2.3000 0.99 2734 304 0.2140 0.2592 REMARK 3 18 2.3000 - 2.2500 0.99 2658 296 0.2098 0.2767 REMARK 3 19 2.2500 - 2.2100 0.99 2687 299 0.2177 0.2894 REMARK 3 20 2.2100 - 2.1700 0.99 2646 293 0.2366 0.2769 REMARK 3 21 2.1700 - 2.1400 0.99 2714 302 0.2350 0.3009 REMARK 3 22 2.1400 - 2.1100 0.99 2677 297 0.2299 0.2828 REMARK 3 23 2.1100 - 2.0800 0.99 2671 297 0.2370 0.2947 REMARK 3 24 2.0800 - 2.0500 0.99 2654 294 0.2437 0.3053 REMARK 3 25 2.0500 - 2.0200 0.95 2555 285 0.2694 0.3155 REMARK 3 26 2.0200 - 1.9900 0.92 2487 276 0.2794 0.3107 REMARK 3 27 1.9900 - 1.9700 0.98 2605 290 0.2781 0.3345 REMARK 3 28 1.9700 - 1.9400 0.98 2672 297 0.2875 0.3282 REMARK 3 29 1.9400 - 1.9200 0.99 2666 294 0.3038 0.3304 REMARK 3 30 1.9200 - 1.9000 0.99 2622 292 0.3596 0.3882 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) : 0.257 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.670 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 30.72 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.86 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 8039 REMARK 3 ANGLE : 0.872 10913 REMARK 3 CHIRALITY : 0.059 1146 REMARK 3 PLANARITY : 0.008 1442 REMARK 3 DIHEDRAL : 7.069 1133 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 9EZW 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_1292137922. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JUL-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 : 89487 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 129.940 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 200 DATA REDUNDANCY : 13.90 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.6100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01 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 (%): 49.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44 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 294K 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 30.43350 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.14200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.97050 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.14200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.43350 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.97050 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F 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 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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 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 465 ALA C 119 REMARK 465 ALA C 120 REMARK 465 ALA C 121 REMARK 465 HIS C 122 REMARK 465 HIS C 123 REMARK 465 HIS C 124 REMARK 465 HIS C 125 REMARK 465 HIS C 126 REMARK 465 HIS C 127 REMARK 465 ALA D 125 REMARK 465 ALA D 126 REMARK 465 ALA D 127 REMARK 465 HIS D 128 REMARK 465 HIS D 129 REMARK 465 HIS D 130 REMARK 465 HIS D 131 REMARK 465 HIS D 132 REMARK 465 HIS D 133 REMARK 465 HIS E 127 REMARK 465 ARG F 26 REMARK 465 HIS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 REMARK 465 HIS F 132 REMARK 465 HIS F 133 REMARK 465 ALA G 120 REMARK 465 ALA G 121 REMARK 465 HIS G 122 REMARK 465 HIS G 123 REMARK 465 HIS G 124 REMARK 465 HIS G 125 REMARK 465 HIS G 126 REMARK 465 HIS G 127 REMARK 465 ALA H 125 REMARK 465 ALA H 126 REMARK 465 ALA H 127 REMARK 465 HIS H 128 REMARK 465 HIS H 129 REMARK 465 HIS H 130 REMARK 465 HIS H 131 REMARK 465 HIS H 132 REMARK 465 HIS H 133 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 72 CD CE NZ REMARK 470 LYS B 64 CD CE NZ REMARK 470 LYS E 72 CG CD CE NZ REMARK 470 HIS E 125 CG ND1 CD2 CE1 NE2 REMARK 470 HIS E 126 CG ND1 CD2 CE1 NE2 REMARK 470 PHE H 28 CG CD1 CD2 CE1 CE2 CZ 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 OH TYR B 109 OE2 GLU G 5 2.00 REMARK 500 OG1 THR E 100 OD1 ASP E 102 2.11 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 SER A 90 166.05 175.58 REMARK 500 PHE B 53 -104.92 55.82 REMARK 500 HIS C 71 26.23 -149.05 REMARK 500 PHE D 53 -107.75 60.57 REMARK 500 ASN D 101 -68.29 -108.64 REMARK 500 THR E 83 72.88 47.81 REMARK 500 PHE F 53 -101.05 62.77 REMARK 500 ASP G 52 -162.93 -129.92 REMARK 500 HIS G 71 3.62 -150.99 REMARK 500 LYS G 118 -177.39 -67.72 REMARK 500 PHE H 53 -102.87 65.47 REMARK 500 ALA H 91 165.56 179.02 REMARK 500 REMARK 500 REMARK: NULL DBREF 9EZW A 1 118 UNP Q9Y279 VSIG4_HUMAN 20 137 DBREF 9EZW B 0 133 PDB 9EZW 9EZW 0 133 DBREF 9EZW C 1 118 UNP Q9Y279 VSIG4_HUMAN 20 137 DBREF 9EZW D 0 133 PDB 9EZW 9EZW 0 133 DBREF 9EZW E 1 118 UNP Q9Y279 VSIG4_HUMAN 20 137 DBREF 9EZW F 0 133 PDB 9EZW 9EZW 0 133 DBREF 9EZW G 1 118 UNP Q9Y279 VSIG4_HUMAN 20 137 DBREF 9EZW H 0 133 PDB 9EZW 9EZW 0 133 SEQADV 9EZW ALA A 119 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW ALA A 120 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW ALA A 121 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS A 122 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS A 123 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS A 124 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS A 125 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS A 126 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS A 127 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW ALA C 119 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW ALA C 120 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW ALA C 121 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS C 122 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS C 123 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS C 124 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS C 125 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS C 126 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS C 127 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW ALA E 119 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW ALA E 120 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW ALA E 121 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS E 122 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS E 123 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS E 124 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS E 125 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS E 126 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS E 127 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW ALA G 119 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW ALA G 120 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW ALA G 121 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS G 122 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS G 123 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS G 124 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS G 125 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS G 126 UNP Q9Y279 EXPRESSION TAG SEQADV 9EZW HIS G 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 GLY SEQRES 5 B 134 PRO PHE GLY GLY THR 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 GLU GLN ASP GLN TYR ASN TYR GLU 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 SEQRES 1 C 127 ARG PRO ILE LEU GLU VAL PRO GLU SER VAL THR GLY PRO SEQRES 2 C 127 TRP LYS GLY ASP VAL ASN LEU PRO CYS THR TYR ASP PRO SEQRES 3 C 127 LEU GLN GLY TYR THR GLN VAL LEU VAL LYS TRP LEU VAL SEQRES 4 C 127 GLN ARG GLY SER ASP PRO VAL THR ILE PHE LEU ARG ASP SEQRES 5 C 127 SER SER GLY ASP HIS ILE GLN GLN ALA LYS TYR GLN GLY SEQRES 6 C 127 ARG LEU HIS VAL SER HIS LYS VAL PRO GLY ASP VAL SER SEQRES 7 C 127 LEU GLN LEU SER THR LEU GLU MET ASP ASP ARG SER HIS SEQRES 8 C 127 TYR THR CYS GLU VAL THR TRP GLN THR PRO ASP GLY ASN SEQRES 9 C 127 GLN VAL VAL ARG ASP LYS ILE THR GLU LEU ARG VAL GLN SEQRES 10 C 127 LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 1 D 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 134 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 134 ARG THR PHE SER SER TYR GLY MET GLY TRP PHE ARG GLN SEQRES 4 D 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE GLY SEQRES 5 D 134 PRO PHE GLY GLY THR THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 D 134 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 D 134 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 D 134 ALA VAL TYR TYR CYS ALA ALA GLY ARG TRP ASN ARG TYR SEQRES 9 D 134 GLY GLU GLN ASP GLN TYR ASN TYR GLU TYR TRP GLY GLN SEQRES 10 D 134 GLY THR GLN VAL THR VAL SER SER ALA ALA ALA HIS HIS SEQRES 11 D 134 HIS HIS HIS HIS SEQRES 1 E 127 ARG PRO ILE LEU GLU VAL PRO GLU SER VAL THR GLY PRO SEQRES 2 E 127 TRP LYS GLY ASP VAL ASN LEU PRO CYS THR TYR ASP PRO SEQRES 3 E 127 LEU GLN GLY TYR THR GLN VAL LEU VAL LYS TRP LEU VAL SEQRES 4 E 127 GLN ARG GLY SER ASP PRO VAL THR ILE PHE LEU ARG ASP SEQRES 5 E 127 SER SER GLY ASP HIS ILE GLN GLN ALA LYS TYR GLN GLY SEQRES 6 E 127 ARG LEU HIS VAL SER HIS LYS VAL PRO GLY ASP VAL SER SEQRES 7 E 127 LEU GLN LEU SER THR LEU GLU MET ASP ASP ARG SER HIS SEQRES 8 E 127 TYR THR CYS GLU VAL THR TRP GLN THR PRO ASP GLY ASN SEQRES 9 E 127 GLN VAL VAL ARG ASP LYS ILE THR GLU LEU ARG VAL GLN SEQRES 10 E 127 LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 1 F 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 134 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 134 ARG THR PHE SER SER TYR GLY MET GLY TRP PHE ARG GLN SEQRES 4 F 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE GLY SEQRES 5 F 134 PRO PHE GLY GLY THR THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 F 134 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 F 134 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 F 134 ALA VAL TYR TYR CYS ALA ALA GLY ARG TRP ASN ARG TYR SEQRES 9 F 134 GLY GLU GLN ASP GLN TYR ASN TYR GLU TYR TRP GLY GLN SEQRES 10 F 134 GLY THR GLN VAL THR VAL SER SER ALA ALA ALA HIS HIS SEQRES 11 F 134 HIS HIS HIS HIS SEQRES 1 G 127 ARG PRO ILE LEU GLU VAL PRO GLU SER VAL THR GLY PRO SEQRES 2 G 127 TRP LYS GLY ASP VAL ASN LEU PRO CYS THR TYR ASP PRO SEQRES 3 G 127 LEU GLN GLY TYR THR GLN VAL LEU VAL LYS TRP LEU VAL SEQRES 4 G 127 GLN ARG GLY SER ASP PRO VAL THR ILE PHE LEU ARG ASP SEQRES 5 G 127 SER SER GLY ASP HIS ILE GLN GLN ALA LYS TYR GLN GLY SEQRES 6 G 127 ARG LEU HIS VAL SER HIS LYS VAL PRO GLY ASP VAL SER SEQRES 7 G 127 LEU GLN LEU SER THR LEU GLU MET ASP ASP ARG SER HIS SEQRES 8 G 127 TYR THR CYS GLU VAL THR TRP GLN THR PRO ASP GLY ASN SEQRES 9 G 127 GLN VAL VAL ARG ASP LYS ILE THR GLU LEU ARG VAL GLN SEQRES 10 G 127 LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 1 H 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 134 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 134 ARG THR PHE SER SER TYR GLY MET GLY TRP PHE ARG GLN SEQRES 4 H 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE GLY SEQRES 5 H 134 PRO PHE GLY GLY THR THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 134 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 H 134 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 H 134 ALA VAL TYR TYR CYS ALA ALA GLY ARG TRP ASN ARG TYR SEQRES 9 H 134 GLY GLU GLN ASP GLN TYR ASN TYR GLU TYR TRP GLY GLN SEQRES 10 H 134 GLY THR GLN VAL THR VAL SER SER ALA ALA ALA HIS HIS SEQRES 11 H 134 HIS HIS HIS HIS HET EDO A 201 4 HET EDO A 202 4 HET EDO C 201 4 HET EDO E 201 4 HET EDO E 202 4 HET EDO F 201 4 HET EDO G 201 4 HET EDO G 202 4 HET EDO G 203 4 HET PEG G 204 7 HET EDO H 201 4 HETNAM EDO 1,2-ETHANEDIOL HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN EDO ETHYLENE GLYCOL FORMUL 9 EDO 10(C2 H6 O2) FORMUL 18 PEG C4 H10 O3 FORMUL 20 HOH *519(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 LYS B 86 THR B 90 5 5 HELIX 6 AA6 ASP B 107 TYR B 111 5 5 HELIX 7 AA7 GLN C 60 GLN C 64 5 5 HELIX 8 AA8 GLU C 85 ARG C 89 5 5 HELIX 9 AA9 THR D 27 TYR D 31 5 5 HELIX 10 AB1 ASP D 61 LYS D 64 5 4 HELIX 11 AB2 LYS D 86 THR D 90 5 5 HELIX 12 AB3 ASP D 107 TYR D 111 5 5 HELIX 13 AB4 GLN E 60 GLN E 64 5 5 HELIX 14 AB5 GLU E 85 ARG E 89 5 5 HELIX 15 AB6 THR F 27 TYR F 31 5 5 HELIX 16 AB7 ASP F 61 LYS F 64 5 4 HELIX 17 AB8 ASN F 73 LYS F 75 5 3 HELIX 18 AB9 LYS F 86 THR F 90 5 5 HELIX 19 AC1 ASP F 107 TYR F 111 5 5 HELIX 20 AC2 GLN G 60 GLN G 64 5 5 HELIX 21 AC3 GLU G 85 ARG G 89 5 5 HELIX 22 AC4 THR H 27 TYR H 31 5 5 HELIX 23 AC5 LYS H 86 THR H 90 5 5 HELIX 24 AC6 ASP H 107 TYR H 109 5 3 SHEET 1 AA1 6 SER A 9 PRO A 13 0 SHEET 2 AA1 6 GLN A 105 GLN A 117 1 O ARG A 115 N VAL A 10 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 LEU A 38 O THR A 93 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 GLN B 2 SER B 6 0 SHEET 2 AA3 4 LEU B 17 SER B 24 -1 O SER B 20 N SER B 6 SHEET 3 AA3 4 THR B 77 MET B 82 -1 O MET B 82 N LEU B 17 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 THR B 121 N GLY B 9 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 THR B 121 N GLY B 9 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 SHEET 1 AA6 6 SER C 9 PRO C 13 0 SHEET 2 AA6 6 GLN C 105 GLN C 117 1 O ARG C 115 N VAL C 10 SHEET 3 AA6 6 SER C 90 GLN C 99 -1 N TYR C 92 O THR C 112 SHEET 4 AA6 6 THR C 31 ARG C 41 -1 N LEU C 38 O THR C 93 SHEET 5 AA6 6 ASP C 44 ASP C 52 -1 O VAL C 46 N VAL C 39 SHEET 6 AA6 6 GLY C 55 ILE C 58 -1 O HIS C 57 N LEU C 50 SHEET 1 AA7 3 VAL C 18 LEU C 20 0 SHEET 2 AA7 3 LEU C 79 LEU C 81 -1 O LEU C 79 N LEU C 20 SHEET 3 AA7 3 LEU C 67 VAL C 69 -1 N HIS C 68 O GLN C 80 SHEET 1 AA8 4 LEU D 3 SER D 6 0 SHEET 2 AA8 4 LEU D 17 ALA D 23 -1 O SER D 20 N SER D 6 SHEET 3 AA8 4 THR D 77 MET D 82 -1 O MET D 82 N LEU D 17 SHEET 4 AA8 4 PHE D 67 ASP D 72 -1 N THR D 68 O GLN D 81 SHEET 1 AA9 6 GLY D 9 GLN D 12 0 SHEET 2 AA9 6 THR D 118 SER D 123 1 O SER D 123 N VAL D 11 SHEET 3 AA9 6 ALA D 91 GLY D 98 -1 N TYR D 93 O THR D 118 SHEET 4 AA9 6 GLY D 32 GLN D 38 -1 N PHE D 36 O TYR D 94 SHEET 5 AA9 6 GLU D 45 ILE D 50 -1 O ALA D 48 N TRP D 35 SHEET 6 AA9 6 THR D 57 TYR D 59 -1 O TYR D 58 N ALA D 49 SHEET 1 AB1 4 GLY D 9 GLN D 12 0 SHEET 2 AB1 4 THR D 118 SER D 123 1 O SER D 123 N VAL D 11 SHEET 3 AB1 4 ALA D 91 GLY D 98 -1 N TYR D 93 O THR D 118 SHEET 4 AB1 4 TYR D 113 TRP D 114 -1 O TYR D 113 N ALA D 97 SHEET 1 AB2 6 SER E 9 PRO E 13 0 SHEET 2 AB2 6 GLN E 105 GLN E 117 1 O ARG E 115 N VAL E 10 SHEET 3 AB2 6 SER E 90 GLN E 99 -1 N SER E 90 O LEU E 114 SHEET 4 AB2 6 THR E 31 ARG E 41 -1 N THR E 31 O GLN E 99 SHEET 5 AB2 6 ASP E 44 ASP E 52 -1 O VAL E 46 N VAL E 39 SHEET 6 AB2 6 GLY E 55 ILE E 58 -1 O HIS E 57 N LEU E 50 SHEET 1 AB3 3 VAL E 18 LEU E 20 0 SHEET 2 AB3 3 LEU E 79 LEU E 81 -1 O LEU E 79 N LEU E 20 SHEET 3 AB3 3 LEU E 67 VAL E 69 -1 N HIS E 68 O GLN E 80 SHEET 1 AB4 4 GLN F 2 SER F 6 0 SHEET 2 AB4 4 LEU F 17 SER F 24 -1 O SER F 20 N SER F 6 SHEET 3 AB4 4 THR F 77 MET F 82 -1 O MET F 82 N LEU F 17 SHEET 4 AB4 4 PHE F 67 ASP F 72 -1 N THR F 68 O GLN F 81 SHEET 1 AB5 6 GLY F 9 GLN F 12 0 SHEET 2 AB5 6 THR F 118 SER F 123 1 O THR F 121 N VAL F 11 SHEET 3 AB5 6 ALA F 91 GLY F 98 -1 N TYR F 93 O THR F 118 SHEET 4 AB5 6 GLY F 32 GLN F 38 -1 N GLY F 32 O GLY F 98 SHEET 5 AB5 6 GLU F 45 ILE F 50 -1 O ALA F 48 N TRP F 35 SHEET 6 AB5 6 THR F 57 TYR F 59 -1 O TYR F 58 N ALA F 49 SHEET 1 AB6 4 GLY F 9 GLN F 12 0 SHEET 2 AB6 4 THR F 118 SER F 123 1 O THR F 121 N VAL F 11 SHEET 3 AB6 4 ALA F 91 GLY F 98 -1 N TYR F 93 O THR F 118 SHEET 4 AB6 4 TYR F 113 TRP F 114 -1 O TYR F 113 N ALA F 97 SHEET 1 AB7 6 SER G 9 PRO G 13 0 SHEET 2 AB7 6 GLN G 105 GLN G 117 1 O ARG G 115 N VAL G 10 SHEET 3 AB7 6 SER G 90 GLN G 99 -1 N TYR G 92 O THR G 112 SHEET 4 AB7 6 THR G 31 ARG G 41 -1 N LYS G 36 O GLU G 95 SHEET 5 AB7 6 ASP G 44 ASP G 52 -1 O VAL G 46 N VAL G 39 SHEET 6 AB7 6 GLY G 55 ILE G 58 -1 O HIS G 57 N LEU G 50 SHEET 1 AB8 3 VAL G 18 LEU G 20 0 SHEET 2 AB8 3 LEU G 79 LEU G 81 -1 O LEU G 79 N LEU G 20 SHEET 3 AB8 3 LEU G 67 VAL G 69 -1 N HIS G 68 O GLN G 80 SHEET 1 AB9 4 GLN H 2 SER H 6 0 SHEET 2 AB9 4 LEU H 17 SER H 24 -1 O ALA H 22 N VAL H 4 SHEET 3 AB9 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 17 SHEET 4 AB9 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AC1 6 GLY H 9 GLN H 12 0 SHEET 2 AC1 6 THR H 118 SER H 123 1 O THR H 121 N GLY H 9 SHEET 3 AC1 6 ALA H 91 GLY H 98 -1 N TYR H 93 O THR H 118 SHEET 4 AC1 6 GLY H 32 GLN H 38 -1 N PHE H 36 O TYR H 94 SHEET 5 AC1 6 GLU H 45 ILE H 50 -1 O ALA H 48 N TRP H 35 SHEET 6 AC1 6 THR H 57 TYR H 59 -1 O TYR H 58 N ALA H 49 SHEET 1 AC2 4 GLY H 9 GLN H 12 0 SHEET 2 AC2 4 THR H 118 SER H 123 1 O THR H 121 N GLY H 9 SHEET 3 AC2 4 ALA H 91 GLY H 98 -1 N TYR H 93 O THR H 118 SHEET 4 AC2 4 TYR H 111 TRP H 114 -1 O GLU H 112 N ALA H 97 SSBOND 1 CYS A 22 CYS A 94 1555 1555 2.04 SSBOND 2 CYS B 21 CYS B 95 1555 1555 2.04 SSBOND 3 CYS C 22 CYS C 94 1555 1555 2.05 SSBOND 4 CYS D 21 CYS D 95 1555 1555 2.04 SSBOND 5 CYS E 22 CYS E 94 1555 1555 2.04 SSBOND 6 CYS F 21 CYS F 95 1555 1555 2.04 SSBOND 7 CYS G 22 CYS G 94 1555 1555 2.05 SSBOND 8 CYS H 21 CYS H 95 1555 1555 2.05 CRYST1 60.867 129.941 144.284 90.00 90.00 90.00 P 21 21 21 16 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 0.016429 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007696 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006931 0.00000