HEADER TRANSFERASE 26-MAR-24 9B71 TITLE CRYO-EM STRUCTURE OF MRAY IN COMPLEX WITH ANALOGUE 3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MRAYAA NANOBODY; COMPND 3 CHAIN: H, G; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; COMPND 7 CHAIN: A, B; COMPND 8 SYNONYM: UDP-MURNAC-PENTAPEPTIDE PHOSPHOTRANSFERASE; COMPND 9 EC: 2.7.8.13; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_COMMON: LLAMA; SOURCE 4 ORGANISM_TAXID: 9844; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS VF5; SOURCE 9 ORGANISM_TAXID: 224324; SOURCE 10 GENE: MRAY, AQ_053; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS INHIBITOR, ANTIBIOTICS, TRANSFERASE EXPDTA ELECTRON MICROSCOPY AUTHOR A.HAO,S.-Y.LEE JRNL AUTH K.YAMAMOTO,T.SATO,A.HAO,K.ASAO,R.KAGUCHI,S.KUSAKA, JRNL AUTH 2 R.R.RUDDARRAJU,D.KAZAMORI,K.SEO,S.TAKAHASHI,M.HORIUCHI, JRNL AUTH 3 S.I.YOKOTA,S.Y.LEE,S.ICHIKAWA JRNL TITL DEVELOPMENT OF A NATURAL PRODUCT OPTIMIZATION STRATEGY FOR JRNL TITL 2 INHIBITORS AGAINST MRAY, A PROMISING ANTIBACTERIAL TARGET. JRNL REF NAT COMMUN V. 15 5085 2024 JRNL REFN ESSN 2041-1723 JRNL PMID 38877016 JRNL DOI 10.1038/S41467-024-49484-7 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LATITUDE, CRYOSPARC, COOT, PHENIX, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 5CKR 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) : 2.700 REMARK 3 NUMBER OF PARTICLES : 68364 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 9B71 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000282751. 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 : COMPLEX OF MRAY AA DIMER WITH REMARK 245 NANOBODY BOUND REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 7.70 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL 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 : 2087 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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) : 60.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 81000 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, A, G, B 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 H -2 REMARK 465 VAL H -1 REMARK 465 PRO H 0 REMARK 465 ASP H 1 REMARK 465 VAL H 2 REMARK 465 LEU H 127 REMARK 465 GLU H 128 REMARK 465 HIS H 129 REMARK 465 HIS H 130 REMARK 465 HIS H 131 REMARK 465 HIS H 132 REMARK 465 HIS H 133 REMARK 465 HIS H 134 REMARK 465 GLY A -5 REMARK 465 PRO A -4 REMARK 465 ALA A -3 REMARK 465 VAL A -2 REMARK 465 PRO A -1 REMARK 465 ARG A 0 REMARK 465 MET A 1 REMARK 465 LEU A 2 REMARK 465 TYR A 3 REMARK 465 GLN A 4 REMARK 465 LEU A 5 REMARK 465 ALA A 6 REMARK 465 LEU A 7 REMARK 465 LEU A 8 REMARK 465 LEU A 9 REMARK 465 LYS A 10 REMARK 465 ASP A 11 REMARK 465 TYR A 12 REMARK 465 TRP A 13 REMARK 465 PHE A 14 REMARK 465 ALA A 15 REMARK 465 PHE A 16 REMARK 465 ASN A 17 REMARK 465 ARG A 359 REMARK 465 MET G -2 REMARK 465 VAL G -1 REMARK 465 PRO G 0 REMARK 465 ASP G 1 REMARK 465 VAL G 2 REMARK 465 LEU G 127 REMARK 465 GLU G 128 REMARK 465 HIS G 129 REMARK 465 HIS G 130 REMARK 465 HIS G 131 REMARK 465 HIS G 132 REMARK 465 HIS G 133 REMARK 465 HIS G 134 REMARK 465 GLY B -5 REMARK 465 PRO B -4 REMARK 465 ALA B -3 REMARK 465 VAL B -2 REMARK 465 PRO B -1 REMARK 465 ARG B 0 REMARK 465 MET B 1 REMARK 465 LEU B 2 REMARK 465 TYR B 3 REMARK 465 GLN B 4 REMARK 465 LEU B 5 REMARK 465 ALA B 6 REMARK 465 LEU B 7 REMARK 465 LEU B 8 REMARK 465 LEU B 9 REMARK 465 LYS B 10 REMARK 465 ASP B 11 REMARK 465 TYR B 12 REMARK 465 TRP B 13 REMARK 465 PHE B 14 REMARK 465 ALA B 15 REMARK 465 PHE B 16 REMARK 465 ASN B 17 REMARK 465 ARG B 359 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 GLN H 3 CG CD OE1 NE2 REMARK 470 GLN H 13 CG CD OE1 NE2 REMARK 470 LEU H 18 CG CD1 CD2 REMARK 470 ARG H 27 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 GLU H 44 CG CD OE1 OE2 REMARK 470 VAL H 48 CG1 CG2 REMARK 470 LYS H 64 CG CD CE NZ REMARK 470 GLN H 81 CG CD OE1 NE2 REMARK 470 LEU H 85 CG CD1 CD2 REMARK 470 LYS H 86 CG CD CE NZ REMARK 470 GLU H 88 CG CD OE1 OE2 REMARK 470 GLN H 118 CG CD OE1 NE2 REMARK 470 SER H 125 OG REMARK 470 VAL A 18 CG1 CG2 REMARK 470 LEU A 19 CG CD1 CD2 REMARK 470 LYS A 20 CG CD CE NZ REMARK 470 LYS A 50 CG CD CE NZ REMARK 470 ARG A 60 CG CD NE CZ NH1 NH2 REMARK 470 TYR A 62 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 65 CG CD OE1 OE2 REMARK 470 SER A 66 OG REMARK 470 HIS A 67 CG ND1 CD2 CE1 NE2 REMARK 470 GLU A 68 CG CD OE1 OE2 REMARK 470 LYS A 125 CG CD CE NZ REMARK 470 LYS A 315 CG CD CE NZ REMARK 470 LYS A 357 CG CD CE NZ REMARK 470 GLN G 3 CG CD OE1 NE2 REMARK 470 GLN G 13 CG CD OE1 NE2 REMARK 470 LEU G 18 CG CD1 CD2 REMARK 470 ARG G 27 CG CD NE CZ NH1 NH2 REMARK 470 LYS G 43 CG CD CE NZ REMARK 470 GLU G 44 CG CD OE1 OE2 REMARK 470 VAL G 48 CG1 CG2 REMARK 470 LYS G 64 CG CD CE NZ REMARK 470 GLN G 81 CG CD OE1 NE2 REMARK 470 LEU G 85 CG CD1 CD2 REMARK 470 LYS G 86 CG CD CE NZ REMARK 470 GLU G 88 CG CD OE1 OE2 REMARK 470 GLN G 118 CG CD OE1 NE2 REMARK 470 SER G 125 OG REMARK 470 VAL B 18 CG1 CG2 REMARK 470 LEU B 19 CG CD1 CD2 REMARK 470 LYS B 20 CG CD CE NZ REMARK 470 LYS B 50 CG CD CE NZ REMARK 470 ARG B 60 CG CD NE CZ NH1 NH2 REMARK 470 TYR B 62 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU B 65 CG CD OE1 OE2 REMARK 470 SER B 66 OG REMARK 470 HIS B 67 CG ND1 CD2 CE1 NE2 REMARK 470 GLU B 68 CG CD OE1 OE2 REMARK 470 LYS B 125 CG CD CE NZ REMARK 470 LYS B 315 CG CD CE NZ REMARK 470 LYS B 357 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 OG SER H 107 OE1 GLU H 112 2.18 REMARK 500 OG SER G 107 OE1 GLU G 112 2.18 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 28 53.48 -90.72 REMARK 500 MET A 76 30.88 71.09 REMARK 500 TYR A 233 60.68 61.49 REMARK 500 ALA A 292 33.55 -94.47 REMARK 500 SER G 28 53.47 -90.75 REMARK 500 MET B 76 30.89 71.05 REMARK 500 TYR B 233 60.67 61.47 REMARK 500 ALA B 292 33.59 -94.45 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9B70 RELATED DB: PDB REMARK 900 9B70 CONTAINS THE SAME PROTEIN IN COMPLEX WITH DIFFERENT ANALOGUE REMARK 900 RELATED ID: EMD-44294 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF MRAY IN COMPLEX WITH ANALOGUE 3 DBREF 9B71 H -2 134 PDB 9B71 9B71 -2 134 DBREF 9B71 A 1 359 UNP O66465 MRAY_AQUAE 1 359 DBREF 9B71 G -2 134 PDB 9B71 9B71 -2 134 DBREF 9B71 B 1 359 UNP O66465 MRAY_AQUAE 1 359 SEQADV 9B71 GLY A -5 UNP O66465 EXPRESSION TAG SEQADV 9B71 PRO A -4 UNP O66465 EXPRESSION TAG SEQADV 9B71 ALA A -3 UNP O66465 EXPRESSION TAG SEQADV 9B71 VAL A -2 UNP O66465 EXPRESSION TAG SEQADV 9B71 PRO A -1 UNP O66465 EXPRESSION TAG SEQADV 9B71 ARG A 0 UNP O66465 EXPRESSION TAG SEQADV 9B71 GLY B -5 UNP O66465 EXPRESSION TAG SEQADV 9B71 PRO B -4 UNP O66465 EXPRESSION TAG SEQADV 9B71 ALA B -3 UNP O66465 EXPRESSION TAG SEQADV 9B71 VAL B -2 UNP O66465 EXPRESSION TAG SEQADV 9B71 PRO B -1 UNP O66465 EXPRESSION TAG SEQADV 9B71 ARG B 0 UNP O66465 EXPRESSION TAG SEQRES 1 H 137 MET VAL PRO ASP VAL GLN LEU GLN GLU SER GLY GLY GLY SEQRES 2 H 137 LEU VAL GLN THR GLY GLY SER LEU THR LEU SER CYS ALA SEQRES 3 H 137 THR SER GLY ARG SER PHE SER LEU TYR ALA MET ALA TRP SEQRES 4 H 137 PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA SEQRES 5 H 137 GLY VAL SER ARG ARG GLY ASN THR ALA TYR ALA ASP ALA SEQRES 6 H 137 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA ALA SEQRES 7 H 137 ASN THR VAL TYR LEU GLN MET THR SER LEU LYS PRO GLU SEQRES 8 H 137 ASP THR ALA VAL TYR PHE CYS ALA ALA PHE ARG VAL ALA SEQRES 9 H 137 VAL THR THR TYR THR SER GLN GLN ALA ASN GLU TYR ASN SEQRES 10 H 137 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER LEU SEQRES 11 H 137 GLU HIS HIS HIS HIS HIS HIS SEQRES 1 A 365 GLY PRO ALA VAL PRO ARG MET LEU TYR GLN LEU ALA LEU SEQRES 2 A 365 LEU LEU LYS ASP TYR TRP PHE ALA PHE ASN VAL LEU LYS SEQRES 3 A 365 TYR ILE THR PHE ARG SER PHE THR ALA VAL LEU ILE ALA SEQRES 4 A 365 PHE PHE LEU THR LEU VAL LEU SER PRO SER PHE ILE ASN SEQRES 5 A 365 ARG LEU ARG LYS ILE GLN ARG LEU PHE GLY GLY TYR VAL SEQRES 6 A 365 ARG GLU TYR THR PRO GLU SER HIS GLU VAL LYS LYS TYR SEQRES 7 A 365 THR PRO THR MET GLY GLY ILE VAL ILE LEU ILE VAL VAL SEQRES 8 A 365 THR LEU SER THR LEU LEU LEU MET ARG TRP ASP ILE LYS SEQRES 9 A 365 TYR THR TRP VAL VAL LEU LEU SER PHE LEU SER PHE GLY SEQRES 10 A 365 THR ILE GLY PHE TRP ASP ASP TYR VAL LYS LEU LYS ASN SEQRES 11 A 365 LYS LYS GLY ILE SER ILE LYS THR LYS PHE LEU LEU GLN SEQRES 12 A 365 VAL LEU SER ALA SER LEU ILE SER VAL LEU ILE TYR TYR SEQRES 13 A 365 TRP ALA ASP ILE ASP THR ILE LEU TYR PHE PRO PHE PHE SEQRES 14 A 365 LYS GLU LEU TYR VAL ASP LEU GLY VAL LEU TYR LEU PRO SEQRES 15 A 365 PHE ALA VAL PHE VAL ILE VAL GLY SER ALA ASN ALA VAL SEQRES 16 A 365 ASN LEU THR ASP GLY LEU ASP GLY LEU ALA ILE GLY PRO SEQRES 17 A 365 ALA MET THR THR ALA THR ALA LEU GLY VAL VAL ALA TYR SEQRES 18 A 365 ALA VAL GLY HIS SER LYS ILE ALA GLN TYR LEU ASN ILE SEQRES 19 A 365 PRO TYR VAL PRO TYR ALA GLY GLU LEU THR VAL PHE CYS SEQRES 20 A 365 PHE ALA LEU VAL GLY ALA GLY LEU GLY PHE LEU TRP PHE SEQRES 21 A 365 ASN SER PHE PRO ALA GLN MET PHE MET GLY ASP VAL GLY SEQRES 22 A 365 SER LEU SER ILE GLY ALA SER LEU ALA THR VAL ALA LEU SEQRES 23 A 365 LEU THR LYS SER GLU PHE ILE PHE ALA VAL ALA ALA GLY SEQRES 24 A 365 VAL PHE VAL PHE GLU THR ILE SER VAL ILE LEU GLN ILE SEQRES 25 A 365 ILE TYR PHE ARG TRP THR GLY GLY LYS ARG LEU PHE LYS SEQRES 26 A 365 ARG ALA PRO PHE HIS HIS HIS LEU GLU LEU ASN GLY LEU SEQRES 27 A 365 PRO GLU PRO LYS ILE VAL VAL ARG MET TRP ILE ILE SER SEQRES 28 A 365 ILE LEU LEU ALA ILE ILE ALA ILE SER MET LEU LYS LEU SEQRES 29 A 365 ARG SEQRES 1 G 137 MET VAL PRO ASP VAL GLN LEU GLN GLU SER GLY GLY GLY SEQRES 2 G 137 LEU VAL GLN THR GLY GLY SER LEU THR LEU SER CYS ALA SEQRES 3 G 137 THR SER GLY ARG SER PHE SER LEU TYR ALA MET ALA TRP SEQRES 4 G 137 PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA SEQRES 5 G 137 GLY VAL SER ARG ARG GLY ASN THR ALA TYR ALA ASP ALA SEQRES 6 G 137 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA ALA SEQRES 7 G 137 ASN THR VAL TYR LEU GLN MET THR SER LEU LYS PRO GLU SEQRES 8 G 137 ASP THR ALA VAL TYR PHE CYS ALA ALA PHE ARG VAL ALA SEQRES 9 G 137 VAL THR THR TYR THR SER GLN GLN ALA ASN GLU TYR ASN SEQRES 10 G 137 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER LEU SEQRES 11 G 137 GLU HIS HIS HIS HIS HIS HIS SEQRES 1 B 365 GLY PRO ALA VAL PRO ARG MET LEU TYR GLN LEU ALA LEU SEQRES 2 B 365 LEU LEU LYS ASP TYR TRP PHE ALA PHE ASN VAL LEU LYS SEQRES 3 B 365 TYR ILE THR PHE ARG SER PHE THR ALA VAL LEU ILE ALA SEQRES 4 B 365 PHE PHE LEU THR LEU VAL LEU SER PRO SER PHE ILE ASN SEQRES 5 B 365 ARG LEU ARG LYS ILE GLN ARG LEU PHE GLY GLY TYR VAL SEQRES 6 B 365 ARG GLU TYR THR PRO GLU SER HIS GLU VAL LYS LYS TYR SEQRES 7 B 365 THR PRO THR MET GLY GLY ILE VAL ILE LEU ILE VAL VAL SEQRES 8 B 365 THR LEU SER THR LEU LEU LEU MET ARG TRP ASP ILE LYS SEQRES 9 B 365 TYR THR TRP VAL VAL LEU LEU SER PHE LEU SER PHE GLY SEQRES 10 B 365 THR ILE GLY PHE TRP ASP ASP TYR VAL LYS LEU LYS ASN SEQRES 11 B 365 LYS LYS GLY ILE SER ILE LYS THR LYS PHE LEU LEU GLN SEQRES 12 B 365 VAL LEU SER ALA SER LEU ILE SER VAL LEU ILE TYR TYR SEQRES 13 B 365 TRP ALA ASP ILE ASP THR ILE LEU TYR PHE PRO PHE PHE SEQRES 14 B 365 LYS GLU LEU TYR VAL ASP LEU GLY VAL LEU TYR LEU PRO SEQRES 15 B 365 PHE ALA VAL PHE VAL ILE VAL GLY SER ALA ASN ALA VAL SEQRES 16 B 365 ASN LEU THR ASP GLY LEU ASP GLY LEU ALA ILE GLY PRO SEQRES 17 B 365 ALA MET THR THR ALA THR ALA LEU GLY VAL VAL ALA TYR SEQRES 18 B 365 ALA VAL GLY HIS SER LYS ILE ALA GLN TYR LEU ASN ILE SEQRES 19 B 365 PRO TYR VAL PRO TYR ALA GLY GLU LEU THR VAL PHE CYS SEQRES 20 B 365 PHE ALA LEU VAL GLY ALA GLY LEU GLY PHE LEU TRP PHE SEQRES 21 B 365 ASN SER PHE PRO ALA GLN MET PHE MET GLY ASP VAL GLY SEQRES 22 B 365 SER LEU SER ILE GLY ALA SER LEU ALA THR VAL ALA LEU SEQRES 23 B 365 LEU THR LYS SER GLU PHE ILE PHE ALA VAL ALA ALA GLY SEQRES 24 B 365 VAL PHE VAL PHE GLU THR ILE SER VAL ILE LEU GLN ILE SEQRES 25 B 365 ILE TYR PHE ARG TRP THR GLY GLY LYS ARG LEU PHE LYS SEQRES 26 B 365 ARG ALA PRO PHE HIS HIS HIS LEU GLU LEU ASN GLY LEU SEQRES 27 B 365 PRO GLU PRO LYS ILE VAL VAL ARG MET TRP ILE ILE SER SEQRES 28 B 365 ILE LEU LEU ALA ILE ILE ALA ILE SER MET LEU LYS LEU SEQRES 29 B 365 ARG HET AI2 A 601 68 HET AI2 B 601 68 FORMUL 5 AI2 FORMUL 7 HOH *6(H2 O) HELIX 1 AA1 SER H 28 SER H 30 5 3 HELIX 2 AA2 LYS H 86 THR H 90 5 5 HELIX 3 AA3 GLN H 109 TYR H 113 5 5 HELIX 4 AA4 PHE A 24 GLY A 57 1 34 HELIX 5 AA5 GLY A 77 MET A 93 1 17 HELIX 6 AA6 LYS A 98 LYS A 125 1 28 HELIX 7 AA7 SER A 129 TRP A 151 1 23 HELIX 8 AA8 LEU A 173 ASP A 193 1 21 HELIX 9 AA9 ILE A 200 HIS A 219 1 20 HELIX 10 AB1 HIS A 219 ASN A 227 1 9 HELIX 11 AB2 ALA A 234 SER A 256 1 23 HELIX 12 AB3 MET A 263 THR A 282 1 20 HELIX 13 AB4 GLU A 285 ALA A 292 1 8 HELIX 14 AB5 ALA A 292 GLY A 313 1 22 HELIX 15 AB6 PRO A 322 GLY A 331 1 10 HELIX 16 AB7 PRO A 333 MET A 355 1 23 HELIX 17 AB8 SER G 28 SER G 30 5 3 HELIX 18 AB9 LYS G 86 THR G 90 5 5 HELIX 19 AC1 GLN G 109 TYR G 113 5 5 HELIX 20 AC2 PHE B 24 GLY B 57 1 34 HELIX 21 AC3 GLY B 77 MET B 93 1 17 HELIX 22 AC4 LYS B 98 LYS B 125 1 28 HELIX 23 AC5 SER B 129 TRP B 151 1 23 HELIX 24 AC6 LEU B 173 ASP B 193 1 21 HELIX 25 AC7 ILE B 200 HIS B 219 1 20 HELIX 26 AC8 HIS B 219 ASN B 227 1 9 HELIX 27 AC9 ALA B 234 SER B 256 1 23 HELIX 28 AD1 MET B 263 THR B 282 1 20 HELIX 29 AD2 GLU B 285 ALA B 292 1 8 HELIX 30 AD3 ALA B 292 GLY B 313 1 22 HELIX 31 AD4 PRO B 322 GLY B 331 1 10 HELIX 32 AD5 PRO B 333 MET B 355 1 23 SHEET 1 AA1 4 LEU H 4 SER H 7 0 SHEET 2 AA1 4 LEU H 18 THR H 24 -1 O ALA H 23 N GLN H 5 SHEET 3 AA1 4 THR H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA1 4 THR H 68 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA2 6 GLY H 10 GLN H 13 0 SHEET 2 AA2 6 THR H 120 SER H 125 1 O THR H 123 N GLY H 10 SHEET 3 AA2 6 ALA H 91 ARG H 99 -1 N TYR H 93 O THR H 120 SHEET 4 AA2 6 TYR H 32 GLN H 39 -1 N ALA H 33 O PHE H 98 SHEET 5 AA2 6 GLU H 46 VAL H 51 -1 O VAL H 51 N MET H 34 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O ALA H 58 N GLY H 50 SHEET 1 AA3 4 GLY H 10 GLN H 13 0 SHEET 2 AA3 4 THR H 120 SER H 125 1 O THR H 123 N GLY H 10 SHEET 3 AA3 4 ALA H 91 ARG H 99 -1 N TYR H 93 O THR H 120 SHEET 4 AA3 4 TYR H 115 TRP H 116 -1 O TYR H 115 N ALA H 97 SHEET 1 AA4 2 ILE A 157 TYR A 159 0 SHEET 2 AA4 2 TYR A 167 ASP A 169 -1 O VAL A 168 N LEU A 158 SHEET 1 AA5 4 LEU G 4 SER G 7 0 SHEET 2 AA5 4 LEU G 18 THR G 24 -1 O ALA G 23 N GLN G 5 SHEET 3 AA5 4 THR G 77 MET G 82 -1 O LEU G 80 N LEU G 20 SHEET 4 AA5 4 THR G 68 ASP G 72 -1 N THR G 68 O GLN G 81 SHEET 1 AA6 6 GLY G 10 GLN G 13 0 SHEET 2 AA6 6 THR G 120 SER G 125 1 O THR G 123 N GLY G 10 SHEET 3 AA6 6 ALA G 91 ARG G 99 -1 N TYR G 93 O THR G 120 SHEET 4 AA6 6 TYR G 32 GLN G 39 -1 N ALA G 33 O PHE G 98 SHEET 5 AA6 6 GLU G 46 VAL G 51 -1 O VAL G 51 N MET G 34 SHEET 6 AA6 6 THR G 57 TYR G 59 -1 O ALA G 58 N GLY G 50 SHEET 1 AA7 4 GLY G 10 GLN G 13 0 SHEET 2 AA7 4 THR G 120 SER G 125 1 O THR G 123 N GLY G 10 SHEET 3 AA7 4 ALA G 91 ARG G 99 -1 N TYR G 93 O THR G 120 SHEET 4 AA7 4 TYR G 115 TRP G 116 -1 O TYR G 115 N ALA G 97 SHEET 1 AA8 2 ILE B 157 TYR B 159 0 SHEET 2 AA8 2 TYR B 167 ASP B 169 -1 O VAL B 168 N LEU B 158 SSBOND 1 CYS H 22 CYS H 95 1555 1555 2.03 SSBOND 2 CYS G 22 CYS G 95 1555 1555 2.03 CISPEP 1 PHE A 257 PRO A 258 0 -7.91 CISPEP 2 ALA A 321 PRO A 322 0 2.84 CISPEP 3 PHE B 257 PRO B 258 0 -7.93 CISPEP 4 ALA B 321 PRO B 322 0 2.85 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