HEADER MEMBRANE PROTEIN 05-DEC-24 9HLW TITLE PROSTATE SPECIFIC MEMBRANE ANTIGEN (PSMA) IN COMPLEX WITH NANOBODY7 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLUTAMATE CARBOXYPEPTIDASE 2; COMPND 3 CHAIN: A, E; COMPND 4 SYNONYM: CELL GROWTH-INHIBITING GENE 27 PROTEIN,FOLATE HYDROLASE 1, COMPND 5 FOLYLPOLY-GAMMA-GLUTAMATE CARBOXYPEPTIDASE,FGCP,GLUTAMATE COMPND 6 CARBOXYPEPTIDASE II,GCPII,MEMBRANE GLUTAMATE CARBOXYPEPTIDASE,MGCP,N- COMPND 7 ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE I,NAALADASE I,PROSTATE- COMPND 8 SPECIFIC MEMBRANE ANTIGEN,PSM,PSMA,PTEROYLPOLY-GAMMA-GLUTAMATE COMPND 9 CARBOXYPEPTIDASE; COMPND 10 EC: 3.4.17.21; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 2; COMPND 13 MOLECULE: NANO BODY 7; COMPND 14 CHAIN: H, Q; COMPND 15 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 NANOBODIES THEIR PROSTATE SPECIFIC MEMBRANE ANTIGEN PSMA PROSTATE KEYWDS 2 CANCER, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR G.ALON,N.PAPO,R.ZARIVACH,R.ZALK REVDAT 1 16-JUL-25 9HLW 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. 2.66 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 1Z8L REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT 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) : 2.660 REMARK 3 NUMBER OF PARTICLES : 478371 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 9HLW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292143438. 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 7 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : HOMEMADE PLUNGER, MANUALLY REMARK 245 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 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 MET A 1 REMARK 465 TRP A 2 REMARK 465 ASN A 3 REMARK 465 LEU A 4 REMARK 465 LEU A 5 REMARK 465 HIS A 6 REMARK 465 GLU A 7 REMARK 465 THR A 8 REMARK 465 ASP A 9 REMARK 465 SER A 10 REMARK 465 ALA A 11 REMARK 465 VAL A 12 REMARK 465 ALA A 13 REMARK 465 THR A 14 REMARK 465 ALA A 15 REMARK 465 ARG A 16 REMARK 465 ARG A 17 REMARK 465 PRO A 18 REMARK 465 ARG A 19 REMARK 465 TRP A 20 REMARK 465 LEU A 21 REMARK 465 CYS A 22 REMARK 465 ALA A 23 REMARK 465 GLY A 24 REMARK 465 ALA A 25 REMARK 465 LEU A 26 REMARK 465 VAL A 27 REMARK 465 LEU A 28 REMARK 465 ALA A 29 REMARK 465 GLY A 30 REMARK 465 GLY A 31 REMARK 465 PHE A 32 REMARK 465 PHE A 33 REMARK 465 LEU A 34 REMARK 465 LEU A 35 REMARK 465 GLY A 36 REMARK 465 PHE A 37 REMARK 465 LEU A 38 REMARK 465 PHE A 39 REMARK 465 GLY A 40 REMARK 465 TRP A 41 REMARK 465 PHE A 42 REMARK 465 ILE A 43 REMARK 465 LYS A 44 REMARK 465 SER A 45 REMARK 465 SER A 46 REMARK 465 ASN A 47 REMARK 465 GLU A 48 REMARK 465 ALA A 49 REMARK 465 THR A 50 REMARK 465 ASN A 51 REMARK 465 ILE A 52 REMARK 465 THR A 53 REMARK 465 PRO A 54 REMARK 465 LYS A 55 REMARK 465 GLY A 335 REMARK 465 ASN A 336 REMARK 465 TYR A 700 REMARK 465 ALA A 701 REMARK 465 GLY A 702 REMARK 465 MET E 1 REMARK 465 TRP E 2 REMARK 465 ASN E 3 REMARK 465 LEU E 4 REMARK 465 LEU E 5 REMARK 465 HIS E 6 REMARK 465 GLU E 7 REMARK 465 THR E 8 REMARK 465 ASP E 9 REMARK 465 SER E 10 REMARK 465 ALA E 11 REMARK 465 VAL E 12 REMARK 465 ALA E 13 REMARK 465 THR E 14 REMARK 465 ALA E 15 REMARK 465 ARG E 16 REMARK 465 ARG E 17 REMARK 465 PRO E 18 REMARK 465 ARG E 19 REMARK 465 TRP E 20 REMARK 465 LEU E 21 REMARK 465 CYS E 22 REMARK 465 ALA E 23 REMARK 465 GLY E 24 REMARK 465 ALA E 25 REMARK 465 LEU E 26 REMARK 465 VAL E 27 REMARK 465 LEU E 28 REMARK 465 ALA E 29 REMARK 465 GLY E 30 REMARK 465 GLY E 31 REMARK 465 PHE E 32 REMARK 465 PHE E 33 REMARK 465 LEU E 34 REMARK 465 LEU E 35 REMARK 465 GLY E 36 REMARK 465 PHE E 37 REMARK 465 LEU E 38 REMARK 465 PHE E 39 REMARK 465 GLY E 40 REMARK 465 TRP E 41 REMARK 465 PHE E 42 REMARK 465 ILE E 43 REMARK 465 LYS E 44 REMARK 465 SER E 45 REMARK 465 SER E 46 REMARK 465 ASN E 47 REMARK 465 GLU E 48 REMARK 465 ALA E 49 REMARK 465 THR E 50 REMARK 465 ASN E 51 REMARK 465 ILE E 52 REMARK 465 THR E 53 REMARK 465 PRO E 54 REMARK 465 LYS E 55 REMARK 465 GLY E 335 REMARK 465 ASN E 336 REMARK 465 TYR E 700 REMARK 465 ALA E 701 REMARK 465 GLY E 702 REMARK 465 SER H 127 REMARK 465 ALA H 128 REMARK 465 ALA H 129 REMARK 465 ALA H 130 REMARK 465 TYR H 131 REMARK 465 PRO H 132 REMARK 465 TYR H 133 REMARK 465 ASP H 134 REMARK 465 VAL H 135 REMARK 465 PRO H 136 REMARK 465 ASP H 137 REMARK 465 TYR H 138 REMARK 465 GLY H 139 REMARK 465 SER H 140 REMARK 465 HIS H 141 REMARK 465 HIS H 142 REMARK 465 HIS H 143 REMARK 465 HIS H 144 REMARK 465 HIS H 145 REMARK 465 HIS H 146 REMARK 465 SER Q 127 REMARK 465 ALA Q 128 REMARK 465 ALA Q 129 REMARK 465 ALA Q 130 REMARK 465 TYR Q 131 REMARK 465 PRO Q 132 REMARK 465 TYR Q 133 REMARK 465 ASP Q 134 REMARK 465 VAL Q 135 REMARK 465 PRO Q 136 REMARK 465 ASP Q 137 REMARK 465 TYR Q 138 REMARK 465 GLY Q 139 REMARK 465 SER Q 140 REMARK 465 HIS Q 141 REMARK 465 HIS Q 142 REMARK 465 HIS Q 143 REMARK 465 HIS Q 144 REMARK 465 HIS Q 145 REMARK 465 HIS Q 146 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 OG SER E 613 O ALA H 100 2.11 REMARK 500 O PRO A 273 OH TYR E 733 2.15 REMARK 500 OH TYR A 733 O PRO E 273 2.16 REMARK 500 OG SER A 517 OE2 GLU A 522 2.16 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 H 81 CA - CB - CG ANGL. DEV. = 14.2 DEGREES REMARK 500 LEU Q 116 CA - CB - CG ANGL. DEV. = 14.7 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 178 -130.05 58.43 REMARK 500 ASP A 191 -61.34 -92.97 REMARK 500 ASN A 275 -169.38 -78.81 REMARK 500 PRO A 368 0.36 -68.11 REMARK 500 VAL A 382 -61.38 -125.81 REMARK 500 SER A 501 69.79 -155.04 REMARK 500 LEU A 551 57.02 -92.10 REMARK 500 PRO A 594 49.26 -74.70 REMARK 500 ASN E 132 -167.54 -79.78 REMARK 500 ASN E 178 -129.74 58.22 REMARK 500 ASN E 275 -169.74 -78.95 REMARK 500 VAL E 382 -61.84 -126.21 REMARK 500 SER E 501 69.85 -155.32 REMARK 500 LEU E 551 52.49 -91.08 REMARK 500 PRO E 594 49.76 -74.70 REMARK 500 TYR H 33 40.34 -106.18 REMARK 500 VAL H 48 -61.56 -124.42 REMARK 500 TYR Q 33 40.91 -105.20 REMARK 500 MET Q 34 125.08 -36.60 REMARK 500 VAL Q 48 -62.68 -122.87 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 65.9 REMARK 620 3 TYR A 272 O 84.4 89.7 REMARK 620 4 GLU A 433 OE1 160.0 94.3 93.2 REMARK 620 5 GLU A 433 OE2 134.5 110.6 140.4 53.1 REMARK 620 6 GLU A 436 OE1 108.2 159.1 69.5 89.4 88.0 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 83.0 REMARK 620 3 ASP A 453 OD2 117.4 101.4 REMARK 620 N 1 2 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 147.8 REMARK 620 3 GLU A 425 OE2 84.9 63.1 REMARK 620 4 HIS A 553 NE2 116.8 76.5 102.3 REMARK 620 N 1 2 3 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 66.4 REMARK 620 3 TYR E 272 O 85.1 90.2 REMARK 620 4 GLU E 433 OE1 160.3 94.1 92.5 REMARK 620 5 GLU E 433 OE2 134.5 108.6 140.0 52.4 REMARK 620 6 GLU E 436 OE1 108.3 159.8 69.7 89.0 89.0 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 83.3 REMARK 620 3 ASP E 453 OD2 117.7 101.9 REMARK 620 N 1 2 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 148.0 REMARK 620 3 GLU E 425 OE2 84.8 63.3 REMARK 620 4 HIS E 553 NE2 117.1 76.3 104.0 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-52273 RELATED DB: EMDB REMARK 900 PROSTATE SPECIFIC MEMBRANE ANTIGEN (PSMA) IN COMPLEX WITH NANOBODY7 DBREF 9HLW A 1 750 UNP Q04609 FOLH1_HUMAN 1 750 DBREF 9HLW E 1 750 UNP Q04609 FOLH1_HUMAN 1 750 DBREF 9HLW H 1 146 PDB 9HLW 9HLW 1 146 DBREF 9HLW Q 1 146 PDB 9HLW 9HLW 1 146 SEQRES 1 A 750 MET TRP ASN LEU LEU HIS GLU THR ASP SER ALA VAL ALA SEQRES 2 A 750 THR ALA ARG ARG PRO ARG TRP LEU CYS ALA GLY ALA LEU SEQRES 3 A 750 VAL LEU ALA GLY GLY PHE PHE LEU LEU GLY PHE LEU PHE SEQRES 4 A 750 GLY TRP PHE ILE LYS SER SER ASN GLU ALA THR ASN ILE SEQRES 5 A 750 THR PRO LYS HIS ASN MET LYS ALA PHE LEU ASP GLU LEU SEQRES 6 A 750 LYS ALA GLU ASN ILE LYS LYS PHE LEU TYR ASN PHE THR SEQRES 7 A 750 GLN ILE PRO HIS LEU ALA GLY THR GLU GLN ASN PHE GLN SEQRES 8 A 750 LEU ALA LYS GLN ILE GLN SER GLN TRP LYS GLU PHE GLY SEQRES 9 A 750 LEU ASP SER VAL GLU LEU ALA HIS TYR ASP VAL LEU LEU SEQRES 10 A 750 SER TYR PRO ASN LYS THR HIS PRO ASN TYR ILE SER ILE SEQRES 11 A 750 ILE ASN GLU ASP GLY ASN GLU ILE PHE ASN THR SER LEU SEQRES 12 A 750 PHE GLU PRO PRO PRO PRO GLY TYR GLU ASN VAL SER ASP SEQRES 13 A 750 ILE VAL PRO PRO PHE SER ALA PHE SER PRO GLN GLY MET SEQRES 14 A 750 PRO GLU GLY ASP LEU VAL TYR VAL ASN TYR ALA ARG THR SEQRES 15 A 750 GLU ASP PHE PHE LYS LEU GLU ARG ASP MET LYS ILE ASN SEQRES 16 A 750 CYS SER GLY LYS ILE VAL ILE ALA ARG TYR GLY LYS VAL SEQRES 17 A 750 PHE ARG GLY ASN LYS VAL LYS ASN ALA GLN LEU ALA GLY SEQRES 18 A 750 ALA LYS GLY VAL ILE LEU TYR SER ASP PRO ALA ASP TYR SEQRES 19 A 750 PHE ALA PRO GLY VAL LYS SER TYR PRO ASP GLY TRP ASN SEQRES 20 A 750 LEU PRO GLY GLY GLY VAL GLN ARG GLY ASN ILE LEU ASN SEQRES 21 A 750 LEU ASN GLY ALA GLY ASP PRO LEU THR PRO GLY TYR PRO SEQRES 22 A 750 ALA ASN GLU TYR ALA TYR ARG ARG GLY ILE ALA GLU ALA SEQRES 23 A 750 VAL GLY LEU PRO SER ILE PRO VAL HIS PRO ILE GLY TYR SEQRES 24 A 750 TYR ASP ALA GLN LYS LEU LEU GLU LYS MET GLY GLY SER SEQRES 25 A 750 ALA PRO PRO ASP SER SER TRP ARG GLY SER LEU LYS VAL SEQRES 26 A 750 PRO TYR ASN VAL GLY PRO GLY PHE THR GLY ASN PHE SER SEQRES 27 A 750 THR GLN LYS VAL LYS MET HIS ILE HIS SER THR ASN GLU SEQRES 28 A 750 VAL THR ARG ILE TYR ASN VAL ILE GLY THR LEU ARG GLY SEQRES 29 A 750 ALA VAL GLU PRO ASP ARG TYR VAL ILE LEU GLY GLY HIS SEQRES 30 A 750 ARG ASP SER TRP VAL PHE GLY GLY ILE ASP PRO GLN SER SEQRES 31 A 750 GLY ALA ALA VAL VAL HIS GLU ILE VAL ARG SER PHE GLY SEQRES 32 A 750 THR LEU LYS LYS GLU GLY TRP ARG PRO ARG ARG THR ILE SEQRES 33 A 750 LEU PHE ALA SER TRP ASP ALA GLU GLU PHE GLY LEU LEU SEQRES 34 A 750 GLY SER THR GLU TRP ALA GLU GLU ASN SER ARG LEU LEU SEQRES 35 A 750 GLN GLU ARG GLY VAL ALA TYR ILE ASN ALA ASP SER SER SEQRES 36 A 750 ILE GLU GLY ASN TYR THR LEU ARG VAL ASP CYS THR PRO SEQRES 37 A 750 LEU MET TYR SER LEU VAL HIS ASN LEU THR LYS GLU LEU SEQRES 38 A 750 LYS SER PRO ASP GLU GLY PHE GLU GLY LYS SER LEU TYR SEQRES 39 A 750 GLU SER TRP THR LYS LYS SER PRO SER PRO GLU PHE SER SEQRES 40 A 750 GLY MET PRO ARG ILE SER LYS LEU GLY SER GLY ASN ASP SEQRES 41 A 750 PHE GLU VAL PHE PHE GLN ARG LEU GLY ILE ALA SER GLY SEQRES 42 A 750 ARG ALA ARG TYR THR LYS ASN TRP GLU THR ASN LYS PHE SEQRES 43 A 750 SER GLY TYR PRO LEU TYR HIS SER VAL TYR GLU THR TYR SEQRES 44 A 750 GLU LEU VAL GLU LYS PHE TYR ASP PRO MET PHE LYS TYR SEQRES 45 A 750 HIS LEU THR VAL ALA GLN VAL ARG GLY GLY MET VAL PHE SEQRES 46 A 750 GLU LEU ALA ASN SER ILE VAL LEU PRO PHE ASP CYS ARG SEQRES 47 A 750 ASP TYR ALA VAL VAL LEU ARG LYS TYR ALA ASP LYS ILE SEQRES 48 A 750 TYR SER ILE SER MET LYS HIS PRO GLN GLU MET LYS THR SEQRES 49 A 750 TYR SER VAL SER PHE ASP SER LEU PHE SER ALA VAL LYS SEQRES 50 A 750 ASN PHE THR GLU ILE ALA SER LYS PHE SER GLU ARG LEU SEQRES 51 A 750 GLN ASP PHE ASP LYS SER ASN PRO ILE VAL LEU ARG MET SEQRES 52 A 750 MET ASN ASP GLN LEU MET PHE LEU GLU ARG ALA PHE ILE SEQRES 53 A 750 ASP PRO LEU GLY LEU PRO ASP ARG PRO PHE TYR ARG HIS SEQRES 54 A 750 VAL ILE TYR ALA PRO SER SER HIS ASN LYS TYR ALA GLY SEQRES 55 A 750 GLU SER PHE PRO GLY ILE TYR ASP ALA LEU PHE ASP ILE SEQRES 56 A 750 GLU SER LYS VAL ASP PRO SER LYS ALA TRP GLY GLU VAL SEQRES 57 A 750 LYS ARG GLN ILE TYR VAL ALA ALA PHE THR VAL GLN ALA SEQRES 58 A 750 ALA ALA GLU THR LEU SER GLU VAL ALA SEQRES 1 E 750 MET TRP ASN LEU LEU HIS GLU THR ASP SER ALA VAL ALA SEQRES 2 E 750 THR ALA ARG ARG PRO ARG TRP LEU CYS ALA GLY ALA LEU SEQRES 3 E 750 VAL LEU ALA GLY GLY PHE PHE LEU LEU GLY PHE LEU PHE SEQRES 4 E 750 GLY TRP PHE ILE LYS SER SER ASN GLU ALA THR ASN ILE SEQRES 5 E 750 THR PRO LYS HIS ASN MET LYS ALA PHE LEU ASP GLU LEU SEQRES 6 E 750 LYS ALA GLU ASN ILE LYS LYS PHE LEU TYR ASN PHE THR SEQRES 7 E 750 GLN ILE PRO HIS LEU ALA GLY THR GLU GLN ASN PHE GLN SEQRES 8 E 750 LEU ALA LYS GLN ILE GLN SER GLN TRP LYS GLU PHE GLY SEQRES 9 E 750 LEU ASP SER VAL GLU LEU ALA HIS TYR ASP VAL LEU LEU SEQRES 10 E 750 SER TYR PRO ASN LYS THR HIS PRO ASN TYR ILE SER ILE SEQRES 11 E 750 ILE ASN GLU ASP GLY ASN GLU ILE PHE ASN THR SER LEU SEQRES 12 E 750 PHE GLU PRO PRO PRO PRO GLY TYR GLU ASN VAL SER ASP SEQRES 13 E 750 ILE VAL PRO PRO PHE SER ALA PHE SER PRO GLN GLY MET SEQRES 14 E 750 PRO GLU GLY ASP LEU VAL TYR VAL ASN TYR ALA ARG THR SEQRES 15 E 750 GLU ASP PHE PHE LYS LEU GLU ARG ASP MET LYS ILE ASN SEQRES 16 E 750 CYS SER GLY LYS ILE VAL ILE ALA ARG TYR GLY LYS VAL SEQRES 17 E 750 PHE ARG GLY ASN LYS VAL LYS ASN ALA GLN LEU ALA GLY SEQRES 18 E 750 ALA LYS GLY VAL ILE LEU TYR SER ASP PRO ALA ASP TYR SEQRES 19 E 750 PHE ALA PRO GLY VAL LYS SER TYR PRO ASP GLY TRP ASN SEQRES 20 E 750 LEU PRO GLY GLY GLY VAL GLN ARG GLY ASN ILE LEU ASN SEQRES 21 E 750 LEU ASN GLY ALA GLY ASP PRO LEU THR PRO GLY TYR PRO SEQRES 22 E 750 ALA ASN GLU TYR ALA TYR ARG ARG GLY ILE ALA GLU ALA SEQRES 23 E 750 VAL GLY LEU PRO SER ILE PRO VAL HIS PRO ILE GLY TYR SEQRES 24 E 750 TYR ASP ALA GLN LYS LEU LEU GLU LYS MET GLY GLY SER SEQRES 25 E 750 ALA PRO PRO ASP SER SER TRP ARG GLY SER LEU LYS VAL SEQRES 26 E 750 PRO TYR ASN VAL GLY PRO GLY PHE THR GLY ASN PHE SER SEQRES 27 E 750 THR GLN LYS VAL LYS MET HIS ILE HIS SER THR ASN GLU SEQRES 28 E 750 VAL THR ARG ILE TYR ASN VAL ILE GLY THR LEU ARG GLY SEQRES 29 E 750 ALA VAL GLU PRO ASP ARG TYR VAL ILE LEU GLY GLY HIS SEQRES 30 E 750 ARG ASP SER TRP VAL PHE GLY GLY ILE ASP PRO GLN SER SEQRES 31 E 750 GLY ALA ALA VAL VAL HIS GLU ILE VAL ARG SER PHE GLY SEQRES 32 E 750 THR LEU LYS LYS GLU GLY TRP ARG PRO ARG ARG THR ILE SEQRES 33 E 750 LEU PHE ALA SER TRP ASP ALA GLU GLU PHE GLY LEU LEU SEQRES 34 E 750 GLY SER THR GLU TRP ALA GLU GLU ASN SER ARG LEU LEU SEQRES 35 E 750 GLN GLU ARG GLY VAL ALA TYR ILE ASN ALA ASP SER SER SEQRES 36 E 750 ILE GLU GLY ASN TYR THR LEU ARG VAL ASP CYS THR PRO SEQRES 37 E 750 LEU MET TYR SER LEU VAL HIS ASN LEU THR LYS GLU LEU SEQRES 38 E 750 LYS SER PRO ASP GLU GLY PHE GLU GLY LYS SER LEU TYR SEQRES 39 E 750 GLU SER TRP THR LYS LYS SER PRO SER PRO GLU PHE SER SEQRES 40 E 750 GLY MET PRO ARG ILE SER LYS LEU GLY SER GLY ASN ASP SEQRES 41 E 750 PHE GLU VAL PHE PHE GLN ARG LEU GLY ILE ALA SER GLY SEQRES 42 E 750 ARG ALA ARG TYR THR LYS ASN TRP GLU THR ASN LYS PHE SEQRES 43 E 750 SER GLY TYR PRO LEU TYR HIS SER VAL TYR GLU THR TYR SEQRES 44 E 750 GLU LEU VAL GLU LYS PHE TYR ASP PRO MET PHE LYS TYR SEQRES 45 E 750 HIS LEU THR VAL ALA GLN VAL ARG GLY GLY MET VAL PHE SEQRES 46 E 750 GLU LEU ALA ASN SER ILE VAL LEU PRO PHE ASP CYS ARG SEQRES 47 E 750 ASP TYR ALA VAL VAL LEU ARG LYS TYR ALA ASP LYS ILE SEQRES 48 E 750 TYR SER ILE SER MET LYS HIS PRO GLN GLU MET LYS THR SEQRES 49 E 750 TYR SER VAL SER PHE ASP SER LEU PHE SER ALA VAL LYS SEQRES 50 E 750 ASN PHE THR GLU ILE ALA SER LYS PHE SER GLU ARG LEU SEQRES 51 E 750 GLN ASP PHE ASP LYS SER ASN PRO ILE VAL LEU ARG MET SEQRES 52 E 750 MET ASN ASP GLN LEU MET PHE LEU GLU ARG ALA PHE ILE SEQRES 53 E 750 ASP PRO LEU GLY LEU PRO ASP ARG PRO PHE TYR ARG HIS SEQRES 54 E 750 VAL ILE TYR ALA PRO SER SER HIS ASN LYS TYR ALA GLY SEQRES 55 E 750 GLU SER PHE PRO GLY ILE TYR ASP ALA LEU PHE ASP ILE SEQRES 56 E 750 GLU SER LYS VAL ASP PRO SER LYS ALA TRP GLY GLU VAL SEQRES 57 E 750 LYS ARG GLN ILE TYR VAL ALA ALA PHE THR VAL GLN ALA SEQRES 58 E 750 ALA ALA GLU THR LEU SER GLU VAL ALA SEQRES 1 H 146 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 H 146 ALA GLY GLY SER LEU ARG LEU SER CYS THR ALA PRO GLY SEQRES 3 H 146 TYR THR ASP SER ASN TYR TYR MET SER TRP PHE ARG GLN SEQRES 4 H 146 ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA GLY VAL ASN SEQRES 5 H 146 THR GLY ARG GLY SER THR SER TYR ALA ASP SER VAL LYS SEQRES 6 H 146 GLY ARG PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR SEQRES 7 H 146 MET PHE LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 H 146 ALA ILE TYR TYR CYS ALA VAL ALA ALA CYS HIS PHE CYS SEQRES 9 H 146 ASP SER LEU PRO LYS THR GLN ASP GLU TYR ILE LEU TRP SEQRES 10 H 146 GLY GLN GLY THR GLN VAL THR VAL SER SER ALA ALA ALA SEQRES 11 H 146 TYR PRO TYR ASP VAL PRO ASP TYR GLY SER HIS HIS HIS SEQRES 12 H 146 HIS HIS HIS SEQRES 1 Q 146 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 Q 146 ALA GLY GLY SER LEU ARG LEU SER CYS THR ALA PRO GLY SEQRES 3 Q 146 TYR THR ASP SER ASN TYR TYR MET SER TRP PHE ARG GLN SEQRES 4 Q 146 ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA GLY VAL ASN SEQRES 5 Q 146 THR GLY ARG GLY SER THR SER TYR ALA ASP SER VAL LYS SEQRES 6 Q 146 GLY ARG PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR SEQRES 7 Q 146 MET PHE LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 Q 146 ALA ILE TYR TYR CYS ALA VAL ALA ALA CYS HIS PHE CYS SEQRES 9 Q 146 ASP SER LEU PRO LYS THR GLN ASP GLU TYR ILE LEU TRP SEQRES 10 Q 146 GLY GLN GLY THR GLN VAL THR VAL SER SER ALA ALA ALA SEQRES 11 Q 146 TYR PRO TYR ASP VAL PRO ASP TYR GLY SER HIS HIS HIS SEQRES 12 Q 146 HIS HIS HIS 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 ASP A 63 1 7 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 ASP A 191 1 11 HELIX 5 AA5 PHE A 209 ALA A 220 1 12 HELIX 6 AA6 ASP A 230 PHE A 235 1 6 HELIX 7 AA7 GLY A 298 LYS A 304 1 7 HELIX 8 AA8 PRO A 388 GLY A 409 1 22 HELIX 9 AA9 GLY A 430 ASN A 438 1 9 HELIX 10 AB1 ASN A 438 ARG A 445 1 8 HELIX 11 AB2 MET A 470 LYS A 479 1 10 HELIX 12 AB3 SER A 492 SER A 501 1 10 HELIX 13 AB4 PHE A 521 GLN A 526 1 6 HELIX 14 AB5 THR A 558 TYR A 566 1 9 HELIX 15 AB6 PHE A 570 SER A 590 1 21 HELIX 16 AB7 ASP A 596 MET A 616 1 21 HELIX 17 AB8 HIS A 618 SER A 626 1 9 HELIX 18 AB9 PHE A 629 PHE A 653 1 25 HELIX 19 AC1 ASN A 657 PHE A 670 1 14 HELIX 20 AC2 LEU A 671 ILE A 676 5 6 HELIX 21 AC3 PHE A 705 LEU A 712 1 8 HELIX 22 AC4 ASP A 720 LEU A 746 1 27 HELIX 23 AC5 ASN E 57 ASP E 63 1 7 HELIX 24 AC6 LYS E 66 THR E 78 1 13 HELIX 25 AC7 THR E 86 GLY E 104 1 19 HELIX 26 AC8 ARG E 181 LYS E 193 1 13 HELIX 27 AC9 PHE E 209 ALA E 220 1 12 HELIX 28 AD1 ASP E 230 PHE E 235 1 6 HELIX 29 AD2 GLY E 298 LYS E 304 1 7 HELIX 30 AD3 PRO E 388 GLY E 409 1 22 HELIX 31 AD4 GLY E 430 ASN E 438 1 9 HELIX 32 AD5 ASN E 438 ARG E 445 1 8 HELIX 33 AD6 MET E 470 LYS E 479 1 10 HELIX 34 AD7 SER E 492 SER E 501 1 10 HELIX 35 AD8 PHE E 521 GLN E 526 1 6 HELIX 36 AD9 THR E 558 TYR E 566 1 9 HELIX 37 AE1 PHE E 570 SER E 590 1 21 HELIX 38 AE2 ASP E 596 LYS E 617 1 22 HELIX 39 AE3 HIS E 618 SER E 626 1 9 HELIX 40 AE4 PHE E 629 PHE E 653 1 25 HELIX 41 AE5 ASN E 657 PHE E 670 1 14 HELIX 42 AE6 LEU E 671 ILE E 676 5 6 HELIX 43 AE7 PHE E 705 LEU E 712 1 8 HELIX 44 AE8 ASP E 720 LEU E 746 1 27 HELIX 45 AE9 THR H 110 TYR H 114 5 5 HELIX 46 AF1 THR Q 110 TYR Q 114 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 TRP A 421 -1 O PHE A 418 N GLY A 360 SHEET 4 AA1 7 GLU A 367 HIS A 377 1 N GLY A 376 O TRP A 421 SHEET 5 AA1 7 GLY A 446 ASN A 451 1 O ILE A 450 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 GLU A 137 ASN A 140 0 SHEET 2 AA2 4 ILE A 128 ILE A 131 -1 N ILE A 130 O PHE A 139 SHEET 3 AA2 4 LYS A 341 MET A 344 -1 O LYS A 341 N ILE A 131 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 O GLY A 256 N ALA A 163 SHEET 1 AA4 3 ILE A 200 ARG A 204 0 SHEET 2 AA4 3 GLY A 224 TYR A 228 1 O ILE A 226 N ALA A 203 SHEET 3 AA4 3 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 TRP E 421 -1 O PHE E 418 N GLY E 360 SHEET 4 AA5 7 GLU E 367 HIS E 377 1 N GLY E 376 O TRP E 421 SHEET 5 AA5 7 GLY E 446 ASN E 451 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 AA6 4 GLU E 137 ASN E 140 0 SHEET 2 AA6 4 ILE E 128 ILE E 131 -1 N ILE E 130 O PHE E 139 SHEET 3 AA6 4 LYS E 341 MET E 344 -1 O LYS E 341 N ILE E 131 SHEET 4 AA6 4 GLU E 171 GLY E 172 -1 N GLY E 172 O VAL E 342 SHEET 1 AA7 2 SER E 162 ALA E 163 0 SHEET 2 AA7 2 GLY E 256 ASN E 257 1 O GLY E 256 N ALA E 163 SHEET 1 AA8 4 LEU E 174 TYR E 176 0 SHEET 2 AA8 4 ILE E 200 ARG E 204 1 O ILE E 202 N VAL E 175 SHEET 3 AA8 4 GLY E 224 TYR E 228 1 O ILE E 226 N ALA E 203 SHEET 4 AA8 4 VAL E 294 ILE E 297 1 O ILE E 297 N LEU E 227 SHEET 1 AA9 4 GLU H 6 SER H 7 0 SHEET 2 AA9 4 LEU H 18 THR H 23 -1 O SER H 21 N SER H 7 SHEET 3 AA9 4 THR H 78 MET H 83 -1 O LEU H 81 N LEU H 20 SHEET 4 AA9 4 PHE H 68 GLN H 72 -1 N SER H 71 O PHE H 80 SHEET 1 AB1 2 SER H 11 VAL H 12 0 SHEET 2 AB1 2 VAL H 123 THR H 124 1 O VAL H 123 N VAL H 12 SHEET 1 AB2 2 ASN H 31 TYR H 32 0 SHEET 2 AB2 2 ALA H 100 CYS H 101 -1 O CYS H 101 N ASN H 31 SHEET 1 AB3 5 SER H 57 TYR H 60 0 SHEET 2 AB3 5 ARG H 45 ASN H 52 -1 N GLY H 50 O SER H 59 SHEET 3 AB3 5 SER H 35 GLN H 39 -1 N TRP H 36 O ALA H 49 SHEET 4 AB3 5 ILE H 93 VAL H 98 -1 O ALA H 97 N SER H 35 SHEET 5 AB3 5 LEU H 116 TRP H 117 -1 O LEU H 116 N VAL H 98 SHEET 1 AB4 4 GLU Q 6 SER Q 7 0 SHEET 2 AB4 4 SER Q 17 THR Q 23 -1 O SER Q 21 N SER Q 7 SHEET 3 AB4 4 THR Q 78 ASN Q 84 -1 O MET Q 83 N LEU Q 18 SHEET 4 AB4 4 PHE Q 68 GLN Q 72 -1 N THR Q 69 O GLN Q 82 SHEET 1 AB5 2 ASN Q 31 TYR Q 32 0 SHEET 2 AB5 2 ALA Q 100 CYS Q 101 -1 O CYS Q 101 N ASN Q 31 SHEET 1 AB6 5 SER Q 57 TYR Q 60 0 SHEET 2 AB6 5 ARG Q 45 ASN Q 52 -1 N GLY Q 50 O SER Q 59 SHEET 3 AB6 5 SER Q 35 GLN Q 39 -1 N ARG Q 38 O GLU Q 46 SHEET 4 AB6 5 ILE Q 93 VAL Q 98 -1 O ALA Q 97 N SER Q 35 SHEET 5 AB6 5 LEU Q 116 TRP Q 117 -1 O LEU Q 116 N VAL Q 98 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 101 CYS H 104 1555 1555 2.03 SSBOND 3 CYS Q 22 CYS Q 96 1555 1555 2.04 SSBOND 4 CYS Q 101 CYS Q 104 1555 1555 2.03 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 1.44 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44 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 1.44 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 1.44 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.44 LINK O6 BMA I 3 C1 MAN I 5 1555 1555 1.44 LINK O THR A 269 CA CA A 807 1555 1555 2.22 LINK OG1 THR A 269 CA CA A 807 1555 1555 2.43 LINK O TYR A 272 CA CA A 807 1555 1555 2.29 LINK NE2 HIS A 377 ZN ZN A 806 1555 1555 2.30 LINK OD2 ASP A 387 ZN ZN A 805 1555 1555 2.21 LINK OD1 ASP A 387 ZN ZN A 806 1555 1555 2.04 LINK OE1 GLU A 425 ZN ZN A 805 1555 1555 2.18 LINK OE2 GLU A 425 ZN ZN A 805 1555 1555 1.99 LINK OE1 GLU A 433 CA CA A 807 1555 1555 2.62 LINK OE2 GLU A 433 CA CA A 807 1555 1555 2.22 LINK OE1 GLU A 436 CA CA A 807 1555 1555 2.76 LINK OD2 ASP A 453 ZN ZN A 806 1555 1555 2.66 LINK NE2 HIS A 553 ZN ZN A 805 1555 1555 2.30 LINK O THR E 269 CA CA E 807 1555 1555 2.22 LINK OG1 THR E 269 CA CA E 807 1555 1555 2.44 LINK O TYR E 272 CA CA E 807 1555 1555 2.28 LINK NE2 HIS E 377 ZN ZN E 806 1555 1555 2.30 LINK OD2 ASP E 387 ZN ZN E 805 1555 1555 2.21 LINK OD1 ASP E 387 ZN ZN E 806 1555 1555 2.04 LINK OE1 GLU E 425 ZN ZN E 805 1555 1555 2.17 LINK OE2 GLU E 425 ZN ZN E 805 1555 1555 2.00 LINK OE1 GLU E 433 CA CA E 807 1555 1555 2.67 LINK OE2 GLU E 433 CA CA E 807 1555 1555 2.21 LINK OE1 GLU E 436 CA CA E 807 1555 1555 2.75 LINK OD2 ASP E 453 ZN ZN E 806 1555 1555 2.66 LINK NE2 HIS E 553 ZN ZN E 805 1555 1555 2.30 CISPEP 1 TYR A 242 PRO A 243 0 3.13 CISPEP 2 ASP A 387 PRO A 388 0 0.08 CISPEP 3 TYR E 242 PRO E 243 0 3.14 CISPEP 4 ASP E 387 PRO E 388 0 -0.08 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