HEADER VIRAL PROTEIN/IMMUNE SYSTEM 11-JAN-25 9MTF TITLE STRUCTURE OF PORCINE FAB 14-1 IN COMPLEX WITH INFLUENZA H1N1 A/SOLOMON TITLE 2 ISLAND/3/2006 HEMAGGLUTININ COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ (HA1 POLYPEPTIDE) FROM INFLUENZA H1N1 COMPND 3 A/SOLOMON ISLAND/3/2006; COMPND 4 CHAIN: A, C, E; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEMAGGLUTININ (HA2 POLYPEPTIDE) FROM INFLUENZA H1N1 COMPND 8 A/SOLOMON ISLAND/3/2006; COMPND 9 CHAIN: B, D, F; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: HEAVY CHAIN OF FAB FROM PORCINE ANTIBODY 14-1; COMPND 13 CHAIN: H, I, M; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: LIGHT CHAIN OF FAB FROM PORCINE ANTIBODY 14-1; COMPND 17 CHAIN: J, L, N; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_COMMON: A/SOLOMON ISLANDS/3/2006(H1N1); SOURCE 4 ORGANISM_TAXID: 464623; SOURCE 5 GENE: HA; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 11 ORGANISM_COMMON: A/SOLOMON ISLANDS/3/2006(H1N1); SOURCE 12 ORGANISM_TAXID: 464623; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 18 ORGANISM_COMMON: PIG; SOURCE 19 ORGANISM_TAXID: 9823; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 23 MOL_ID: 4; SOURCE 24 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 25 ORGANISM_COMMON: PIG; SOURCE 26 ORGANISM_TAXID: 9823; SOURCE 27 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 28 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS INFLUENZA, HEMAGGLUTININ, ANTIBODY, IMMUNE RESPONSE, PIG, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR H.LV,T.PHOLCHAREE,N.C.WU REVDAT 1 24-SEP-25 9MTF 0 JRNL AUTH H.LV,T.PHOLCHAREE,N.C.WU JRNL TITL STRUCTURAL ANALYSIS OF BROADLY NEUTRALIZING PORCINE JRNL TITL 2 ANTIBODIES TO INFLUENZA HEMAGGLUTININ STEM JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.61 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC, CRYOSPARC 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) : 2.610 REMARK 3 NUMBER OF PARTICLES : 363401 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 9MTF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291811. 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 : A COMPLEX OF HEMAGGLUTININ FROM REMARK 245 A A/HAWAII/70/2019 WITH PIG FAB REMARK 245 24-1G17 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 3.00 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 : HEMAGGLUTININ WAS EXPRESSED REMARK 245 RECOMBINANTLY IN SF9 CELLS. FAB 24-1G17 WAS EXPRESSED REMARK 245 RECOMBINANTLY IN EXPI293F CELLS. 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 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5735.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, L, REMARK 350 AND CHAINS: M, N 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 ILE A 80 REMARK 465 SER A 325 REMARK 465 ILE A 326 REMARK 465 GLN A 327 REMARK 465 SER A 328 REMARK 465 ARG A 329 REMARK 465 GLY B 1 REMARK 465 ILE B 173 REMARK 465 ASP B 174 REMARK 465 GLY B 175 REMARK 465 VAL B 176 REMARK 465 LYS B 177 REMARK 465 LEU B 178 REMARK 465 GLU B 179 REMARK 465 SER B 180 REMARK 465 MET B 181 REMARK 465 GLY B 182 REMARK 465 VAL B 183 REMARK 465 TYR B 184 REMARK 465 GLN B 185 REMARK 465 ILE B 186 REMARK 465 LEU B 187 REMARK 465 ALA B 188 REMARK 465 ILE B 189 REMARK 465 TYR B 190 REMARK 465 SER B 191 REMARK 465 THR B 192 REMARK 465 VAL B 193 REMARK 465 ALA B 194 REMARK 465 SER B 195 REMARK 465 SER B 196 REMARK 465 LEU B 197 REMARK 465 VAL B 198 REMARK 465 LEU B 199 REMARK 465 LEU B 200 REMARK 465 VAL B 201 REMARK 465 SER B 202 REMARK 465 LEU B 203 REMARK 465 GLY B 204 REMARK 465 ALA B 205 REMARK 465 ILE B 206 REMARK 465 SER B 207 REMARK 465 PHE B 208 REMARK 465 TRP B 209 REMARK 465 MET B 210 REMARK 465 CYS B 211 REMARK 465 SER B 212 REMARK 465 ASN B 213 REMARK 465 GLY B 214 REMARK 465 SER B 215 REMARK 465 LEU B 216 REMARK 465 GLN B 217 REMARK 465 CYS B 218 REMARK 465 ARG B 219 REMARK 465 ILE B 220 REMARK 465 CYS B 221 REMARK 465 ILE B 222 REMARK 465 SER C 325 REMARK 465 ILE C 326 REMARK 465 GLN C 327 REMARK 465 SER C 328 REMARK 465 ARG C 329 REMARK 465 GLY D 1 REMARK 465 ILE D 173 REMARK 465 ASP D 174 REMARK 465 GLY D 175 REMARK 465 VAL D 176 REMARK 465 LYS D 177 REMARK 465 LEU D 178 REMARK 465 GLU D 179 REMARK 465 SER D 180 REMARK 465 MET D 181 REMARK 465 GLY D 182 REMARK 465 VAL D 183 REMARK 465 TYR D 184 REMARK 465 GLN D 185 REMARK 465 ILE D 186 REMARK 465 LEU D 187 REMARK 465 ALA D 188 REMARK 465 ILE D 189 REMARK 465 TYR D 190 REMARK 465 SER D 191 REMARK 465 THR D 192 REMARK 465 VAL D 193 REMARK 465 ALA D 194 REMARK 465 SER D 195 REMARK 465 SER D 196 REMARK 465 LEU D 197 REMARK 465 VAL D 198 REMARK 465 LEU D 199 REMARK 465 LEU D 200 REMARK 465 VAL D 201 REMARK 465 SER D 202 REMARK 465 LEU D 203 REMARK 465 GLY D 204 REMARK 465 ALA D 205 REMARK 465 ILE D 206 REMARK 465 SER D 207 REMARK 465 PHE D 208 REMARK 465 TRP D 209 REMARK 465 MET D 210 REMARK 465 CYS D 211 REMARK 465 SER D 212 REMARK 465 ASN D 213 REMARK 465 GLY D 214 REMARK 465 SER D 215 REMARK 465 LEU D 216 REMARK 465 GLN D 217 REMARK 465 CYS D 218 REMARK 465 ARG D 219 REMARK 465 ILE D 220 REMARK 465 CYS D 221 REMARK 465 ILE D 222 REMARK 465 ALA E 10 REMARK 465 SER E 332 REMARK 465 ILE E 333 REMARK 465 GLN E 334 REMARK 465 SER E 335 REMARK 465 ARG E 336 REMARK 465 GLY F 1 REMARK 465 ILE F 173 REMARK 465 ASP F 174 REMARK 465 GLY F 175 REMARK 465 VAL F 176 REMARK 465 LYS F 177 REMARK 465 LEU F 178 REMARK 465 GLU F 179 REMARK 465 SER F 180 REMARK 465 MET F 181 REMARK 465 GLY F 182 REMARK 465 VAL F 183 REMARK 465 TYR F 184 REMARK 465 GLN F 185 REMARK 465 ILE F 186 REMARK 465 LEU F 187 REMARK 465 ALA F 188 REMARK 465 ILE F 189 REMARK 465 TYR F 190 REMARK 465 SER F 191 REMARK 465 THR F 192 REMARK 465 VAL F 193 REMARK 465 ALA F 194 REMARK 465 SER F 195 REMARK 465 SER F 196 REMARK 465 LEU F 197 REMARK 465 VAL F 198 REMARK 465 LEU F 199 REMARK 465 LEU F 200 REMARK 465 VAL F 201 REMARK 465 SER F 202 REMARK 465 LEU F 203 REMARK 465 GLY F 204 REMARK 465 ALA F 205 REMARK 465 ILE F 206 REMARK 465 SER F 207 REMARK 465 PHE F 208 REMARK 465 TRP F 209 REMARK 465 MET F 210 REMARK 465 CYS F 211 REMARK 465 SER F 212 REMARK 465 ASN F 213 REMARK 465 GLY F 214 REMARK 465 SER F 215 REMARK 465 LEU F 216 REMARK 465 GLN F 217 REMARK 465 CYS F 218 REMARK 465 ARG F 219 REMARK 465 ILE F 220 REMARK 465 CYS F 221 REMARK 465 ILE F 222 REMARK 465 LEU J 107 REMARK 465 GLY J 108 REMARK 465 GLN J 109 REMARK 465 PRO J 110 REMARK 465 LEU L 107 REMARK 465 GLY L 108 REMARK 465 GLN L 109 REMARK 465 PRO L 110 REMARK 465 LEU N 107 REMARK 465 GLY N 108 REMARK 465 GLN N 109 REMARK 465 PRO N 110 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 ARG A 192 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 192 CG CD NE CZ NH1 NH2 REMARK 470 ARG E 198 CG CD NE CZ NH1 NH2 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 OG1 THR J 39 OE1 GLN J 42 1.91 REMARK 500 OG SER L 63 OG1 THR L 74 2.18 REMARK 500 O ASP F 19 OH TYR M 100G 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 LYS A 54 19.40 58.98 REMARK 500 SER A 126 -8.86 70.34 REMARK 500 ASN A 142 49.66 39.05 REMARK 500 GLU A 173 17.68 51.14 REMARK 500 PRO A 221 178.53 -59.32 REMARK 500 GLU A 276 59.82 -92.56 REMARK 500 PRO A 284 4.49 -65.93 REMARK 500 ARG A 310 55.44 -92.06 REMARK 500 ASN B 28 -168.12 -122.21 REMARK 500 LYS B 127 -133.58 54.06 REMARK 500 ASP B 158 66.27 60.85 REMARK 500 ASN C 33 62.02 60.07 REMARK 500 GLU C 75 37.24 -97.99 REMARK 500 ARG C 81A 146.97 -171.95 REMARK 500 SER C 126 -7.36 68.39 REMARK 500 ASN C 142 57.55 39.64 REMARK 500 THR C 155 -168.75 -126.24 REMARK 500 ASN C 158 45.09 39.93 REMARK 500 LEU C 160 149.35 -174.35 REMARK 500 LYS C 197 119.58 -177.66 REMARK 500 SER C 206 -169.94 -160.87 REMARK 500 SER C 210 119.60 -161.04 REMARK 500 ASP C 225 -2.81 55.93 REMARK 500 LYS D 127 -129.52 57.15 REMARK 500 GLU D 171 55.55 -92.41 REMARK 500 GLU E 76 48.29 -91.44 REMARK 500 CYS E 77 17.61 -142.76 REMARK 500 LEU E 80 -67.88 -93.50 REMARK 500 ILE E 81 53.64 22.19 REMARK 500 ARG E 83 143.77 73.22 REMARK 500 SER E 131 -169.19 -101.52 REMARK 500 SER E 132 -10.73 71.09 REMARK 500 ASN E 148 57.14 39.68 REMARK 500 ASN E 164 -125.56 56.33 REMARK 500 GLU E 179 15.78 56.94 REMARK 500 ASP E 231 -28.56 77.12 REMARK 500 CYS E 284 -166.58 -79.87 REMARK 500 PRO E 291 4.75 -64.82 REMARK 500 ASN E 296 79.96 -101.82 REMARK 500 VAL F 66 55.78 -94.14 REMARK 500 LYS F 127 -138.65 59.30 REMARK 500 HIS F 142 -153.30 -132.50 REMARK 500 ASN F 145 -168.06 -75.41 REMARK 500 ASP F 158 66.09 60.14 REMARK 500 SER J 26 49.36 -90.95 REMARK 500 SER J 27 -162.52 -164.35 REMARK 500 GLN J 42 144.68 -171.06 REMARK 500 THR J 51 -58.67 68.89 REMARK 500 ALA J 80 -1.14 66.26 REMARK 500 SER L 26 51.03 -91.02 REMARK 500 REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG C 224 0.19 SIDE CHAIN REMARK 500 ARG C 229 0.13 SIDE CHAIN REMARK 500 ARG C 310 0.29 SIDE CHAIN REMARK 500 ARG C 315 0.21 SIDE CHAIN REMARK 500 ARG N 50 0.22 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48607 RELATED DB: EMDB REMARK 900 STRUCTURE OF PORCINE FAB 14-1 IN COMPLEX WITH INFLUENZA H1N1 A/ REMARK 900 SOLOMON ISLAND/3/2006 HEMAGGLUTININ DBREF1 9MTF A 10 329 UNP A0A0G2RTI0_9INFA DBREF2 9MTF A A0A0G2RTI0 17 343 DBREF 9MTF B 1 222 PDB 9MTF 9MTF 1 222 DBREF1 9MTF C 10 329 UNP A0A0G2RTI0_9INFA DBREF2 9MTF C A0A0G2RTI0 17 343 DBREF 9MTF D 1 222 PDB 9MTF 9MTF 1 222 DBREF1 9MTF E 10 336 UNP A0A0G2RTI0_9INFA DBREF2 9MTF E A0A0G2RTI0 17 343 DBREF 9MTF F 1 222 PDB 9MTF 9MTF 1 222 DBREF 9MTF H 1 113 PDB 9MTF 9MTF 1 113 DBREF 9MTF I 1 113 PDB 9MTF 9MTF 1 113 DBREF 9MTF J 1 110 PDB 9MTF 9MTF 1 110 DBREF 9MTF L 1 110 PDB 9MTF 9MTF 1 110 DBREF 9MTF M 1 113 PDB 9MTF 9MTF 1 113 DBREF 9MTF N 1 110 PDB 9MTF 9MTF 1 110 SEQRES 1 A 327 ALA ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER SEQRES 2 A 327 THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR SEQRES 3 A 327 VAL THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN SEQRES 4 A 327 GLY LYS LEU CYS LEU LEU LYS GLY ILE ALA PRO LEU GLN SEQRES 5 A 327 LEU GLY ASN CYS SER VAL ALA GLY TRP ILE LEU GLY ASN SEQRES 6 A 327 PRO GLU CYS GLU LEU LEU ILE SER ARG GLU SER TRP SER SEQRES 7 A 327 TYR ILE VAL GLU LYS PRO ASN PRO GLU ASN GLY THR CYS SEQRES 8 A 327 TYR PRO GLY HIS PHE ALA ASP TYR GLU GLU LEU ARG GLU SEQRES 9 A 327 GLN LEU SER SER VAL SER SER PHE GLU ARG PHE GLU ILE SEQRES 10 A 327 PHE PRO LYS GLU SER SER TRP PRO ASN HIS THR THR THR SEQRES 11 A 327 GLY VAL SER ALA SER CYS SER HIS ASN GLY GLU SER SER SEQRES 12 A 327 PHE TYR LYS ASN LEU LEU TRP LEU THR GLY LYS ASN GLY SEQRES 13 A 327 LEU TYR PRO ASN LEU SER LYS SER TYR ALA ASN ASN LYS SEQRES 14 A 327 GLU LYS GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO SEQRES 15 A 327 PRO ASN ILE GLY ASP GLN ARG ALA LEU TYR HIS LYS GLU SEQRES 16 A 327 ASN ALA TYR VAL SER VAL VAL SER SER HIS TYR SER ARG SEQRES 17 A 327 LYS PHE THR PRO GLU ILE ALA LYS ARG PRO LYS VAL ARG SEQRES 18 A 327 ASP GLN GLU GLY ARG ILE ASN TYR TYR TRP THR LEU LEU SEQRES 19 A 327 GLU PRO GLY ASP THR ILE ILE PHE GLU ALA ASN GLY ASN SEQRES 20 A 327 LEU ILE ALA PRO ARG TYR ALA PHE ALA LEU SER ARG GLY SEQRES 21 A 327 PHE GLY SER GLY ILE ILE ASN SER ASN ALA PRO MET ASP SEQRES 22 A 327 GLU CYS ASP ALA LYS CYS GLN THR PRO GLN GLY ALA ILE SEQRES 23 A 327 ASN SER SER LEU PRO PHE GLN ASN VAL HIS PRO VAL THR SEQRES 24 A 327 ILE GLY GLU CYS PRO LYS TYR VAL ARG SER ALA LYS LEU SEQRES 25 A 327 ARG MET VAL THR GLY LEU ARG ASN ILE PRO SER ILE GLN SEQRES 26 A 327 SER ARG SEQRES 1 B 222 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 B 222 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 B 222 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS SEQRES 4 B 222 SER THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL SEQRES 5 B 222 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 B 222 VAL GLY LYS GLU PHE ASN LYS LEU GLU ARG ARG MET GLU SEQRES 7 B 222 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE ILE ASP ILE SEQRES 8 B 222 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 B 222 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN SEQRES 10 B 222 LEU TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA SEQRES 11 B 222 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 B 222 CYS ASN ASP GLU CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 B 222 TYR ASP TYR PRO LYS TYR SER GLU GLU SER LYS LEU ASN SEQRES 14 B 222 ARG GLU LYS ILE ASP GLY VAL LYS LEU GLU SER MET GLY SEQRES 15 B 222 VAL TYR GLN ILE LEU ALA ILE TYR SER THR VAL ALA SER SEQRES 16 B 222 SER LEU VAL LEU LEU VAL SER LEU GLY ALA ILE SER PHE SEQRES 17 B 222 TRP MET CYS SER ASN GLY SER LEU GLN CYS ARG ILE CYS SEQRES 18 B 222 ILE SEQRES 1 C 327 ALA ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER SEQRES 2 C 327 THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR SEQRES 3 C 327 VAL THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN SEQRES 4 C 327 GLY LYS LEU CYS LEU LEU LYS GLY ILE ALA PRO LEU GLN SEQRES 5 C 327 LEU GLY ASN CYS SER VAL ALA GLY TRP ILE LEU GLY ASN SEQRES 6 C 327 PRO GLU CYS GLU LEU LEU ILE SER ARG GLU SER TRP SER SEQRES 7 C 327 TYR ILE VAL GLU LYS PRO ASN PRO GLU ASN GLY THR CYS SEQRES 8 C 327 TYR PRO GLY HIS PHE ALA ASP TYR GLU GLU LEU ARG GLU SEQRES 9 C 327 GLN LEU SER SER VAL SER SER PHE GLU ARG PHE GLU ILE SEQRES 10 C 327 PHE PRO LYS GLU SER SER TRP PRO ASN HIS THR THR THR SEQRES 11 C 327 GLY VAL SER ALA SER CYS SER HIS ASN GLY GLU SER SER SEQRES 12 C 327 PHE TYR LYS ASN LEU LEU TRP LEU THR GLY LYS ASN GLY SEQRES 13 C 327 LEU TYR PRO ASN LEU SER LYS SER TYR ALA ASN ASN LYS SEQRES 14 C 327 GLU LYS GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO SEQRES 15 C 327 PRO ASN ILE GLY ASP GLN ARG ALA LEU TYR HIS LYS GLU SEQRES 16 C 327 ASN ALA TYR VAL SER VAL VAL SER SER HIS TYR SER ARG SEQRES 17 C 327 LYS PHE THR PRO GLU ILE ALA LYS ARG PRO LYS VAL ARG SEQRES 18 C 327 ASP GLN GLU GLY ARG ILE ASN TYR TYR TRP THR LEU LEU SEQRES 19 C 327 GLU PRO GLY ASP THR ILE ILE PHE GLU ALA ASN GLY ASN SEQRES 20 C 327 LEU ILE ALA PRO ARG TYR ALA PHE ALA LEU SER ARG GLY SEQRES 21 C 327 PHE GLY SER GLY ILE ILE ASN SER ASN ALA PRO MET ASP SEQRES 22 C 327 GLU CYS ASP ALA LYS CYS GLN THR PRO GLN GLY ALA ILE SEQRES 23 C 327 ASN SER SER LEU PRO PHE GLN ASN VAL HIS PRO VAL THR SEQRES 24 C 327 ILE GLY GLU CYS PRO LYS TYR VAL ARG SER ALA LYS LEU SEQRES 25 C 327 ARG MET VAL THR GLY LEU ARG ASN ILE PRO SER ILE GLN SEQRES 26 C 327 SER ARG SEQRES 1 D 222 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 D 222 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 D 222 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS SEQRES 4 D 222 SER THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL SEQRES 5 D 222 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 D 222 VAL GLY LYS GLU PHE ASN LYS LEU GLU ARG ARG MET GLU SEQRES 7 D 222 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE ILE ASP ILE SEQRES 8 D 222 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 D 222 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN SEQRES 10 D 222 LEU TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA SEQRES 11 D 222 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 D 222 CYS ASN ASP GLU CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 D 222 TYR ASP TYR PRO LYS TYR SER GLU GLU SER LYS LEU ASN SEQRES 14 D 222 ARG GLU LYS ILE ASP GLY VAL LYS LEU GLU SER MET GLY SEQRES 15 D 222 VAL TYR GLN ILE LEU ALA ILE TYR SER THR VAL ALA SER SEQRES 16 D 222 SER LEU VAL LEU LEU VAL SER LEU GLY ALA ILE SER PHE SEQRES 17 D 222 TRP MET CYS SER ASN GLY SER LEU GLN CYS ARG ILE CYS SEQRES 18 D 222 ILE SEQRES 1 E 327 ALA ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER SEQRES 2 E 327 THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR SEQRES 3 E 327 VAL THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN SEQRES 4 E 327 GLY LYS LEU CYS LEU LEU LYS GLY ILE ALA PRO LEU GLN SEQRES 5 E 327 LEU GLY ASN CYS SER VAL ALA GLY TRP ILE LEU GLY ASN SEQRES 6 E 327 PRO GLU CYS GLU LEU LEU ILE SER ARG GLU SER TRP SER SEQRES 7 E 327 TYR ILE VAL GLU LYS PRO ASN PRO GLU ASN GLY THR CYS SEQRES 8 E 327 TYR PRO GLY HIS PHE ALA ASP TYR GLU GLU LEU ARG GLU SEQRES 9 E 327 GLN LEU SER SER VAL SER SER PHE GLU ARG PHE GLU ILE SEQRES 10 E 327 PHE PRO LYS GLU SER SER TRP PRO ASN HIS THR THR THR SEQRES 11 E 327 GLY VAL SER ALA SER CYS SER HIS ASN GLY GLU SER SER SEQRES 12 E 327 PHE TYR LYS ASN LEU LEU TRP LEU THR GLY LYS ASN GLY SEQRES 13 E 327 LEU TYR PRO ASN LEU SER LYS SER TYR ALA ASN ASN LYS SEQRES 14 E 327 GLU LYS GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO SEQRES 15 E 327 PRO ASN ILE GLY ASP GLN ARG ALA LEU TYR HIS LYS GLU SEQRES 16 E 327 ASN ALA TYR VAL SER VAL VAL SER SER HIS TYR SER ARG SEQRES 17 E 327 LYS PHE THR PRO GLU ILE ALA LYS ARG PRO LYS VAL ARG SEQRES 18 E 327 ASP GLN GLU GLY ARG ILE ASN TYR TYR TRP THR LEU LEU SEQRES 19 E 327 GLU PRO GLY ASP THR ILE ILE PHE GLU ALA ASN GLY ASN SEQRES 20 E 327 LEU ILE ALA PRO ARG TYR ALA PHE ALA LEU SER ARG GLY SEQRES 21 E 327 PHE GLY SER GLY ILE ILE ASN SER ASN ALA PRO MET ASP SEQRES 22 E 327 GLU CYS ASP ALA LYS CYS GLN THR PRO GLN GLY ALA ILE SEQRES 23 E 327 ASN SER SER LEU PRO PHE GLN ASN VAL HIS PRO VAL THR SEQRES 24 E 327 ILE GLY GLU CYS PRO LYS TYR VAL ARG SER ALA LYS LEU SEQRES 25 E 327 ARG MET VAL THR GLY LEU ARG ASN ILE PRO SER ILE GLN SEQRES 26 E 327 SER ARG SEQRES 1 F 222 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 F 222 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 F 222 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS SEQRES 4 F 222 SER THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL SEQRES 5 F 222 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 F 222 VAL GLY LYS GLU PHE ASN LYS LEU GLU ARG ARG MET GLU SEQRES 7 F 222 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE ILE ASP ILE SEQRES 8 F 222 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 F 222 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN SEQRES 10 F 222 LEU TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA SEQRES 11 F 222 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 F 222 CYS ASN ASP GLU CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 F 222 TYR ASP TYR PRO LYS TYR SER GLU GLU SER LYS LEU ASN SEQRES 14 F 222 ARG GLU LYS ILE ASP GLY VAL LYS LEU GLU SER MET GLY SEQRES 15 F 222 VAL TYR GLN ILE LEU ALA ILE TYR SER THR VAL ALA SER SEQRES 16 F 222 SER LEU VAL LEU LEU VAL SER LEU GLY ALA ILE SER PHE SEQRES 17 F 222 TRP MET CYS SER ASN GLY SER LEU GLN CYS ARG ILE CYS SEQRES 18 F 222 ILE SEQRES 1 H 127 GLU GLU LYS LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 127 PRO GLY GLY SER LEU ARG LEU GLY CYS VAL GLY SER GLY SEQRES 3 H 127 PHE THR PHE SER SER ALA TYR ILE ASN TRP VAL ARG GLN SEQRES 4 H 127 ALA PRO GLY LYS GLY LEU GLU TRP LEU ALA ALA ILE ARG SEQRES 5 H 127 THR SER GLY GLY GLY THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 127 GLY ARG PHE THR ILE SER ARG ASP ASP SER GLN ASN THR SEQRES 7 H 127 ALA TYR LEU GLN MET ASN SER LEU ARG THR GLU ASP THR SEQRES 8 H 127 ALA ARG TYR TYR CYS ALA ALA GLY ALA MET THR MET VAL SEQRES 9 H 127 VAL ALA SER PHE PHE GLN TYR TYR ALA MET ASP LEU TRP SEQRES 10 H 127 GLY PRO GLY VAL GLU VAL VAL VAL SER SER SEQRES 1 I 127 GLU GLU LYS LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 I 127 PRO GLY GLY SER LEU ARG LEU GLY CYS VAL GLY SER GLY SEQRES 3 I 127 PHE THR PHE SER SER ALA TYR ILE ASN TRP VAL ARG GLN SEQRES 4 I 127 ALA PRO GLY LYS GLY LEU GLU TRP LEU ALA ALA ILE ARG SEQRES 5 I 127 THR SER GLY GLY GLY THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 I 127 GLY ARG PHE THR ILE SER ARG ASP ASP SER GLN ASN THR SEQRES 7 I 127 ALA TYR LEU GLN MET ASN SER LEU ARG THR GLU ASP THR SEQRES 8 I 127 ALA ARG TYR TYR CYS ALA ALA GLY ALA MET THR MET VAL SEQRES 9 I 127 VAL ALA SER PHE PHE GLN TYR TYR ALA MET ASP LEU TRP SEQRES 10 I 127 GLY PRO GLY VAL GLU VAL VAL VAL SER SER SEQRES 1 J 112 GLN THR VAL ILE GLN GLU PRO ALA MET SER VAL SER PRO SEQRES 2 J 112 GLY GLY THR VAL THR LEU THR CYS ALA PHE SER SER GLY SEQRES 3 J 112 SER VAL THR SER GLY ASP TYR PRO SER TRP PHE GLN GLN SEQRES 4 J 112 THR PRO GLY GLN PRO PRO ARG LEU LEU ILE TYR ARG THR SEQRES 5 J 112 ASN ASN ARG PRO THR GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 J 112 ALA ILE SER GLY ASN LYS ALA ALA LEU THR ILE THR GLY SEQRES 7 J 112 ALA GLN ALA ASN ASP GLU ALA ASP TYR TYR CYS THR LEU SEQRES 8 J 112 TYR THR SER SER LEU ASN ASN ILE PHE GLY GLY GLY THR SEQRES 9 J 112 HIS LEU THR VAL LEU GLY GLN PRO SEQRES 1 L 112 GLN THR VAL ILE GLN GLU PRO ALA MET SER VAL SER PRO SEQRES 2 L 112 GLY GLY THR VAL THR LEU THR CYS ALA PHE SER SER GLY SEQRES 3 L 112 SER VAL THR SER GLY ASP TYR PRO SER TRP PHE GLN GLN SEQRES 4 L 112 THR PRO GLY GLN PRO PRO ARG LEU LEU ILE TYR ARG THR SEQRES 5 L 112 ASN ASN ARG PRO THR GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 112 ALA ILE SER GLY ASN LYS ALA ALA LEU THR ILE THR GLY SEQRES 7 L 112 ALA GLN ALA ASN ASP GLU ALA ASP TYR TYR CYS THR LEU SEQRES 8 L 112 TYR THR SER SER LEU ASN ASN ILE PHE GLY GLY GLY THR SEQRES 9 L 112 HIS LEU THR VAL LEU GLY GLN PRO SEQRES 1 M 127 GLU GLU LYS LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 M 127 PRO GLY GLY SER LEU ARG LEU GLY CYS VAL GLY SER GLY SEQRES 3 M 127 PHE THR PHE SER SER ALA TYR ILE ASN TRP VAL ARG GLN SEQRES 4 M 127 ALA PRO GLY LYS GLY LEU GLU TRP LEU ALA ALA ILE ARG SEQRES 5 M 127 THR SER GLY GLY GLY THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 M 127 GLY ARG PHE THR ILE SER ARG ASP ASP SER GLN ASN THR SEQRES 7 M 127 ALA TYR LEU GLN MET ASN SER LEU ARG THR GLU ASP THR SEQRES 8 M 127 ALA ARG TYR TYR CYS ALA ALA GLY ALA MET THR MET VAL SEQRES 9 M 127 VAL ALA SER PHE PHE GLN TYR TYR ALA MET ASP LEU TRP SEQRES 10 M 127 GLY PRO GLY VAL GLU VAL VAL VAL SER SER SEQRES 1 N 112 GLN THR VAL ILE GLN GLU PRO ALA MET SER VAL SER PRO SEQRES 2 N 112 GLY GLY THR VAL THR LEU THR CYS ALA PHE SER SER GLY SEQRES 3 N 112 SER VAL THR SER GLY ASP TYR PRO SER TRP PHE GLN GLN SEQRES 4 N 112 THR PRO GLY GLN PRO PRO ARG LEU LEU ILE TYR ARG THR SEQRES 5 N 112 ASN ASN ARG PRO THR GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 N 112 ALA ILE SER GLY ASN LYS ALA ALA LEU THR ILE THR GLY SEQRES 7 N 112 ALA GLN ALA ASN ASP GLU ALA ASP TYR TYR CYS THR LEU SEQRES 8 N 112 TYR THR SER SER LEU ASN ASN ILE PHE GLY GLY GLY THR SEQRES 9 N 112 HIS LEU THR VAL LEU GLY GLN PRO HELIX 1 AA1 SER A 65 GLY A 72 1 8 HELIX 2 AA2 ASP A 104 LEU A 112 1 9 HELIX 3 AA3 ASN A 187 HIS A 196 1 10 HELIX 4 AA4 LYS A 222 GLN A 226 5 5 HELIX 5 AA5 ASP B 37 LYS B 58 1 22 HELIX 6 AA6 GLU B 74 LYS B 127 1 54 HELIX 7 AA7 ASN B 145 GLY B 155 1 11 HELIX 8 AA8 ASP B 158 GLU B 171 1 14 HELIX 9 AA9 SER C 65 GLY C 72 1 8 HELIX 10 AB1 ASP C 104 LEU C 112 1 9 HELIX 11 AB2 ASN C 187 HIS C 196 1 10 HELIX 12 AB3 ASP D 37 LYS D 58 1 22 HELIX 13 AB4 ARG D 75 LYS D 127 1 53 HELIX 14 AB5 ASN D 145 GLY D 155 1 11 HELIX 15 AB6 ASP D 158 GLU D 171 1 14 HELIX 16 AB7 SER E 66 GLY E 73 1 8 HELIX 17 AB8 ASN E 74 GLU E 78 5 5 HELIX 18 AB9 ASP E 107 LEU E 115 1 9 HELIX 19 AC1 ASN E 193 HIS E 202 1 10 HELIX 20 AC2 ASP F 37 LYS F 58 1 22 HELIX 21 AC3 GLU F 74 LYS F 127 1 54 HELIX 22 AC4 ASN F 145 GLY F 155 1 11 HELIX 23 AC5 ASP F 158 GLU F 171 1 14 HELIX 24 AC6 THR H 28 ALA H 32 5 5 HELIX 25 AC7 ARG H 83 THR H 87 5 5 HELIX 26 AC8 THR I 28 ALA I 32 5 5 HELIX 27 AC9 ARG I 83 THR I 87 5 5 HELIX 28 AD1 THR J 28 TYR J 32 5 5 HELIX 29 AD2 THR L 28 TYR L 32 5 5 HELIX 30 AD3 THR M 28 ALA M 32 5 5 HELIX 31 AD4 ARG M 83 THR M 87 5 5 HELIX 32 AD5 THR N 28 TYR N 32 5 5 SHEET 1 AA1 5 ALA B 35 ALA B 36 0 SHEET 2 AA1 5 TYR B 22 GLN B 27 -1 N TYR B 24 O ALA B 35 SHEET 3 AA1 5 THR A 12 TYR A 17 -1 N THR A 12 O GLN B 27 SHEET 4 AA1 5 CYS B 137 PHE B 140 -1 O PHE B 138 N ILE A 13 SHEET 5 AA1 5 ALA B 130 GLU B 132 -1 N LYS B 131 O GLU B 139 SHEET 1 AA2 2 THR A 25 VAL A 26 0 SHEET 2 AA2 2 VAL A 34 THR A 35 -1 O VAL A 34 N VAL A 26 SHEET 1 AA3 2 SER A 39 ASN A 41 0 SHEET 2 AA3 2 ARG A 315 VAL A 317 -1 O MET A 316 N VAL A 40 SHEET 1 AA4 3 LEU A 43 GLU A 44 0 SHEET 2 AA4 3 PHE A 294 GLN A 295 1 O PHE A 294 N GLU A 44 SHEET 3 AA4 3 LYS A 307 TYR A 308 1 O LYS A 307 N GLN A 295 SHEET 1 AA5 2 LEU A 51 LEU A 53A 0 SHEET 2 AA5 2 MET A 274 ALA A 279 1 O ALA A 279 N LEU A 53 SHEET 1 AA6 3 LEU A 59 GLN A 60 0 SHEET 2 AA6 3 ILE A 87 GLU A 89 1 O VAL A 88 N LEU A 59 SHEET 3 AA6 3 ILE A 267 ASN A 269 1 O ILE A 268 N ILE A 87 SHEET 1 AA7 5 VAL A 115 GLU A 121A 0 SHEET 2 AA7 5 TYR A 256 ARG A 261 -1 O ALA A 257 N PHE A 121 SHEET 3 AA7 5 GLU A 175 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 4 AA7 5 LEU A 251 PRO A 254 -1 O ILE A 252 N GLY A 181 SHEET 5 AA7 5 LEU A 151 TRP A 153 -1 N LEU A 152 O ALA A 253 SHEET 1 AA8 4 VAL A 115 GLU A 121A 0 SHEET 2 AA8 4 TYR A 256 ARG A 261 -1 O ALA A 257 N PHE A 121 SHEET 3 AA8 4 GLU A 175 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 4 AA8 4 ARG A 229 LEU A 237 -1 O TYR A 233 N TRP A 180 SHEET 1 AA9 2 HIS A 130 THR A 131 0 SHEET 2 AA9 2 THR A 155 GLY A 156 -1 O THR A 155 N THR A 131 SHEET 1 AB1 2 SER A 136 HIS A 141 0 SHEET 2 AB1 2 GLU A 144 SER A 146 -1 O GLU A 144 N HIS A 141 SHEET 1 AB2 4 LEU A 164 ALA A 169 0 SHEET 2 AB2 4 THR A 242 ALA A 247 -1 O PHE A 245 N LYS A 166 SHEET 3 AB2 4 VAL A 202 VAL A 205 -1 N SER A 203 O GLU A 246 SHEET 4 AB2 4 SER A 210 PHE A 213 -1 O PHE A 213 N VAL A 202 SHEET 1 AB3 3 CYS A 281 GLN A 282 0 SHEET 2 AB3 3 ILE A 302 GLY A 303 -1 O ILE A 302 N GLN A 282 SHEET 3 AB3 3 THR B 64 ALA B 65 -1 O THR B 64 N GLY A 303 SHEET 1 AB4 5 SER D 32 ALA D 36 0 SHEET 2 AB4 5 TYR D 22 GLN D 27 -1 N TYR D 24 O ALA D 35 SHEET 3 AB4 5 THR C 12 TYR C 17 -1 N CYS C 14 O HIS D 25 SHEET 4 AB4 5 CYS D 137 PHE D 140 -1 O PHE D 138 N ILE C 13 SHEET 5 AB4 5 ALA D 130 GLU D 132 -1 N LYS D 131 O GLU D 139 SHEET 1 AB5 2 THR C 25 VAL C 26 0 SHEET 2 AB5 2 VAL C 34 THR C 35 -1 O VAL C 34 N VAL C 26 SHEET 1 AB6 2 SER C 39 ASN C 41 0 SHEET 2 AB6 2 ARG C 315 VAL C 317 -1 O MET C 316 N VAL C 40 SHEET 1 AB7 3 LEU C 43 GLU C 44 0 SHEET 2 AB7 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLU C 44 SHEET 3 AB7 3 LYS C 307 TYR C 308 1 O LYS C 307 N GLN C 295 SHEET 1 AB8 2 LEU C 51 LEU C 53A 0 SHEET 2 AB8 2 MET C 274 ALA C 279 1 O CYS C 277 N LEU C 53 SHEET 1 AB9 3 LEU C 59 GLN C 60 0 SHEET 2 AB9 3 ILE C 87 GLU C 89 1 O VAL C 88 N LEU C 59 SHEET 3 AB9 3 ILE C 267 ASN C 269 1 O ILE C 268 N ILE C 87 SHEET 1 AC1 5 VAL C 115 GLU C 121A 0 SHEET 2 AC1 5 TYR C 256 ARG C 261 -1 O ALA C 257 N PHE C 121 SHEET 3 AC1 5 GLU C 175 HIS C 184 -1 N GLU C 175 O LEU C 260 SHEET 4 AC1 5 LEU C 251 PRO C 254 -1 O ILE C 252 N GLY C 181 SHEET 5 AC1 5 LEU C 151 TRP C 153 -1 N LEU C 152 O ALA C 253 SHEET 1 AC2 4 VAL C 115 GLU C 121A 0 SHEET 2 AC2 4 TYR C 256 ARG C 261 -1 O ALA C 257 N PHE C 121 SHEET 3 AC2 4 GLU C 175 HIS C 184 -1 N GLU C 175 O LEU C 260 SHEET 4 AC2 4 ARG C 229 LEU C 237 -1 O LEU C 237 N VAL C 176 SHEET 1 AC3 2 HIS C 130 THR C 131 0 SHEET 2 AC3 2 THR C 155 GLY C 156 -1 O THR C 155 N THR C 131 SHEET 1 AC4 2 SER C 136 HIS C 141 0 SHEET 2 AC4 2 GLU C 144 SER C 146 -1 O GLU C 144 N HIS C 141 SHEET 1 AC5 4 LEU C 164 ALA C 169 0 SHEET 2 AC5 4 THR C 242 ALA C 247 -1 O PHE C 245 N LYS C 166 SHEET 3 AC5 4 VAL C 202 VAL C 205 -1 N VAL C 205 O ILE C 244 SHEET 4 AC5 4 SER C 210 PHE C 213 -1 O ARG C 211 N VAL C 204 SHEET 1 AC6 3 CYS C 281 GLN C 282 0 SHEET 2 AC6 3 ILE C 302 GLY C 303 -1 O ILE C 302 N GLN C 282 SHEET 3 AC6 3 THR D 64 ALA D 65 -1 O THR D 64 N GLY C 303 SHEET 1 AC7 3 GLY F 31 SER F 32 0 SHEET 2 AC7 3 TYR F 22 ASN F 28 -1 N ASN F 28 O GLY F 31 SHEET 3 AC7 3 ALA F 35 ALA F 36 -1 O ALA F 35 N TYR F 24 SHEET 1 AC8 5 GLY F 31 SER F 32 0 SHEET 2 AC8 5 TYR F 22 ASN F 28 -1 N ASN F 28 O GLY F 31 SHEET 3 AC8 5 THR E 12 TYR E 17 -1 N CYS E 14 O HIS F 25 SHEET 4 AC8 5 CYS F 137 PHE F 140 -1 O PHE F 138 N ILE E 13 SHEET 5 AC8 5 ALA F 130 GLU F 132 -1 N LYS F 131 O GLU F 139 SHEET 1 AC9 2 THR E 25 VAL E 26 0 SHEET 2 AC9 2 VAL E 34 THR E 35 -1 O VAL E 34 N VAL E 26 SHEET 1 AD1 2 SER E 39 ASN E 41 0 SHEET 2 AD1 2 ARG E 322 VAL E 324 -1 O MET E 323 N VAL E 40 SHEET 1 AD2 3 LEU E 43 GLU E 44 0 SHEET 2 AD2 3 PHE E 301 GLN E 302 1 O PHE E 301 N GLU E 44 SHEET 3 AD2 3 LYS E 314 TYR E 315 1 O LYS E 314 N GLN E 302 SHEET 1 AD3 2 LEU E 51 LEU E 54 0 SHEET 2 AD3 2 MET E 281 ALA E 286 1 O ASP E 282 N LEU E 51 SHEET 1 AD4 3 LEU E 60 GLN E 61 0 SHEET 2 AD4 3 ILE E 89 GLU E 91 1 O VAL E 90 N LEU E 60 SHEET 3 AD4 3 ILE E 274 ASN E 276 1 O ILE E 275 N GLU E 91 SHEET 1 AD5 4 VAL E 118 GLU E 125 0 SHEET 2 AD5 4 TYR E 262 ARG E 268 -1 O ALA E 263 N PHE E 124 SHEET 3 AD5 4 GLU E 181 HIS E 190 -1 N GLU E 181 O LEU E 266 SHEET 4 AD5 4 ARG E 235 LEU E 243 -1 O ARG E 235 N HIS E 190 SHEET 1 AD6 2 HIS E 136 THR E 137 0 SHEET 2 AD6 2 THR E 161 GLY E 162 -1 O THR E 161 N THR E 137 SHEET 1 AD7 2 SER E 142 HIS E 147 0 SHEET 2 AD7 2 GLU E 150 SER E 152 -1 O GLU E 150 N HIS E 147 SHEET 1 AD8 2 LEU E 157 TRP E 159 0 SHEET 2 AD8 2 ILE E 258 PRO E 260 -1 O ALA E 259 N LEU E 158 SHEET 1 AD9 4 LEU E 170 ALA E 175 0 SHEET 2 AD9 4 THR E 248 ALA E 253 -1 O PHE E 251 N LYS E 172 SHEET 3 AD9 4 VAL E 208 VAL E 211 -1 N SER E 209 O GLU E 252 SHEET 4 AD9 4 SER E 216 PHE E 219 -1 O ARG E 217 N VAL E 210 SHEET 1 AE1 3 ALA E 294 ILE E 295 0 SHEET 2 AE1 3 CYS E 288 GLN E 289 -1 N CYS E 288 O ILE E 295 SHEET 3 AE1 3 ILE E 309 GLY E 310 -1 O ILE E 309 N GLN E 289 SHEET 1 AE2 4 LYS H 3 SER H 7 0 SHEET 2 AE2 4 SER H 17 SER H 25 -1 O GLY H 21 N SER H 7 SHEET 3 AE2 4 THR H 77 ASN H 82A-1 O LEU H 80 N LEU H 20 SHEET 4 AE2 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AE3 6 GLY H 10 LEU H 11 0 SHEET 2 AE3 6 VAL H 107 VAL H 110 1 O VAL H 110 N GLY H 10 SHEET 3 AE3 6 ALA H 88 ALA H 94 -1 N TYR H 90 O VAL H 107 SHEET 4 AE3 6 ILE H 34 GLN H 39 -1 N ASN H 35 O ALA H 93 SHEET 5 AE3 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AE3 6 THR H 57 TYR H 59 -1 O TYR H 58 N ALA H 50 SHEET 1 AE4 4 GLY H 10 LEU H 11 0 SHEET 2 AE4 4 VAL H 107 VAL H 110 1 O VAL H 110 N GLY H 10 SHEET 3 AE4 4 ALA H 88 ALA H 94 -1 N TYR H 90 O VAL H 107 SHEET 4 AE4 4 LEU H 102 TRP H 103 -1 O LEU H 102 N ALA H 94 SHEET 1 AE5 4 LYS I 3 SER I 7 0 SHEET 2 AE5 4 SER I 17 SER I 25 -1 O GLY I 21 N SER I 7 SHEET 3 AE5 4 THR I 77 ASN I 82A-1 O LEU I 80 N LEU I 20 SHEET 4 AE5 4 PHE I 67 ASP I 72 -1 N ASP I 72 O THR I 77 SHEET 1 AE6 6 GLY I 10 VAL I 12 0 SHEET 2 AE6 6 VAL I 107 VAL I 111 1 O VAL I 110 N GLY I 10 SHEET 3 AE6 6 ALA I 88 ALA I 94 -1 N TYR I 90 O VAL I 107 SHEET 4 AE6 6 ILE I 34 GLN I 39 -1 N VAL I 37 O TYR I 91 SHEET 5 AE6 6 LEU I 45 ILE I 51 -1 O GLU I 46 N ARG I 38 SHEET 6 AE6 6 THR I 57 TYR I 59 -1 O TYR I 58 N ALA I 50 SHEET 1 AE7 4 GLY I 10 VAL I 12 0 SHEET 2 AE7 4 VAL I 107 VAL I 111 1 O VAL I 110 N GLY I 10 SHEET 3 AE7 4 ALA I 88 ALA I 94 -1 N TYR I 90 O VAL I 107 SHEET 4 AE7 4 LEU I 102 TRP I 103 -1 O LEU I 102 N ALA I 94 SHEET 1 AE8 4 VAL J 3 GLN J 5 0 SHEET 2 AE8 4 LEU J 21 PHE J 25 -1 O ALA J 24 N ILE J 4 SHEET 3 AE8 4 LYS J 70 ILE J 75 -1 O ALA J 71 N CYS J 23 SHEET 4 AE8 4 PHE J 62 SER J 67 -1 N SER J 67 O LYS J 70 SHEET 1 AE9 5 ALA J 8 SER J 12 0 SHEET 2 AE9 5 THR J 102 THR J 105 1 O HIS J 103 N MET J 11 SHEET 3 AE9 5 ASP J 85 TYR J 91 -1 N TYR J 86 O THR J 102 SHEET 4 AE9 5 SER J 34 GLN J 38 -1 N GLN J 38 O ASP J 85 SHEET 5 AE9 5 ARG J 45 ILE J 48 -1 O ARG J 45 N GLN J 37 SHEET 1 AF1 4 ALA J 8 SER J 12 0 SHEET 2 AF1 4 THR J 102 THR J 105 1 O HIS J 103 N MET J 11 SHEET 3 AF1 4 ASP J 85 TYR J 91 -1 N TYR J 86 O THR J 102 SHEET 4 AF1 4 ASN J 96 PHE J 98 -1 O ILE J 97 N LEU J 90 SHEET 1 AF2 4 VAL L 3 GLN L 5 0 SHEET 2 AF2 4 LEU L 21 PHE L 25 -1 O ALA L 24 N ILE L 4 SHEET 3 AF2 4 LYS L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AF2 4 PHE L 62 SER L 67 -1 N ALA L 65 O ALA L 72 SHEET 1 AF3 5 ALA L 8 SER L 12 0 SHEET 2 AF3 5 THR L 102 THR L 105 1 O HIS L 103 N MET L 11 SHEET 3 AF3 5 ASP L 85 TYR L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AF3 5 SER L 34 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AF3 5 ARG L 45 LEU L 46 -1 O ARG L 45 N GLN L 37 SHEET 1 AF4 4 ALA L 8 SER L 12 0 SHEET 2 AF4 4 THR L 102 THR L 105 1 O HIS L 103 N MET L 11 SHEET 3 AF4 4 ASP L 85 TYR L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AF4 4 ASN L 96 PHE L 98 -1 O ILE L 97 N LEU L 90 SHEET 1 AF5 4 LYS M 3 GLU M 6 0 SHEET 2 AF5 4 SER M 17 SER M 25 -1 O VAL M 23 N VAL M 5 SHEET 3 AF5 4 THR M 77 ASN M 82A-1 O LEU M 80 N LEU M 20 SHEET 4 AF5 4 PHE M 67 ASP M 72 -1 N ASP M 72 O THR M 77 SHEET 1 AF6 6 GLY M 10 VAL M 12 0 SHEET 2 AF6 6 VAL M 107 VAL M 111 1 O VAL M 110 N GLY M 10 SHEET 3 AF6 6 ALA M 88 ALA M 94 -1 N TYR M 90 O VAL M 107 SHEET 4 AF6 6 ILE M 34 GLN M 39 -1 N VAL M 37 O TYR M 91 SHEET 5 AF6 6 LEU M 45 ILE M 51 -1 O GLU M 46 N ARG M 38 SHEET 6 AF6 6 THR M 57 TYR M 59 -1 O TYR M 58 N ALA M 50 SHEET 1 AF7 4 GLY M 10 VAL M 12 0 SHEET 2 AF7 4 VAL M 107 VAL M 111 1 O VAL M 110 N GLY M 10 SHEET 3 AF7 4 ALA M 88 ALA M 94 -1 N TYR M 90 O VAL M 107 SHEET 4 AF7 4 LEU M 102 TRP M 103 -1 O LEU M 102 N ALA M 94 SHEET 1 AF8 4 VAL N 3 GLN N 5 0 SHEET 2 AF8 4 LEU N 21 PHE N 25 -1 O ALA N 24 N ILE N 4 SHEET 3 AF8 4 LYS N 70 ILE N 75 -1 O ALA N 71 N CYS N 23 SHEET 4 AF8 4 PHE N 62 SER N 67 -1 N ALA N 65 O ALA N 72 SHEET 1 AF9 5 ALA N 8 SER N 12 0 SHEET 2 AF9 5 THR N 102 THR N 105 1 O HIS N 103 N MET N 11 SHEET 3 AF9 5 ASP N 85 TYR N 91 -1 N TYR N 86 O THR N 102 SHEET 4 AF9 5 SER N 34 GLN N 38 -1 N GLN N 38 O ASP N 85 SHEET 5 AF9 5 ARG N 45 ILE N 48 -1 O ARG N 45 N GLN N 37 SHEET 1 AG1 4 ALA N 8 SER N 12 0 SHEET 2 AG1 4 THR N 102 THR N 105 1 O HIS N 103 N MET N 11 SHEET 3 AG1 4 ASP N 85 TYR N 91 -1 N TYR N 86 O THR N 102 SHEET 4 AG1 4 ASN N 96 PHE N 98 -1 O ILE N 97 N LEU N 90 SSBOND 1 CYS A 14 CYS B 137 1555 1555 2.03 SSBOND 2 CYS A 52 CYS A 277 1555 1555 2.03 SSBOND 3 CYS A 64 CYS A 76 1555 1555 2.03 SSBOND 4 CYS A 97 CYS A 139 1555 1555 2.03 SSBOND 5 CYS A 281 CYS A 305 1555 1555 2.02 SSBOND 6 CYS B 144 CYS B 148 1555 1555 2.04 SSBOND 7 CYS C 14 CYS D 137 1555 1555 2.03 SSBOND 8 CYS C 52 CYS C 277 1555 1555 2.03 SSBOND 9 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 10 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 11 CYS C 281 CYS C 305 1555 1555 2.02 SSBOND 12 CYS D 144 CYS D 148 1555 1555 2.04 SSBOND 13 CYS E 14 CYS F 137 1555 1555 2.03 SSBOND 14 CYS E 52 CYS E 284 1555 1555 2.03 SSBOND 15 CYS E 65 CYS E 77 1555 1555 2.03 SSBOND 16 CYS E 100 CYS E 145 1555 1555 2.03 SSBOND 17 CYS E 288 CYS E 312 1555 1555 2.02 SSBOND 18 CYS F 144 CYS F 148 1555 1555 2.06 SSBOND 19 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 20 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 21 CYS J 23 CYS J 88 1555 1555 2.03 SSBOND 22 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 23 CYS M 22 CYS M 92 1555 1555 2.03 SSBOND 24 CYS N 23 CYS N 88 1555 1555 2.03 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