HEADER MEMBRANE PROTEIN 29-DEC-24 9HVK TITLE PSMA IN COMPLEX WITH NANOBODY 7 AND 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: NANOBODY 7; COMPND 15 CHAIN: H, Q; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 3; COMPND 18 MOLECULE: NANOBODY 8; COMPND 19 CHAIN: P, M; COMPND 20 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; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: CAMELUS DROMEDARIUS; SOURCE 15 ORGANISM_TAXID: 9838; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 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 9HVK 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. 3.00 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) : 3.000 REMARK 3 NUMBER OF PARTICLES : 774655 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 9HVK 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_1292144313. 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, H, Q, P, M, B, C, D, F, REMARK 350 AND CHAINS: 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 VAL A 474 OG1 THR A 478 2.19 REMARK 500 OH TYR A 733 O PRO E 273 2.19 REMARK 500 NZ LYS A 71 OH TYR A 559 2.19 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 57 -165.93 -162.69 REMARK 500 LEU A 110 51.78 -119.20 REMARK 500 ILE A 138 -62.34 -98.38 REMARK 500 ASN A 178 -135.77 56.81 REMARK 500 LYS A 207 -9.78 72.68 REMARK 500 TYR A 234 32.11 -143.71 REMARK 500 ALA A 423 17.95 58.93 REMARK 500 LEU A 429 -86.60 11.30 REMARK 500 VAL A 447 -60.18 -109.52 REMARK 500 ASN A 519 -174.12 59.04 REMARK 500 ASP A 567 105.44 -44.65 REMARK 500 ILE E 138 -60.25 -98.32 REMARK 500 ASN E 178 -134.57 55.32 REMARK 500 LYS E 207 -10.51 72.96 REMARK 500 TYR E 234 44.36 -141.19 REMARK 500 PRO E 267 1.05 -66.71 REMARK 500 PHE E 383 -31.42 -39.95 REMARK 500 ALA E 423 17.71 59.71 REMARK 500 PHE E 426 37.60 -99.83 REMARK 500 LEU E 429 -84.27 17.50 REMARK 500 TYR E 460 -57.53 -121.89 REMARK 500 ASN E 519 -175.68 61.16 REMARK 500 PRO Q 88 -8.34 -51.66 REMARK 500 ASP Q 90 48.96 -88.14 REMARK 500 VAL P 48 -62.49 -97.13 REMARK 500 LYS P 64 53.54 -93.12 REMARK 500 VAL M 48 -62.47 -100.60 REMARK 500 MET M 55 -1.07 68.41 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 801 REMARK 610 NAG A 802 REMARK 610 NAG A 803 REMARK 610 NAG A 804 REMARK 610 NAG E 801 REMARK 610 NAG E 802 REMARK 610 NAG E 803 REMARK 610 NAG E 804 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 ZN A 805 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ARG A 255 O REMARK 620 2 HIS A 553 ND1 66.1 REMARK 620 N 1 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 60.7 REMARK 620 3 TYR A 272 O 74.5 70.2 REMARK 620 4 GLU A 433 OE1 143.8 84.9 83.9 REMARK 620 5 GLU A 433 OE2 142.3 111.9 141.1 58.4 REMARK 620 6 GLU A 436 OE1 111.0 144.0 73.9 89.8 95.0 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 85.3 REMARK 620 3 ASP A 453 OD2 72.9 92.4 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 ARG E 255 O REMARK 620 2 HIS E 553 ND1 81.6 REMARK 620 N 1 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 69.5 REMARK 620 3 TYR E 272 O 69.7 71.4 REMARK 620 4 GLU E 433 OE1 149.1 88.6 82.9 REMARK 620 5 GLU E 433 OE2 151.4 119.5 138.1 58.7 REMARK 620 6 GLU E 436 OE1 100.5 136.1 65.2 79.9 90.2 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 453 OD2 75.6 REMARK 620 N 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-52436 RELATED DB: EMDB REMARK 900 PSMA IN COMPLEX WITH NANOBODY 8 DBREF 9HVK A 56 750 UNP Q04609 FOLH1_HUMAN 56 750 DBREF 9HVK E 56 750 UNP Q04609 FOLH1_HUMAN 56 750 DBREF 9HVK H 1 126 PDB 9HVK 9HVK 1 126 DBREF 9HVK Q 1 126 PDB 9HVK 9HVK 1 126 DBREF 9HVK P 2 123 PDB 9HVK 9HVK 2 123 DBREF 9HVK M 2 123 PDB 9HVK 9HVK 2 123 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 126 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 H 126 ALA GLY GLY SER LEU ARG LEU SER CYS THR ALA PRO GLY SEQRES 3 H 126 TYR THR ASP SER ASN TYR TYR MET SER TRP PHE ARG GLN SEQRES 4 H 126 ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA GLY VAL ASN SEQRES 5 H 126 THR GLY ARG GLY SER THR SER TYR ALA ASP SER VAL LYS SEQRES 6 H 126 GLY ARG PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR SEQRES 7 H 126 MET PHE LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 H 126 ALA GLN TYR TYR CYS ALA VAL ALA ALA CYS HIS PHE CYS SEQRES 9 H 126 ASP SER LEU PRO LYS THR GLN ASP GLU TYR ILE LEU TRP SEQRES 10 H 126 GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 1 Q 126 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 Q 126 ALA GLY GLY SER LEU ARG LEU SER CYS THR ALA PRO GLY SEQRES 3 Q 126 TYR THR ASP SER ASN TYR TYR MET SER TRP PHE ARG GLN SEQRES 4 Q 126 ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA GLY VAL ASN SEQRES 5 Q 126 THR GLY ARG GLY SER THR SER TYR ALA ASP SER VAL LYS SEQRES 6 Q 126 GLY ARG PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR SEQRES 7 Q 126 MET PHE LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 Q 126 ALA GLN TYR TYR CYS ALA VAL ALA ALA CYS HIS PHE CYS SEQRES 9 Q 126 ASP SER LEU PRO LYS THR GLN ASP GLU TYR ILE LEU TRP SEQRES 10 Q 126 GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 1 P 122 VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN ALA SEQRES 2 P 122 GLY GLY SER LEU ARG LEU SER CYS ALA ARG SER GLY TRP SEQRES 3 P 122 PRO TYR SER THR TYR SER MET ASN TRP PHE ARG GLN ALA SEQRES 4 P 122 PRO GLY LYS GLU ARG GLU ALA VAL ALA GLY ILE SER SER SEQRES 5 P 122 THR MET SER GLY ILE ILE PHE ALA GLU SER LYS ALA GLY SEQRES 6 P 122 GLN PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR VAL SEQRES 7 P 122 TYR LEU GLN MET ASN ASN LEU LYS PRO GLU ASP THR ALA SEQRES 8 P 122 ILE TYR TYR CYS ALA ALA ARG ARG ASP TYR SER LEU SER SEQRES 9 P 122 SER SER SER ASP ASP PHE ASP TYR TRP GLY GLN GLY THR SEQRES 10 P 122 GLN VAL THR VAL SER SEQRES 1 M 122 VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN ALA SEQRES 2 M 122 GLY GLY SER LEU ARG LEU SER CYS ALA ARG SER GLY TRP SEQRES 3 M 122 PRO TYR SER THR TYR SER MET ASN TRP PHE ARG GLN ALA SEQRES 4 M 122 PRO GLY LYS GLU ARG GLU ALA VAL ALA GLY ILE SER SER SEQRES 5 M 122 THR MET SER GLY ILE ILE PHE ALA GLU SER LYS ALA GLY SEQRES 6 M 122 GLN PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR VAL SEQRES 7 M 122 TYR LEU GLN MET ASN ASN LEU LYS PRO GLU ASP THR ALA SEQRES 8 M 122 ILE TYR TYR CYS ALA ALA ARG ARG ASP TYR SER LEU SER SEQRES 9 M 122 SER SER SER ASP ASP PHE ASP TYR TRP GLY GLN GLY THR SEQRES 10 M 122 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 7 NAG 20(C8 H15 N O6) FORMUL 9 BMA 4(C6 H12 O6) FORMUL 10 MAN 4(C6 H12 O6) FORMUL 17 ZN 4(ZN 2+) FORMUL 19 CA 2(CA 2+) FORMUL 27 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 ASP A 191 1 11 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 TYR A 299 GLU A 307 1 9 HELIX 8 AA8 THR A 334 SER A 338 5 5 HELIX 9 AA9 PRO A 388 GLY A 409 1 22 HELIX 10 AB1 ALA A 423 GLY A 427 5 5 HELIX 11 AB2 LEU A 428 ASN A 438 1 11 HELIX 12 AB3 ASN A 438 ARG A 445 1 8 HELIX 13 AB4 MET A 470 LEU A 481 1 12 HELIX 14 AB5 SER A 492 SER A 501 1 10 HELIX 15 AB6 ASP A 520 ARG A 527 1 8 HELIX 16 AB7 THR A 558 PHE A 565 1 8 HELIX 17 AB8 PHE A 570 ASN A 589 1 20 HELIX 18 AB9 ASP A 596 MET A 616 1 21 HELIX 19 AC1 HIS A 618 TYR A 625 1 8 HELIX 20 AC2 PHE A 629 PHE A 653 1 25 HELIX 21 AC3 ASN A 657 ALA A 674 1 18 HELIX 22 AC4 PHE A 705 PHE A 713 1 9 HELIX 23 AC5 ASP A 720 LEU A 746 1 27 HELIX 24 AC6 ASN E 57 ASP E 63 1 7 HELIX 25 AC7 LYS E 66 THR E 78 1 13 HELIX 26 AC8 THR E 86 GLY E 104 1 19 HELIX 27 AC9 ARG E 181 ASP E 191 1 11 HELIX 28 AD1 PHE E 209 ALA E 220 1 12 HELIX 29 AD2 ASP E 230 PHE E 235 1 6 HELIX 30 AD3 TYR E 299 GLU E 307 1 9 HELIX 31 AD4 ASP E 316 ARG E 320 5 5 HELIX 32 AD5 PRO E 388 GLY E 409 1 22 HELIX 33 AD6 ALA E 423 GLY E 427 5 5 HELIX 34 AD7 LEU E 428 ASN E 438 1 11 HELIX 35 AD8 ASN E 438 ARG E 445 1 8 HELIX 36 AD9 MET E 470 LEU E 481 1 12 HELIX 37 AE1 SER E 492 SER E 501 1 10 HELIX 38 AE2 ASP E 520 ARG E 527 1 8 HELIX 39 AE3 ASN E 540 ASN E 544 5 5 HELIX 40 AE4 THR E 558 TYR E 566 1 9 HELIX 41 AE5 PHE E 570 ASN E 589 1 20 HELIX 42 AE6 ASP E 596 MET E 616 1 21 HELIX 43 AE7 HIS E 618 TYR E 625 1 8 HELIX 44 AE8 PHE E 629 PHE E 653 1 25 HELIX 45 AE9 ASN E 657 ALA E 674 1 18 HELIX 46 AF1 PHE E 705 PHE E 713 1 9 HELIX 47 AF2 ASP E 720 LEU E 746 1 27 HELIX 48 AF3 ALA P 61 ALA P 65 5 5 HELIX 49 AF4 LYS P 87 THR P 91 5 5 HELIX 50 AF5 ALA M 61 ALA M 65 5 5 HELIX 51 AF6 LYS M 87 THR M 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 THR A 361 N SER A 107 SHEET 3 AA1 7 ARG A 414 TRP A 421 -1 O ILE A 416 N LEU A 362 SHEET 4 AA1 7 GLU A 367 HIS A 377 1 N LEU A 374 O LEU A 417 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 ILE A 138 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 4 LEU A 174 TYR A 176 0 SHEET 2 AA3 4 ILE A 200 ARG A 204 1 O ILE A 202 N VAL A 175 SHEET 3 AA3 4 GLY A 224 TYR A 228 1 O GLY A 224 N VAL A 201 SHEET 4 AA3 4 VAL A 294 PRO A 296 1 O HIS A 295 N VAL A 225 SHEET 1 AA4 7 SER E 107 PRO E 120 0 SHEET 2 AA4 7 SER E 348 LEU E 362 -1 O ILE E 355 N TYR E 113 SHEET 3 AA4 7 ARG E 414 TRP E 421 -1 O ILE E 416 N LEU E 362 SHEET 4 AA4 7 GLU E 367 HIS E 377 1 N VAL E 372 O LEU E 417 SHEET 5 AA4 7 GLY E 446 ASN E 451 1 O VAL E 447 N TYR E 371 SHEET 6 AA4 7 ALA E 531 THR E 538 1 O ALA E 531 N TYR E 449 SHEET 7 AA4 7 THR E 461 CYS E 466 -1 N ASP E 465 O ARG E 534 SHEET 1 AA5 4 GLU E 137 ASN E 140 0 SHEET 2 AA5 4 ILE E 128 ILE E 131 -1 N ILE E 130 O ILE E 138 SHEET 3 AA5 4 LYS E 341 MET E 344 -1 O LYS E 343 N SER E 129 SHEET 4 AA5 4 GLU E 171 GLY E 172 -1 N GLY E 172 O VAL E 342 SHEET 1 AA6 4 LEU E 174 TYR E 176 0 SHEET 2 AA6 4 ILE E 200 ARG E 204 1 O ILE E 202 N VAL E 175 SHEET 3 AA6 4 VAL E 225 TYR E 228 1 O ILE E 226 N ALA E 203 SHEET 4 AA6 4 VAL E 294 PRO E 296 1 O HIS E 295 N VAL E 225 SHEET 1 AA7 4 GLN H 5 GLY H 8 0 SHEET 2 AA7 4 SER H 17 THR H 23 -1 O SER H 21 N SER H 7 SHEET 3 AA7 4 THR H 78 ASN H 84 -1 O MET H 83 N LEU H 18 SHEET 4 AA7 4 THR H 69 GLN H 72 -1 N SER H 71 O PHE H 80 SHEET 1 AA8 2 SER H 11 GLN H 13 0 SHEET 2 AA8 2 VAL H 123 VAL H 125 1 O VAL H 123 N VAL H 12 SHEET 1 AA9 5 SER H 57 TYR H 60 0 SHEET 2 AA9 5 ARG H 45 ASN H 52 -1 N GLY H 50 O SER H 59 SHEET 3 AA9 5 TYR H 32 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AA9 5 GLN H 93 ALA H 100 -1 O TYR H 95 N PHE H 37 SHEET 5 AA9 5 LEU H 116 TRP H 117 -1 O LEU H 116 N VAL H 98 SHEET 1 AB1 4 GLN Q 5 GLY Q 8 0 SHEET 2 AB1 4 SER Q 17 THR Q 23 -1 O SER Q 21 N SER Q 7 SHEET 3 AB1 4 THR Q 78 ASN Q 84 -1 O MET Q 83 N LEU Q 18 SHEET 4 AB1 4 THR Q 69 GLN Q 72 -1 N SER Q 71 O PHE Q 80 SHEET 1 AB2 2 VAL Q 12 GLN Q 13 0 SHEET 2 AB2 2 THR Q 124 VAL Q 125 1 O VAL Q 125 N VAL Q 12 SHEET 1 AB3 5 THR Q 58 TYR Q 60 0 SHEET 2 AB3 5 ARG Q 45 ASN Q 52 -1 N GLY Q 50 O SER Q 59 SHEET 3 AB3 5 TYR Q 32 GLN Q 39 -1 N MET Q 34 O VAL Q 51 SHEET 4 AB3 5 GLN Q 93 ALA Q 100 -1 O TYR Q 95 N PHE Q 37 SHEET 5 AB3 5 LEU Q 116 TRP Q 117 -1 O LEU Q 116 N VAL Q 98 SHEET 1 AB4 4 GLN P 3 SER P 7 0 SHEET 2 AB4 4 ARG P 19 SER P 25 -1 O SER P 25 N GLN P 3 SHEET 3 AB4 4 THR P 78 MET P 83 -1 O VAL P 79 N CYS P 22 SHEET 4 AB4 4 PHE P 68 ASP P 73 -1 N SER P 71 O TYR P 80 SHEET 1 AB5 5 GLY P 57 ILE P 59 0 SHEET 2 AB5 5 GLU P 46 ILE P 51 -1 N GLY P 50 O ILE P 58 SHEET 3 AB5 5 ASN P 35 GLN P 39 -1 N ARG P 38 O GLU P 46 SHEET 4 AB5 5 ALA P 92 ALA P 98 -1 O ILE P 93 N GLN P 39 SHEET 5 AB5 5 TYR P 113 TRP P 114 -1 O TYR P 113 N ALA P 98 SHEET 1 AB6 5 GLY P 57 ILE P 59 0 SHEET 2 AB6 5 GLU P 46 ILE P 51 -1 N GLY P 50 O ILE P 58 SHEET 3 AB6 5 ASN P 35 GLN P 39 -1 N ARG P 38 O GLU P 46 SHEET 4 AB6 5 ALA P 92 ALA P 98 -1 O ILE P 93 N GLN P 39 SHEET 5 AB6 5 GLN P 119 VAL P 120 -1 O VAL P 120 N ALA P 92 SHEET 1 AB7 4 GLU M 6 SER M 7 0 SHEET 2 AB7 4 ARG M 19 ALA M 23 -1 O SER M 21 N SER M 7 SHEET 3 AB7 4 THR M 78 MET M 83 -1 O LEU M 81 N LEU M 20 SHEET 4 AB7 4 PHE M 68 ASP M 73 -1 N ASP M 73 O THR M 78 SHEET 1 AB8 5 GLY M 57 ILE M 59 0 SHEET 2 AB8 5 GLU M 46 ILE M 51 -1 N GLY M 50 O ILE M 58 SHEET 3 AB8 5 ASN M 35 GLN M 39 -1 N TRP M 36 O VAL M 48 SHEET 4 AB8 5 ALA M 92 ALA M 98 -1 O TYR M 95 N PHE M 37 SHEET 5 AB8 5 TYR M 113 TRP M 114 -1 O TYR M 113 N ALA M 98 SHEET 1 AB9 5 GLY M 57 ILE M 59 0 SHEET 2 AB9 5 GLU M 46 ILE M 51 -1 N GLY M 50 O ILE M 58 SHEET 3 AB9 5 ASN M 35 GLN M 39 -1 N TRP M 36 O VAL M 48 SHEET 4 AB9 5 ALA M 92 ALA M 98 -1 O TYR M 95 N PHE M 37 SHEET 5 AB9 5 THR M 118 VAL M 120 -1 O THR M 118 N TYR M 94 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 2.03 SSBOND 4 CYS Q 101 CYS Q 104 1555 1555 2.03 SSBOND 5 CYS M 22 CYS M 96 1555 1555 2.03 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 1.45 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.45 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 1.44 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 ARG A 255 ZN ZN A 805 1555 1555 2.12 LINK O THR A 269 CA CA A 807 1555 1555 2.17 LINK OG1 THR A 269 CA CA A 807 1555 1555 2.74 LINK O TYR A 272 CA CA A 807 1555 1555 2.53 LINK NE2 HIS A 377 ZN ZN A 806 1555 1555 2.30 LINK OD1 ASP A 387 ZN ZN A 806 1555 1555 2.44 LINK OE1 GLU A 433 CA CA A 807 1555 1555 2.23 LINK OE2 GLU A 433 CA CA A 807 1555 1555 2.26 LINK OE1 GLU A 436 CA CA A 807 1555 1555 2.28 LINK OD2 ASP A 453 ZN ZN A 806 1555 1555 2.10 LINK ND1 HIS A 553 ZN ZN A 805 1555 1555 2.30 LINK O ARG E 255 ZN ZN E 805 1555 1555 2.12 LINK O THR E 269 CA CA E 807 1555 1555 2.16 LINK OG1 THR E 269 CA CA E 807 1555 1555 2.42 LINK O TYR E 272 CA CA E 807 1555 1555 2.75 LINK NE2 HIS E 377 ZN ZN E 806 1555 1555 2.30 LINK OE1 GLU E 433 CA CA E 807 1555 1555 2.23 LINK OE2 GLU E 433 CA CA E 807 1555 1555 2.25 LINK OE1 GLU E 436 CA CA E 807 1555 1555 2.42 LINK OD2 ASP E 453 ZN ZN E 806 1555 1555 2.10 LINK ND1 HIS E 553 ZN ZN E 805 1555 1555 2.30 CISPEP 1 TYR A 242 PRO A 243 0 1.70 CISPEP 2 ASP A 387 PRO A 388 0 -2.39 CISPEP 3 TYR E 242 PRO E 243 0 2.21 CISPEP 4 ASP E 387 PRO E 388 0 -5.23 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