HEADER VIRAL PROTEIN 08-SEP-20 7K22 TITLE MURINE POLYOMAVIRUS PENTAVALENT CAPSOMER WITH 8A7H5 FAB, SUBPARTICLE TITLE 2 RECONSTRUCTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: 8A7H5 FAB LIGHT CHAIN; COMPND 3 CHAIN: L1, L2, L3, L4, L5; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: 8A7H5 FAB HEAVY CHAIN; COMPND 6 CHAIN: H1, H2, H3, H4, H5; COMPND 7 MOL_ID: 3; COMPND 8 MOLECULE: CAPSID PROTEIN VP1; COMPND 9 CHAIN: F1, F2, F3, F4, F5; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 7 ORGANISM_COMMON: NORWAY RAT; SOURCE 8 ORGANISM_TAXID: 10116; SOURCE 9 MOL_ID: 3; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS POLYOMAVIRUS 1; SOURCE 11 ORGANISM_COMMON: MPYV; SOURCE 12 ORGANISM_TAXID: 1891730; SOURCE 13 EXPRESSION_SYSTEM: MUS MUSCULOIDES; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 60742 KEYWDS POLYOMAVIRUS, CAPSOMER, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR D.J.GOETSCHIUS,S.L.HAFENSTEIN JRNL AUTH M.D.LAUVER,D.J.GOETSCHIUS,C.S.NETHERBY-WINSLOW,K.N.AYERS, JRNL AUTH 2 G.JIN,D.G.HAAS,E.L.FROST,S.H.CHO,C.BATOR,S.M.BYWATERS, JRNL AUTH 3 N.D.CHRISTENSEN,S.L.HAFENSTEIN,A.E.LUKACHER JRNL TITL ANTIBODY ESCAPE BY POLYOMAVIRUS CAPSID MUTATION FACILITATES JRNL TITL 2 NEUROVIRULENCE. JRNL REF ELIFE V. 9 2020 JRNL REFN ESSN 2050-084X JRNL PMID 32940605 JRNL DOI 10.7554/ELIFE.61056 REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : RELION 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) : 3.200 REMARK 3 NUMBER OF PARTICLES : 109752 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 7K22 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_1000250840. 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 : 8A7H5 FAB LIGHT CHAIN, 8A7H5 REMARK 245 FAB HEAVY CHAIN, CAPSID PROTEIN REMARK 245 VP1; 8A7H5 FAB LIGHT CHAIN, REMARK 245 8A7H5 FAB HEAVY CHAIN; CAPSID REMARK 245 PROTEIN VP1 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.80 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.90 REMARK 245 SAMPLE DETAILS : FAB FRAGMENT GENERATED FROM RAT REMARK 245 IGG 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON III (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL 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) : 45.00 REMARK 245 ILLUMINATION MODE : OTHER 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: PENTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L1, H1, F1, L2, H2, F2, L3, REMARK 350 AND CHAINS: H3, F3, L4, H4, F4, L5, H5, REMARK 350 AND CHAINS: F5 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 GLY L 99 REMARK 465 SER L 100 REMARK 465 GLY L 101 REMARK 465 THR L 102 REMARK 465 LYS L 103 REMARK 465 LEU L 104 REMARK 465 GLU L 105 REMARK 465 THR L 106 REMARK 465 THR L 107 REMARK 465 ARG L 108 REMARK 465 ALA L 109 REMARK 465 GLU H 1 REMARK 465 GLU H 2 REMARK 465 SER H 3 REMARK 465 GLY H 4 REMARK 465 GLY H 5 REMARK 465 GLY H 6 REMARK 465 LEU H 7 REMARK 465 VAL H 8 REMARK 465 GLN H 9 REMARK 465 PRO H 10 REMARK 465 GLY H 11 REMARK 465 LYS H 12 REMARK 465 SER H 13 REMARK 465 LEU H 113 REMARK 465 VAL H 114 REMARK 465 THR H 115 REMARK 465 VAL H 116 REMARK 465 SER H 117 REMARK 465 ALA F 1 REMARK 465 PRO F 2 REMARK 465 LYS F 3 REMARK 465 ARG F 4 REMARK 465 LYS F 5 REMARK 465 SER F 6 REMARK 465 GLY F 7 REMARK 465 VAL F 8 REMARK 465 SER F 9 REMARK 465 LYS F 10 REMARK 465 CYS F 11 REMARK 465 GLU F 12 REMARK 465 THR F 13 REMARK 465 LYS F 14 REMARK 465 CYS F 15 REMARK 465 THR F 16 REMARK 465 LYS F 17 REMARK 465 ASP F 371 REMARK 465 ARG F 372 REMARK 465 PHE F 373 REMARK 465 GLY F 374 REMARK 465 LYS F 375 REMARK 465 THR F 376 REMARK 465 LYS F 377 REMARK 465 THR F 378 REMARK 465 VAL F 379 REMARK 465 PHE F 380 REMARK 465 PRO F 381 REMARK 465 GLY F 382 REMARK 465 ASN F 383 REMARK 465 GLY L 99 REMARK 465 SER L 100 REMARK 465 GLY L 101 REMARK 465 THR L 102 REMARK 465 LYS L 103 REMARK 465 LEU L 104 REMARK 465 GLU L 105 REMARK 465 THR L 106 REMARK 465 THR L 107 REMARK 465 ARG L 108 REMARK 465 ALA L 109 REMARK 465 GLU H 1 REMARK 465 GLU H 2 REMARK 465 SER H 3 REMARK 465 GLY H 4 REMARK 465 GLY H 5 REMARK 465 GLY H 6 REMARK 465 LEU H 7 REMARK 465 VAL H 8 REMARK 465 GLN H 9 REMARK 465 PRO H 10 REMARK 465 GLY H 11 REMARK 465 LYS H 12 REMARK 465 SER H 13 REMARK 465 LEU H 113 REMARK 465 VAL H 114 REMARK 465 THR H 115 REMARK 465 VAL H 116 REMARK 465 SER H 117 REMARK 465 ALA F 1 REMARK 465 PRO F 2 REMARK 465 LYS F 3 REMARK 465 ARG F 4 REMARK 465 LYS F 5 REMARK 465 SER F 6 REMARK 465 GLY F 7 REMARK 465 VAL F 8 REMARK 465 SER F 9 REMARK 465 LYS F 10 REMARK 465 CYS F 11 REMARK 465 GLU F 12 REMARK 465 THR F 13 REMARK 465 LYS F 14 REMARK 465 CYS F 15 REMARK 465 THR F 16 REMARK 465 LYS F 17 REMARK 465 ASP F 371 REMARK 465 ARG F 372 REMARK 465 PHE F 373 REMARK 465 GLY F 374 REMARK 465 LYS F 375 REMARK 465 THR F 376 REMARK 465 LYS F 377 REMARK 465 THR F 378 REMARK 465 VAL F 379 REMARK 465 PHE F 380 REMARK 465 PRO F 381 REMARK 465 GLY F 382 REMARK 465 ASN F 383 REMARK 465 GLY L 99 REMARK 465 SER L 100 REMARK 465 GLY L 101 REMARK 465 THR L 102 REMARK 465 LYS L 103 REMARK 465 LEU L 104 REMARK 465 GLU L 105 REMARK 465 THR L 106 REMARK 465 THR L 107 REMARK 465 ARG L 108 REMARK 465 ALA L 109 REMARK 465 GLU H 1 REMARK 465 GLU H 2 REMARK 465 SER H 3 REMARK 465 GLY H 4 REMARK 465 GLY H 5 REMARK 465 GLY H 6 REMARK 465 LEU H 7 REMARK 465 VAL H 8 REMARK 465 GLN H 9 REMARK 465 PRO H 10 REMARK 465 GLY H 11 REMARK 465 LYS H 12 REMARK 465 SER H 13 REMARK 465 LEU H 113 REMARK 465 VAL H 114 REMARK 465 THR H 115 REMARK 465 VAL H 116 REMARK 465 SER H 117 REMARK 465 ALA F 1 REMARK 465 PRO F 2 REMARK 465 LYS F 3 REMARK 465 ARG F 4 REMARK 465 LYS F 5 REMARK 465 SER F 6 REMARK 465 GLY F 7 REMARK 465 VAL F 8 REMARK 465 SER F 9 REMARK 465 LYS F 10 REMARK 465 CYS F 11 REMARK 465 GLU F 12 REMARK 465 THR F 13 REMARK 465 LYS F 14 REMARK 465 CYS F 15 REMARK 465 THR F 16 REMARK 465 LYS F 17 REMARK 465 ASP F 371 REMARK 465 ARG F 372 REMARK 465 PHE F 373 REMARK 465 GLY F 374 REMARK 465 LYS F 375 REMARK 465 THR F 376 REMARK 465 LYS F 377 REMARK 465 THR F 378 REMARK 465 VAL F 379 REMARK 465 PHE F 380 REMARK 465 PRO F 381 REMARK 465 GLY F 382 REMARK 465 ASN F 383 REMARK 465 GLY L 99 REMARK 465 SER L 100 REMARK 465 GLY L 101 REMARK 465 THR L 102 REMARK 465 LYS L 103 REMARK 465 LEU L 104 REMARK 465 GLU L 105 REMARK 465 THR L 106 REMARK 465 THR L 107 REMARK 465 ARG L 108 REMARK 465 ALA L 109 REMARK 465 GLU H 1 REMARK 465 GLU H 2 REMARK 465 SER H 3 REMARK 465 GLY H 4 REMARK 465 GLY H 5 REMARK 465 GLY H 6 REMARK 465 LEU H 7 REMARK 465 VAL H 8 REMARK 465 GLN H 9 REMARK 465 PRO H 10 REMARK 465 GLY H 11 REMARK 465 LYS H 12 REMARK 465 SER H 13 REMARK 465 LEU H 113 REMARK 465 VAL H 114 REMARK 465 THR H 115 REMARK 465 VAL H 116 REMARK 465 SER H 117 REMARK 465 ALA F 1 REMARK 465 PRO F 2 REMARK 465 LYS F 3 REMARK 465 ARG F 4 REMARK 465 LYS F 5 REMARK 465 SER F 6 REMARK 465 GLY F 7 REMARK 465 VAL F 8 REMARK 465 SER F 9 REMARK 465 LYS F 10 REMARK 465 CYS F 11 REMARK 465 GLU F 12 REMARK 465 THR F 13 REMARK 465 LYS F 14 REMARK 465 CYS F 15 REMARK 465 THR F 16 REMARK 465 LYS F 17 REMARK 465 ASP F 371 REMARK 465 ARG F 372 REMARK 465 PHE F 373 REMARK 465 GLY F 374 REMARK 465 LYS F 375 REMARK 465 THR F 376 REMARK 465 LYS F 377 REMARK 465 THR F 378 REMARK 465 VAL F 379 REMARK 465 PHE F 380 REMARK 465 PRO F 381 REMARK 465 GLY F 382 REMARK 465 ASN F 383 REMARK 465 GLY L 99 REMARK 465 SER L 100 REMARK 465 GLY L 101 REMARK 465 THR L 102 REMARK 465 LYS L 103 REMARK 465 LEU L 104 REMARK 465 GLU L 105 REMARK 465 THR L 106 REMARK 465 THR L 107 REMARK 465 ARG L 108 REMARK 465 ALA L 109 REMARK 465 GLU H 1 REMARK 465 GLU H 2 REMARK 465 SER H 3 REMARK 465 GLY H 4 REMARK 465 GLY H 5 REMARK 465 GLY H 6 REMARK 465 LEU H 7 REMARK 465 VAL H 8 REMARK 465 GLN H 9 REMARK 465 PRO H 10 REMARK 465 GLY H 11 REMARK 465 LYS H 12 REMARK 465 SER H 13 REMARK 465 LEU H 113 REMARK 465 VAL H 114 REMARK 465 THR H 115 REMARK 465 VAL H 116 REMARK 465 SER H 117 REMARK 465 ALA F 1 REMARK 465 PRO F 2 REMARK 465 LYS F 3 REMARK 465 ARG F 4 REMARK 465 LYS F 5 REMARK 465 SER F 6 REMARK 465 GLY F 7 REMARK 465 VAL F 8 REMARK 465 SER F 9 REMARK 465 LYS F 10 REMARK 465 CYS F 11 REMARK 465 GLU F 12 REMARK 465 THR F 13 REMARK 465 LYS F 14 REMARK 465 CYS F 15 REMARK 465 THR F 16 REMARK 465 LYS F 17 REMARK 465 ASP F 371 REMARK 465 ARG F 372 REMARK 465 PHE F 373 REMARK 465 GLY F 374 REMARK 465 LYS F 375 REMARK 465 THR F 376 REMARK 465 LYS F 377 REMARK 465 THR F 378 REMARK 465 VAL F 379 REMARK 465 PHE F 380 REMARK 465 PRO F 381 REMARK 465 GLY F 382 REMARK 465 ASN F 383 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 SERH5 48 OD1 ASPH5 52 2.09 REMARK 500 OG SERH2 48 OD1 ASPH2 52 2.09 REMARK 500 OG SERH1 48 OD1 ASPH1 52 2.09 REMARK 500 OG SERH4 48 OD1 ASPH4 52 2.09 REMARK 500 OG SERH3 48 OD1 ASPH3 52 2.09 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 SERL1 31 18.34 -142.65 REMARK 500 ALAL1 51 -0.03 67.74 REMARK 500 VALH1 44 -62.13 -121.18 REMARK 500 ALAH1 70 -4.03 69.19 REMARK 500 SERH1 80 -3.16 64.85 REMARK 500 ALAH1 87 -178.81 -172.65 REMARK 500 LEUF1 66 46.20 -87.17 REMARK 500 GLNF1 71 70.58 59.23 REMARK 500 TYRF1 72 10.40 -68.75 REMARK 500 GLUF1 91 78.84 59.12 REMARK 500 ASNF1 92 -36.58 -31.37 REMARK 500 THRF1 179 -163.32 -77.38 REMARK 500 ASPF1 180 126.24 -35.04 REMARK 500 VALF1 207 -68.01 -122.27 REMARK 500 LEUF1 208 116.91 -166.55 REMARK 500 PROF1 210 2.92 -65.21 REMARK 500 LEUF1 216 42.09 -104.43 REMARK 500 ASPF1 295 37.68 -96.95 REMARK 500 SERF1 323 -8.55 -56.50 REMARK 500 ARGF1 368 123.97 -38.87 REMARK 500 SERL2 31 18.33 -142.64 REMARK 500 ALAL2 51 -0.06 67.70 REMARK 500 VALH2 44 -62.07 -121.14 REMARK 500 ALAH2 70 -4.00 69.08 REMARK 500 SERH2 80 -3.08 64.77 REMARK 500 ALAH2 87 -178.77 -172.68 REMARK 500 LEUF2 66 46.20 -87.14 REMARK 500 GLNF2 71 70.66 59.18 REMARK 500 TYRF2 72 10.44 -68.81 REMARK 500 GLUF2 91 78.89 59.07 REMARK 500 ASNF2 92 -36.50 -31.47 REMARK 500 THRF2 179 -163.32 -77.31 REMARK 500 ASPF2 180 126.22 -35.12 REMARK 500 VALF2 207 -68.00 -122.24 REMARK 500 LEUF2 208 116.89 -166.56 REMARK 500 PROF2 210 2.89 -65.24 REMARK 500 LEUF2 216 42.08 -104.47 REMARK 500 ASPF2 295 37.70 -96.88 REMARK 500 SERF2 323 -8.59 -56.44 REMARK 500 ARGF2 368 124.06 -38.95 REMARK 500 SERL3 31 18.32 -142.63 REMARK 500 ALAL3 51 -0.02 67.66 REMARK 500 VALH3 44 -62.19 -121.07 REMARK 500 ALAH3 70 -3.98 69.10 REMARK 500 SERH3 80 -3.08 64.76 REMARK 500 ALAH3 87 -178.79 -172.70 REMARK 500 LEUF3 66 46.19 -87.16 REMARK 500 GLNF3 71 70.63 59.21 REMARK 500 TYRF3 72 10.45 -68.80 REMARK 500 GLUF3 91 78.84 59.14 REMARK 500 REMARK 500 THIS ENTRY HAS 100 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-22640 RELATED DB: EMDB REMARK 900 MURINE POLYOMAVIRUS PENTAVALENT CAPSOMER WITH 8A7H5 FAB, REMARK 900 SUBPARTICLE RECONSTRUCTION DBREF 7K22L1 1 109 PDB 7K22 7K22 1 109 DBREF 7K22H1 1 117 PDB 7K22 7K22 1 117 DBREF1 7K22F1 1 383 UNP A0A247D727_POVM1 DBREF2 7K22F1 A0A247D727 2 384 DBREF 7K22L2 1 109 PDB 7K22 7K22 1 109 DBREF 7K22H2 1 117 PDB 7K22 7K22 1 117 DBREF1 7K22F2 1 383 UNP A0A247D727_POVM1 DBREF2 7K22F2 A0A247D727 2 384 DBREF 7K22L3 1 109 PDB 7K22 7K22 1 109 DBREF 7K22H3 1 117 PDB 7K22 7K22 1 117 DBREF1 7K22F3 1 383 UNP A0A247D727_POVM1 DBREF2 7K22F3 A0A247D727 2 384 DBREF 7K22L4 1 109 PDB 7K22 7K22 1 109 DBREF 7K22H4 1 117 PDB 7K22 7K22 1 117 DBREF1 7K22F4 1 383 UNP A0A247D727_POVM1 DBREF2 7K22F4 A0A247D727 2 384 DBREF 7K22L5 1 109 PDB 7K22 7K22 1 109 DBREF 7K22H5 1 117 PDB 7K22 7K22 1 117 DBREF1 7K22F5 1 383 UNP A0A247D727_POVM1 DBREF2 7K22F5 A0A247D727 2 384 SEQRES 1L1 109 ASP ILE VAL MET THR GLN SER PRO THR SER MET SER ILE SEQRES 2L1 109 SER VAL GLY ASP ARG VAL THR MET ASN CYS ARG ALA SER SEQRES 3L1 109 GLN ASN VAL TYR SER ASN VAL ASP TRP TYR GLN GLN LYS SEQRES 4L1 109 THR GLY GLN SER PRO LYS LEU VAL ILE TYR LYS ALA SER SEQRES 5L1 109 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6L1 109 GLY SER GLY THR TYR PHE THR LEU THR ILE THR ASN ILE SEQRES 7L1 109 GLN THR GLU ASP LEU ALA VAL TYR TYR CYS LEU GLN SER SEQRES 8L1 109 ASN ALA PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9L1 109 GLU THR THR ARG ALA SEQRES 1H1 117 GLU GLU SER GLY GLY GLY LEU VAL GLN PRO GLY LYS SER SEQRES 2H1 117 LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SER SEQRES 3H1 117 SER TYR GLY MET HIS TRP ILE ARG GLN VAL PRO GLY LYS SEQRES 4H1 117 GLY LEU ASP TRP VAL ALA TYR ILE SER SER ALA SER ASP SEQRES 5H1 117 THR PHE TYR ALA ASP ALA VAL LYS GLU ARG PHE THR ILE SEQRES 6H1 117 SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU ARG LEU SEQRES 7H1 117 ASN SER LEU LYS SER GLU ASP THR ALA ILE TYR TYR CYS SEQRES 8H1 117 ALA ARG THR ARG TYR PRO THR ASP HIS PHE TYR ASP TRP SEQRES 9H1 117 PHE PRO TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1F1 383 ALA PRO LYS ARG LYS SER GLY VAL SER LYS CYS GLU THR SEQRES 2F1 383 LYS CYS THR LYS ALA CYS PRO ARG PRO ALA PRO VAL PRO SEQRES 3F1 383 LYS LEU LEU ILE LYS GLY GLY MET GLU VAL LEU ASP LEU SEQRES 4F1 383 VAL THR GLY PRO ASP SER VAL THR GLU ILE GLU ALA PHE SEQRES 5F1 383 LEU ASN PRO ARG MET GLY GLN PRO PRO THR PRO GLU SER SEQRES 6F1 383 LEU THR GLU GLY GLY GLN TYR TYR GLY TRP SER ARG GLY SEQRES 7F1 383 ILE ASN LEU ALA THR SER ASP THR GLU ASP SER PRO GLU SEQRES 8F1 383 ASN ASN THR LEU PRO THR TRP SER MET ALA LYS LEU GLN SEQRES 9F1 383 LEU PRO MET LEU ASN GLU ASP LEU THR CYS ASP THR LEU SEQRES 10F1 383 GLN MET TRP GLU ALA VAL SER VAL LYS THR GLU VAL VAL SEQRES 11F1 383 GLY SER GLY SER LEU LEU ASP VAL HIS GLY PHE ASN LYS SEQRES 12F1 383 PRO THR ASP THR VAL ASN THR LYS GLY ILE SER THR PRO SEQRES 13F1 383 VAL GLU GLY SER GLN TYR HIS VAL PHE ALA VAL GLY GLY SEQRES 14F1 383 GLU PRO LEU ASP LEU GLN GLY LEU VAL THR ASP ALA ARG SEQRES 15F1 383 THR LYS TYR LYS GLU GLU GLY VAL VAL THR ILE LYS THR SEQRES 16F1 383 ILE THR LYS LYS ASP MET VAL ASN LYS ASP GLN VAL LEU SEQRES 17F1 383 ASN PRO ILE SER LYS ALA LYS LEU ASP LYS ASP GLY MET SEQRES 18F1 383 TYR PRO VAL GLU ILE TRP HIS PRO ASP PRO ALA LYS ASN SEQRES 19F1 383 GLU ASN THR ARG TYR PHE GLY ASN TYR THR GLY GLY THR SEQRES 20F1 383 THR THR PRO PRO VAL LEU GLN PHE THR ASN THR LEU THR SEQRES 21F1 383 THR VAL LEU LEU ASP GLU ASN GLY VAL GLY PRO LEU CYS SEQRES 22F1 383 LYS GLY GLU GLY LEU TYR LEU SER CYS VAL ASP ILE MET SEQRES 23F1 383 GLY TRP ARG VAL THR ARG ASN TYR ASP VAL HIS HIS TRP SEQRES 24F1 383 ARG GLY LEU PRO ARG TYR PHE LYS ILE THR LEU ARG LYS SEQRES 25F1 383 ARG TRP VAL LYS ASN PRO TYR PRO MET ALA SER LEU ILE SEQRES 26F1 383 SER SER LEU PHE ASN ASN MET LEU PRO GLN VAL GLN GLY SEQRES 27F1 383 GLN PRO MET GLU GLY GLU ASN THR GLN VAL GLU GLU VAL SEQRES 28F1 383 ARG VAL TYR ASP GLY THR GLU PRO VAL PRO GLY ASP PRO SEQRES 29F1 383 ASP MET THR ARG TYR VAL ASP ARG PHE GLY LYS THR LYS SEQRES 30F1 383 THR VAL PHE PRO GLY ASN SEQRES 1L2 109 ASP ILE VAL MET THR GLN SER PRO THR SER MET SER ILE SEQRES 2L2 109 SER VAL GLY ASP ARG VAL THR MET ASN CYS ARG ALA SER SEQRES 3L2 109 GLN ASN VAL TYR SER ASN VAL ASP TRP TYR GLN GLN LYS SEQRES 4L2 109 THR GLY GLN SER PRO LYS LEU VAL ILE TYR LYS ALA SER SEQRES 5L2 109 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6L2 109 GLY SER GLY THR TYR PHE THR LEU THR ILE THR ASN ILE SEQRES 7L2 109 GLN THR GLU ASP LEU ALA VAL TYR TYR CYS LEU GLN SER SEQRES 8L2 109 ASN ALA PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9L2 109 GLU THR THR ARG ALA SEQRES 1H2 117 GLU GLU SER GLY GLY GLY LEU VAL GLN PRO GLY LYS SER SEQRES 2H2 117 LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SER SEQRES 3H2 117 SER TYR GLY MET HIS TRP ILE ARG GLN VAL PRO GLY LYS SEQRES 4H2 117 GLY LEU ASP TRP VAL ALA TYR ILE SER SER ALA SER ASP SEQRES 5H2 117 THR PHE TYR ALA ASP ALA VAL LYS GLU ARG PHE THR ILE SEQRES 6H2 117 SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU ARG LEU SEQRES 7H2 117 ASN SER LEU LYS SER GLU ASP THR ALA ILE TYR TYR CYS SEQRES 8H2 117 ALA ARG THR ARG TYR PRO THR ASP HIS PHE TYR ASP TRP SEQRES 9H2 117 PHE PRO TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1F2 383 ALA PRO LYS ARG LYS SER GLY VAL SER LYS CYS GLU THR SEQRES 2F2 383 LYS CYS THR LYS ALA CYS PRO ARG PRO ALA PRO VAL PRO SEQRES 3F2 383 LYS LEU LEU ILE LYS GLY GLY MET GLU VAL LEU ASP LEU SEQRES 4F2 383 VAL THR GLY PRO ASP SER VAL THR GLU ILE GLU ALA PHE SEQRES 5F2 383 LEU ASN PRO ARG MET GLY GLN PRO PRO THR PRO GLU SER SEQRES 6F2 383 LEU THR GLU GLY GLY GLN TYR TYR GLY TRP SER ARG GLY SEQRES 7F2 383 ILE ASN LEU ALA THR SER ASP THR GLU ASP SER PRO GLU SEQRES 8F2 383 ASN ASN THR LEU PRO THR TRP SER MET ALA LYS LEU GLN SEQRES 9F2 383 LEU PRO MET LEU ASN GLU ASP LEU THR CYS ASP THR LEU SEQRES 10F2 383 GLN MET TRP GLU ALA VAL SER VAL LYS THR GLU VAL VAL SEQRES 11F2 383 GLY SER GLY SER LEU LEU ASP VAL HIS GLY PHE ASN LYS SEQRES 12F2 383 PRO THR ASP THR VAL ASN THR LYS GLY ILE SER THR PRO SEQRES 13F2 383 VAL GLU GLY SER GLN TYR HIS VAL PHE ALA VAL GLY GLY SEQRES 14F2 383 GLU PRO LEU ASP LEU GLN GLY LEU VAL THR ASP ALA ARG SEQRES 15F2 383 THR LYS TYR LYS GLU GLU GLY VAL VAL THR ILE LYS THR SEQRES 16F2 383 ILE THR LYS LYS ASP MET VAL ASN LYS ASP GLN VAL LEU SEQRES 17F2 383 ASN PRO ILE SER LYS ALA LYS LEU ASP LYS ASP GLY MET SEQRES 18F2 383 TYR PRO VAL GLU ILE TRP HIS PRO ASP PRO ALA LYS ASN SEQRES 19F2 383 GLU ASN THR ARG TYR PHE GLY ASN TYR THR GLY GLY THR SEQRES 20F2 383 THR THR PRO PRO VAL LEU GLN PHE THR ASN THR LEU THR SEQRES 21F2 383 THR VAL LEU LEU ASP GLU ASN GLY VAL GLY PRO LEU CYS SEQRES 22F2 383 LYS GLY GLU GLY LEU TYR LEU SER CYS VAL ASP ILE MET SEQRES 23F2 383 GLY TRP ARG VAL THR ARG ASN TYR ASP VAL HIS HIS TRP SEQRES 24F2 383 ARG GLY LEU PRO ARG TYR PHE LYS ILE THR LEU ARG LYS SEQRES 25F2 383 ARG TRP VAL LYS ASN PRO TYR PRO MET ALA SER LEU ILE SEQRES 26F2 383 SER SER LEU PHE ASN ASN MET LEU PRO GLN VAL GLN GLY SEQRES 27F2 383 GLN PRO MET GLU GLY GLU ASN THR GLN VAL GLU GLU VAL SEQRES 28F2 383 ARG VAL TYR ASP GLY THR GLU PRO VAL PRO GLY ASP PRO SEQRES 29F2 383 ASP MET THR ARG TYR VAL ASP ARG PHE GLY LYS THR LYS SEQRES 30F2 383 THR VAL PHE PRO GLY ASN SEQRES 1L3 109 ASP ILE VAL MET THR GLN SER PRO THR SER MET SER ILE SEQRES 2L3 109 SER VAL GLY ASP ARG VAL THR MET ASN CYS ARG ALA SER SEQRES 3L3 109 GLN ASN VAL TYR SER ASN VAL ASP TRP TYR GLN GLN LYS SEQRES 4L3 109 THR GLY GLN SER PRO LYS LEU VAL ILE TYR LYS ALA SER SEQRES 5L3 109 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6L3 109 GLY SER GLY THR TYR PHE THR LEU THR ILE THR ASN ILE SEQRES 7L3 109 GLN THR GLU ASP LEU ALA VAL TYR TYR CYS LEU GLN SER SEQRES 8L3 109 ASN ALA PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9L3 109 GLU THR THR ARG ALA SEQRES 1H3 117 GLU GLU SER GLY GLY GLY LEU VAL GLN PRO GLY LYS SER SEQRES 2H3 117 LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SER SEQRES 3H3 117 SER TYR GLY MET HIS TRP ILE ARG GLN VAL PRO GLY LYS SEQRES 4H3 117 GLY LEU ASP TRP VAL ALA TYR ILE SER SER ALA SER ASP SEQRES 5H3 117 THR PHE TYR ALA ASP ALA VAL LYS GLU ARG PHE THR ILE SEQRES 6H3 117 SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU ARG LEU SEQRES 7H3 117 ASN SER LEU LYS SER GLU ASP THR ALA ILE TYR TYR CYS SEQRES 8H3 117 ALA ARG THR ARG TYR PRO THR ASP HIS PHE TYR ASP TRP SEQRES 9H3 117 PHE PRO TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1F3 383 ALA PRO LYS ARG LYS SER GLY VAL SER LYS CYS GLU THR SEQRES 2F3 383 LYS CYS THR LYS ALA CYS PRO ARG PRO ALA PRO VAL PRO SEQRES 3F3 383 LYS LEU LEU ILE LYS GLY GLY MET GLU VAL LEU ASP LEU SEQRES 4F3 383 VAL THR GLY PRO ASP SER VAL THR GLU ILE GLU ALA PHE SEQRES 5F3 383 LEU ASN PRO ARG MET GLY GLN PRO PRO THR PRO GLU SER SEQRES 6F3 383 LEU THR GLU GLY GLY GLN TYR TYR GLY TRP SER ARG GLY SEQRES 7F3 383 ILE ASN LEU ALA THR SER ASP THR GLU ASP SER PRO GLU SEQRES 8F3 383 ASN ASN THR LEU PRO THR TRP SER MET ALA LYS LEU GLN SEQRES 9F3 383 LEU PRO MET LEU ASN GLU ASP LEU THR CYS ASP THR LEU SEQRES 10F3 383 GLN MET TRP GLU ALA VAL SER VAL LYS THR GLU VAL VAL SEQRES 11F3 383 GLY SER GLY SER LEU LEU ASP VAL HIS GLY PHE ASN LYS SEQRES 12F3 383 PRO THR ASP THR VAL ASN THR LYS GLY ILE SER THR PRO SEQRES 13F3 383 VAL GLU GLY SER GLN TYR HIS VAL PHE ALA VAL GLY GLY SEQRES 14F3 383 GLU PRO LEU ASP LEU GLN GLY LEU VAL THR ASP ALA ARG SEQRES 15F3 383 THR LYS TYR LYS GLU GLU GLY VAL VAL THR ILE LYS THR SEQRES 16F3 383 ILE THR LYS LYS ASP MET VAL ASN LYS ASP GLN VAL LEU SEQRES 17F3 383 ASN PRO ILE SER LYS ALA LYS LEU ASP LYS ASP GLY MET SEQRES 18F3 383 TYR PRO VAL GLU ILE TRP HIS PRO ASP PRO ALA LYS ASN SEQRES 19F3 383 GLU ASN THR ARG TYR PHE GLY ASN TYR THR GLY GLY THR SEQRES 20F3 383 THR THR PRO PRO VAL LEU GLN PHE THR ASN THR LEU THR SEQRES 21F3 383 THR VAL LEU LEU ASP GLU ASN GLY VAL GLY PRO LEU CYS SEQRES 22F3 383 LYS GLY GLU GLY LEU TYR LEU SER CYS VAL ASP ILE MET SEQRES 23F3 383 GLY TRP ARG VAL THR ARG ASN TYR ASP VAL HIS HIS TRP SEQRES 24F3 383 ARG GLY LEU PRO ARG TYR PHE LYS ILE THR LEU ARG LYS SEQRES 25F3 383 ARG TRP VAL LYS ASN PRO TYR PRO MET ALA SER LEU ILE SEQRES 26F3 383 SER SER LEU PHE ASN ASN MET LEU PRO GLN VAL GLN GLY SEQRES 27F3 383 GLN PRO MET GLU GLY GLU ASN THR GLN VAL GLU GLU VAL SEQRES 28F3 383 ARG VAL TYR ASP GLY THR GLU PRO VAL PRO GLY ASP PRO SEQRES 29F3 383 ASP MET THR ARG TYR VAL ASP ARG PHE GLY LYS THR LYS SEQRES 30F3 383 THR VAL PHE PRO GLY ASN SEQRES 1L4 109 ASP ILE VAL MET THR GLN SER PRO THR SER MET SER ILE SEQRES 2L4 109 SER VAL GLY ASP ARG VAL THR MET ASN CYS ARG ALA SER SEQRES 3L4 109 GLN ASN VAL TYR SER ASN VAL ASP TRP TYR GLN GLN LYS SEQRES 4L4 109 THR GLY GLN SER PRO LYS LEU VAL ILE TYR LYS ALA SER SEQRES 5L4 109 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6L4 109 GLY SER GLY THR TYR PHE THR LEU THR ILE THR ASN ILE SEQRES 7L4 109 GLN THR GLU ASP LEU ALA VAL TYR TYR CYS LEU GLN SER SEQRES 8L4 109 ASN ALA PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9L4 109 GLU THR THR ARG ALA SEQRES 1H4 117 GLU GLU SER GLY GLY GLY LEU VAL GLN PRO GLY LYS SER SEQRES 2H4 117 LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SER SEQRES 3H4 117 SER TYR GLY MET HIS TRP ILE ARG GLN VAL PRO GLY LYS SEQRES 4H4 117 GLY LEU ASP TRP VAL ALA TYR ILE SER SER ALA SER ASP SEQRES 5H4 117 THR PHE TYR ALA ASP ALA VAL LYS GLU ARG PHE THR ILE SEQRES 6H4 117 SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU ARG LEU SEQRES 7H4 117 ASN SER LEU LYS SER GLU ASP THR ALA ILE TYR TYR CYS SEQRES 8H4 117 ALA ARG THR ARG TYR PRO THR ASP HIS PHE TYR ASP TRP SEQRES 9H4 117 PHE PRO TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1F4 383 ALA PRO LYS ARG LYS SER GLY VAL SER LYS CYS GLU THR SEQRES 2F4 383 LYS CYS THR LYS ALA CYS PRO ARG PRO ALA PRO VAL PRO SEQRES 3F4 383 LYS LEU LEU ILE LYS GLY GLY MET GLU VAL LEU ASP LEU SEQRES 4F4 383 VAL THR GLY PRO ASP SER VAL THR GLU ILE GLU ALA PHE SEQRES 5F4 383 LEU ASN PRO ARG MET GLY GLN PRO PRO THR PRO GLU SER SEQRES 6F4 383 LEU THR GLU GLY GLY GLN TYR TYR GLY TRP SER ARG GLY SEQRES 7F4 383 ILE ASN LEU ALA THR SER ASP THR GLU ASP SER PRO GLU SEQRES 8F4 383 ASN ASN THR LEU PRO THR TRP SER MET ALA LYS LEU GLN SEQRES 9F4 383 LEU PRO MET LEU ASN GLU ASP LEU THR CYS ASP THR LEU SEQRES 10F4 383 GLN MET TRP GLU ALA VAL SER VAL LYS THR GLU VAL VAL SEQRES 11F4 383 GLY SER GLY SER LEU LEU ASP VAL HIS GLY PHE ASN LYS SEQRES 12F4 383 PRO THR ASP THR VAL ASN THR LYS GLY ILE SER THR PRO SEQRES 13F4 383 VAL GLU GLY SER GLN TYR HIS VAL PHE ALA VAL GLY GLY SEQRES 14F4 383 GLU PRO LEU ASP LEU GLN GLY LEU VAL THR ASP ALA ARG SEQRES 15F4 383 THR LYS TYR LYS GLU GLU GLY VAL VAL THR ILE LYS THR SEQRES 16F4 383 ILE THR LYS LYS ASP MET VAL ASN LYS ASP GLN VAL LEU SEQRES 17F4 383 ASN PRO ILE SER LYS ALA LYS LEU ASP LYS ASP GLY MET SEQRES 18F4 383 TYR PRO VAL GLU ILE TRP HIS PRO ASP PRO ALA LYS ASN SEQRES 19F4 383 GLU ASN THR ARG TYR PHE GLY ASN TYR THR GLY GLY THR SEQRES 20F4 383 THR THR PRO PRO VAL LEU GLN PHE THR ASN THR LEU THR SEQRES 21F4 383 THR VAL LEU LEU ASP GLU ASN GLY VAL GLY PRO LEU CYS SEQRES 22F4 383 LYS GLY GLU GLY LEU TYR LEU SER CYS VAL ASP ILE MET SEQRES 23F4 383 GLY TRP ARG VAL THR ARG ASN TYR ASP VAL HIS HIS TRP SEQRES 24F4 383 ARG GLY LEU PRO ARG TYR PHE LYS ILE THR LEU ARG LYS SEQRES 25F4 383 ARG TRP VAL LYS ASN PRO TYR PRO MET ALA SER LEU ILE SEQRES 26F4 383 SER SER LEU PHE ASN ASN MET LEU PRO GLN VAL GLN GLY SEQRES 27F4 383 GLN PRO MET GLU GLY GLU ASN THR GLN VAL GLU GLU VAL SEQRES 28F4 383 ARG VAL TYR ASP GLY THR GLU PRO VAL PRO GLY ASP PRO SEQRES 29F4 383 ASP MET THR ARG TYR VAL ASP ARG PHE GLY LYS THR LYS SEQRES 30F4 383 THR VAL PHE PRO GLY ASN SEQRES 1L5 109 ASP ILE VAL MET THR GLN SER PRO THR SER MET SER ILE SEQRES 2L5 109 SER VAL GLY ASP ARG VAL THR MET ASN CYS ARG ALA SER SEQRES 3L5 109 GLN ASN VAL TYR SER ASN VAL ASP TRP TYR GLN GLN LYS SEQRES 4L5 109 THR GLY GLN SER PRO LYS LEU VAL ILE TYR LYS ALA SER SEQRES 5L5 109 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6L5 109 GLY SER GLY THR TYR PHE THR LEU THR ILE THR ASN ILE SEQRES 7L5 109 GLN THR GLU ASP LEU ALA VAL TYR TYR CYS LEU GLN SER SEQRES 8L5 109 ASN ALA PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9L5 109 GLU THR THR ARG ALA SEQRES 1H5 117 GLU GLU SER GLY GLY GLY LEU VAL GLN PRO GLY LYS SER SEQRES 2H5 117 LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SER SEQRES 3H5 117 SER TYR GLY MET HIS TRP ILE ARG GLN VAL PRO GLY LYS SEQRES 4H5 117 GLY LEU ASP TRP VAL ALA TYR ILE SER SER ALA SER ASP SEQRES 5H5 117 THR PHE TYR ALA ASP ALA VAL LYS GLU ARG PHE THR ILE SEQRES 6H5 117 SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU ARG LEU SEQRES 7H5 117 ASN SER LEU LYS SER GLU ASP THR ALA ILE TYR TYR CYS SEQRES 8H5 117 ALA ARG THR ARG TYR PRO THR ASP HIS PHE TYR ASP TRP SEQRES 9H5 117 PHE PRO TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1F5 383 ALA PRO LYS ARG LYS SER GLY VAL SER LYS CYS GLU THR SEQRES 2F5 383 LYS CYS THR LYS ALA CYS PRO ARG PRO ALA PRO VAL PRO SEQRES 3F5 383 LYS LEU LEU ILE LYS GLY GLY MET GLU VAL LEU ASP LEU SEQRES 4F5 383 VAL THR GLY PRO ASP SER VAL THR GLU ILE GLU ALA PHE SEQRES 5F5 383 LEU ASN PRO ARG MET GLY GLN PRO PRO THR PRO GLU SER SEQRES 6F5 383 LEU THR GLU GLY GLY GLN TYR TYR GLY TRP SER ARG GLY SEQRES 7F5 383 ILE ASN LEU ALA THR SER ASP THR GLU ASP SER PRO GLU SEQRES 8F5 383 ASN ASN THR LEU PRO THR TRP SER MET ALA LYS LEU GLN SEQRES 9F5 383 LEU PRO MET LEU ASN GLU ASP LEU THR CYS ASP THR LEU SEQRES 10F5 383 GLN MET TRP GLU ALA VAL SER VAL LYS THR GLU VAL VAL SEQRES 11F5 383 GLY SER GLY SER LEU LEU ASP VAL HIS GLY PHE ASN LYS SEQRES 12F5 383 PRO THR ASP THR VAL ASN THR LYS GLY ILE SER THR PRO SEQRES 13F5 383 VAL GLU GLY SER GLN TYR HIS VAL PHE ALA VAL GLY GLY SEQRES 14F5 383 GLU PRO LEU ASP LEU GLN GLY LEU VAL THR ASP ALA ARG SEQRES 15F5 383 THR LYS TYR LYS GLU GLU GLY VAL VAL THR ILE LYS THR SEQRES 16F5 383 ILE THR LYS LYS ASP MET VAL ASN LYS ASP GLN VAL LEU SEQRES 17F5 383 ASN PRO ILE SER LYS ALA LYS LEU ASP LYS ASP GLY MET SEQRES 18F5 383 TYR PRO VAL GLU ILE TRP HIS PRO ASP PRO ALA LYS ASN SEQRES 19F5 383 GLU ASN THR ARG TYR PHE GLY ASN TYR THR GLY GLY THR SEQRES 20F5 383 THR THR PRO PRO VAL LEU GLN PHE THR ASN THR LEU THR SEQRES 21F5 383 THR VAL LEU LEU ASP GLU ASN GLY VAL GLY PRO LEU CYS SEQRES 22F5 383 LYS GLY GLU GLY LEU TYR LEU SER CYS VAL ASP ILE MET SEQRES 23F5 383 GLY TRP ARG VAL THR ARG ASN TYR ASP VAL HIS HIS TRP SEQRES 24F5 383 ARG GLY LEU PRO ARG TYR PHE LYS ILE THR LEU ARG LYS SEQRES 25F5 383 ARG TRP VAL LYS ASN PRO TYR PRO MET ALA SER LEU ILE SEQRES 26F5 383 SER SER LEU PHE ASN ASN MET LEU PRO GLN VAL GLN GLY SEQRES 27F5 383 GLN PRO MET GLU GLY GLU ASN THR GLN VAL GLU GLU VAL SEQRES 28F5 383 ARG VAL TYR ASP GLY THR GLU PRO VAL PRO GLY ASP PRO SEQRES 29F5 383 ASP MET THR ARG TYR VAL ASP ARG PHE GLY LYS THR LYS SEQRES 30F5 383 THR VAL PHE PRO GLY ASN HELIX 1 AA1 LYSL1 50 SERL1 52 5 3 HELIX 2 AA2 GLNL1 79 LEUL1 83 5 5 HELIX 3 AA3 THRH1 24 TYRH1 28 5 5 HELIX 4 AA4 ASPH1 57 LYSH1 60 5 4 HELIX 5 AA5 GLYF1 33 LEUF1 39 5 7 HELIX 6 AA6 GLUF1 91 LEUF1 95 5 5 HELIX 7 AA7 SERF1 132 ASPF1 137 5 6 HELIX 8 AA8 THRF1 192 THRF1 197 1 6 HELIX 9 AA9 VALF1 202 VALF1 207 5 6 HELIX 10 AB1 PROF1 320 ALAF1 322 5 3 HELIX 11 AB2 SERF1 323 LEUF1 333 1 11 HELIX 12 AB3 LYSL2 50 SERL2 52 5 3 HELIX 13 AB4 GLNL2 79 LEUL2 83 5 5 HELIX 14 AB5 THRH2 24 TYRH2 28 5 5 HELIX 15 AB6 ASPH2 57 LYSH2 60 5 4 HELIX 16 AB7 GLYF2 33 LEUF2 39 5 7 HELIX 17 AB8 GLUF2 91 LEUF2 95 5 5 HELIX 18 AB9 SERF2 132 ASPF2 137 5 6 HELIX 19 AC1 THRF2 192 THRF2 197 1 6 HELIX 20 AC2 VALF2 202 VALF2 207 5 6 HELIX 21 AC3 PROF2 320 ALAF2 322 5 3 HELIX 22 AC4 SERF2 323 LEUF2 333 1 11 HELIX 23 AC5 LYSL3 50 SERL3 52 5 3 HELIX 24 AC6 GLNL3 79 LEUL3 83 5 5 HELIX 25 AC7 THRH3 24 TYRH3 28 5 5 HELIX 26 AC8 ASPH3 57 LYSH3 60 5 4 HELIX 27 AC9 GLYF3 33 LEUF3 39 5 7 HELIX 28 AD1 GLUF3 91 LEUF3 95 5 5 HELIX 29 AD2 SERF3 132 ASPF3 137 5 6 HELIX 30 AD3 THRF3 192 THRF3 197 1 6 HELIX 31 AD4 VALF3 202 VALF3 207 5 6 HELIX 32 AD5 PROF3 320 ALAF3 322 5 3 HELIX 33 AD6 SERF3 323 LEUF3 333 1 11 HELIX 34 AD7 LYSL4 50 SERL4 52 5 3 HELIX 35 AD8 GLNL4 79 LEUL4 83 5 5 HELIX 36 AD9 THRH4 24 TYRH4 28 5 5 HELIX 37 AE1 ASPH4 57 LYSH4 60 5 4 HELIX 38 AE2 GLYF4 33 LEUF4 39 5 7 HELIX 39 AE3 GLUF4 91 LEUF4 95 5 5 HELIX 40 AE4 SERF4 132 ASPF4 137 5 6 HELIX 41 AE5 THRF4 192 THRF4 197 1 6 HELIX 42 AE6 VALF4 202 VALF4 207 5 6 HELIX 43 AE7 PROF4 320 ALAF4 322 5 3 HELIX 44 AE8 SERF4 323 LEUF4 333 1 11 HELIX 45 AE9 LYSL5 50 SERL5 52 5 3 HELIX 46 AF1 GLNL5 79 LEUL5 83 5 5 HELIX 47 AF2 THRH5 24 TYRH5 28 5 5 HELIX 48 AF3 ASPH5 57 LYSH5 60 5 4 HELIX 49 AF4 GLYF5 33 LEUF5 39 5 7 HELIX 50 AF5 GLUF5 91 LEUF5 95 5 5 HELIX 51 AF6 SERF5 132 ASPF5 137 5 6 HELIX 52 AF7 THRF5 192 THRF5 197 1 6 HELIX 53 AF8 VALF5 202 VALF5 207 5 6 HELIX 54 AF9 PROF5 320 ALAF5 322 5 3 HELIX 55 AG1 SERF5 323 LEUF5 333 1 11 SHEET 1 AA1 3 METL1 4 GLNL1 6 0 SHEET 2 AA1 3 VALL1 19 VALL1 29 -1 O ARGL1 24 N THRL1 5 SHEET 3 AA1 3 PHEL1 62 ILEL1 75 -1 O LEUL1 73 N METL1 21 SHEET 1 AA2 4 ASNL1 53 ARGL1 54 0 SHEET 2 AA2 4 LYSL1 45 TYRL1 49 -1 N TYRL1 49 O ASNL1 53 SHEET 3 AA2 4 VALL1 33 GLNL1 38 -1 N GLNL1 37 O LYSL1 45 SHEET 4 AA2 4 VALL1 85 GLNL1 90 -1 O LEUL1 89 N ASPL1 34 SHEET 1 AA3 3 CYSH1 18 SERH1 19 0 SHEET 2 AA3 3 THRH1 73 ARGH1 77 -1 O LEUH1 74 N CYSH1 18 SHEET 3 AA3 3 THRH1 64 ASPH1 68 -1 N SERH1 66 O TYRH1 75 SHEET 1 AA4 5 THRH1 53 TYRH1 55 0 SHEET 2 AA4 5 GLYH1 40 ILEH1 47 -1 N TYRH1 46 O PHEH1 54 SHEET 3 AA4 5 METH1 30 VALH1 36 -1 N METH1 30 O ILEH1 47 SHEET 4 AA4 5 ILEH1 88 ARGH1 93 -1 O TYRH1 90 N ILEH1 33 SHEET 5 AA4 5 TYRH1 107 TRPH1 108 -1 O TYRH1 107 N ARGH1 93 SHEET 1 AA5 4 VALF1 46 LEUF1 53 0 SHEET 2 AA5 4 ARGF1 304 VALF1 315 -1 O ILEF1 308 N ILEF1 49 SHEET 3 AA5 4 LEUF1 117 VALF1 129 -1 N LEUF1 117 O VALF1 315 SHEET 4 AA5 4 THRF1 261 VALF1 262 -1 O THRF1 261 N VALF1 125 SHEET 1 AA6 3 SERF1 99 GLNF1 104 0 SHEET 2 AA6 3 GLYF1 277 VALF1 290 -1 O CYSF1 282 N SERF1 99 SHEET 3 AA6 3 HISF1 297 GLYF1 301 -1 O ARGF1 300 N METF1 286 SHEET 1 AA7 5 SERF1 99 GLNF1 104 0 SHEET 2 AA7 5 GLYF1 277 VALF1 290 -1 O CYSF1 282 N SERF1 99 SHEET 3 AA7 5 GLNF1 161 GLYF1 168 -1 N VALF1 164 O VALF1 283 SHEET 4 AA7 5 THRF1 237 THRF1 244 -1 O ARGF1 238 N VALF1 167 SHEET 5 AA7 5 VALF5 252 THRF5 256 -1 O LEUF5 253 N TYRF1 243 SHEET 1 AA8 2 PROF1 144 ASPF1 146 0 SHEET 2 AA8 2 LYSF1 151 SERF1 154 -1 O LYSF1 151 N ASPF1 146 SHEET 1 AA9 3 LYSF1 213 LYSF1 215 0 SHEET 2 AA9 3 ASPF1 173 GLYF1 176 -1 N LEUF1 174 O ALAF1 214 SHEET 3 AA9 3 TRPF1 227 PROF1 229 -1 O HISF1 228 N GLNF1 175 SHEET 1 AB1 5 VALF1 252 THRF1 256 0 SHEET 2 AB1 5 THRF2 237 THRF2 244 -1 O TYRF2 243 N LEUF1 253 SHEET 3 AB1 5 GLNF2 161 GLYF2 168 -1 N VALF2 167 O ARGF2 238 SHEET 4 AB1 5 GLYF2 277 VALF2 290 -1 O VALF2 283 N VALF2 164 SHEET 5 AB1 5 SERF2 99 GLNF2 104 -1 N SERF2 99 O CYSF2 282 SHEET 1 AB2 5 VALF1 252 THRF1 256 0 SHEET 2 AB2 5 THRF2 237 THRF2 244 -1 O TYRF2 243 N LEUF1 253 SHEET 3 AB2 5 GLNF2 161 GLYF2 168 -1 N VALF2 167 O ARGF2 238 SHEET 4 AB2 5 GLYF2 277 VALF2 290 -1 O VALF2 283 N VALF2 164 SHEET 5 AB2 5 HISF2 297 GLYF2 301 -1 O ARGF2 300 N METF2 286 SHEET 1 AB3 3 METL2 4 GLNL2 6 0 SHEET 2 AB3 3 VALL2 19 VALL2 29 -1 O ARGL2 24 N THRL2 5 SHEET 3 AB3 3 PHEL2 62 ILEL2 75 -1 O LEUL2 73 N METL2 21 SHEET 1 AB4 4 ASNL2 53 ARGL2 54 0 SHEET 2 AB4 4 LYSL2 45 TYRL2 49 -1 N TYRL2 49 O ASNL2 53 SHEET 3 AB4 4 VALL2 33 GLNL2 38 -1 N GLNL2 37 O LYSL2 45 SHEET 4 AB4 4 VALL2 85 GLNL2 90 -1 O LEUL2 89 N ASPL2 34 SHEET 1 AB5 3 CYSH2 18 SERH2 19 0 SHEET 2 AB5 3 THRH2 73 ARGH2 77 -1 O LEUH2 74 N CYSH2 18 SHEET 3 AB5 3 THRH2 64 ASPH2 68 -1 N SERH2 66 O TYRH2 75 SHEET 1 AB6 5 THRH2 53 TYRH2 55 0 SHEET 2 AB6 5 GLYH2 40 ILEH2 47 -1 N TYRH2 46 O PHEH2 54 SHEET 3 AB6 5 METH2 30 VALH2 36 -1 N METH2 30 O ILEH2 47 SHEET 4 AB6 5 ILEH2 88 ARGH2 93 -1 O TYRH2 90 N ILEH2 33 SHEET 5 AB6 5 TYRH2 107 TRPH2 108 -1 O TYRH2 107 N ARGH2 93 SHEET 1 AB7 4 VALF2 46 LEUF2 53 0 SHEET 2 AB7 4 ARGF2 304 VALF2 315 -1 O ILEF2 308 N ILEF2 49 SHEET 3 AB7 4 LEUF2 117 VALF2 129 -1 N LEUF2 117 O VALF2 315 SHEET 4 AB7 4 THRF2 261 VALF2 262 -1 O THRF2 261 N VALF2 125 SHEET 1 AB8 2 PROF2 144 ASPF2 146 0 SHEET 2 AB8 2 LYSF2 151 SERF2 154 -1 O LYSF2 151 N ASPF2 146 SHEET 1 AB9 3 LYSF2 213 LYSF2 215 0 SHEET 2 AB9 3 ASPF2 173 GLYF2 176 -1 N LEUF2 174 O ALAF2 214 SHEET 3 AB9 3 TRPF2 227 PROF2 229 -1 O HISF2 228 N GLNF2 175 SHEET 1 AC1 5 VALF2 252 THRF2 256 0 SHEET 2 AC1 5 THRF3 237 THRF3 244 -1 O TYRF3 243 N LEUF2 253 SHEET 3 AC1 5 GLNF3 161 GLYF3 168 -1 N VALF3 167 O ARGF3 238 SHEET 4 AC1 5 GLYF3 277 VALF3 290 -1 O VALF3 283 N VALF3 164 SHEET 5 AC1 5 SERF3 99 GLNF3 104 -1 N SERF3 99 O CYSF3 282 SHEET 1 AC2 5 VALF2 252 THRF2 256 0 SHEET 2 AC2 5 THRF3 237 THRF3 244 -1 O TYRF3 243 N LEUF2 253 SHEET 3 AC2 5 GLNF3 161 GLYF3 168 -1 N VALF3 167 O ARGF3 238 SHEET 4 AC2 5 GLYF3 277 VALF3 290 -1 O VALF3 283 N VALF3 164 SHEET 5 AC2 5 HISF3 297 GLYF3 301 -1 O ARGF3 300 N METF3 286 SHEET 1 AC3 3 METL3 4 GLNL3 6 0 SHEET 2 AC3 3 VALL3 19 VALL3 29 -1 O ARGL3 24 N THRL3 5 SHEET 3 AC3 3 PHEL3 62 ILEL3 75 -1 O LEUL3 73 N METL3 21 SHEET 1 AC4 4 ASNL3 53 ARGL3 54 0 SHEET 2 AC4 4 LYSL3 45 TYRL3 49 -1 N TYRL3 49 O ASNL3 53 SHEET 3 AC4 4 VALL3 33 GLNL3 38 -1 N GLNL3 37 O LYSL3 45 SHEET 4 AC4 4 VALL3 85 GLNL3 90 -1 O LEUL3 89 N ASPL3 34 SHEET 1 AC5 3 CYSH3 18 SERH3 19 0 SHEET 2 AC5 3 THRH3 73 ARGH3 77 -1 O LEUH3 74 N CYSH3 18 SHEET 3 AC5 3 THRH3 64 ASPH3 68 -1 N SERH3 66 O TYRH3 75 SHEET 1 AC6 5 THRH3 53 TYRH3 55 0 SHEET 2 AC6 5 GLYH3 40 ILEH3 47 -1 N TYRH3 46 O PHEH3 54 SHEET 3 AC6 5 METH3 30 VALH3 36 -1 N METH3 30 O ILEH3 47 SHEET 4 AC6 5 ILEH3 88 ARGH3 93 -1 O TYRH3 90 N ILEH3 33 SHEET 5 AC6 5 TYRH3 107 TRPH3 108 -1 O TYRH3 107 N ARGH3 93 SHEET 1 AC7 4 VALF3 46 LEUF3 53 0 SHEET 2 AC7 4 ARGF3 304 VALF3 315 -1 O ILEF3 308 N ILEF3 49 SHEET 3 AC7 4 LEUF3 117 VALF3 129 -1 N LEUF3 117 O VALF3 315 SHEET 4 AC7 4 THRF3 261 VALF3 262 -1 O THRF3 261 N VALF3 125 SHEET 1 AC8 2 PROF3 144 ASPF3 146 0 SHEET 2 AC8 2 LYSF3 151 SERF3 154 -1 O LYSF3 151 N ASPF3 146 SHEET 1 AC9 3 LYSF3 213 LYSF3 215 0 SHEET 2 AC9 3 ASPF3 173 GLYF3 176 -1 N LEUF3 174 O ALAF3 214 SHEET 3 AC9 3 TRPF3 227 PROF3 229 -1 O HISF3 228 N GLNF3 175 SHEET 1 AD1 5 VALF3 252 THRF3 256 0 SHEET 2 AD1 5 THRF4 237 THRF4 244 -1 O TYRF4 243 N LEUF3 253 SHEET 3 AD1 5 GLNF4 161 GLYF4 168 -1 N VALF4 167 O ARGF4 238 SHEET 4 AD1 5 GLYF4 277 VALF4 290 -1 O VALF4 283 N VALF4 164 SHEET 5 AD1 5 SERF4 99 GLNF4 104 -1 N SERF4 99 O CYSF4 282 SHEET 1 AD2 5 VALF3 252 THRF3 256 0 SHEET 2 AD2 5 THRF4 237 THRF4 244 -1 O TYRF4 243 N LEUF3 253 SHEET 3 AD2 5 GLNF4 161 GLYF4 168 -1 N VALF4 167 O ARGF4 238 SHEET 4 AD2 5 GLYF4 277 VALF4 290 -1 O VALF4 283 N VALF4 164 SHEET 5 AD2 5 HISF4 297 GLYF4 301 -1 O ARGF4 300 N METF4 286 SHEET 1 AD3 3 METL4 4 GLNL4 6 0 SHEET 2 AD3 3 VALL4 19 VALL4 29 -1 O ARGL4 24 N THRL4 5 SHEET 3 AD3 3 PHEL4 62 ILEL4 75 -1 O LEUL4 73 N METL4 21 SHEET 1 AD4 4 ASNL4 53 ARGL4 54 0 SHEET 2 AD4 4 LYSL4 45 TYRL4 49 -1 N TYRL4 49 O ASNL4 53 SHEET 3 AD4 4 VALL4 33 GLNL4 38 -1 N GLNL4 37 O LYSL4 45 SHEET 4 AD4 4 VALL4 85 GLNL4 90 -1 O LEUL4 89 N ASPL4 34 SHEET 1 AD5 3 CYSH4 18 SERH4 19 0 SHEET 2 AD5 3 THRH4 73 ARGH4 77 -1 O LEUH4 74 N CYSH4 18 SHEET 3 AD5 3 THRH4 64 ASPH4 68 -1 N SERH4 66 O TYRH4 75 SHEET 1 AD6 5 THRH4 53 TYRH4 55 0 SHEET 2 AD6 5 GLYH4 40 ILEH4 47 -1 N TYRH4 46 O PHEH4 54 SHEET 3 AD6 5 METH4 30 VALH4 36 -1 N METH4 30 O ILEH4 47 SHEET 4 AD6 5 ILEH4 88 ARGH4 93 -1 O TYRH4 90 N ILEH4 33 SHEET 5 AD6 5 TYRH4 107 TRPH4 108 -1 O TYRH4 107 N ARGH4 93 SHEET 1 AD7 4 VALF4 46 LEUF4 53 0 SHEET 2 AD7 4 ARGF4 304 VALF4 315 -1 O ILEF4 308 N ILEF4 49 SHEET 3 AD7 4 LEUF4 117 VALF4 129 -1 N LEUF4 117 O VALF4 315 SHEET 4 AD7 4 THRF4 261 VALF4 262 -1 O THRF4 261 N VALF4 125 SHEET 1 AD8 2 PROF4 144 ASPF4 146 0 SHEET 2 AD8 2 LYSF4 151 SERF4 154 -1 O LYSF4 151 N ASPF4 146 SHEET 1 AD9 3 LYSF4 213 LYSF4 215 0 SHEET 2 AD9 3 ASPF4 173 GLYF4 176 -1 N LEUF4 174 O ALAF4 214 SHEET 3 AD9 3 TRPF4 227 PROF4 229 -1 O HISF4 228 N GLNF4 175 SHEET 1 AE1 5 VALF4 252 THRF4 256 0 SHEET 2 AE1 5 THRF5 237 THRF5 244 -1 O TYRF5 243 N LEUF4 253 SHEET 3 AE1 5 GLNF5 161 GLYF5 168 -1 N VALF5 167 O ARGF5 238 SHEET 4 AE1 5 GLYF5 277 VALF5 290 -1 O VALF5 283 N VALF5 164 SHEET 5 AE1 5 SERF5 99 GLNF5 104 -1 N SERF5 99 O CYSF5 282 SHEET 1 AE2 5 VALF4 252 THRF4 256 0 SHEET 2 AE2 5 THRF5 237 THRF5 244 -1 O TYRF5 243 N LEUF4 253 SHEET 3 AE2 5 GLNF5 161 GLYF5 168 -1 N VALF5 167 O ARGF5 238 SHEET 4 AE2 5 GLYF5 277 VALF5 290 -1 O VALF5 283 N VALF5 164 SHEET 5 AE2 5 HISF5 297 GLYF5 301 -1 O ARGF5 300 N METF5 286 SHEET 1 AE3 3 METL5 4 GLNL5 6 0 SHEET 2 AE3 3 VALL5 19 VALL5 29 -1 O ARGL5 24 N THRL5 5 SHEET 3 AE3 3 PHEL5 62 ILEL5 75 -1 O LEUL5 73 N METL5 21 SHEET 1 AE4 4 ASNL5 53 ARGL5 54 0 SHEET 2 AE4 4 LYSL5 45 TYRL5 49 -1 N TYRL5 49 O ASNL5 53 SHEET 3 AE4 4 VALL5 33 GLNL5 38 -1 N GLNL5 37 O LYSL5 45 SHEET 4 AE4 4 VALL5 85 GLNL5 90 -1 O LEUL5 89 N ASPL5 34 SHEET 1 AE5 3 CYSH5 18 SERH5 19 0 SHEET 2 AE5 3 THRH5 73 ARGH5 77 -1 O LEUH5 74 N CYSH5 18 SHEET 3 AE5 3 THRH5 64 ASPH5 68 -1 N SERH5 66 O TYRH5 75 SHEET 1 AE6 5 THRH5 53 TYRH5 55 0 SHEET 2 AE6 5 GLYH5 40 ILEH5 47 -1 N TYRH5 46 O PHEH5 54 SHEET 3 AE6 5 METH5 30 VALH5 36 -1 N METH5 30 O ILEH5 47 SHEET 4 AE6 5 ILEH5 88 ARGH5 93 -1 O TYRH5 90 N ILEH5 33 SHEET 5 AE6 5 TYRH5 107 TRPH5 108 -1 O TYRH5 107 N ARGH5 93 SHEET 1 AE7 4 VALF5 46 LEUF5 53 0 SHEET 2 AE7 4 ARGF5 304 VALF5 315 -1 O ILEF5 308 N ILEF5 49 SHEET 3 AE7 4 LEUF5 117 VALF5 129 -1 N LEUF5 117 O VALF5 315 SHEET 4 AE7 4 THRF5 261 VALF5 262 -1 O THRF5 261 N VALF5 125 SHEET 1 AE8 2 PROF5 144 ASPF5 146 0 SHEET 2 AE8 2 LYSF5 151 SERF5 154 -1 O LYSF5 151 N ASPF5 146 SHEET 1 AE9 3 LYSF5 213 LYSF5 215 0 SHEET 2 AE9 3 ASPF5 173 GLYF5 176 -1 N LEUF5 174 O ALAF5 214 SHEET 3 AE9 3 TRPF5 227 PROF5 229 -1 O HISF5 228 N GLNF5 175 SSBOND 1 CYSL1 23 CYSL1 88 1555 1555 2.03 SSBOND 2 CYSH1 18 CYSH1 91 1555 1555 2.03 SSBOND 3 CYSF1 19 CYSF2 114 1555 1555 2.03 SSBOND 4 CYSF1 114 CYSF5 19 1555 1555 2.03 SSBOND 5 CYSL2 23 CYSL2 88 1555 1555 2.03 SSBOND 6 CYSH2 18 CYSH2 91 1555 1555 2.03 SSBOND 7 CYSF2 19 CYSF3 114 1555 1555 2.06 SSBOND 8 CYSL3 23 CYSL3 88 1555 1555 2.03 SSBOND 9 CYSH3 18 CYSH3 91 1555 1555 2.03 SSBOND 10 CYSF3 19 CYSF4 114 1555 1555 2.07 SSBOND 11 CYSL4 23 CYSL4 88 1555 1555 2.03 SSBOND 12 CYSH4 18 CYSH4 91 1555 1555 2.03 SSBOND 13 CYSF4 19 CYSF5 114 1555 1555 1.93 SSBOND 14 CYSL5 23 CYSL5 88 1555 1555 2.03 SSBOND 15 CYSH5 18 CYSH5 91 1555 1555 2.03 CISPEP 1 PHEL1 94 PROL1 95 0 6.20 CISPEP 2 PHEL2 94 PROL2 95 0 6.21 CISPEP 3 PHEL3 94 PROL3 95 0 6.25 CISPEP 4 PHEL4 94 PROL4 95 0 6.22 CISPEP 5 PHEL5 94 PROL5 95 0 6.16 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