HEADER IMMUNE SYSTEM/VIRAL PROTEIN 04-FEB-25 9N5Z TITLE HEMAGGLUTININ CA09 HOMOTRIMER BOUND TO AMB38310/AMB38599 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN ANTIBODY FAB AMB38599; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT CHAIN ANTIBODY FAB AMB38310; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HEMAGGLUTININ; COMPND 11 CHAIN: C, D, E; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: HEMAGGLUTININ; COMPND 15 CHAIN: F, G, H; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/CALIFORNIA/01/2009(H1N1)); SOURCE 17 ORGANISM_TAXID: 666207; SOURCE 18 GENE: HA; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_STRAIN: EXPIHEK293F; SOURCE 23 MOL_ID: 4; SOURCE 24 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/CALIFORNIA/01/2009(H1N1)); SOURCE 25 ORGANISM_TAXID: 666207; SOURCE 26 GENE: HA; SOURCE 27 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 28 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 30 EXPRESSION_SYSTEM_STRAIN: EXPIHEK293F KEYWDS COMPLEX OF ANTIBODY WITH INFLUENZA A ANTIGEN HEMAGGLUTININ, IMMUNE KEYWDS 2 SYSTEM-VIRAL PROTEIN COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR M.L.FERNANDEZ-QUINTERO,S.S.R.RAGHAVAN,A.GHARPURE,H.L.TURNER,A.B.WARD REVDAT 1 12-NOV-25 9N5Z 0 JRNL AUTH F.C.SPOENDLIN,M.L.FERNANDEZ-QUINTERO,S.S.R.RAGHAVAN, JRNL AUTH 2 H.L.TURNER,A.GHARPURE,J.R.LOEFFLER,W.K.WONG,A.BUJOTZEK, JRNL AUTH 3 G.GEORGES,A.B.WARD,C.M.DEANE JRNL TITL PREDICTING THE CONFORMATIONAL FLEXIBILITY OF ANTIBODY AND T JRNL TITL 2 CELL RECEPTOR COMPLEMENTARITY-DETERMINING REGIONS. JRNL REF NAT MACH INTELL V. 7 1755 2025 JRNL REFN ESSN 2522-5839 JRNL PMID 41143207 JRNL DOI 10.1038/S42256-025-01131-6 REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, COOT, PHENIX, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7T3D REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : AB INITIO MODEL 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) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.200 REMARK 3 NUMBER OF PARTICLES : 142446 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9N5Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1000292614. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : HEMAGGLUTININ CA09 HOMOTRIMER REMARK 245 BOUND TO AMB38310/AMB38599 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.60 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1600.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4484.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL 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 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: OCTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, 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 ASP C 8 REMARK 465 PRO C 9 REMARK 465 ASP D 8 REMARK 465 PRO D 9 REMARK 465 SER D 325 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 CYS E 139 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 CYS E 305 CA - CB - SG ANGL. DEV. = 8.5 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 VAL A 48 -62.71 -99.35 REMARK 500 VAL A 104 -71.63 65.24 REMARK 500 ASP B 175 -164.79 -168.10 REMARK 500 ASP B 178 148.55 -173.49 REMARK 500 ARG C 55 -110.72 46.53 REMARK 500 ALA C 264 -5.69 72.67 REMARK 500 ASP D 11 144.91 69.23 REMARK 500 ASN D 33 50.42 36.16 REMARK 500 ARG D 55 21.50 49.31 REMARK 500 GLN D 196 -6.93 72.69 REMARK 500 ALA D 264 -2.90 68.88 REMARK 500 PRO E 74 2.42 -67.32 REMARK 500 SER E 207 -1.32 68.07 REMARK 500 ALA E 264 145.99 68.63 REMARK 500 ALA F 5 -60.93 -93.26 REMARK 500 LYS F 127 -125.34 56.68 REMARK 500 LYS G 127 -124.65 58.92 REMARK 500 ASN G 135 17.86 59.34 REMARK 500 CYS G 144 70.60 53.69 REMARK 500 LYS H 127 -136.56 57.62 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG D 405 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-49044 RELATED DB: EMDB REMARK 900 HEMAGGLUTININ CA09 HOMOTRIMER BOUND TO AMB38310/AMB38599 FAB DBREF 9N5Z A 1 126 PDB 9N5Z 9N5Z 1 126 DBREF 9N5Z B 127 234 PDB 9N5Z 9N5Z 127 234 DBREF1 9N5Z C 11 325 UNP A0A3S5H8L7_9INFA DBREF2 9N5Z C A0A3S5H8L7 18 340 DBREF1 9N5Z D 11 325 UNP A0A3S5H8L7_9INFA DBREF2 9N5Z D A0A3S5H8L7 18 340 DBREF1 9N5Z E 11 325 UNP A0A3S5H8L7_9INFA DBREF2 9N5Z E A0A3S5H8L7 18 340 DBREF 9N5Z F 1 171 UNP G0KSL8 G0KSL8_9INFA 345 515 DBREF 9N5Z G 1 171 UNP G0KSL8 G0KSL8_9INFA 345 515 DBREF 9N5Z H 1 171 UNP G0KSL8 G0KSL8_9INFA 345 515 SEQADV 9N5Z ASP C 8 UNP A0A3S5H8L EXPRESSION TAG SEQADV 9N5Z PRO C 9 UNP A0A3S5H8L EXPRESSION TAG SEQADV 9N5Z GLY C 10 UNP A0A3S5H8L EXPRESSION TAG SEQADV 9N5Z ASP D 8 UNP A0A3S5H8L EXPRESSION TAG SEQADV 9N5Z PRO D 9 UNP A0A3S5H8L EXPRESSION TAG SEQADV 9N5Z GLY D 10 UNP A0A3S5H8L EXPRESSION TAG SEQADV 9N5Z ASP E 8 UNP A0A3S5H8L EXPRESSION TAG SEQADV 9N5Z PRO E 9 UNP A0A3S5H8L EXPRESSION TAG SEQADV 9N5Z GLY E 10 UNP A0A3S5H8L EXPRESSION TAG SEQRES 1 A 126 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 126 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 126 PHE THR PHE THR HIS PHE ALA MET THR TRP VAL ARG GLN SEQRES 4 A 126 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER THR ILE ASP SEQRES 5 A 126 GLY SER GLY GLY GLY THR TYR SER ALA ASP PHE VAL LYS SEQRES 6 A 126 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 126 LEU PHE LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 126 ALA LEU TYR TYR CYS ALA LYS VAL SER PRO GLY MET VAL SEQRES 9 A 126 ASP ASP PRO HIS LEU GLY GLY ALA PHE HIS ILE TRP GLY SEQRES 10 A 126 GLN GLY THR MET VAL THR VAL SER SER SEQRES 1 B 108 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA SEQRES 2 B 108 PRO GLY GLN THR ALA THR ILE THR CYS GLY GLY ASN ASN SEQRES 3 B 108 ILE GLY LEU LYS THR VAL HIS TRP CYS GLN GLN LYS PRO SEQRES 4 B 108 GLY GLN ALA PRO VAL VAL VAL VAL TYR ASP ASN ASN ASP SEQRES 5 B 108 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SEQRES 6 B 108 SER TRP ASN THR ALA THR LEU THR ILE THR GLY VAL GLU SEQRES 7 B 108 ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP ASP SEQRES 8 B 108 SER GLY SER HIS GLN VAL VAL PHE GLY GLY GLY THR LYS SEQRES 9 B 108 LEU THR PHE LEU SEQRES 1 C 326 ASP PRO GLY ASP THR LEU CYS ILE GLY TYR HIS ALA ASN SEQRES 2 C 326 ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN SEQRES 3 C 326 VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP LYS SEQRES 4 C 326 HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA PRO SEQRES 5 C 326 LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE LEU SEQRES 6 C 326 GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SER SEQRES 7 C 326 TRP SER TYR ILE VAL GLU THR PRO SER SER ASP ASN GLY SEQRES 8 C 326 THR CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU LEU SEQRES 9 C 326 ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG PHE SEQRES 10 C 326 GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS ASP SEQRES 11 C 326 SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA GLY SEQRES 12 C 326 ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL LYS SEQRES 13 C 326 LYS GLY ASN SER TYR PRO LYS LEU SER LYS SER TYR ILE SEQRES 14 C 326 ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE SEQRES 15 C 326 HIS HIS PRO SER THR SER ALA ASP GLN GLN SER LEU TYR SEQRES 16 C 326 GLN ASN ALA ASP THR TYR VAL PHE VAL GLY SER SER ARG SEQRES 17 C 326 TYR SER LYS LYS PHE LYS PRO GLU ILE ALA ILE ARG PRO SEQRES 18 C 326 LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR TRP SEQRES 19 C 326 THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU ALA SEQRES 20 C 326 THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE ALA MET SEQRES 21 C 326 GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP THR SEQRES 22 C 326 PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO LYS SEQRES 23 C 326 GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE HIS SEQRES 24 C 326 PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SER SEQRES 25 C 326 THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN ILE PRO SEQRES 26 C 326 SER SEQRES 1 D 326 ASP PRO GLY ASP THR LEU CYS ILE GLY TYR HIS ALA ASN SEQRES 2 D 326 ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN SEQRES 3 D 326 VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP LYS SEQRES 4 D 326 HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA PRO SEQRES 5 D 326 LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE LEU SEQRES 6 D 326 GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SER SEQRES 7 D 326 TRP SER TYR ILE VAL GLU THR PRO SER SER ASP ASN GLY SEQRES 8 D 326 THR CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU LEU SEQRES 9 D 326 ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG PHE SEQRES 10 D 326 GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS ASP SEQRES 11 D 326 SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA GLY SEQRES 12 D 326 ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL LYS SEQRES 13 D 326 LYS GLY ASN SER TYR PRO LYS LEU SER LYS SER TYR ILE SEQRES 14 D 326 ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE SEQRES 15 D 326 HIS HIS PRO SER THR SER ALA ASP GLN GLN SER LEU TYR SEQRES 16 D 326 GLN ASN ALA ASP THR TYR VAL PHE VAL GLY SER SER ARG SEQRES 17 D 326 TYR SER LYS LYS PHE LYS PRO GLU ILE ALA ILE ARG PRO SEQRES 18 D 326 LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR TRP SEQRES 19 D 326 THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU ALA SEQRES 20 D 326 THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE ALA MET SEQRES 21 D 326 GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP THR SEQRES 22 D 326 PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO LYS SEQRES 23 D 326 GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE HIS SEQRES 24 D 326 PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SER SEQRES 25 D 326 THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN ILE PRO SEQRES 26 D 326 SER SEQRES 1 E 326 ASP PRO GLY ASP THR LEU CYS ILE GLY TYR HIS ALA ASN SEQRES 2 E 326 ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN SEQRES 3 E 326 VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP LYS SEQRES 4 E 326 HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA PRO SEQRES 5 E 326 LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE LEU SEQRES 6 E 326 GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SER SEQRES 7 E 326 TRP SER TYR ILE VAL GLU THR PRO SER SER ASP ASN GLY SEQRES 8 E 326 THR CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU LEU SEQRES 9 E 326 ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG PHE SEQRES 10 E 326 GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS ASP SEQRES 11 E 326 SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA GLY SEQRES 12 E 326 ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL LYS SEQRES 13 E 326 LYS GLY ASN SER TYR PRO LYS LEU SER LYS SER TYR ILE SEQRES 14 E 326 ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE SEQRES 15 E 326 HIS HIS PRO SER THR SER ALA ASP GLN GLN SER LEU TYR SEQRES 16 E 326 GLN ASN ALA ASP THR TYR VAL PHE VAL GLY SER SER ARG SEQRES 17 E 326 TYR SER LYS LYS PHE LYS PRO GLU ILE ALA ILE ARG PRO SEQRES 18 E 326 LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR TRP SEQRES 19 E 326 THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU ALA SEQRES 20 E 326 THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE ALA MET SEQRES 21 E 326 GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP THR SEQRES 22 E 326 PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO LYS SEQRES 23 E 326 GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE HIS SEQRES 24 E 326 PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SER SEQRES 25 E 326 THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN ILE PRO SEQRES 26 E 326 SER SEQRES 1 F 171 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 F 171 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 F 171 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 F 171 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 F 171 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 F 171 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 F 171 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 F 171 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 F 171 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 F 171 LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN ASN ALA SEQRES 11 F 171 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 F 171 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 F 171 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 F 171 ARG GLU SEQRES 1 G 171 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 G 171 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 G 171 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 G 171 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 G 171 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 G 171 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 G 171 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 G 171 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 G 171 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 G 171 LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN ASN ALA SEQRES 11 G 171 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 G 171 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 G 171 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 G 171 ARG GLU SEQRES 1 H 171 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 H 171 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 H 171 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 H 171 SER THR GLN ASN ALA ILE ASP LYS ILE THR ASN LYS VAL SEQRES 5 H 171 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 H 171 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 H 171 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 H 171 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 H 171 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 H 171 LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN ASN ALA SEQRES 11 H 171 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 H 171 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 H 171 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 H 171 ARG GLU HET NAG C 401 14 HET NAG C 402 14 HET NAG C 403 14 HET NAG C 404 14 HET NAG C 405 14 HET NAG D 401 14 HET NAG D 402 14 HET NAG D 403 14 HET NAG D 404 14 HET NAG D 405 14 HET NAG E 401 14 HET NAG E 402 14 HET NAG E 403 14 HET NAG E 404 14 HET NAG E 405 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 9 NAG 15(C8 H15 N O6) HELIX 1 AA1 ASN B 152 LYS B 156 5 5 HELIX 2 AA2 GLU B 204 GLU B 208 5 5 HELIX 3 AA3 ASN C 65 ILE C 70 1 6 HELIX 4 AA4 ASN C 73 GLU C 77 5 5 HELIX 5 AA5 ASP C 104 LEU C 112 1 9 HELIX 6 AA6 THR C 187 TYR C 195 1 9 HELIX 7 AA7 ASN D 65 GLY D 72 1 8 HELIX 8 AA8 ASP D 104 LEU D 112 1 9 HELIX 9 AA9 THR D 187 GLN D 196 1 10 HELIX 10 AB1 ASN E 65 GLY E 72 1 8 HELIX 11 AB2 ASP E 104 LEU E 112 1 9 HELIX 12 AB3 THR E 187 TYR E 195 1 9 HELIX 13 AB4 ASP F 37 LYS F 58 1 22 HELIX 14 AB5 LYS F 75 ASN F 95 1 21 HELIX 15 AB6 ALA F 96 LYS F 127 1 32 HELIX 16 AB7 ASP F 145 GLY F 155 1 11 HELIX 17 AB8 ASP F 158 ARG F 170 1 13 HELIX 18 AB9 ASP G 37 LYS G 58 1 22 HELIX 19 AC1 ASN G 71 LEU G 73 5 3 HELIX 20 AC2 GLU G 74 LYS G 127 1 54 HELIX 21 AC3 ASP G 145 GLY G 155 1 11 HELIX 22 AC4 ASP G 158 ASN G 169 1 12 HELIX 23 AC5 ASP H 37 GLU H 57 1 21 HELIX 24 AC6 LYS H 75 LYS H 127 1 53 HELIX 25 AC7 ASP H 145 GLY H 155 1 11 HELIX 26 AC8 TYR H 159 LYS H 161 5 3 HELIX 27 AC9 TYR H 162 GLU H 171 1 10 SHEET 1 AA1 3 LEU A 18 CYS A 22 0 SHEET 2 AA1 3 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 3 AA1 3 VAL A 70 ASP A 73 -1 N SER A 71 O PHE A 80 SHEET 1 AA2 5 TYR A 59 SER A 60 0 SHEET 2 AA2 5 LEU A 45 THR A 50 -1 N THR A 50 O TYR A 59 SHEET 3 AA2 5 THR A 35 GLN A 39 -1 N ARG A 38 O GLU A 46 SHEET 4 AA2 5 ALA A 92 TYR A 95 -1 O TYR A 95 N VAL A 37 SHEET 5 AA2 5 THR A 120 VAL A 122 -1 O VAL A 122 N ALA A 92 SHEET 1 AA3 2 ALA A 97 LYS A 98 0 SHEET 2 AA3 2 ILE A 115 TRP A 116 -1 O ILE A 115 N LYS A 98 SHEET 1 AA4 4 LEU B 130 THR B 131 0 SHEET 2 AA4 4 ALA B 144 GLY B 150 -1 O GLY B 149 N THR B 131 SHEET 3 AA4 4 ALA B 196 ILE B 200 -1 O LEU B 198 N ILE B 146 SHEET 4 AA4 4 SER B 190 ASN B 191 -1 N SER B 190 O THR B 197 SHEET 1 AA5 4 VAL B 170 VAL B 173 0 SHEET 2 AA5 4 VAL B 158 GLN B 163 -1 N GLN B 162 O VAL B 170 SHEET 3 AA5 4 ASP B 210 ASP B 217 -1 O GLN B 214 N HIS B 159 SHEET 4 AA5 4 GLN B 222 VAL B 224 -1 O GLN B 222 N ASP B 217 SHEET 1 AA6 4 VAL B 170 VAL B 173 0 SHEET 2 AA6 4 VAL B 158 GLN B 163 -1 N GLN B 162 O VAL B 170 SHEET 3 AA6 4 ASP B 210 ASP B 217 -1 O GLN B 214 N HIS B 159 SHEET 4 AA6 4 THR B 229 LYS B 230 -1 O THR B 229 N TYR B 211 SHEET 1 AA7 2 GLY C 16 TYR C 17 0 SHEET 2 AA7 2 TYR F 22 GLY F 23 -1 O GLY F 23 N GLY C 16 SHEET 1 AA8 2 THR C 25 VAL C 26 0 SHEET 2 AA8 2 VAL C 34 THR C 35 -1 O VAL C 34 N VAL C 26 SHEET 1 AA9 2 VAL C 40 ASN C 41 0 SHEET 2 AA9 2 ARG C 315 LEU C 316 -1 O LEU C 316 N VAL C 40 SHEET 1 AB1 3 LEU C 43 GLU C 44 0 SHEET 2 AB1 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLU C 44 SHEET 3 AB1 3 LYS C 307 TYR C 308 1 O LYS C 307 N GLN C 295 SHEET 1 AB2 3 LEU C 59 HIS C 60 0 SHEET 2 AB2 3 ILE C 87 GLU C 89 1 O VAL C 88 N LEU C 59 SHEET 3 AB2 3 ILE C 267 ILE C 269 1 O ILE C 268 N ILE C 87 SHEET 1 AB3 2 THR C 136 PRO C 140 0 SHEET 2 AB3 2 LYS C 145 SER C 146 -1 O SER C 146 N THR C 136 SHEET 1 AB4 2 LEU C 151 TRP C 153 0 SHEET 2 AB4 2 VAL C 252 PRO C 254 -1 O VAL C 253 N ILE C 152 SHEET 1 AB5 4 LEU C 164 ILE C 169 0 SHEET 2 AB5 4 LYS C 242 ALA C 247 -1 O ALA C 247 N LEU C 164 SHEET 3 AB5 4 VAL C 202 SER C 206 -1 N GLY C 205 O THR C 244 SHEET 4 AB5 4 SER C 210 PHE C 213 -1 O LYS C 211 N VAL C 204 SHEET 1 AB6 3 ARG C 229 VAL C 237 0 SHEET 2 AB6 3 GLU C 175 HIS C 184 -1 N ILE C 182 O ASN C 231 SHEET 3 AB6 3 PHE C 258 MET C 260 -1 O PHE C 258 N LEU C 177 SHEET 1 AB7 4 ALA C 287 ILE C 288 0 SHEET 2 AB7 4 CYS C 281 GLN C 282 -1 N CYS C 281 O ILE C 288 SHEET 3 AB7 4 ILE C 302 GLY C 303 -1 O ILE C 302 N GLN C 282 SHEET 4 AB7 4 THR F 64 ALA F 65 -1 N THR F 64 O GLY C 303 SHEET 1 AB8 3 GLY D 16 TYR D 17 0 SHEET 2 AB8 3 TYR G 22 HIS G 25 -1 O GLY G 23 N GLY D 16 SHEET 3 AB8 3 TYR G 34 ALA G 35 -1 O ALA G 35 N TYR G 24 SHEET 1 AB9 2 THR D 25 VAL D 26 0 SHEET 2 AB9 2 VAL D 34 THR D 35 -1 O VAL D 34 N VAL D 26 SHEET 1 AC1 2 SER D 39 ASN D 41 0 SHEET 2 AC1 2 ARG D 315 ALA D 317 -1 O LEU D 316 N VAL D 40 SHEET 1 AC2 3 LEU D 43 GLU D 44 0 SHEET 2 AC2 3 PHE D 294 GLN D 295 1 O PHE D 294 N GLU D 44 SHEET 3 AC2 3 LYS D 307 TYR D 308 1 O LYS D 307 N GLN D 295 SHEET 1 AC3 3 LEU D 59 HIS D 60 0 SHEET 2 AC3 3 ILE D 87 GLU D 89 1 O VAL D 88 N LEU D 59 SHEET 3 AC3 3 ILE D 267 ILE D 269 1 O ILE D 268 N ILE D 87 SHEET 1 AC4 4 GLU D 116C PHE D 118 0 SHEET 2 AC4 4 ALA D 257 MET D 260 -1 O ALA D 259 N GLU D 116C SHEET 3 AC4 4 GLU D 175 HIS D 184 -1 N LEU D 177 O PHE D 258 SHEET 4 AC4 4 ARG D 229 VAL D 237 -1 O TYR D 233 N TRP D 180 SHEET 1 AC5 2 HIS D 130 ASP D 131 0 SHEET 2 AC5 2 VAL D 155 LYS D 156 -1 O VAL D 155 N ASP D 131 SHEET 1 AC6 2 THR D 136 HIS D 141 0 SHEET 2 AC6 2 ALA D 144 SER D 146 -1 O SER D 146 N THR D 136 SHEET 1 AC7 2 LEU D 151 TRP D 153 0 SHEET 2 AC7 2 VAL D 252 PRO D 254 -1 O VAL D 253 N ILE D 152 SHEET 1 AC8 4 LEU D 164 ILE D 169 0 SHEET 2 AC8 4 LYS D 242 ALA D 247 -1 O PHE D 245 N LYS D 166 SHEET 3 AC8 4 VAL D 202 GLY D 205 -1 N PHE D 203 O GLU D 246 SHEET 4 AC8 4 SER D 210 PHE D 213 -1 O PHE D 213 N VAL D 202 SHEET 1 AC9 2 CYS D 281 GLN D 282 0 SHEET 2 AC9 2 ILE D 302 GLY D 303 -1 O ILE D 302 N GLN D 282 SHEET 1 AD1 3 LEU E 13 TYR E 17 0 SHEET 2 AD1 3 TYR H 22 HIS H 26 -1 O GLY H 23 N GLY E 16 SHEET 3 AD1 3 GLY H 33 ALA H 35 -1 O ALA H 35 N TYR H 24 SHEET 1 AD2 2 THR E 25 VAL E 26 0 SHEET 2 AD2 2 VAL E 34 THR E 35 -1 O VAL E 34 N VAL E 26 SHEET 1 AD3 2 VAL E 40 ASN E 41 0 SHEET 2 AD3 2 ARG E 315 LEU E 316 -1 O LEU E 316 N VAL E 40 SHEET 1 AD4 3 LEU E 43 GLU E 44 0 SHEET 2 AD4 3 PHE E 294 GLN E 295 1 O PHE E 294 N GLU E 44 SHEET 3 AD4 3 LYS E 307 TYR E 308 1 O LYS E 307 N GLN E 295 SHEET 1 AD5 3 LEU E 59 HIS E 60 0 SHEET 2 AD5 3 ILE E 87 GLU E 89 1 O VAL E 88 N LEU E 59 SHEET 3 AD5 3 ILE E 267 ILE E 269 1 O ILE E 268 N GLU E 89 SHEET 1 AD6 4 GLU E 116C PHE E 118 0 SHEET 2 AD6 4 ALA E 257 MET E 260 -1 O ALA E 257 N PHE E 118 SHEET 3 AD6 4 GLU E 175 HIS E 184 -1 N GLU E 175 O MET E 260 SHEET 4 AD6 4 ARG E 229 VAL E 237 -1 O ARG E 229 N HIS E 184 SHEET 1 AD7 2 THR E 136 HIS E 141 0 SHEET 2 AD7 2 ALA E 144 SER E 146 -1 O ALA E 144 N HIS E 141 SHEET 1 AD8 2 LEU E 151 TRP E 153 0 SHEET 2 AD8 2 VAL E 252 PRO E 254 -1 O VAL E 253 N ILE E 152 SHEET 1 AD9 4 LEU E 164 ILE E 169 0 SHEET 2 AD9 4 LYS E 242 ALA E 247 -1 O ALA E 247 N LEU E 164 SHEET 3 AD9 4 VAL E 202 GLY E 205 -1 N PHE E 203 O GLU E 246 SHEET 4 AD9 4 LYS E 212 PHE E 213 -1 O PHE E 213 N VAL E 202 SHEET 1 AE1 4 GLY E 286 ILE E 288 0 SHEET 2 AE1 4 CYS E 281 THR E 283 -1 N CYS E 281 O ILE E 288 SHEET 3 AE1 4 ILE E 302 GLY E 303 -1 O ILE E 302 N GLN E 282 SHEET 4 AE1 4 THR H 64 ALA H 65 -1 O THR H 64 N GLY E 303 SHEET 1 AE2 2 ALA F 130 GLY F 134 0 SHEET 2 AE2 2 CYS F 137 PHE F 140 -1 O GLU F 139 N LYS F 131 SHEET 1 AE3 2 LYS G 131 GLU G 132 0 SHEET 2 AE3 2 PHE G 138 GLU G 139 -1 O GLU G 139 N LYS G 131 SHEET 1 AE4 2 LYS H 131 GLY H 134 0 SHEET 2 AE4 2 CYS H 137 GLU H 139 -1 O CYS H 137 N GLY H 134 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS B 148 CYS B 213 1555 1555 2.03 SSBOND 3 CYS C 52 CYS C 277 1555 1555 2.03 SSBOND 4 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 5 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 6 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 7 CYS D 14 CYS G 137 1555 1555 2.04 SSBOND 8 CYS D 52 CYS D 277 1555 1555 2.03 SSBOND 9 CYS D 64 CYS D 76 1555 1555 2.03 SSBOND 10 CYS D 97 CYS D 139 1555 1555 2.02 SSBOND 11 CYS D 281 CYS D 305 1555 1555 2.03 SSBOND 12 CYS E 14 CYS H 137 1555 1555 2.03 SSBOND 13 CYS E 52 CYS E 277 1555 1555 2.03 SSBOND 14 CYS E 64 CYS E 76 1555 1555 2.03 SSBOND 15 CYS E 97 CYS E 139 1555 1555 2.02 SSBOND 16 CYS E 281 CYS E 305 1555 1555 2.03 SSBOND 17 CYS F 144 CYS F 148 1555 1555 2.03 SSBOND 18 CYS G 144 CYS G 148 1555 1555 2.03 SSBOND 19 CYS H 144 CYS H 148 1555 1555 2.03 LINK ND2 ASN C 21 C1 NAG C 402 1555 1555 1.44 LINK ND2 ASN C 33 C1 NAG C 403 1555 1555 1.44 LINK ND2 ASN C 94 C1 NAG C 401 1555 1555 1.43 LINK ND2 ASN C 278 C1 NAG C 404 1555 1555 1.45 LINK ND2 ASN C 289 C1 NAG C 405 1555 1555 1.44 LINK ND2 ASN D 21 C1 NAG D 403 1555 1555 1.44 LINK ND2 ASN D 94 C1 NAG D 401 1555 1555 1.43 LINK ND2 ASN D 278 C1 NAG D 402 1555 1555 1.45 LINK ND2 ASN D 289 C1 NAG D 404 1555 1555 1.44 LINK ND2 ASN E 21 C1 NAG E 405 1555 1555 1.44 LINK ND2 ASN E 33 C1 NAG E 404 1555 1555 1.44 LINK ND2 ASN E 94 C1 NAG E 401 1555 1555 1.44 LINK ND2 ASN E 278 C1 NAG E 402 1555 1555 1.47 LINK ND2 ASN E 289 C1 NAG E 403 1555 1555 1.44 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000