HEADER CELL ADHESION/IMMUNE SYSTEM 06-DEC-24 9ME5 TITLE ANTIBODY FRAGMENTS FROM MAB824 AND MAB926 BOUND TO THE ADHESIN PROTEIN TITLE 2 FIMH COMPND MOL_ID: 1; COMPND 2 MOLECULE: TYPE 1 FIMBRIN D-MANNOSE SPECIFIC ADHESIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PROTEIN FIMH; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: PROTEIN FIMG; COMPND 8 CHAIN: G; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: MAB926 HEAVY CHAIN FRAGMENT; COMPND 12 CHAIN: H; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: MAB824 HEAVY CHAIN FRAGMENT; COMPND 15 CHAIN: I; COMPND 16 MOL_ID: 5; COMPND 17 MOLECULE: MAB926 LIGHT CHAIN FRAGMENT; COMPND 18 CHAIN: L; COMPND 19 MOL_ID: 6; COMPND 20 MOLECULE: MAB824 LIGHT CHAIN FRAGMENT; COMPND 21 CHAIN: M SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: FIMH, B4320, JW4283; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 9 ORGANISM_TAXID: 562; SOURCE 10 GENE: FIMG, B4319, JW4282; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_COMMON: MOUSE; SOURCE 16 ORGANISM_TAXID: 10090; SOURCE 17 CELL_LINE: B CELL HYBRIDOMA; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 20 ORGANISM_COMMON: MOUSE; SOURCE 21 ORGANISM_TAXID: 10090; SOURCE 22 CELL_LINE: B CELL HYBRIDOMA; SOURCE 23 MOL_ID: 5; SOURCE 24 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 25 ORGANISM_COMMON: MOUSE; SOURCE 26 ORGANISM_TAXID: 10090; SOURCE 27 CELL_LINE: B CELL HYBRIDOMA; SOURCE 28 MOL_ID: 6; SOURCE 29 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 30 ORGANISM_COMMON: MOUSE; SOURCE 31 ORGANISM_TAXID: 10090; SOURCE 32 CELL_LINE: B CELL HYBRIDOMA KEYWDS FIMBRIAL TIP, LECTIN DOMAIN, ANTIBODY FRAGMENTS, ANTIBODY-TARGET KEYWDS 2 COMPLEX, CELL ADHESION, CELL ADHESION-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR K.L.HVORECNY,P.MAGALA,R.E.KLEVIT,J.M.KOLLMAN REVDAT 1 26-NOV-25 9ME5 0 JRNL AUTH K.L.HVORECNY,J.M.KOLLMAN JRNL TITL ANTIBODIES DISRUPT BACTERIAL ADHESION BY LIGAND MIMICRY AND JRNL TITL 2 ALLOSTERY JRNL REF TO BE PUBLISHED JRNL REFN JRNL DOI 10.1038/S41467-025-65666-3 REMARK 2 REMARK 2 RESOLUTION. 3.10 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 : 3JWN 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) : 3.100 REMARK 3 NUMBER OF PARTICLES : 253258 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 9ME5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000289938. 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 : ANTIBODY FRAGMENTS FROM MAB824 REMARK 245 AND MAB926 BOUND TO THE E. COLI REMARK 245 ADHESIN PROTEIN FIMH; FIMBRIAL REMARK 245 TIP (FIMH AND FIMG); ANTIBODY REMARK 245 FRAGMENTS, HEAVY AND LIGHT REMARK 245 CHAINS REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 1651 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) : 750.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1500.00 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) : 5500.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 105000 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, H, I, L, M 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 -20 REMARK 465 LYS A -19 REMARK 465 ARG A -18 REMARK 465 VAL A -17 REMARK 465 ILE A -16 REMARK 465 THR A -15 REMARK 465 LEU A -14 REMARK 465 PHE A -13 REMARK 465 ALA A -12 REMARK 465 VAL A -11 REMARK 465 LEU A -10 REMARK 465 LEU A -9 REMARK 465 MET A -8 REMARK 465 GLY A -7 REMARK 465 TRP A -6 REMARK 465 SER A -5 REMARK 465 VAL A -4 REMARK 465 ASN A -3 REMARK 465 ALA A -2 REMARK 465 TRP A -1 REMARK 465 SER A 0 REMARK 465 MET G -22 REMARK 465 LYS G -21 REMARK 465 TRP G -20 REMARK 465 CYS G -19 REMARK 465 LYS G -18 REMARK 465 ARG G -17 REMARK 465 GLY G -16 REMARK 465 TYR G -15 REMARK 465 VAL G -14 REMARK 465 LEU G -13 REMARK 465 ALA G -12 REMARK 465 ALA G -11 REMARK 465 ILE G -10 REMARK 465 LEU G -9 REMARK 465 ALA G -8 REMARK 465 LEU G -7 REMARK 465 ALA G -6 REMARK 465 SER G -5 REMARK 465 ALA G -4 REMARK 465 THR G -3 REMARK 465 ILE G -2 REMARK 465 GLN G -1 REMARK 465 ALA G 0 REMARK 465 VAL G 12 REMARK 465 ALA G 13 REMARK 465 LYS G 14 REMARK 465 PRO G 15 REMARK 465 CYS G 16 REMARK 465 THR G 17 REMARK 465 VAL G 18 REMARK 465 SER G 19 REMARK 465 THR G 20 REMARK 465 THR G 21 REMARK 465 ASN G 22 REMARK 465 ALA G 23 REMARK 465 THR G 24 REMARK 465 VAL G 25 REMARK 465 ASP G 26 REMARK 465 LEU G 27 REMARK 465 GLY G 28 REMARK 465 ASP G 29 REMARK 465 LEU G 30 REMARK 465 TYR G 31 REMARK 465 SER G 32 REMARK 465 PHE G 33 REMARK 465 SER G 34 REMARK 465 LEU G 35 REMARK 465 MET G 36 REMARK 465 SER G 37 REMARK 465 ALA G 38 REMARK 465 GLY G 39 REMARK 465 ALA G 40 REMARK 465 ALA G 41 REMARK 465 SER G 42 REMARK 465 ALA G 43 REMARK 465 TRP G 44 REMARK 465 HIS G 45 REMARK 465 ASP G 46 REMARK 465 VAL G 47 REMARK 465 ALA G 48 REMARK 465 LEU G 49 REMARK 465 GLU G 50 REMARK 465 LEU G 51 REMARK 465 THR G 52 REMARK 465 ASN G 53 REMARK 465 CYS G 54 REMARK 465 PRO G 55 REMARK 465 VAL G 56 REMARK 465 GLY G 57 REMARK 465 THR G 58 REMARK 465 SER G 59 REMARK 465 ARG G 60 REMARK 465 VAL G 61 REMARK 465 THR G 62 REMARK 465 ALA G 63 REMARK 465 SER G 64 REMARK 465 PHE G 65 REMARK 465 SER G 66 REMARK 465 GLY G 67 REMARK 465 ALA G 68 REMARK 465 ALA G 69 REMARK 465 ASP G 70 REMARK 465 SER G 71 REMARK 465 THR G 72 REMARK 465 GLY G 73 REMARK 465 TYR G 74 REMARK 465 TYR G 75 REMARK 465 LYS G 76 REMARK 465 ASN G 77 REMARK 465 GLN G 78 REMARK 465 GLY G 79 REMARK 465 THR G 80 REMARK 465 ALA G 81 REMARK 465 GLN G 82 REMARK 465 ASN G 83 REMARK 465 ILE G 84 REMARK 465 GLN G 85 REMARK 465 LEU G 86 REMARK 465 GLU G 87 REMARK 465 LEU G 88 REMARK 465 GLN G 89 REMARK 465 ASP G 90 REMARK 465 ASP G 91 REMARK 465 SER G 92 REMARK 465 GLY G 93 REMARK 465 ASN G 94 REMARK 465 THR G 95 REMARK 465 LEU G 96 REMARK 465 ASN G 97 REMARK 465 THR G 98 REMARK 465 GLY G 99 REMARK 465 ALA G 100 REMARK 465 THR G 101 REMARK 465 LYS G 102 REMARK 465 THR G 103 REMARK 465 VAL G 104 REMARK 465 GLN G 105 REMARK 465 VAL G 106 REMARK 465 ASP G 107 REMARK 465 ASP G 108 REMARK 465 SER G 109 REMARK 465 SER G 110 REMARK 465 GLN G 111 REMARK 465 SER G 112 REMARK 465 ALA G 113 REMARK 465 HIS G 114 REMARK 465 PHE G 115 REMARK 465 PRO G 116 REMARK 465 LEU G 117 REMARK 465 GLN G 118 REMARK 465 VAL G 119 REMARK 465 ARG G 120 REMARK 465 ALA G 121 REMARK 465 LEU G 122 REMARK 465 THR G 123 REMARK 465 VAL G 124 REMARK 465 ASN G 125 REMARK 465 GLY G 126 REMARK 465 GLY G 127 REMARK 465 ALA G 128 REMARK 465 THR G 129 REMARK 465 GLN G 130 REMARK 465 GLY G 131 REMARK 465 THR G 132 REMARK 465 ILE G 133 REMARK 465 GLN G 134 REMARK 465 ALA G 135 REMARK 465 VAL G 136 REMARK 465 ILE G 137 REMARK 465 SER G 138 REMARK 465 ILE G 139 REMARK 465 THR G 140 REMARK 465 TYR G 141 REMARK 465 THR G 142 REMARK 465 TYR G 143 REMARK 465 SER G 144 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 A 17 147.64 -172.86 REMARK 500 ALA A 25 66.99 -153.00 REMARK 500 VAL A 35 -61.53 -98.37 REMARK 500 PRO A 91 -177.01 -68.21 REMARK 500 ALA A 115 -156.37 51.06 REMARK 500 SER H 7 -172.99 -66.82 REMARK 500 ALA H 16 -166.99 54.80 REMARK 500 ALA H 24 137.83 -170.12 REMARK 500 TYR H 27 51.91 -92.39 REMARK 500 ALA H 92 -179.47 -172.31 REMARK 500 SER H 136 -10.43 72.66 REMARK 500 SER H 188 79.24 -112.76 REMARK 500 ILE I 47 -60.61 -92.09 REMARK 500 ALA I 91 -175.73 -170.91 REMARK 500 SER I 164 -1.34 78.82 REMARK 500 VAL L 56 -57.04 81.72 REMARK 500 SER L 72 147.85 -171.71 REMARK 500 ALA L 135 119.05 -160.88 REMARK 500 SER L 173 -8.09 71.10 REMARK 500 ASN L 217 61.71 62.83 REMARK 500 THR M 51 -35.42 72.28 REMARK 500 ALA M 84 -168.17 -163.58 REMARK 500 ALA M 130 116.81 -160.98 REMARK 500 PRO M 141 -164.46 -77.05 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48184 RELATED DB: EMDB REMARK 900 ANTIBODY FRAGMENTS FROM MAB824 AND MAB926 BOUND TO THE ADHESIN REMARK 900 PROTEIN FIMH DBREF 9ME5 A -20 279 UNP P08191 FIMH_ECOLI 1 300 DBREF 9ME5 G -22 144 UNP P08190 FIMG_ECOLI 1 167 DBREF 9ME5 H 1 212 PDB 9ME5 9ME5 1 212 DBREF 9ME5 I 0 207 PDB 9ME5 9ME5 0 207 DBREF 9ME5 L 1 219 PDB 9ME5 9ME5 1 219 DBREF 9ME5 M 1 197 PDB 9ME5 9ME5 1 197 SEQRES 1 A 300 MET LYS ARG VAL ILE THR LEU PHE ALA VAL LEU LEU MET SEQRES 2 A 300 GLY TRP SER VAL ASN ALA TRP SER PHE ALA CYS LYS THR SEQRES 3 A 300 ALA ASN GLY THR ALA ILE PRO ILE GLY GLY GLY SER ALA SEQRES 4 A 300 ASN VAL TYR VAL ASN LEU ALA PRO VAL VAL ASN VAL GLY SEQRES 5 A 300 GLN ASN LEU VAL VAL ASP LEU SER THR GLN ILE PHE CYS SEQRES 6 A 300 HIS ASN ASP TYR PRO GLU THR ILE THR ASP TYR VAL THR SEQRES 7 A 300 LEU GLN ARG GLY SER ALA TYR GLY GLY VAL LEU SER ASN SEQRES 8 A 300 PHE SER GLY THR VAL LYS TYR SER GLY SER SER TYR PRO SEQRES 9 A 300 PHE PRO THR THR SER GLU THR PRO ARG VAL VAL TYR ASN SEQRES 10 A 300 SER ARG THR ASP LYS PRO TRP PRO VAL ALA LEU TYR LEU SEQRES 11 A 300 THR PRO VAL SER SER ALA GLY GLY VAL ALA ILE LYS ALA SEQRES 12 A 300 GLY SER LEU ILE ALA VAL LEU ILE LEU ARG GLN THR ASN SEQRES 13 A 300 ASN TYR ASN SER ASP ASP PHE GLN PHE VAL TRP ASN ILE SEQRES 14 A 300 TYR ALA ASN ASN ASP VAL VAL VAL PRO THR GLY GLY CYS SEQRES 15 A 300 ASP VAL SER ALA ARG ASP VAL THR VAL THR LEU PRO ASP SEQRES 16 A 300 TYR PRO GLY SER VAL PRO ILE PRO LEU THR VAL TYR CYS SEQRES 17 A 300 ALA LYS SER GLN ASN LEU GLY TYR TYR LEU SER GLY THR SEQRES 18 A 300 THR ALA ASP ALA GLY ASN SER ILE PHE THR ASN THR ALA SEQRES 19 A 300 SER PHE SER PRO ALA GLN GLY VAL GLY VAL GLN LEU THR SEQRES 20 A 300 ARG ASN GLY THR ILE ILE PRO ALA ASN ASN THR VAL SER SEQRES 21 A 300 LEU GLY ALA VAL GLY THR SER ALA VAL SER LEU GLY LEU SEQRES 22 A 300 THR ALA ASN TYR ALA ARG THR GLY GLY GLN VAL THR ALA SEQRES 23 A 300 GLY ASN VAL GLN SER ILE ILE GLY VAL THR PHE VAL TYR SEQRES 24 A 300 GLN SEQRES 1 G 167 MET LYS TRP CYS LYS ARG GLY TYR VAL LEU ALA ALA ILE SEQRES 2 G 167 LEU ALA LEU ALA SER ALA THR ILE GLN ALA ALA ASP VAL SEQRES 3 G 167 THR ILE THR VAL ASN GLY LYS VAL VAL ALA LYS PRO CYS SEQRES 4 G 167 THR VAL SER THR THR ASN ALA THR VAL ASP LEU GLY ASP SEQRES 5 G 167 LEU TYR SER PHE SER LEU MET SER ALA GLY ALA ALA SER SEQRES 6 G 167 ALA TRP HIS ASP VAL ALA LEU GLU LEU THR ASN CYS PRO SEQRES 7 G 167 VAL GLY THR SER ARG VAL THR ALA SER PHE SER GLY ALA SEQRES 8 G 167 ALA ASP SER THR GLY TYR TYR LYS ASN GLN GLY THR ALA SEQRES 9 G 167 GLN ASN ILE GLN LEU GLU LEU GLN ASP ASP SER GLY ASN SEQRES 10 G 167 THR LEU ASN THR GLY ALA THR LYS THR VAL GLN VAL ASP SEQRES 11 G 167 ASP SER SER GLN SER ALA HIS PHE PRO LEU GLN VAL ARG SEQRES 12 G 167 ALA LEU THR VAL ASN GLY GLY ALA THR GLN GLY THR ILE SEQRES 13 G 167 GLN ALA VAL ILE SER ILE THR TYR THR TYR SER SEQRES 1 H 212 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU ALA THR SEQRES 2 H 212 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 H 212 TYR THR SER THR ASN TYR TRP ILE HIS TRP VAL LYS GLN SEQRES 4 H 212 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE ASN SEQRES 5 H 212 PRO THR SER GLY TYR THR GLU TYR ASN GLN ASN PHE LYS SEQRES 6 H 212 ASP LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 212 ALA TYR MET GLN LEU THR SER LEU THR SER GLU ASP SER SEQRES 8 H 212 ALA VAL TYR TYR CYS ALA ARG GLY VAL ILE ARG ASP PHE SEQRES 9 H 212 TRP GLY GLN GLY THR THR LEU THR VAL SER SER ALA LYS SEQRES 10 H 212 THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER SEQRES 11 H 212 ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS LEU SEQRES 12 H 212 VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP SEQRES 13 H 212 ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO SEQRES 14 H 212 ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER SEQRES 15 H 212 VAL THR VAL PRO SER SER PRO ARG PRO SER GLU THR VAL SEQRES 16 H 212 THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL SEQRES 17 H 212 ASP LYS LYS ILE SEQRES 1 I 208 GLU ILE GLN LEU GLN GLN SER GLY PRO GLU ARG MET LYS SEQRES 2 I 208 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 I 208 TYR SER PHE THR THR TYR TYR ILE HIS TRP VAL LYS GLN SEQRES 4 I 208 SER HIS GLY ARG SER LEU GLU TRP ILE GLY TYR ILE ASP SEQRES 5 I 208 PRO PHE ASN ASP ASP THR ASN TYR ASN GLN LYS PHE LYS SEQRES 6 I 208 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 I 208 ALA TYR MET HIS LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 I 208 ALA VAL TYR TYR CYS ALA ARG SER TYR TYR GLY SER LEU SEQRES 9 I 208 ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER SEQRES 10 I 208 ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO SEQRES 11 I 208 GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY SEQRES 12 I 208 CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 I 208 THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR SEQRES 14 I 208 PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SEQRES 15 I 208 SER SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU SEQRES 16 I 208 THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR SEQRES 1 L 219 GLU LEU VAL MET THR GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 L 219 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 219 GLN ASN ILE VAL HIS ASN ASN GLY ASN THR TYR LEU GLU SEQRES 4 L 219 TRP TYR LEU GLN SER PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 L 219 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 L 219 TYR CYS PHE GLN GLY SER HIS VAL PRO PHE THR PHE GLY SEQRES 9 L 219 SER GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA SEQRES 10 L 219 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU SEQRES 11 L 219 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP SEQRES 13 L 219 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR SEQRES 14 L 219 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER SEQRES 15 L 219 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SEQRES 16 L 219 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER SEQRES 17 L 219 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 M 197 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 M 197 SER LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER SEQRES 3 M 197 GLN GLY VAL ASN ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 M 197 PRO ASP GLY SER VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 M 197 ASN LEU HIS SER GLY ALA PRO SER ARG PHE SER GLY SER SEQRES 6 M 197 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 M 197 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN ALA SEQRES 8 M 197 ASN MET VAL PRO TRP THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 M 197 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 M 197 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 M 197 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 M 197 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 M 197 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 M 197 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 M 197 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 M 197 ALA ARG HELIX 1 AA1 GLY A 66 SER A 69 5 4 HELIX 2 AA2 THR H 87 SER H 91 5 5 HELIX 3 AA3 SER H 130 THR H 134 5 5 HELIX 4 AA4 SER H 158 SER H 160 5 3 HELIX 5 AA5 SER I 27 TYR I 31 5 5 HELIX 6 AA6 THR I 86 SER I 90 5 5 HELIX 7 AA7 SER I 159 SER I 161 5 3 HELIX 8 AA8 SER I 189 TRP I 191 5 3 HELIX 9 AA9 GLU L 84 LEU L 88 5 5 HELIX 10 AB1 SER L 126 SER L 132 1 7 HELIX 11 AB2 LYS L 188 ARG L 193 1 6 HELIX 12 AB3 GLU M 79 ILE M 83 5 5 HELIX 13 AB4 SER M 121 SER M 127 1 7 HELIX 14 AB5 LYS M 183 GLU M 187 1 5 SHEET 1 AA1 4 ALA A 10 ILE A 11 0 SHEET 2 AA1 4 ALA A 2 THR A 5 -1 N CYS A 3 O ILE A 11 SHEET 3 AA1 4 ILE A 42 HIS A 45 -1 O PHE A 43 N LYS A 4 SHEET 4 AA1 4 LYS A 101 PRO A 102 -1 O LYS A 101 N CYS A 44 SHEET 1 AA2 4 ALA A 18 VAL A 22 0 SHEET 2 AA2 4 PHE A 142 ALA A 150 1 O ASN A 147 N ALA A 18 SHEET 3 AA2 4 LEU A 125 ASN A 135 -1 N ILE A 126 O ILE A 148 SHEET 4 AA2 4 ALA A 63 TYR A 64 -1 N ALA A 63 O VAL A 128 SHEET 1 AA3 5 ALA A 18 VAL A 22 0 SHEET 2 AA3 5 PHE A 142 ALA A 150 1 O ASN A 147 N ALA A 18 SHEET 3 AA3 5 LEU A 125 ASN A 135 -1 N ILE A 126 O ILE A 148 SHEET 4 AA3 5 ASP A 54 LEU A 58 -1 N TYR A 55 O THR A 134 SHEET 5 AA3 5 ARG A 92 TYR A 95 -1 O VAL A 93 N VAL A 56 SHEET 1 AA4 4 ASN A 33 ASP A 37 0 SHEET 2 AA4 4 VAL A 105 LEU A 109 -1 O LEU A 109 N ASN A 33 SHEET 3 AA4 4 GLY A 73 TYR A 77 -1 N THR A 74 O TYR A 108 SHEET 4 AA4 4 SER A 81 PHE A 84 -1 O PHE A 84 N GLY A 73 SHEET 1 AA5 2 GLY A 117 ILE A 120 0 SHEET 2 AA5 2 VAL A 154 PRO A 157 -1 O VAL A 154 N ILE A 120 SHEET 1 AA6 3 CYS A 161 VAL A 163 0 SHEET 2 AA6 3 THR A 184 CYS A 187 -1 O TYR A 186 N ASP A 162 SHEET 3 AA6 3 VAL A 248 SER A 249 -1 O VAL A 248 N VAL A 185 SHEET 1 AA7 5 ASP A 167 THR A 171 0 SHEET 2 AA7 5 VAL G 3 LYS G 10 1 O THR G 6 N VAL A 168 SHEET 3 AA7 5 ASN A 267 TYR A 278 -1 N ILE A 272 O ILE G 5 SHEET 4 AA7 5 GLN A 191 SER A 198 -1 N GLY A 194 O VAL A 277 SHEET 5 AA7 5 THR A 237 VAL A 243 -1 O VAL A 238 N TYR A 195 SHEET 1 AA8 4 SER A 178 PRO A 180 0 SHEET 2 AA8 4 LEU A 252 ARG A 258 -1 O ALA A 254 N VAL A 179 SHEET 3 AA8 4 VAL A 221 ARG A 227 -1 N THR A 226 O THR A 253 SHEET 4 AA8 4 ILE A 208 PHE A 209 -1 N PHE A 209 O VAL A 223 SHEET 1 AA9 4 SER A 178 PRO A 180 0 SHEET 2 AA9 4 LEU A 252 ARG A 258 -1 O ALA A 254 N VAL A 179 SHEET 3 AA9 4 VAL A 221 ARG A 227 -1 N THR A 226 O THR A 253 SHEET 4 AA9 4 THR A 230 ILE A 231 -1 O THR A 230 N ARG A 227 SHEET 1 AB1 6 ALA H 9 ALA H 12 0 SHEET 2 AB1 6 THR H 109 VAL H 113 1 O THR H 112 N GLU H 10 SHEET 3 AB1 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 109 SHEET 4 AB1 6 ILE H 34 GLN H 39 -1 N HIS H 35 O ALA H 97 SHEET 5 AB1 6 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AB1 6 THR H 58 TYR H 60 -1 O GLU H 59 N TYR H 50 SHEET 1 AB2 4 ALA H 9 ALA H 12 0 SHEET 2 AB2 4 THR H 109 VAL H 113 1 O THR H 112 N GLU H 10 SHEET 3 AB2 4 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 109 SHEET 4 AB2 4 PHE H 104 TRP H 105 -1 O PHE H 104 N ARG H 98 SHEET 1 AB3 3 GLY H 15 CYS H 22 0 SHEET 2 AB3 3 THR H 78 LEU H 86 -1 O LEU H 86 N GLY H 15 SHEET 3 AB3 3 ALA H 68 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AB4 4 SER H 122 LEU H 126 0 SHEET 2 AB4 4 VAL H 138 TYR H 147 -1 O GLY H 141 N LEU H 126 SHEET 3 AB4 4 LEU H 176 VAL H 185 -1 O LEU H 179 N VAL H 144 SHEET 4 AB4 4 HIS H 166 THR H 167 -1 N HIS H 166 O SER H 182 SHEET 1 AB5 4 SER H 122 LEU H 126 0 SHEET 2 AB5 4 VAL H 138 TYR H 147 -1 O GLY H 141 N LEU H 126 SHEET 3 AB5 4 LEU H 176 VAL H 185 -1 O LEU H 179 N VAL H 144 SHEET 4 AB5 4 VAL H 171 GLN H 173 -1 N VAL H 171 O THR H 178 SHEET 1 AB6 3 THR H 153 TRP H 156 0 SHEET 2 AB6 3 THR H 196 HIS H 201 -1 O ASN H 198 N THR H 155 SHEET 3 AB6 3 THR H 206 LYS H 211 -1 O THR H 206 N HIS H 201 SHEET 1 AB7 4 GLN I 2 GLN I 5 0 SHEET 2 AB7 4 VAL I 17 SER I 24 -1 O LYS I 22 N GLN I 4 SHEET 3 AB7 4 THR I 77 LEU I 82 -1 O MET I 80 N ILE I 19 SHEET 4 AB7 4 ALA I 67 ASP I 72 -1 N THR I 70 O TYR I 79 SHEET 1 AB8 6 GLU I 9 MET I 11 0 SHEET 2 AB8 6 THR I 110 VAL I 114 1 O THR I 113 N MET I 11 SHEET 3 AB8 6 ALA I 91 SER I 98 -1 N ALA I 91 O LEU I 112 SHEET 4 AB8 6 TYR I 32 GLN I 38 -1 N GLN I 38 O VAL I 92 SHEET 5 AB8 6 LEU I 44 ILE I 50 -1 O GLU I 45 N LYS I 37 SHEET 6 AB8 6 THR I 57 TYR I 59 -1 O ASN I 58 N TYR I 49 SHEET 1 AB9 4 GLU I 9 MET I 11 0 SHEET 2 AB9 4 THR I 110 VAL I 114 1 O THR I 113 N MET I 11 SHEET 3 AB9 4 ALA I 91 SER I 98 -1 N ALA I 91 O LEU I 112 SHEET 4 AB9 4 TYR I 105 TRP I 106 -1 O TYR I 105 N ARG I 97 SHEET 1 AC1 4 SER I 123 LEU I 127 0 SHEET 2 AC1 4 MET I 138 TYR I 148 -1 O LEU I 144 N TYR I 125 SHEET 3 AC1 4 LEU I 177 PRO I 187 -1 O VAL I 184 N LEU I 141 SHEET 4 AC1 4 VAL I 166 THR I 168 -1 N HIS I 167 O SER I 183 SHEET 1 AC2 4 SER I 123 LEU I 127 0 SHEET 2 AC2 4 MET I 138 TYR I 148 -1 O LEU I 144 N TYR I 125 SHEET 3 AC2 4 LEU I 177 PRO I 187 -1 O VAL I 184 N LEU I 141 SHEET 4 AC2 4 VAL I 172 GLN I 174 -1 N VAL I 172 O THR I 179 SHEET 1 AC3 2 THR I 154 TRP I 157 0 SHEET 2 AC3 2 CYS I 198 ALA I 201 -1 O ASN I 199 N THR I 156 SHEET 1 AC4 4 MET L 4 THR L 7 0 SHEET 2 AC4 4 ALA L 19 SER L 25 -1 O SER L 22 N THR L 7 SHEET 3 AC4 4 ASP L 75 ILE L 80 -1 O ILE L 80 N ALA L 19 SHEET 4 AC4 4 PHE L 67 SER L 72 -1 N SER L 70 O THR L 77 SHEET 1 AC5 5 SER L 10 VAL L 13 0 SHEET 2 AC5 5 THR L 107 ILE L 111 1 O GLU L 110 N VAL L 13 SHEET 3 AC5 5 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AC5 5 LEU L 38 GLN L 43 -1 N GLU L 39 O PHE L 94 SHEET 5 AC5 5 LYS L 50 ILE L 53 -1 O LEU L 52 N TRP L 40 SHEET 1 AC6 4 SER L 10 VAL L 13 0 SHEET 2 AC6 4 THR L 107 ILE L 111 1 O GLU L 110 N VAL L 13 SHEET 3 AC6 4 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AC6 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AC7 4 THR L 119 PHE L 123 0 SHEET 2 AC7 4 GLY L 134 PHE L 144 -1 O PHE L 140 N SER L 121 SHEET 3 AC7 4 TYR L 178 THR L 187 -1 O LEU L 184 N VAL L 137 SHEET 4 AC7 4 VAL L 164 TRP L 168 -1 N LEU L 165 O THR L 183 SHEET 1 AC8 4 SER L 158 ARG L 160 0 SHEET 2 AC8 4 ILE L 149 ILE L 155 -1 N ILE L 155 O SER L 158 SHEET 3 AC8 4 SER L 196 HIS L 203 -1 O THR L 202 N ASN L 150 SHEET 4 AC8 4 ILE L 210 ASN L 215 -1 O ILE L 210 N ALA L 201 SHEET 1 AC9 4 MET M 4 GLN M 6 0 SHEET 2 AC9 4 VAL M 19 ALA M 25 -1 O ARG M 24 N THR M 5 SHEET 3 AC9 4 ASP M 70 ILE M 75 -1 O LEU M 73 N ILE M 21 SHEET 4 AC9 4 PHE M 62 SER M 67 -1 N SER M 63 O THR M 74 SHEET 1 AD1 6 SER M 10 ALA M 13 0 SHEET 2 AD1 6 THR M 102 ILE M 106 1 O GLU M 105 N ALA M 13 SHEET 3 AD1 6 THR M 85 GLN M 90 -1 N TYR M 86 O THR M 102 SHEET 4 AD1 6 LEU M 33 GLN M 38 -1 N ASN M 34 O GLN M 89 SHEET 5 AD1 6 VAL M 44 TYR M 49 -1 O LYS M 45 N GLN M 37 SHEET 6 AD1 6 ASN M 53 LEU M 54 -1 O ASN M 53 N TYR M 49 SHEET 1 AD2 4 SER M 10 ALA M 13 0 SHEET 2 AD2 4 THR M 102 ILE M 106 1 O GLU M 105 N ALA M 13 SHEET 3 AD2 4 THR M 85 GLN M 90 -1 N TYR M 86 O THR M 102 SHEET 4 AD2 4 THR M 97 PHE M 98 -1 O THR M 97 N GLN M 90 SHEET 1 AD3 4 THR M 114 PHE M 118 0 SHEET 2 AD3 4 GLY M 129 PHE M 139 -1 O PHE M 135 N SER M 116 SHEET 3 AD3 4 TYR M 173 THR M 182 -1 O LEU M 181 N ALA M 130 SHEET 4 AD3 4 VAL M 159 TRP M 163 -1 N LEU M 160 O THR M 178 SHEET 1 AD4 3 SER M 153 ARG M 155 0 SHEET 2 AD4 3 VAL M 146 ILE M 150 -1 N ILE M 150 O SER M 153 SHEET 3 AD4 3 TYR M 192 ALA M 196 -1 O GLU M 195 N LYS M 147 SSBOND 1 CYS A 3 CYS A 44 1555 1555 2.03 SSBOND 2 CYS A 161 CYS A 187 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 4 CYS H 142 CYS H 197 1555 1555 2.03 SSBOND 5 CYS I 21 CYS I 95 1555 1555 2.03 SSBOND 6 CYS I 143 CYS I 198 1555 1555 2.03 SSBOND 7 CYS L 23 CYS L 93 1555 1555 2.03 SSBOND 8 CYS L 139 CYS L 199 1555 1555 2.03 SSBOND 9 CYS M 23 CYS M 88 1555 1555 2.04 SSBOND 10 CYS M 134 CYS M 194 1555 1555 2.03 CISPEP 1 PHE A 84 PRO A 85 0 5.27 CISPEP 2 TYR A 175 PRO A 176 0 0.99 CISPEP 3 PHE H 148 PRO H 149 0 -6.48 CISPEP 4 GLU H 150 PRO H 151 0 -4.19 CISPEP 5 ARG H 190 PRO H 191 0 -3.23 CISPEP 6 PHE I 149 PRO I 150 0 -3.40 CISPEP 7 GLU I 151 PRO I 152 0 -2.45 CISPEP 8 TRP I 191 PRO I 192 0 -1.71 CISPEP 9 THR L 7 PRO L 8 0 -2.43 CISPEP 10 VAL L 99 PRO L 100 0 -0.31 CISPEP 11 TYR L 145 PRO L 146 0 0.09 CISPEP 12 VAL M 94 PRO M 95 0 -1.12 CISPEP 13 TYR M 140 PRO M 141 0 -0.44 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