HEADER MEMBRANE PROTEIN 29-DEC-24 9HVI TITLE PSMA IN COMPLEX WITH NANOBODY 8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLUTAMATE CARBOXYPEPTIDASE 2; COMPND 3 CHAIN: A, E; COMPND 4 FRAGMENT: UNP RESIDUES 56-750; COMPND 5 SYNONYM: CELL GROWTH-INHIBITING GENE 27 PROTEIN,FOLATE HYDROLASE 1, COMPND 6 FOLYLPOLY-GAMMA-GLUTAMATE CARBOXYPEPTIDASE,FGCP,GLUTAMATE COMPND 7 CARBOXYPEPTIDASE II,GCPII,MEMBRANE GLUTAMATE CARBOXYPEPTIDASE,MGCP,N- COMPND 8 ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE I,NAALADASE I,PROSTATE- COMPND 9 SPECIFIC MEMBRANE ANTIGEN,PSMA,PTEROYLPOLY-GAMMA-GLUTAMATE COMPND 10 CARBOXYPEPTIDASE; COMPND 11 EC: 3.4.17.21; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 2; COMPND 14 MOLECULE: NANO BODY 8; COMPND 15 CHAIN: H, Q; 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 GENE: FOLH1, FOLH, NAALAD1, PSM, PSMA, GIG27; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: CAMELUS DROMEDARIUS; SOURCE 10 ORGANISM_TAXID: 9838; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CARBOXYPEPTIDASE COMPLEX NANOBODY, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR G.ALON,R.ZALK,T.T.HUYNH,M.R.ZALUTSKY,Y.WEIZMANN,R.ZARIVACH,N.PAPO REVDAT 1 16-JUL-25 9HVI 0 JRNL AUTH G.ALON-ZCHUT,R.ZALK,T.T.HUYNH,M.R.ZALUTSKY,Y.WEIZMANN, JRNL AUTH 2 R.ZARIVACH,N.PAPO JRNL TITL STRUCTURAL ANALYSIS OF NANOBODY INTERACTIONS WITH THEIR JRNL TITL 2 PROSTATE-SPECIFIC MEMBRANE ANTIGEN BINDING EPITOPES. JRNL REF INT.J.BIOL.MACROMOL. 45693 2025 JRNL REFN ISSN 0141-8130 JRNL PMID 40609945 JRNL DOI 10.1016/J.IJBIOMAC.2025.145693 REMARK 2 REMARK 2 RESOLUTION. 2.46 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX, EPU REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL 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) : 2.460 REMARK 3 NUMBER OF PARTICLES : 241910 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 9HVI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292143928. 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 : PSMA IN COMPLEX WITH NANOBODY 8 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : MANUALLY BLOTTED FOR 3 SECONDS REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 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 : TFS FALCON 4I (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 3000.00 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, H, Q, B, C, D, F, G, I 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 PRO A 273 OH TYR E 733 2.11 REMARK 500 NE2 GLN H 119 OG1 THR H 121 2.11 REMARK 500 OH TYR A 733 O PRO E 273 2.13 REMARK 500 REMARK 500 REMARK: NULL 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 LEU A 188 CA - CB - CG ANGL. DEV. = 14.2 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 ASN A 132 -167.10 -79.60 REMARK 500 ASN A 178 -124.66 54.72 REMARK 500 LYS A 207 -10.17 72.59 REMARK 500 TYR A 277 49.45 -89.08 REMARK 500 VAL A 382 -61.92 -122.26 REMARK 500 LEU A 551 33.05 -98.83 REMARK 500 ASP A 567 73.39 -160.51 REMARK 500 ASN A 698 63.43 -101.09 REMARK 500 ALA A 701 10.52 -141.42 REMARK 500 ASN E 178 -126.35 53.35 REMARK 500 LYS E 207 -10.52 73.18 REMARK 500 TYR E 277 49.69 -90.97 REMARK 500 VAL E 382 -61.99 -122.28 REMARK 500 LEU E 551 31.75 -98.64 REMARK 500 ASP E 567 73.85 -161.60 REMARK 500 SER H 7 -169.77 -160.45 REMARK 500 VAL Q 48 -55.59 -123.58 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 B 1 REMARK 610 NAG C 1 REMARK 610 NAG D 1 REMARK 610 NAG F 1 REMARK 610 NAG G 1 REMARK 610 NAG I 1 REMARK 610 NAG A 803 REMARK 610 NAG E 803 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 807 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR A 269 O REMARK 620 2 THR A 269 OG1 61.4 REMARK 620 3 TYR A 272 O 84.1 75.8 REMARK 620 4 GLU A 433 OE1 152.3 90.9 88.3 REMARK 620 5 GLU A 433 OE2 131.8 106.8 141.5 53.7 REMARK 620 6 GLU A 436 OE1 116.1 149.4 73.6 86.9 96.3 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 806 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 377 NE2 REMARK 620 2 ASP A 387 OD1 108.9 REMARK 620 3 ASP A 453 OD1 90.1 84.7 REMARK 620 4 ASP A 453 OD2 111.1 125.7 60.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 805 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 387 OD2 REMARK 620 2 GLU A 425 OE1 109.3 REMARK 620 3 HIS A 553 NE2 69.7 80.3 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA E 807 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR E 269 O REMARK 620 2 THR E 269 OG1 61.4 REMARK 620 3 TYR E 272 O 82.6 75.6 REMARK 620 4 GLU E 433 OE1 152.3 90.9 89.1 REMARK 620 5 GLU E 433 OE2 132.5 107.1 142.5 53.8 REMARK 620 6 GLU E 436 OE1 115.9 148.7 73.2 86.5 96.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN E 806 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS E 377 NE2 REMARK 620 2 ASP E 387 OD1 109.3 REMARK 620 3 ASP E 453 OD1 90.2 81.5 REMARK 620 4 ASP E 453 OD2 116.4 117.4 58.9 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN E 805 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP E 387 OD2 REMARK 620 2 GLU E 425 OE1 113.9 REMARK 620 3 HIS E 553 NE2 71.6 82.7 REMARK 620 N 1 2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-52435 RELATED DB: EMDB REMARK 900 PSMA IN COMPLEX WITH NANOBODY 8 DBREF 9HVI A 56 750 UNP Q04609 FOLH1_HUMAN 56 750 DBREF 9HVI E 56 750 UNP Q04609 FOLH1_HUMAN 56 750 DBREF 9HVI H 1 123 PDB 9HVI 9HVI 1 123 DBREF 9HVI Q 1 123 PDB 9HVI 9HVI 1 123 SEQRES 1 A 695 HIS ASN MET LYS ALA PHE LEU ASP GLU LEU LYS ALA GLU SEQRES 2 A 695 ASN ILE LYS LYS PHE LEU TYR ASN PHE THR GLN ILE PRO SEQRES 3 A 695 HIS LEU ALA GLY THR GLU GLN ASN PHE GLN LEU ALA LYS SEQRES 4 A 695 GLN ILE GLN SER GLN TRP LYS GLU PHE GLY LEU ASP SER SEQRES 5 A 695 VAL GLU LEU ALA HIS TYR ASP VAL LEU LEU SER TYR PRO SEQRES 6 A 695 ASN LYS THR HIS PRO ASN TYR ILE SER ILE ILE ASN GLU SEQRES 7 A 695 ASP GLY ASN GLU ILE PHE ASN THR SER LEU PHE GLU PRO SEQRES 8 A 695 PRO PRO PRO GLY TYR GLU ASN VAL SER ASP ILE VAL PRO SEQRES 9 A 695 PRO PHE SER ALA PHE SER PRO GLN GLY MET PRO GLU GLY SEQRES 10 A 695 ASP LEU VAL TYR VAL ASN TYR ALA ARG THR GLU ASP PHE SEQRES 11 A 695 PHE LYS LEU GLU ARG ASP MET LYS ILE ASN CYS SER GLY SEQRES 12 A 695 LYS ILE VAL ILE ALA ARG TYR GLY LYS VAL PHE ARG GLY SEQRES 13 A 695 ASN LYS VAL LYS ASN ALA GLN LEU ALA GLY ALA LYS GLY SEQRES 14 A 695 VAL ILE LEU TYR SER ASP PRO ALA ASP TYR PHE ALA PRO SEQRES 15 A 695 GLY VAL LYS SER TYR PRO ASP GLY TRP ASN LEU PRO GLY SEQRES 16 A 695 GLY GLY VAL GLN ARG GLY ASN ILE LEU ASN LEU ASN GLY SEQRES 17 A 695 ALA GLY ASP PRO LEU THR PRO GLY TYR PRO ALA ASN GLU SEQRES 18 A 695 TYR ALA TYR ARG ARG GLY ILE ALA GLU ALA VAL GLY LEU SEQRES 19 A 695 PRO SER ILE PRO VAL HIS PRO ILE GLY TYR TYR ASP ALA SEQRES 20 A 695 GLN LYS LEU LEU GLU LYS MET GLY GLY SER ALA PRO PRO SEQRES 21 A 695 ASP SER SER TRP ARG GLY SER LEU LYS VAL PRO TYR ASN SEQRES 22 A 695 VAL GLY PRO GLY PHE THR GLY ASN PHE SER THR GLN LYS SEQRES 23 A 695 VAL LYS MET HIS ILE HIS SER THR ASN GLU VAL THR ARG SEQRES 24 A 695 ILE TYR ASN VAL ILE GLY THR LEU ARG GLY ALA VAL GLU SEQRES 25 A 695 PRO ASP ARG TYR VAL ILE LEU GLY GLY HIS ARG ASP SER SEQRES 26 A 695 TRP VAL PHE GLY GLY ILE ASP PRO GLN SER GLY ALA ALA SEQRES 27 A 695 VAL VAL HIS GLU ILE VAL ARG SER PHE GLY THR LEU LYS SEQRES 28 A 695 LYS GLU GLY TRP ARG PRO ARG ARG THR ILE LEU PHE ALA SEQRES 29 A 695 SER TRP ASP ALA GLU GLU PHE GLY LEU LEU GLY SER THR SEQRES 30 A 695 GLU TRP ALA GLU GLU ASN SER ARG LEU LEU GLN GLU ARG SEQRES 31 A 695 GLY VAL ALA TYR ILE ASN ALA ASP SER SER ILE GLU GLY SEQRES 32 A 695 ASN TYR THR LEU ARG VAL ASP CYS THR PRO LEU MET TYR SEQRES 33 A 695 SER LEU VAL HIS ASN LEU THR LYS GLU LEU LYS SER PRO SEQRES 34 A 695 ASP GLU GLY PHE GLU GLY LYS SER LEU TYR GLU SER TRP SEQRES 35 A 695 THR LYS LYS SER PRO SER PRO GLU PHE SER GLY MET PRO SEQRES 36 A 695 ARG ILE SER LYS LEU GLY SER GLY ASN ASP PHE GLU VAL SEQRES 37 A 695 PHE PHE GLN ARG LEU GLY ILE ALA SER GLY ARG ALA ARG SEQRES 38 A 695 TYR THR LYS ASN TRP GLU THR ASN LYS PHE SER GLY TYR SEQRES 39 A 695 PRO LEU TYR HIS SER VAL TYR GLU THR TYR GLU LEU VAL SEQRES 40 A 695 GLU LYS PHE TYR ASP PRO MET PHE LYS TYR HIS LEU THR SEQRES 41 A 695 VAL ALA GLN VAL ARG GLY GLY MET VAL PHE GLU LEU ALA SEQRES 42 A 695 ASN SER ILE VAL LEU PRO PHE ASP CYS ARG ASP TYR ALA SEQRES 43 A 695 VAL VAL LEU ARG LYS TYR ALA ASP LYS ILE TYR SER ILE SEQRES 44 A 695 SER MET LYS HIS PRO GLN GLU MET LYS THR TYR SER VAL SEQRES 45 A 695 SER PHE ASP SER LEU PHE SER ALA VAL LYS ASN PHE THR SEQRES 46 A 695 GLU ILE ALA SER LYS PHE SER GLU ARG LEU GLN ASP PHE SEQRES 47 A 695 ASP LYS SER ASN PRO ILE VAL LEU ARG MET MET ASN ASP SEQRES 48 A 695 GLN LEU MET PHE LEU GLU ARG ALA PHE ILE ASP PRO LEU SEQRES 49 A 695 GLY LEU PRO ASP ARG PRO PHE TYR ARG HIS VAL ILE TYR SEQRES 50 A 695 ALA PRO SER SER HIS ASN LYS TYR ALA GLY GLU SER PHE SEQRES 51 A 695 PRO GLY ILE TYR ASP ALA LEU PHE ASP ILE GLU SER LYS SEQRES 52 A 695 VAL ASP PRO SER LYS ALA TRP GLY GLU VAL LYS ARG GLN SEQRES 53 A 695 ILE TYR VAL ALA ALA PHE THR VAL GLN ALA ALA ALA GLU SEQRES 54 A 695 THR LEU SER GLU VAL ALA SEQRES 1 E 695 HIS ASN MET LYS ALA PHE LEU ASP GLU LEU LYS ALA GLU SEQRES 2 E 695 ASN ILE LYS LYS PHE LEU TYR ASN PHE THR GLN ILE PRO SEQRES 3 E 695 HIS LEU ALA GLY THR GLU GLN ASN PHE GLN LEU ALA LYS SEQRES 4 E 695 GLN ILE GLN SER GLN TRP LYS GLU PHE GLY LEU ASP SER SEQRES 5 E 695 VAL GLU LEU ALA HIS TYR ASP VAL LEU LEU SER TYR PRO SEQRES 6 E 695 ASN LYS THR HIS PRO ASN TYR ILE SER ILE ILE ASN GLU SEQRES 7 E 695 ASP GLY ASN GLU ILE PHE ASN THR SER LEU PHE GLU PRO SEQRES 8 E 695 PRO PRO PRO GLY TYR GLU ASN VAL SER ASP ILE VAL PRO SEQRES 9 E 695 PRO PHE SER ALA PHE SER PRO GLN GLY MET PRO GLU GLY SEQRES 10 E 695 ASP LEU VAL TYR VAL ASN TYR ALA ARG THR GLU ASP PHE SEQRES 11 E 695 PHE LYS LEU GLU ARG ASP MET LYS ILE ASN CYS SER GLY SEQRES 12 E 695 LYS ILE VAL ILE ALA ARG TYR GLY LYS VAL PHE ARG GLY SEQRES 13 E 695 ASN LYS VAL LYS ASN ALA GLN LEU ALA GLY ALA LYS GLY SEQRES 14 E 695 VAL ILE LEU TYR SER ASP PRO ALA ASP TYR PHE ALA PRO SEQRES 15 E 695 GLY VAL LYS SER TYR PRO ASP GLY TRP ASN LEU PRO GLY SEQRES 16 E 695 GLY GLY VAL GLN ARG GLY ASN ILE LEU ASN LEU ASN GLY SEQRES 17 E 695 ALA GLY ASP PRO LEU THR PRO GLY TYR PRO ALA ASN GLU SEQRES 18 E 695 TYR ALA TYR ARG ARG GLY ILE ALA GLU ALA VAL GLY LEU SEQRES 19 E 695 PRO SER ILE PRO VAL HIS PRO ILE GLY TYR TYR ASP ALA SEQRES 20 E 695 GLN LYS LEU LEU GLU LYS MET GLY GLY SER ALA PRO PRO SEQRES 21 E 695 ASP SER SER TRP ARG GLY SER LEU LYS VAL PRO TYR ASN SEQRES 22 E 695 VAL GLY PRO GLY PHE THR GLY ASN PHE SER THR GLN LYS SEQRES 23 E 695 VAL LYS MET HIS ILE HIS SER THR ASN GLU VAL THR ARG SEQRES 24 E 695 ILE TYR ASN VAL ILE GLY THR LEU ARG GLY ALA VAL GLU SEQRES 25 E 695 PRO ASP ARG TYR VAL ILE LEU GLY GLY HIS ARG ASP SER SEQRES 26 E 695 TRP VAL PHE GLY GLY ILE ASP PRO GLN SER GLY ALA ALA SEQRES 27 E 695 VAL VAL HIS GLU ILE VAL ARG SER PHE GLY THR LEU LYS SEQRES 28 E 695 LYS GLU GLY TRP ARG PRO ARG ARG THR ILE LEU PHE ALA SEQRES 29 E 695 SER TRP ASP ALA GLU GLU PHE GLY LEU LEU GLY SER THR SEQRES 30 E 695 GLU TRP ALA GLU GLU ASN SER ARG LEU LEU GLN GLU ARG SEQRES 31 E 695 GLY VAL ALA TYR ILE ASN ALA ASP SER SER ILE GLU GLY SEQRES 32 E 695 ASN TYR THR LEU ARG VAL ASP CYS THR PRO LEU MET TYR SEQRES 33 E 695 SER LEU VAL HIS ASN LEU THR LYS GLU LEU LYS SER PRO SEQRES 34 E 695 ASP GLU GLY PHE GLU GLY LYS SER LEU TYR GLU SER TRP SEQRES 35 E 695 THR LYS LYS SER PRO SER PRO GLU PHE SER GLY MET PRO SEQRES 36 E 695 ARG ILE SER LYS LEU GLY SER GLY ASN ASP PHE GLU VAL SEQRES 37 E 695 PHE PHE GLN ARG LEU GLY ILE ALA SER GLY ARG ALA ARG SEQRES 38 E 695 TYR THR LYS ASN TRP GLU THR ASN LYS PHE SER GLY TYR SEQRES 39 E 695 PRO LEU TYR HIS SER VAL TYR GLU THR TYR GLU LEU VAL SEQRES 40 E 695 GLU LYS PHE TYR ASP PRO MET PHE LYS TYR HIS LEU THR SEQRES 41 E 695 VAL ALA GLN VAL ARG GLY GLY MET VAL PHE GLU LEU ALA SEQRES 42 E 695 ASN SER ILE VAL LEU PRO PHE ASP CYS ARG ASP TYR ALA SEQRES 43 E 695 VAL VAL LEU ARG LYS TYR ALA ASP LYS ILE TYR SER ILE SEQRES 44 E 695 SER MET LYS HIS PRO GLN GLU MET LYS THR TYR SER VAL SEQRES 45 E 695 SER PHE ASP SER LEU PHE SER ALA VAL LYS ASN PHE THR SEQRES 46 E 695 GLU ILE ALA SER LYS PHE SER GLU ARG LEU GLN ASP PHE SEQRES 47 E 695 ASP LYS SER ASN PRO ILE VAL LEU ARG MET MET ASN ASP SEQRES 48 E 695 GLN LEU MET PHE LEU GLU ARG ALA PHE ILE ASP PRO LEU SEQRES 49 E 695 GLY LEU PRO ASP ARG PRO PHE TYR ARG HIS VAL ILE TYR SEQRES 50 E 695 ALA PRO SER SER HIS ASN LYS TYR ALA GLY GLU SER PHE SEQRES 51 E 695 PRO GLY ILE TYR ASP ALA LEU PHE ASP ILE GLU SER LYS SEQRES 52 E 695 VAL ASP PRO SER LYS ALA TRP GLY GLU VAL LYS ARG GLN SEQRES 53 E 695 ILE TYR VAL ALA ALA PHE THR VAL GLN ALA ALA ALA GLU SEQRES 54 E 695 THR LEU SER GLU VAL ALA SEQRES 1 H 123 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 H 123 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ARG SER GLY SEQRES 3 H 123 TRP PRO TYR SER THR TYR SER MET ASN TRP PHE ARG GLN SEQRES 4 H 123 ALA PRO GLY LYS GLU ARG GLU ALA VAL ALA GLY ILE SER SEQRES 5 H 123 SER THR MET SER GLY ILE ILE PHE ALA GLU SER LYS ALA SEQRES 6 H 123 GLY GLN PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR SEQRES 7 H 123 VAL TYR LEU GLN MET ASN ASN LEU LYS PRO GLU ASP THR SEQRES 8 H 123 ALA ILE TYR TYR CYS ALA ALA ARG ARG ASP TYR SER LEU SEQRES 9 H 123 SER SER SER SER ASP ASP PHE ASP TYR TRP GLY GLN GLY SEQRES 10 H 123 THR GLN VAL THR VAL SER SEQRES 1 Q 123 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 Q 123 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ARG SER GLY SEQRES 3 Q 123 TRP PRO TYR SER THR TYR SER MET ASN TRP PHE ARG GLN SEQRES 4 Q 123 ALA PRO GLY LYS GLU ARG GLU ALA VAL ALA GLY ILE SER SEQRES 5 Q 123 SER THR MET SER GLY ILE ILE PHE ALA GLU SER LYS ALA SEQRES 6 Q 123 GLY GLN PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR SEQRES 7 Q 123 VAL TYR LEU GLN MET ASN ASN LEU LYS PRO GLU ASP THR SEQRES 8 Q 123 ALA ILE TYR TYR CYS ALA ALA ARG ARG ASP TYR SER LEU SEQRES 9 Q 123 SER SER SER SER ASP ASP PHE ASP TYR TRP GLY GLN GLY SEQRES 10 Q 123 THR GLN VAL THR VAL SER HET NAG B 1 14 HET NAG B 2 14 HET NAG C 1 14 HET NAG C 2 14 HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET MAN F 4 11 HET MAN F 5 11 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET MAN I 4 11 HET MAN I 5 11 HET NAG A 801 14 HET NAG A 802 14 HET NAG A 803 14 HET NAG A 804 14 HET ZN A 805 1 HET ZN A 806 1 HET CA A 807 1 HET NAG E 801 14 HET NAG E 802 14 HET NAG E 803 14 HET NAG E 804 14 HET ZN E 805 1 HET ZN E 806 1 HET CA E 807 1 HET CL E 808 1 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM ZN ZINC ION HETNAM CA CALCIUM ION HETNAM CL CHLORIDE ION 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 HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 NAG 20(C8 H15 N O6) FORMUL 7 BMA 4(C6 H12 O6) FORMUL 8 MAN 4(C6 H12 O6) FORMUL 15 ZN 4(ZN 2+) FORMUL 17 CA 2(CA 2+) FORMUL 25 CL CL 1- HELIX 1 AA1 ASN A 57 LEU A 65 1 9 HELIX 2 AA2 LYS A 66 THR A 78 1 13 HELIX 3 AA3 THR A 86 GLY A 104 1 19 HELIX 4 AA4 ARG A 181 ARG A 190 1 10 HELIX 5 AA5 PHE A 209 GLY A 221 1 13 HELIX 6 AA6 ASP A 230 PHE A 235 1 6 HELIX 7 AA7 SER A 241 GLY A 245 5 5 HELIX 8 AA8 GLY A 282 ALA A 286 5 5 HELIX 9 AA9 GLY A 298 LYS A 308 1 11 HELIX 10 AB1 THR A 334 SER A 338 5 5 HELIX 11 AB2 PRO A 388 GLY A 409 1 22 HELIX 12 AB3 ALA A 423 GLY A 427 5 5 HELIX 13 AB4 LEU A 428 ASN A 438 1 11 HELIX 14 AB5 ASN A 438 ARG A 445 1 8 HELIX 15 AB6 MET A 470 LEU A 481 1 12 HELIX 16 AB7 SER A 492 SER A 501 1 10 HELIX 17 AB8 ASP A 520 ARG A 527 1 8 HELIX 18 AB9 THR A 558 TYR A 566 1 9 HELIX 19 AC1 PHE A 570 SER A 590 1 21 HELIX 20 AC2 CYS A 597 LYS A 617 1 21 HELIX 21 AC3 HIS A 618 SER A 626 1 9 HELIX 22 AC4 PHE A 629 ASP A 652 1 24 HELIX 23 AC5 ASN A 657 PHE A 675 1 19 HELIX 24 AC6 PHE A 705 PHE A 713 1 9 HELIX 25 AC7 ASP A 714 LYS A 718 5 5 HELIX 26 AC8 ASP A 720 LEU A 746 1 27 HELIX 27 AC9 ASN E 57 LEU E 65 1 9 HELIX 28 AD1 LYS E 66 THR E 78 1 13 HELIX 29 AD2 THR E 86 GLY E 104 1 19 HELIX 30 AD3 ARG E 181 ASP E 191 1 11 HELIX 31 AD4 PHE E 209 GLY E 221 1 13 HELIX 32 AD5 ASP E 230 PHE E 235 1 6 HELIX 33 AD6 SER E 241 GLY E 245 5 5 HELIX 34 AD7 GLY E 282 ALA E 286 5 5 HELIX 35 AD8 GLY E 298 LYS E 308 1 11 HELIX 36 AD9 PRO E 388 LYS E 407 1 20 HELIX 37 AE1 ALA E 423 GLY E 427 5 5 HELIX 38 AE2 LEU E 428 ASN E 438 1 11 HELIX 39 AE3 ASN E 438 ARG E 445 1 8 HELIX 40 AE4 MET E 470 LEU E 481 1 12 HELIX 41 AE5 SER E 492 SER E 501 1 10 HELIX 42 AE6 ASP E 520 ARG E 527 1 8 HELIX 43 AE7 THR E 558 TYR E 566 1 9 HELIX 44 AE8 PHE E 570 SER E 590 1 21 HELIX 45 AE9 CYS E 597 LYS E 617 1 21 HELIX 46 AF1 HIS E 618 SER E 626 1 9 HELIX 47 AF2 PHE E 629 ASP E 652 1 24 HELIX 48 AF3 ASN E 657 PHE E 675 1 19 HELIX 49 AF4 PHE E 705 PHE E 713 1 9 HELIX 50 AF5 ASP E 714 LYS E 718 5 5 HELIX 51 AF6 ASP E 720 THR E 745 1 26 HELIX 52 AF7 ALA H 61 ALA H 65 5 5 HELIX 53 AF8 LYS H 87 THR H 91 5 5 HELIX 54 AF9 LYS Q 87 THR Q 91 5 5 SHEET 1 AA1 7 SER A 107 TYR A 119 0 SHEET 2 AA1 7 THR A 349 LEU A 362 -1 O GLU A 351 N LEU A 117 SHEET 3 AA1 7 ARG A 414 SER A 420 -1 O PHE A 418 N GLY A 360 SHEET 4 AA1 7 GLU A 367 LEU A 374 1 N VAL A 372 O THR A 415 SHEET 5 AA1 7 GLY A 446 ILE A 450 1 O ALA A 448 N ILE A 373 SHEET 6 AA1 7 ALA A 531 THR A 538 1 O ALA A 531 N TYR A 449 SHEET 7 AA1 7 THR A 461 CYS A 466 -1 N THR A 461 O THR A 538 SHEET 1 AA2 4 PHE A 139 ASN A 140 0 SHEET 2 AA2 4 TYR A 127 ILE A 131 -1 N ILE A 130 O PHE A 139 SHEET 3 AA2 4 LYS A 341 HIS A 345 -1 O LYS A 343 N SER A 129 SHEET 4 AA2 4 GLU A 171 GLY A 172 -1 N GLY A 172 O VAL A 342 SHEET 1 AA3 2 SER A 162 ALA A 163 0 SHEET 2 AA3 2 GLY A 256 ASN A 257 1 N GLY A 256 O ALA A 163 SHEET 1 AA4 4 LEU A 174 TYR A 176 0 SHEET 2 AA4 4 ILE A 200 ARG A 204 1 O ILE A 202 N VAL A 175 SHEET 3 AA4 4 VAL A 225 TYR A 228 1 O ILE A 226 N ALA A 203 SHEET 4 AA4 4 VAL A 294 ILE A 297 1 O ILE A 297 N LEU A 227 SHEET 1 AA5 7 SER E 107 TYR E 119 0 SHEET 2 AA5 7 THR E 349 LEU E 362 -1 O GLU E 351 N LEU E 117 SHEET 3 AA5 7 ARG E 414 SER E 420 -1 O PHE E 418 N GLY E 360 SHEET 4 AA5 7 GLU E 367 LEU E 374 1 N VAL E 372 O THR E 415 SHEET 5 AA5 7 GLY E 446 ILE E 450 1 O ILE E 450 N ILE E 373 SHEET 6 AA5 7 ALA E 531 THR E 538 1 O ALA E 531 N TYR E 449 SHEET 7 AA5 7 THR E 461 CYS E 466 -1 N THR E 461 O THR E 538 SHEET 1 AA610 GLU E 171 GLY E 172 0 SHEET 2 AA610 LYS E 341 LYS E 343 -1 O VAL E 342 N GLY E 172 SHEET 3 AA610 SER E 129 ILE E 131 -1 N SER E 129 O LYS E 343 SHEET 4 AA610 PHE E 139 ASN E 140 -1 O PHE E 139 N ILE E 130 SHEET 5 AA610 GLY Q 57 ILE Q 59 -1 O GLY Q 57 N ASN E 140 SHEET 6 AA610 ARG Q 45 SER Q 52 -1 N GLY Q 50 O ILE Q 58 SHEET 7 AA610 SER Q 33 GLN Q 39 -1 N MET Q 34 O ILE Q 51 SHEET 8 AA610 ALA Q 92 ARG Q 99 -1 O ILE Q 93 N GLN Q 39 SHEET 9 AA610 THR Q 118 THR Q 121 -1 O THR Q 118 N TYR Q 94 SHEET 10 AA610 GLY Q 10 SER Q 11 1 N GLY Q 10 O THR Q 121 SHEET 1 AA7 9 GLU E 171 GLY E 172 0 SHEET 2 AA7 9 LYS E 341 LYS E 343 -1 O VAL E 342 N GLY E 172 SHEET 3 AA7 9 SER E 129 ILE E 131 -1 N SER E 129 O LYS E 343 SHEET 4 AA7 9 PHE E 139 ASN E 140 -1 O PHE E 139 N ILE E 130 SHEET 5 AA7 9 GLY Q 57 ILE Q 59 -1 O GLY Q 57 N ASN E 140 SHEET 6 AA7 9 ARG Q 45 SER Q 52 -1 N GLY Q 50 O ILE Q 58 SHEET 7 AA7 9 SER Q 33 GLN Q 39 -1 N MET Q 34 O ILE Q 51 SHEET 8 AA7 9 ALA Q 92 ARG Q 99 -1 O ILE Q 93 N GLN Q 39 SHEET 9 AA7 9 TYR Q 113 TRP Q 114 -1 O TYR Q 113 N ALA Q 98 SHEET 1 AA8 2 SER E 162 ALA E 163 0 SHEET 2 AA8 2 GLY E 256 ASN E 257 1 N GLY E 256 O ALA E 163 SHEET 1 AA9 4 LEU E 174 TYR E 176 0 SHEET 2 AA9 4 ILE E 200 ARG E 204 1 O ILE E 202 N VAL E 175 SHEET 3 AA9 4 VAL E 225 TYR E 228 1 O ILE E 226 N ALA E 203 SHEET 4 AA9 4 VAL E 294 ILE E 297 1 O ILE E 297 N LEU E 227 SHEET 1 AB1 4 GLN H 3 GLU H 6 0 SHEET 2 AB1 4 ARG H 19 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AB1 4 THR H 78 GLN H 82 -1 O LEU H 81 N LEU H 20 SHEET 4 AB1 4 THR H 69 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AB2 5 GLY H 57 ILE H 59 0 SHEET 2 AB2 5 ARG H 45 SER H 52 -1 N GLY H 50 O ILE H 58 SHEET 3 AB2 5 SER H 33 GLN H 39 -1 N MET H 34 O ILE H 51 SHEET 4 AB2 5 ALA H 92 ARG H 99 -1 O ILE H 93 N GLN H 39 SHEET 5 AB2 5 TYR H 113 TRP H 114 -1 O TYR H 113 N ALA H 98 SHEET 1 AB3 5 GLY H 57 ILE H 59 0 SHEET 2 AB3 5 ARG H 45 SER H 52 -1 N GLY H 50 O ILE H 58 SHEET 3 AB3 5 SER H 33 GLN H 39 -1 N MET H 34 O ILE H 51 SHEET 4 AB3 5 ALA H 92 ARG H 99 -1 O ILE H 93 N GLN H 39 SHEET 5 AB3 5 THR H 118 VAL H 120 -1 O THR H 118 N TYR H 94 SHEET 1 AB4 4 GLU Q 6 SER Q 7 0 SHEET 2 AB4 4 ARG Q 19 ALA Q 23 -1 O SER Q 21 N SER Q 7 SHEET 3 AB4 4 THR Q 78 MET Q 83 -1 O LEU Q 81 N LEU Q 20 SHEET 4 AB4 4 PHE Q 68 ASP Q 73 -1 N ASP Q 73 O THR Q 78 LINK ND2 ASN A 121 C1 NAG A 801 1555 1555 1.44 LINK ND2 ASN A 140 C1 NAG A 802 1555 1555 1.44 LINK ND2 ASN A 459 C1 NAG A 804 1555 1555 1.44 LINK ND2 ASN E 121 C1 NAG E 801 1555 1555 1.44 LINK ND2 ASN E 140 C1 NAG E 802 1555 1555 1.44 LINK ND2 ASN E 459 C1 NAG E 804 1555 1555 1.45 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.45 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.45 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44 LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.45 LINK O6 BMA F 3 C1 MAN F 5 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.45 LINK O6 BMA I 3 C1 MAN I 5 1555 1555 1.44 LINK O THR A 269 CA CA A 807 1555 1555 2.38 LINK OG1 THR A 269 CA CA A 807 1555 1555 2.66 LINK O TYR A 272 CA CA A 807 1555 1555 2.42 LINK NE2 HIS A 377 ZN ZN A 806 1555 1555 2.30 LINK OD2 ASP A 387 ZN ZN A 805 1555 1555 2.36 LINK OD1 ASP A 387 ZN ZN A 806 1555 1555 2.02 LINK OE1 GLU A 425 ZN ZN A 805 1555 1555 2.32 LINK OE1 GLU A 433 CA CA A 807 1555 1555 2.35 LINK OE2 GLU A 433 CA CA A 807 1555 1555 2.49 LINK OE1 GLU A 436 CA CA A 807 1555 1555 2.40 LINK OD1 ASP A 453 ZN ZN A 806 1555 1555 2.16 LINK OD2 ASP A 453 ZN ZN A 806 1555 1555 2.21 LINK NE2 HIS A 553 ZN ZN A 805 1555 1555 2.30 LINK O THR E 269 CA CA E 807 1555 1555 2.36 LINK OG1 THR E 269 CA CA E 807 1555 1555 2.70 LINK O TYR E 272 CA CA E 807 1555 1555 2.43 LINK NE2 HIS E 377 ZN ZN E 806 1555 1555 2.30 LINK OD2 ASP E 387 ZN ZN E 805 1555 1555 2.34 LINK OD1 ASP E 387 ZN ZN E 806 1555 1555 2.01 LINK OE1 GLU E 425 ZN ZN E 805 1555 1555 2.29 LINK OE1 GLU E 433 CA CA E 807 1555 1555 2.34 LINK OE2 GLU E 433 CA CA E 807 1555 1555 2.49 LINK OE1 GLU E 436 CA CA E 807 1555 1555 2.39 LINK OD1 ASP E 453 ZN ZN E 806 1555 1555 2.28 LINK OD2 ASP E 453 ZN ZN E 806 1555 1555 2.16 LINK NE2 HIS E 553 ZN ZN E 805 1555 1555 2.30 CISPEP 1 ASP A 387 PRO A 388 0 1.05 CISPEP 2 ASP E 387 PRO E 388 0 0.33 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