HEADER MEMBRANE PROTEIN 23-AUG-24 9J9Z TITLE CRYO-EM STRUCTURE OF OUTWARD STATE ANHYDROMUROPEPTIDE PERMEASE (AMPG) TITLE 2 COMPLEX WITH GLCNAC-1,6-ANHMURNAC COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-BRIL FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTI-BRIL FAB NANOBODY; COMPND 7 CHAIN: K; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ANTI-BRIL FAB LIGHT CHAIN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: MUROPEPTIDE TRANSPORTER,SOLUBLE CYTOCHROME B562; COMPND 15 CHAIN: A; COMPND 16 SYNONYM: CYTOCHROME B-562; COMPND 17 ENGINEERED: YES; COMPND 18 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 GENE: IGHG1; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 9 ORGANISM_TAXID: 32630; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: IGHG1; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: YOKENELLA REGENSBURGEI, ESCHERICHIA COLI; SOURCE 20 ORGANISM_TAXID: 158877, 562; SOURCE 21 GENE: AMPG, NCTC11967_01129, CYBC; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS AMPG, MFS, ANHYDROMUROPEPTIDE PERMEASE, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR N.CHANG,U.KIM,H.CHO REVDAT 1 16-JUL-25 9J9Z 0 JRNL AUTH N.CHANG,H.KIM,U.KIM,Y.CHO,Y.YOO,H.LEE,J.W.KIM,M.S.KIM,J.LEE, JRNL AUTH 2 Y.L.CHO,K.KIM,D.YONG,H.S.CHO JRNL TITL STRUCTURAL AND FUNCTIONAL INSIGHTS OF AMPG IN MUROPEPTIDE JRNL TITL 2 TRANSPORT AND MULTIPLE BETA-LACTAM ANTIBIOTICS RESISTANCE. JRNL REF NAT COMMUN V. 16 5744 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 40593790 JRNL DOI 10.1038/S41467-025-61169-3 REMARK 2 REMARK 2 RESOLUTION. 2.97 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL 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) : 2.970 REMARK 3 NUMBER OF PARTICLES : 173837 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9J9Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1300050743. 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 : REMARK 245 AMPG(G50W/L269W)_BRIL_FAB_NANOBODY COMPLEX REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 11.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 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 KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 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) : 5000.00 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) : 300 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 APPLY THE FOLLOWING TO CHAINS: H, K, L, A 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS H 223 CG CD CE NZ REMARK 470 LYS K 76 CG CD CE NZ REMARK 470 LYS L 40 CG CD CE NZ REMARK 470 LYS L 43 CG CD CE NZ 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 CG2 THR K 91 O VAL K 119 1.89 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER H 126 -167.14 -163.06 REMARK 500 TYR H 159 148.45 -171.28 REMARK 500 ARG K 31 -2.16 69.68 REMARK 500 VAL K 48 -63.96 -121.75 REMARK 500 SER K 54 -134.72 46.32 REMARK 500 SER K 63 33.85 -94.46 REMARK 500 THR K 91 97.46 -69.26 REMARK 500 SER L 31 -153.60 60.54 REMARK 500 ALA L 52 -10.69 72.67 REMARK 500 SER L 53 -14.40 -141.54 REMARK 500 ALA L 85 -169.22 -161.88 REMARK 500 PHE L 100 -169.84 -126.02 REMARK 500 THR A 48 -5.54 68.75 REMARK 500 TRP A 50 -4.65 69.84 REMARK 500 SER A 53 -2.24 71.85 REMARK 500 LEU A 77 -132.57 58.74 REMARK 500 ARG A 108 -124.67 56.91 REMARK 500 PRO A 197 75.10 -100.75 REMARK 500 ALA A 199 -128.07 52.71 REMARK 500 ASP A 200 87.04 69.61 REMARK 500 LYS A 217 31.40 -88.25 REMARK 500 LYS A 245 -3.41 70.85 REMARK 500 LYS A 450 -32.65 67.33 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-61285 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF OUTWARD STATE ANHYDROMUROPEPTIDE PERMEASE REMARK 900 (AMPG) COMPLEX WITH GLCNAC-1,6-ANHMURNAC DBREF 9J9Z H 4 228 PDB 9J9Z 9J9Z 4 228 DBREF 9J9Z K 1 120 PDB 9J9Z 9J9Z 1 120 DBREF 9J9Z L 2 213 PDB 9J9Z 9J9Z 2 213 DBREF1 9J9Z A 5 198 UNP A0AB38FS76_9ENTR DBREF2 9J9Z A A0AB38FS76 5 198 DBREF 9J9Z A 203 303 UNP P0ABE7 C562_ECOLX 27 127 DBREF1 9J9Z A 306 593 UNP A0AB38FS76_9ENTR DBREF2 9J9Z A A0AB38FS76 203 490 SEQADV 9J9Z TRP A 50 UNP A0AB38FS7 GLY 50 ENGINEERED MUTATION SEQADV 9J9Z ALA A 199 UNP A0AB38FS7 LINKER SEQADV 9J9Z ASP A 200 UNP A0AB38FS7 LINKER SEQADV 9J9Z LEU A 201 UNP A0AB38FS7 LINKER SEQADV 9J9Z ALA A 202 UNP A0AB38FS7 LINKER SEQADV 9J9Z TRP A 205 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 9J9Z ILE A 300 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 9J9Z LEU A 304 UNP P0ABE7 LINKER SEQADV 9J9Z GLY A 305 UNP P0ABE7 LINKER SEQADV 9J9Z TRP A 372 UNP A0AB38FS7 LEU 269 ENGINEERED MUTATION SEQRES 1 H 225 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 225 PHE ASN VAL VAL ASP PHE SER LEU HIS TRP VAL ARG GLN SEQRES 4 H 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 H 225 SER SER SER GLY SER THR SER TYR ALA ASP SER VAL LYS SEQRES 6 H 225 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 7 H 225 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG TRP GLY TYR TRP PRO GLY SEQRES 9 H 225 GLU PRO TRP TRP LYS ALA PHE ASP TYR TRP GLY GLN GLY SEQRES 10 H 225 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 225 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 225 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 225 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 225 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 225 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 225 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 225 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 H 225 VAL GLU PRO LYS SEQRES 1 K 120 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 K 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 K 120 ARG THR ILE SER ARG TYR ALA MET SER TRP PHE ARG GLN SEQRES 4 K 120 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA VAL ALA ARG SEQRES 5 K 120 ARG SER GLY ASP GLY ALA PHE TYR ALA ASP SER VAL GLN SEQRES 6 K 120 GLY ARG PHE THR VAL SER ARG ASP ASP ALA LYS ASN THR SEQRES 7 K 120 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 K 120 ALA VAL TYR TYR CYS ALA ILE ASP SER ASP THR PHE TYR SEQRES 9 K 120 SER GLY SER TYR ASP TYR TRP GLY GLN GLY THR GLN VAL SEQRES 10 K 120 THR VAL SER SEQRES 1 L 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 212 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 L 212 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 L 212 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 212 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 212 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 212 LEU TYR TYR SER LEU VAL THR PHE GLY GLN GLY THR LYS SEQRES 9 L 212 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 212 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 L 212 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 212 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 212 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 212 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 212 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 212 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 212 SER PHE ASN ARG SEQRES 1 A 589 TYR LEU ARG ILE PHE GLN GLN PRO LYS SER ALA ILE LEU SEQRES 2 A 589 LEU ILE LEU GLY PHE ALA SER GLY LEU PRO LEU ALA LEU SEQRES 3 A 589 THR SER GLY THR LEU GLN ALA TRP MET THR VAL GLU ASN SEQRES 4 A 589 ILE ASP LEU LYS THR ILE TRP PHE PHE SER LEU VAL GLY SEQRES 5 A 589 GLN ALA TYR VAL PHE LYS PHE LEU TRP SER PRO VAL MET SEQRES 6 A 589 ASP ARG TYR THR PRO PRO PHE LEU GLY ARG ARG ARG GLY SEQRES 7 A 589 TRP LEU VAL THR THR GLN ILE LEU LEU LEU ILE ALA ILE SEQRES 8 A 589 ALA ALA MET GLY PHE LEU GLU PRO GLY THR GLN LEU ARG SEQRES 9 A 589 TRP MET ALA ALA LEU ALA VAL VAL ILE ALA PHE CYS SER SEQRES 10 A 589 ALA SER GLN ASP ILE VAL PHE ASP ALA TRP LYS THR ASP SEQRES 11 A 589 VAL LEU PRO ALA GLU GLU ARG GLY THR GLY ALA ALA ILE SEQRES 12 A 589 SER VAL LEU GLY TYR ARG LEU GLY MET LEU VAL SER GLY SEQRES 13 A 589 GLY LEU ALA LEU TRP MET ALA ASP LYS TRP LEU GLY TRP SEQRES 14 A 589 GLN GLY MET TYR TRP LEU MET ALA ALA LEU LEU VAL PRO SEQRES 15 A 589 CYS ILE ILE ALA THR LEU LEU ALA PRO GLU PRO SER ALA SEQRES 16 A 589 ASP LEU ALA ASP ASN TRP GLU THR LEU ASN ASP ASN LEU SEQRES 17 A 589 LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS SEQRES 18 A 589 ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA SEQRES 19 A 589 GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO SEQRES 20 A 589 ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP SEQRES 21 A 589 ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA SEQRES 22 A 589 ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU SEQRES 23 A 589 GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR SEQRES 24 A 589 LEU GLY VAL PRO ARG THR LEU GLU GLN ALA VAL VAL ALA SEQRES 25 A 589 PRO LEU ARG ASP PHE PHE GLY ARG ASN ASN ALA TRP LEU SEQRES 26 A 589 ILE LEU LEU LEU ILE VAL LEU TYR LYS LEU GLY ASP ALA SEQRES 27 A 589 PHE ALA MET SER LEU THR THR THR PHE LEU ILE ARG GLY SEQRES 28 A 589 VAL GLY PHE ASP ALA GLY GLU VAL GLY MET VAL ASN LYS SEQRES 29 A 589 THR LEU GLY TRP ILE ALA THR ILE ILE GLY ALA LEU TYR SEQRES 30 A 589 GLY GLY VAL LEU MET GLN ARG LEU SER LEU PHE ARG ALA SEQRES 31 A 589 LEU LEU ILE PHE GLY ILE LEU GLN GLY VAL SER ASN ALA SEQRES 32 A 589 GLY TYR TRP LEU LEU SER ILE THR ASP LYS HIS LEU MET SEQRES 33 A 589 SER MET ALA VAL ALA VAL PHE PHE GLU ASN LEU CYS GLY SEQRES 34 A 589 GLY MET GLY THR ALA ALA PHE VAL ALA LEU LEU MET THR SEQRES 35 A 589 LEU CYS ASN LYS SER PHE SER ALA THR GLN PHE ALA LEU SEQRES 36 A 589 LEU SER ALA LEU SER ALA VAL GLY ARG VAL TYR VAL GLY SEQRES 37 A 589 PRO ILE ALA GLY TRP PHE VAL GLU ALA HIS GLY TRP PRO SEQRES 38 A 589 THR PHE TYR LEU PHE SER VAL PHE ALA ALA VAL PRO GLY SEQRES 39 A 589 ILE LEU LEU LEU LEU ILE CYS ARG LYS THR LEU GLU TYR SEQRES 40 A 589 THR GLN GLN THR GLU SER PHE MET MET ARG ARG HIS PHE SEQRES 41 A 589 SER GLY ALA TYR GLN PHE ALA LEU TYR LEU LEU LEU LEU SEQRES 42 A 589 GLY CYS LEU LEU LEU ALA LEU TRP LEU ILE MET LEU ALA SEQRES 43 A 589 LEU ASN ALA ILE ASP TYR THR SER PHE SER PHE LEU ALA SEQRES 44 A 589 GLY LEU LEU GLU VAL ALA ALA LEU ILE ALA ILE ALA GLY SEQRES 45 A 589 VAL LEU LEU GLY ALA ILE LEU ASP TYR LEU ALA LEU ARG SEQRES 46 A 589 ARG THR GLU GLU HET 2YP A 601 33 HETNAM 2YP (2R)-2-[[(1R,2S,3R,4R,5R)-4-ACETAMIDO-2-[(2S,3R,4R,5S, HETNAM 2 2YP 6R)-3-ACETAMIDO-6-(HYDROXYMETHYL)-4,5-BIS(OXIDANYL) HETNAM 3 2YP OXAN-2-YL]OXY-6,8-DIOXABICYCLO[3.2.1]OCTAN-3- HETNAM 4 2YP YL]OXY]PROPANOIC ACID FORMUL 5 2YP C19 H30 N2 O12 HELIX 1 AA1 ARG H 90 THR H 94 5 5 HELIX 2 AA2 GLY H 107 LYS H 112 1 6 HELIX 3 AA3 SER H 170 ALA H 172 5 3 HELIX 4 AA4 GLN L 80 PHE L 84 5 5 HELIX 5 AA5 TYR L 94 VAL L 98 5 5 HELIX 6 AA6 GLN L 126 SER L 129 5 4 HELIX 7 AA7 LYS L 185 GLU L 189 1 5 HELIX 8 AA8 LEU A 6 GLN A 11 1 6 HELIX 9 AA9 GLN A 11 SER A 32 1 22 HELIX 10 AB1 SER A 32 GLU A 42 1 11 HELIX 11 AB2 SER A 53 PHE A 61 1 9 HELIX 12 AB3 PHE A 61 TYR A 72 1 12 HELIX 13 AB4 GLY A 78 LEU A 101 1 24 HELIX 14 AB5 TRP A 109 LEU A 136 1 28 HELIX 15 AB6 GLU A 140 LEU A 162 1 23 HELIX 16 AB7 LEU A 162 LYS A 169 1 8 HELIX 17 AB8 LEU A 171 ALA A 194 1 24 HELIX 18 AB9 ASP A 200 GLU A 216 1 17 HELIX 19 AC1 GLN A 223 LYS A 240 1 18 HELIX 20 AC2 SER A 253 GLU A 279 1 27 HELIX 21 AC3 VAL A 282 ASN A 297 1 16 HELIX 22 AC4 TYR A 299 TYR A 303 5 5 HELIX 23 AC5 GLU A 311 ARG A 324 1 14 HELIX 24 AC6 ASN A 326 TYR A 337 1 12 HELIX 25 AC7 LYS A 338 ARG A 354 1 17 HELIX 26 AC8 ASP A 359 LEU A 389 1 31 HELIX 27 AC9 SER A 390 THR A 415 1 26 HELIX 28 AD1 HIS A 418 CYS A 448 1 31 HELIX 29 AD2 PHE A 452 GLY A 483 1 32 HELIX 30 AD3 GLY A 483 CYS A 505 1 23 HELIX 31 AD4 CYS A 505 GLU A 516 1 12 HELIX 32 AD5 GLY A 526 ASP A 555 1 30 HELIX 33 AD6 PHE A 561 GLU A 593 1 33 SHEET 1 AA1 4 GLN H 6 SER H 10 0 SHEET 2 AA1 4 LEU H 21 SER H 28 -1 O SER H 28 N GLN H 6 SHEET 3 AA1 4 THR H 81 MET H 86 -1 O ALA H 82 N CYS H 25 SHEET 4 AA1 4 PHE H 71 ASP H 76 -1 N ASP H 76 O THR H 81 SHEET 1 AA2 5 SER H 60 TYR H 63 0 SHEET 2 AA2 5 LEU H 48 SER H 55 -1 N SER H 55 O SER H 60 SHEET 3 AA2 5 SER H 36 GLN H 42 -1 N ARG H 41 O GLU H 49 SHEET 4 AA2 5 ALA H 95 TRP H 102 -1 O TYR H 98 N VAL H 40 SHEET 5 AA2 5 THR H 121 VAL H 123 -1 O THR H 121 N TYR H 97 SHEET 1 AA3 4 PHE H 136 LEU H 138 0 SHEET 2 AA3 4 THR H 149 LEU H 155 -1 O LEU H 155 N PHE H 136 SHEET 3 AA3 4 SER H 193 PRO H 199 -1 O VAL H 196 N LEU H 152 SHEET 4 AA3 4 VAL H 177 HIS H 178 -1 N HIS H 178 O VAL H 195 SHEET 1 AA4 3 THR H 165 TRP H 168 0 SHEET 2 AA4 3 ILE H 209 HIS H 214 -1 O ASN H 211 N SER H 167 SHEET 3 AA4 3 THR H 219 LYS H 224 -1 O VAL H 221 N VAL H 212 SHEET 1 AA5 2 VAL H 183 LEU H 184 0 SHEET 2 AA5 2 TYR H 190 SER H 191 -1 O SER H 191 N VAL H 183 SHEET 1 AA6 4 GLN K 3 GLU K 6 0 SHEET 2 AA6 4 ARG K 19 SER K 25 -1 O SER K 25 N GLN K 3 SHEET 3 AA6 4 THR K 78 MET K 83 -1 O LEU K 81 N LEU K 20 SHEET 4 AA6 4 PHE K 68 ASP K 73 -1 N THR K 69 O GLN K 82 SHEET 1 AA7 6 GLY K 10 VAL K 12 0 SHEET 2 AA7 6 THR K 115 VAL K 119 1 O GLN K 116 N GLY K 10 SHEET 3 AA7 6 VAL K 93 ILE K 98 -1 N TYR K 94 O THR K 115 SHEET 4 AA7 6 MET K 34 GLN K 39 -1 N SER K 35 O ALA K 97 SHEET 5 AA7 6 ARG K 45 ALA K 51 -1 O ALA K 49 N TRP K 36 SHEET 6 AA7 6 ALA K 58 TYR K 60 -1 O PHE K 59 N VAL K 50 SHEET 1 AA8 3 VAL L 20 ARG L 25 0 SHEET 2 AA8 3 ASP L 71 ILE L 76 -1 O LEU L 74 N ILE L 22 SHEET 3 AA8 3 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AA9 3 LYS L 46 ILE L 49 0 SHEET 2 AA9 3 VAL L 34 GLN L 39 -1 N TRP L 36 O LEU L 48 SHEET 3 AA9 3 THR L 86 GLN L 91 -1 O GLN L 90 N ALA L 35 SHEET 1 AB1 4 SER L 116 PHE L 120 0 SHEET 2 AB1 4 THR L 131 ASN L 139 -1 O VAL L 135 N PHE L 120 SHEET 3 AB1 4 LEU L 177 SER L 184 -1 O LEU L 183 N ALA L 132 SHEET 4 AB1 4 SER L 161 VAL L 165 -1 N GLN L 162 O THR L 180 SHEET 1 AB2 3 LYS L 147 TRP L 150 0 SHEET 2 AB2 3 CYS L 196 THR L 199 -1 O GLU L 197 N GLN L 149 SHEET 3 AB2 3 VAL L 207 LYS L 209 -1 O VAL L 207 N VAL L 198 SSBOND 1 CYS H 25 CYS H 99 1555 1555 2.03 SSBOND 2 CYS H 154 CYS H 210 1555 1555 2.03 SSBOND 3 CYS K 22 CYS K 96 1555 1555 2.03 SSBOND 4 CYS L 24 CYS L 89 1555 1555 2.03 SSBOND 5 CYS L 136 CYS L 196 1555 1555 2.03 CISPEP 1 TRP H 105 PRO H 106 0 1.74 CISPEP 2 TYR L 142 PRO L 143 0 -1.12 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