HEADER VIRAL PROTEIN 08-SEP-20 7K23 TITLE MURINE POLYOMAVIRUS HEXAVALENT CAPSOMER WITH 8A7H5 FAB, SUBPARTICLE TITLE 2 RECONSTRUCTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: 8A7H5 FAB LIGHT CHAIN; COMPND 3 CHAIN: L2, L3, L4, L5, L6; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: 8A7H5 FAB HEAVY CHAIN; COMPND 6 CHAIN: H2, H3, H4, H5, H6; COMPND 7 MOL_ID: 3; COMPND 8 MOLECULE: CAPSID PROTEIN VP1; COMPND 9 CHAIN: A, B, C, D, E; 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, VP1, FAB, 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. 3.30 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) : 3.300 REMARK 3 NUMBER OF PARTICLES : 548769 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 7K23 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_1000250843. 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: L2, H2, A, B, C, D, E, L3, REMARK 350 AND CHAINS: H3, L4, H4, L5, H5, L6, H6 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 A -15 REMARK 465 PRO A -14 REMARK 465 LYS A -13 REMARK 465 ARG A -12 REMARK 465 LYS A -11 REMARK 465 SER A -10 REMARK 465 GLY A -9 REMARK 465 VAL A -8 REMARK 465 SER A -7 REMARK 465 LYS A -6 REMARK 465 CYS A -5 REMARK 465 GLU A -4 REMARK 465 THR A -3 REMARK 465 LYS A -2 REMARK 465 CYS A -1 REMARK 465 THR A 0 REMARK 465 ASN A 367 REMARK 465 ALA B -15 REMARK 465 PRO B -14 REMARK 465 LYS B -13 REMARK 465 ARG B -12 REMARK 465 LYS B -11 REMARK 465 SER B -10 REMARK 465 GLY B -9 REMARK 465 VAL B -8 REMARK 465 SER B -7 REMARK 465 LYS B -6 REMARK 465 CYS B -5 REMARK 465 GLU B -4 REMARK 465 THR B -3 REMARK 465 LYS B -2 REMARK 465 CYS B -1 REMARK 465 THR B 0 REMARK 465 ALA C -15 REMARK 465 PRO C -14 REMARK 465 LYS C -13 REMARK 465 ARG C -12 REMARK 465 LYS C -11 REMARK 465 SER C -10 REMARK 465 GLY C -9 REMARK 465 VAL C -8 REMARK 465 SER C -7 REMARK 465 LYS C -6 REMARK 465 CYS C -5 REMARK 465 GLU C -4 REMARK 465 THR C -3 REMARK 465 LYS C -2 REMARK 465 CYS C -1 REMARK 465 THR C 0 REMARK 465 GLY C 358 REMARK 465 LYS C 359 REMARK 465 THR C 360 REMARK 465 LYS C 361 REMARK 465 THR C 362 REMARK 465 VAL C 363 REMARK 465 PHE C 364 REMARK 465 PRO C 365 REMARK 465 GLY C 366 REMARK 465 ASN C 367 REMARK 465 ALA D -15 REMARK 465 PRO D -14 REMARK 465 LYS D -13 REMARK 465 ARG D -12 REMARK 465 LYS D -11 REMARK 465 SER D -10 REMARK 465 GLY D -9 REMARK 465 VAL D -8 REMARK 465 SER D -7 REMARK 465 LYS D -6 REMARK 465 CYS D -5 REMARK 465 GLU D -4 REMARK 465 THR D -3 REMARK 465 LYS D -2 REMARK 465 CYS D -1 REMARK 465 THR D 0 REMARK 465 THR D 341 REMARK 465 GLU D 342 REMARK 465 PRO D 343 REMARK 465 VAL D 344 REMARK 465 PRO D 345 REMARK 465 GLY D 346 REMARK 465 ASP D 347 REMARK 465 PRO D 348 REMARK 465 ASP D 349 REMARK 465 MET D 350 REMARK 465 THR D 351 REMARK 465 ARG D 352 REMARK 465 TYR D 353 REMARK 465 VAL D 354 REMARK 465 ASP D 355 REMARK 465 ARG D 356 REMARK 465 PHE D 357 REMARK 465 GLY D 358 REMARK 465 LYS D 359 REMARK 465 THR D 360 REMARK 465 LYS D 361 REMARK 465 THR D 362 REMARK 465 VAL D 363 REMARK 465 PHE D 364 REMARK 465 PRO D 365 REMARK 465 GLY D 366 REMARK 465 ASN D 367 REMARK 465 ALA E -15 REMARK 465 PRO E -14 REMARK 465 LYS E -13 REMARK 465 ARG E -12 REMARK 465 LYS E -11 REMARK 465 SER E -10 REMARK 465 GLY E -9 REMARK 465 VAL E -8 REMARK 465 SER E -7 REMARK 465 LYS E -6 REMARK 465 CYS E -5 REMARK 465 GLU E -4 REMARK 465 THR E -3 REMARK 465 LYS E -2 REMARK 465 CYS E -1 REMARK 465 THR E 0 REMARK 465 LYS E 1 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 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 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 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 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 CD2 LEU E 50 CB GLN E 55 1.62 REMARK 500 NE1 TRP E 272 CZ2 TRP E 283 1.77 REMARK 500 CD2 LEU E 50 CG GLN E 55 1.89 REMARK 500 CG2 THRH2 98 ND2 ASN C 277 1.91 REMARK 500 CE MET C 103 O CYS C 257 2.06 REMARK 500 NE1 TRP E 272 CE2 TRP E 283 2.06 REMARK 500 OD2 ASP D 268 NH1 ARG D 288 2.08 REMARK 500 NE1 TRP E 272 CH2 TRP E 283 2.09 REMARK 500 OG SERH6 48 OD1 ASPH6 52 2.09 REMARK 500 OG SERH2 48 OD1 ASPH2 52 2.09 REMARK 500 OG SERH5 48 OD1 ASPH5 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 OD2 ASP E 268 NH1 ARG E 288 2.10 REMARK 500 OD1 ASP C 268 NH1 ARG C 288 2.10 REMARK 500 OD1 ASP B 268 NH1 ARG B 288 2.10 REMARK 500 N MET C 84 OD1 ASP C 203 2.11 REMARK 500 NH1 ARG A 40 OD2 ASP A 203 2.12 REMARK 500 CB SER E 144 CH2 TRP E 272 2.18 REMARK 500 O ILE A 177 OG1 THR A 181 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 SERL2 31 20.87 -141.05 REMARK 500 LYSL2 50 18.56 59.09 REMARK 500 VALH2 44 -61.76 -123.01 REMARK 500 ALAH2 70 -1.27 68.55 REMARK 500 SERH2 80 -3.67 66.28 REMARK 500 GLU A 75 82.18 62.40 REMARK 500 ASP A 99 38.98 -98.91 REMARK 500 GLU A 105 111.06 -160.22 REMARK 500 ARG A 166 -71.01 -83.47 REMARK 500 THR A 167 69.19 36.69 REMARK 500 LYS A 168 89.68 -68.08 REMARK 500 LYS A 182 -1.36 67.99 REMARK 500 LYS A 188 0.76 -67.31 REMARK 500 ASN A 277 -161.03 -165.60 REMARK 500 TYR A 278 127.26 -38.73 REMARK 500 SER A 311 -163.75 -78.23 REMARK 500 TYR B 56 49.57 -89.98 REMARK 500 PRO B 90 -177.82 -69.84 REMARK 500 HIS B 123 -169.60 -79.10 REMARK 500 ASP B 189 3.69 -67.37 REMARK 500 VAL B 191 -67.14 -123.67 REMARK 500 LEU B 192 117.11 -166.28 REMARK 500 PRO B 194 0.27 -67.28 REMARK 500 THR B 233 121.13 -39.27 REMARK 500 THR B 240 147.29 -173.60 REMARK 500 GLU B 260 12.14 -69.97 REMARK 500 ARG B 356 -18.16 58.06 REMARK 500 PHE B 357 -43.14 -139.84 REMARK 500 PHE B 364 109.22 -56.85 REMARK 500 PRO C 74 -73.81 -61.68 REMARK 500 GLU C 75 172.03 173.07 REMARK 500 ASP C 95 40.05 -97.52 REMARK 500 LEU C 96 49.22 -80.14 REMARK 500 THR C 97 -30.43 -134.96 REMARK 500 LEU C 101 144.93 -173.81 REMARK 500 GLU C 105 117.53 -163.07 REMARK 500 LYS C 182 -3.57 67.58 REMARK 500 PRO C 194 3.56 -65.00 REMARK 500 LEU C 200 41.14 -98.39 REMARK 500 LYS C 202 -169.62 -79.98 REMARK 500 ILE C 210 -51.15 -121.96 REMARK 500 THR C 242 -61.53 -93.85 REMARK 500 GLU C 260 19.93 -140.82 REMARK 500 ASN C 277 -161.63 -160.17 REMARK 500 ASP C 279 70.34 -69.95 REMARK 500 ASP C 349 50.59 -90.70 REMARK 500 GLU D 75 80.42 61.18 REMARK 500 ASN D 77 2.27 -68.98 REMARK 500 PHE D 125 59.98 -95.50 REMARK 500 THR D 163 -158.23 -75.81 REMARK 500 REMARK 500 THIS ENTRY HAS 96 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-22641 RELATED DB: EMDB REMARK 900 MURINE POLYOMAVIRUS HEXAVALENT CAPSOMER WITH 8A7H5 FAB, SUBPARTICLE REMARK 900 RECONSTRUCTION DBREF 7K23L2 1 109 PDB 7K23 7K23 1 109 DBREF 7K23H2 1 117 PDB 7K23 7K23 1 117 DBREF1 7K23 A -15 367 UNP A0A247D727_POVM1 DBREF2 7K23 A A0A247D727 2 384 DBREF1 7K23 B -15 367 UNP A0A247D727_POVM1 DBREF2 7K23 B A0A247D727 2 384 DBREF1 7K23 C -15 367 UNP A0A247D727_POVM1 DBREF2 7K23 C A0A247D727 2 384 DBREF1 7K23 D -15 367 UNP A0A247D727_POVM1 DBREF2 7K23 D A0A247D727 2 384 DBREF1 7K23 E -15 367 UNP A0A247D727_POVM1 DBREF2 7K23 E A0A247D727 2 384 DBREF 7K23L3 1 109 PDB 7K23 7K23 1 109 DBREF 7K23H3 1 117 PDB 7K23 7K23 1 117 DBREF 7K23L4 1 109 PDB 7K23 7K23 1 109 DBREF 7K23H4 1 117 PDB 7K23 7K23 1 117 DBREF 7K23L5 1 109 PDB 7K23 7K23 1 109 DBREF 7K23H5 1 117 PDB 7K23 7K23 1 117 DBREF 7K23L6 1 109 PDB 7K23 7K23 1 109 DBREF 7K23H6 1 117 PDB 7K23 7K23 1 117 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 1 A 383 ALA PRO LYS ARG LYS SER GLY VAL SER LYS CYS GLU THR SEQRES 2 A 383 LYS CYS THR LYS ALA CYS PRO ARG PRO ALA PRO VAL PRO SEQRES 3 A 383 LYS LEU LEU ILE LYS GLY GLY MET GLU VAL LEU ASP LEU SEQRES 4 A 383 VAL THR GLY PRO ASP SER VAL THR GLU ILE GLU ALA PHE SEQRES 5 A 383 LEU ASN PRO ARG MET GLY GLN PRO PRO THR PRO GLU SER SEQRES 6 A 383 LEU THR GLU GLY GLY GLN TYR TYR GLY TRP SER ARG GLY SEQRES 7 A 383 ILE ASN LEU ALA THR SER ASP THR GLU ASP SER PRO GLU SEQRES 8 A 383 ASN ASN THR LEU PRO THR TRP SER MET ALA LYS LEU GLN SEQRES 9 A 383 LEU PRO MET LEU ASN GLU ASP LEU THR CYS ASP THR LEU SEQRES 10 A 383 GLN MET TRP GLU ALA VAL SER VAL LYS THR GLU VAL VAL SEQRES 11 A 383 GLY SER GLY SER LEU LEU ASP VAL HIS GLY PHE ASN LYS SEQRES 12 A 383 PRO THR ASP THR VAL ASN THR LYS GLY ILE SER THR PRO SEQRES 13 A 383 VAL GLU GLY SER GLN TYR HIS VAL PHE ALA VAL GLY GLY SEQRES 14 A 383 GLU PRO LEU ASP LEU GLN GLY LEU VAL THR ASP ALA ARG SEQRES 15 A 383 THR LYS TYR LYS GLU GLU GLY VAL VAL THR ILE LYS THR SEQRES 16 A 383 ILE THR LYS LYS ASP MET VAL ASN LYS ASP GLN VAL LEU SEQRES 17 A 383 ASN PRO ILE SER LYS ALA LYS LEU ASP LYS ASP GLY MET SEQRES 18 A 383 TYR PRO VAL GLU ILE TRP HIS PRO ASP PRO ALA LYS ASN SEQRES 19 A 383 GLU ASN THR ARG TYR PHE GLY ASN TYR THR GLY GLY THR SEQRES 20 A 383 THR THR PRO PRO VAL LEU GLN PHE THR ASN THR LEU THR SEQRES 21 A 383 THR VAL LEU LEU ASP GLU ASN GLY VAL GLY PRO LEU CYS SEQRES 22 A 383 LYS GLY GLU GLY LEU TYR LEU SER CYS VAL ASP ILE MET SEQRES 23 A 383 GLY TRP ARG VAL THR ARG ASN TYR ASP VAL HIS HIS TRP SEQRES 24 A 383 ARG GLY LEU PRO ARG TYR PHE LYS ILE THR LEU ARG LYS SEQRES 25 A 383 ARG TRP VAL LYS ASN PRO TYR PRO MET ALA SER LEU ILE SEQRES 26 A 383 SER SER LEU PHE ASN ASN MET LEU PRO GLN VAL GLN GLY SEQRES 27 A 383 GLN PRO MET GLU GLY GLU ASN THR GLN VAL GLU GLU VAL SEQRES 28 A 383 ARG VAL TYR ASP GLY THR GLU PRO VAL PRO GLY ASP PRO SEQRES 29 A 383 ASP MET THR ARG TYR VAL ASP ARG PHE GLY LYS THR LYS SEQRES 30 A 383 THR VAL PHE PRO GLY ASN SEQRES 1 B 383 ALA PRO LYS ARG LYS SER GLY VAL SER LYS CYS GLU THR SEQRES 2 B 383 LYS CYS THR LYS ALA CYS PRO ARG PRO ALA PRO VAL PRO SEQRES 3 B 383 LYS LEU LEU ILE LYS GLY GLY MET GLU VAL LEU ASP LEU SEQRES 4 B 383 VAL THR GLY PRO ASP SER VAL THR GLU ILE GLU ALA PHE SEQRES 5 B 383 LEU ASN PRO ARG MET GLY GLN PRO PRO THR PRO GLU SER SEQRES 6 B 383 LEU THR GLU GLY GLY GLN TYR TYR GLY TRP SER ARG GLY SEQRES 7 B 383 ILE ASN LEU ALA THR SER ASP THR GLU ASP SER PRO GLU SEQRES 8 B 383 ASN ASN THR LEU PRO THR TRP SER MET ALA LYS LEU GLN SEQRES 9 B 383 LEU PRO MET LEU ASN GLU ASP LEU THR CYS ASP THR LEU SEQRES 10 B 383 GLN MET TRP GLU ALA VAL SER VAL LYS THR GLU VAL VAL SEQRES 11 B 383 GLY SER GLY SER LEU LEU ASP VAL HIS GLY PHE ASN LYS SEQRES 12 B 383 PRO THR ASP THR VAL ASN THR LYS GLY ILE SER THR PRO SEQRES 13 B 383 VAL GLU GLY SER GLN TYR HIS VAL PHE ALA VAL GLY GLY SEQRES 14 B 383 GLU PRO LEU ASP LEU GLN GLY LEU VAL THR ASP ALA ARG SEQRES 15 B 383 THR LYS TYR LYS GLU GLU GLY VAL VAL THR ILE LYS THR SEQRES 16 B 383 ILE THR LYS LYS ASP MET VAL ASN LYS ASP GLN VAL LEU SEQRES 17 B 383 ASN PRO ILE SER LYS ALA LYS LEU ASP LYS ASP GLY MET SEQRES 18 B 383 TYR PRO VAL GLU ILE TRP HIS PRO ASP PRO ALA LYS ASN SEQRES 19 B 383 GLU ASN THR ARG TYR PHE GLY ASN TYR THR GLY GLY THR SEQRES 20 B 383 THR THR PRO PRO VAL LEU GLN PHE THR ASN THR LEU THR SEQRES 21 B 383 THR VAL LEU LEU ASP GLU ASN GLY VAL GLY PRO LEU CYS SEQRES 22 B 383 LYS GLY GLU GLY LEU TYR LEU SER CYS VAL ASP ILE MET SEQRES 23 B 383 GLY TRP ARG VAL THR ARG ASN TYR ASP VAL HIS HIS TRP SEQRES 24 B 383 ARG GLY LEU PRO ARG TYR PHE LYS ILE THR LEU ARG LYS SEQRES 25 B 383 ARG TRP VAL LYS ASN PRO TYR PRO MET ALA SER LEU ILE SEQRES 26 B 383 SER SER LEU PHE ASN ASN MET LEU PRO GLN VAL GLN GLY SEQRES 27 B 383 GLN PRO MET GLU GLY GLU ASN THR GLN VAL GLU GLU VAL SEQRES 28 B 383 ARG VAL TYR ASP GLY THR GLU PRO VAL PRO GLY ASP PRO SEQRES 29 B 383 ASP MET THR ARG TYR VAL ASP ARG PHE GLY LYS THR LYS SEQRES 30 B 383 THR VAL PHE PRO GLY ASN SEQRES 1 C 383 ALA PRO LYS ARG LYS SER GLY VAL SER LYS CYS GLU THR SEQRES 2 C 383 LYS CYS THR LYS ALA CYS PRO ARG PRO ALA PRO VAL PRO SEQRES 3 C 383 LYS LEU LEU ILE LYS GLY GLY MET GLU VAL LEU ASP LEU SEQRES 4 C 383 VAL THR GLY PRO ASP SER VAL THR GLU ILE GLU ALA PHE SEQRES 5 C 383 LEU ASN PRO ARG MET GLY GLN PRO PRO THR PRO GLU SER SEQRES 6 C 383 LEU THR GLU GLY GLY GLN TYR TYR GLY TRP SER ARG GLY SEQRES 7 C 383 ILE ASN LEU ALA THR SER ASP THR GLU ASP SER PRO GLU SEQRES 8 C 383 ASN ASN THR LEU PRO THR TRP SER MET ALA LYS LEU GLN SEQRES 9 C 383 LEU PRO MET LEU ASN GLU ASP LEU THR CYS ASP THR LEU SEQRES 10 C 383 GLN MET TRP GLU ALA VAL SER VAL LYS THR GLU VAL VAL SEQRES 11 C 383 GLY SER GLY SER LEU LEU ASP VAL HIS GLY PHE ASN LYS SEQRES 12 C 383 PRO THR ASP THR VAL ASN THR LYS GLY ILE SER THR PRO SEQRES 13 C 383 VAL GLU GLY SER GLN TYR HIS VAL PHE ALA VAL GLY GLY SEQRES 14 C 383 GLU PRO LEU ASP LEU GLN GLY LEU VAL THR ASP ALA ARG SEQRES 15 C 383 THR LYS TYR LYS GLU GLU GLY VAL VAL THR ILE LYS THR SEQRES 16 C 383 ILE THR LYS LYS ASP MET VAL ASN LYS ASP GLN VAL LEU SEQRES 17 C 383 ASN PRO ILE SER LYS ALA LYS LEU ASP LYS ASP GLY MET SEQRES 18 C 383 TYR PRO VAL GLU ILE TRP HIS PRO ASP PRO ALA LYS ASN SEQRES 19 C 383 GLU ASN THR ARG TYR PHE GLY ASN TYR THR GLY GLY THR SEQRES 20 C 383 THR THR PRO PRO VAL LEU GLN PHE THR ASN THR LEU THR SEQRES 21 C 383 THR VAL LEU LEU ASP GLU ASN GLY VAL GLY PRO LEU CYS SEQRES 22 C 383 LYS GLY GLU GLY LEU TYR LEU SER CYS VAL ASP ILE MET SEQRES 23 C 383 GLY TRP ARG VAL THR ARG ASN TYR ASP VAL HIS HIS TRP SEQRES 24 C 383 ARG GLY LEU PRO ARG TYR PHE LYS ILE THR LEU ARG LYS SEQRES 25 C 383 ARG TRP VAL LYS ASN PRO TYR PRO MET ALA SER LEU ILE SEQRES 26 C 383 SER SER LEU PHE ASN ASN MET LEU PRO GLN VAL GLN GLY SEQRES 27 C 383 GLN PRO MET GLU GLY GLU ASN THR GLN VAL GLU GLU VAL SEQRES 28 C 383 ARG VAL TYR ASP GLY THR GLU PRO VAL PRO GLY ASP PRO SEQRES 29 C 383 ASP MET THR ARG TYR VAL ASP ARG PHE GLY LYS THR LYS SEQRES 30 C 383 THR VAL PHE PRO GLY ASN SEQRES 1 D 383 ALA PRO LYS ARG LYS SER GLY VAL SER LYS CYS GLU THR SEQRES 2 D 383 LYS CYS THR LYS ALA CYS PRO ARG PRO ALA PRO VAL PRO SEQRES 3 D 383 LYS LEU LEU ILE LYS GLY GLY MET GLU VAL LEU ASP LEU SEQRES 4 D 383 VAL THR GLY PRO ASP SER VAL THR GLU ILE GLU ALA PHE SEQRES 5 D 383 LEU ASN PRO ARG MET GLY GLN PRO PRO THR PRO GLU SER SEQRES 6 D 383 LEU THR GLU GLY GLY GLN TYR TYR GLY TRP SER ARG GLY SEQRES 7 D 383 ILE ASN LEU ALA THR SER ASP THR GLU ASP SER PRO GLU SEQRES 8 D 383 ASN ASN THR LEU PRO THR TRP SER MET ALA LYS LEU GLN SEQRES 9 D 383 LEU PRO MET LEU ASN GLU ASP LEU THR CYS ASP THR LEU SEQRES 10 D 383 GLN MET TRP GLU ALA VAL SER VAL LYS THR GLU VAL VAL SEQRES 11 D 383 GLY SER GLY SER LEU LEU ASP VAL HIS GLY PHE ASN LYS SEQRES 12 D 383 PRO THR ASP THR VAL ASN THR LYS GLY ILE SER THR PRO SEQRES 13 D 383 VAL GLU GLY SER GLN TYR HIS VAL PHE ALA VAL GLY GLY SEQRES 14 D 383 GLU PRO LEU ASP LEU GLN GLY LEU VAL THR ASP ALA ARG SEQRES 15 D 383 THR LYS TYR LYS GLU GLU GLY VAL VAL THR ILE LYS THR SEQRES 16 D 383 ILE THR LYS LYS ASP MET VAL ASN LYS ASP GLN VAL LEU SEQRES 17 D 383 ASN PRO ILE SER LYS ALA LYS LEU ASP LYS ASP GLY MET SEQRES 18 D 383 TYR PRO VAL GLU ILE TRP HIS PRO ASP PRO ALA LYS ASN SEQRES 19 D 383 GLU ASN THR ARG TYR PHE GLY ASN TYR THR GLY GLY THR SEQRES 20 D 383 THR THR PRO PRO VAL LEU GLN PHE THR ASN THR LEU THR SEQRES 21 D 383 THR VAL LEU LEU ASP GLU ASN GLY VAL GLY PRO LEU CYS SEQRES 22 D 383 LYS GLY GLU GLY LEU TYR LEU SER CYS VAL ASP ILE MET SEQRES 23 D 383 GLY TRP ARG VAL THR ARG ASN TYR ASP VAL HIS HIS TRP SEQRES 24 D 383 ARG GLY LEU PRO ARG TYR PHE LYS ILE THR LEU ARG LYS SEQRES 25 D 383 ARG TRP VAL LYS ASN PRO TYR PRO MET ALA SER LEU ILE SEQRES 26 D 383 SER SER LEU PHE ASN ASN MET LEU PRO GLN VAL GLN GLY SEQRES 27 D 383 GLN PRO MET GLU GLY GLU ASN THR GLN VAL GLU GLU VAL SEQRES 28 D 383 ARG VAL TYR ASP GLY THR GLU PRO VAL PRO GLY ASP PRO SEQRES 29 D 383 ASP MET THR ARG TYR VAL ASP ARG PHE GLY LYS THR LYS SEQRES 30 D 383 THR VAL PHE PRO GLY ASN SEQRES 1 E 383 ALA PRO LYS ARG LYS SER GLY VAL SER LYS CYS GLU THR SEQRES 2 E 383 LYS CYS THR LYS ALA CYS PRO ARG PRO ALA PRO VAL PRO SEQRES 3 E 383 LYS LEU LEU ILE LYS GLY GLY MET GLU VAL LEU ASP LEU SEQRES 4 E 383 VAL THR GLY PRO ASP SER VAL THR GLU ILE GLU ALA PHE SEQRES 5 E 383 LEU ASN PRO ARG MET GLY GLN PRO PRO THR PRO GLU SER SEQRES 6 E 383 LEU THR GLU GLY GLY GLN TYR TYR GLY TRP SER ARG GLY SEQRES 7 E 383 ILE ASN LEU ALA THR SER ASP THR GLU ASP SER PRO GLU SEQRES 8 E 383 ASN ASN THR LEU PRO THR TRP SER MET ALA LYS LEU GLN SEQRES 9 E 383 LEU PRO MET LEU ASN GLU ASP LEU THR CYS ASP THR LEU SEQRES 10 E 383 GLN MET TRP GLU ALA VAL SER VAL LYS THR GLU VAL VAL SEQRES 11 E 383 GLY SER GLY SER LEU LEU ASP VAL HIS GLY PHE ASN LYS SEQRES 12 E 383 PRO THR ASP THR VAL ASN THR LYS GLY ILE SER THR PRO SEQRES 13 E 383 VAL GLU GLY SER GLN TYR HIS VAL PHE ALA VAL GLY GLY SEQRES 14 E 383 GLU PRO LEU ASP LEU GLN GLY LEU VAL THR ASP ALA ARG SEQRES 15 E 383 THR LYS TYR LYS GLU GLU GLY VAL VAL THR ILE LYS THR SEQRES 16 E 383 ILE THR LYS LYS ASP MET VAL ASN LYS ASP GLN VAL LEU SEQRES 17 E 383 ASN PRO ILE SER LYS ALA LYS LEU ASP LYS ASP GLY MET SEQRES 18 E 383 TYR PRO VAL GLU ILE TRP HIS PRO ASP PRO ALA LYS ASN SEQRES 19 E 383 GLU ASN THR ARG TYR PHE GLY ASN TYR THR GLY GLY THR SEQRES 20 E 383 THR THR PRO PRO VAL LEU GLN PHE THR ASN THR LEU THR SEQRES 21 E 383 THR VAL LEU LEU ASP GLU ASN GLY VAL GLY PRO LEU CYS SEQRES 22 E 383 LYS GLY GLU GLY LEU TYR LEU SER CYS VAL ASP ILE MET SEQRES 23 E 383 GLY TRP ARG VAL THR ARG ASN TYR ASP VAL HIS HIS TRP SEQRES 24 E 383 ARG GLY LEU PRO ARG TYR PHE LYS ILE THR LEU ARG LYS SEQRES 25 E 383 ARG TRP VAL LYS ASN PRO TYR PRO MET ALA SER LEU ILE SEQRES 26 E 383 SER SER LEU PHE ASN ASN MET LEU PRO GLN VAL GLN GLY SEQRES 27 E 383 GLN PRO MET GLU GLY GLU ASN THR GLN VAL GLU GLU VAL SEQRES 28 E 383 ARG VAL TYR ASP GLY THR GLU PRO VAL PRO GLY ASP PRO SEQRES 29 E 383 ASP MET THR ARG TYR VAL ASP ARG PHE GLY LYS THR LYS SEQRES 30 E 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 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 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 1L6 109 ASP ILE VAL MET THR GLN SER PRO THR SER MET SER ILE SEQRES 2L6 109 SER VAL GLY ASP ARG VAL THR MET ASN CYS ARG ALA SER SEQRES 3L6 109 GLN ASN VAL TYR SER ASN VAL ASP TRP TYR GLN GLN LYS SEQRES 4L6 109 THR GLY GLN SER PRO LYS LEU VAL ILE TYR LYS ALA SER SEQRES 5L6 109 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6L6 109 GLY SER GLY THR TYR PHE THR LEU THR ILE THR ASN ILE SEQRES 7L6 109 GLN THR GLU ASP LEU ALA VAL TYR TYR CYS LEU GLN SER SEQRES 8L6 109 ASN ALA PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9L6 109 GLU THR THR ARG ALA SEQRES 1H6 117 GLU GLU SER GLY GLY GLY LEU VAL GLN PRO GLY LYS SER SEQRES 2H6 117 LEU LYS LEU SER CYS SER ALA SER GLY PHE THR PHE SER SEQRES 3H6 117 SER TYR GLY MET HIS TRP ILE ARG GLN VAL PRO GLY LYS SEQRES 4H6 117 GLY LEU ASP TRP VAL ALA TYR ILE SER SER ALA SER ASP SEQRES 5H6 117 THR PHE TYR ALA ASP ALA VAL LYS GLU ARG PHE THR ILE SEQRES 6H6 117 SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU ARG LEU SEQRES 7H6 117 ASN SER LEU LYS SER GLU ASP THR ALA ILE TYR TYR CYS SEQRES 8H6 117 ALA ARG THR ARG TYR PRO THR ASP HIS PHE TYR ASP TRP SEQRES 9H6 117 PHE PRO TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER HELIX 1 AA1 TYRL2 49 SERL2 52 5 4 HELIX 2 AA2 GLNL2 79 LEUL2 83 5 5 HELIX 3 AA3 THRH2 24 TYRH2 28 5 5 HELIX 4 AA4 GLY A 17 LEU A 23 5 7 HELIX 5 AA5 GLU A 75 LEU A 79 5 5 HELIX 6 AA6 SER A 116 ASP A 121 5 6 HELIX 7 AA7 THR A 176 LYS A 182 1 7 HELIX 8 AA8 VAL A 186 GLN A 190 5 5 HELIX 9 AA9 GLU A 326 THR A 330 5 5 HELIX 10 AB1 GLY B 17 LEU B 23 5 7 HELIX 11 AB2 SER B 116 ASP B 121 5 6 HELIX 12 AB3 THR B 176 THR B 181 1 6 HELIX 13 AB4 ASN B 187 VAL B 191 5 5 HELIX 14 AB5 PRO B 304 ASN B 315 1 12 HELIX 15 AB6 GLY C 17 LEU C 23 5 7 HELIX 16 AB7 SER C 116 ASP C 121 5 6 HELIX 17 AB8 THR C 176 LYS C 182 1 7 HELIX 18 AB9 VAL C 186 GLN C 190 5 5 HELIX 19 AC1 PRO C 304 ASN C 315 1 12 HELIX 20 AC2 TYR C 353 PHE C 357 5 5 HELIX 21 AC3 GLY D 17 LEU D 23 5 7 HELIX 22 AC4 GLU D 75 LEU D 79 5 5 HELIX 23 AC5 SER D 116 ASP D 121 5 6 HELIX 24 AC6 THR D 176 THR D 181 1 6 HELIX 25 AC7 ASN D 187 VAL D 191 5 5 HELIX 26 AC8 PRO D 304 LEU D 317 1 14 HELIX 27 AC9 GLY E 17 ASP E 22 5 6 HELIX 28 AD1 GLU E 75 LEU E 79 5 5 HELIX 29 AD2 SER E 116 ASP E 121 5 6 HELIX 30 AD3 THR E 176 THR E 181 1 6 HELIX 31 AD4 VAL E 186 VAL E 191 5 6 HELIX 32 AD5 PRO E 304 LEU E 317 1 14 HELIX 33 AD6 TYRL3 49 SERL3 52 5 4 HELIX 34 AD7 GLNL3 79 LEUL3 83 5 5 HELIX 35 AD8 THRH3 24 TYRH3 28 5 5 HELIX 36 AD9 TYRL4 49 SERL4 52 5 4 HELIX 37 AE1 GLNL4 79 LEUL4 83 5 5 HELIX 38 AE2 THRH4 24 TYRH4 28 5 5 HELIX 39 AE3 TYRL5 49 SERL5 52 5 4 HELIX 40 AE4 GLNL5 79 LEUL5 83 5 5 HELIX 41 AE5 THRH5 24 TYRH5 28 5 5 HELIX 42 AE6 TYRL6 49 SERL6 52 5 4 HELIX 43 AE7 GLNL6 79 LEUL6 83 5 5 HELIX 44 AE8 THRH6 24 TYRH6 28 5 5 SHEET 1 AA1 4 METL2 4 GLNL2 6 0 SHEET 2 AA1 4 VALL2 19 VALL2 29 -1 O ARGL2 24 N THRL2 5 SHEET 3 AA1 4 GLYL2 68 ILEL2 75 -1 O PHEL2 71 N CYSL2 23 SHEET 4 AA1 4 PHEL2 62 GLYL2 66 -1 N THRL2 63 O THRL2 74 SHEET 1 AA2 3 LYSL2 45 ILEL2 48 0 SHEET 2 AA2 3 VALL2 33 GLNL2 38 -1 N GLNL2 37 O LYSL2 45 SHEET 3 AA2 3 VALL2 85 GLNL2 90 -1 O TYRL2 87 N TYRL2 36 SHEET 1 AA3 3 CYSH2 18 SERH2 19 0 SHEET 2 AA3 3 THRH2 73 ARGH2 77 -1 O LEUH2 74 N CYSH2 18 SHEET 3 AA3 3 THRH2 64 ASPH2 68 -1 N THRH2 64 O ARGH2 77 SHEET 1 AA4 5 THRH2 53 TYRH2 55 0 SHEET 2 AA4 5 GLYH2 40 ILEH2 47 -1 N TYRH2 46 O PHEH2 54 SHEET 3 AA4 5 METH2 30 VALH2 36 -1 N ARGH2 34 O ASPH2 42 SHEET 4 AA4 5 ILEH2 88 ARGH2 93 -1 O ILEH2 88 N GLNH2 35 SHEET 5 AA4 5 TYRH2 107 TRPH2 108 -1 O TYRH2 107 N ARGH2 93 SHEET 1 AA5 4 VAL A 30 LEU A 37 0 SHEET 2 AA5 4 ARG A 288 LYS A 300 -1 O LEU A 294 N THR A 31 SHEET 3 AA5 4 THR A 100 VAL A 113 -1 N LEU A 101 O VAL A 299 SHEET 4 AA5 4 THR A 245 VAL A 246 -1 O THR A 245 N VAL A 109 SHEET 1 AA6 3 SER A 83 GLN A 88 0 SHEET 2 AA6 3 GLY A 261 VAL A 274 -1 O LEU A 262 N LEU A 87 SHEET 3 AA6 3 HIS A 281 GLY A 285 -1 O ARG A 284 N MET A 270 SHEET 1 AA7 5 SER A 83 GLN A 88 0 SHEET 2 AA7 5 GLY A 261 VAL A 274 -1 O LEU A 262 N LEU A 87 SHEET 3 AA7 5 GLN A 145 GLY A 152 -1 N GLY A 152 O TYR A 263 SHEET 4 AA7 5 THR A 221 THR A 228 -1 O ASN A 226 N HIS A 147 SHEET 5 AA7 5 VAL E 236 THR E 240 -1 O LEU E 237 N TYR A 227 SHEET 1 AA8 2 PRO A 128 ASP A 130 0 SHEET 2 AA8 2 LYS A 135 SER A 138 -1 O LYS A 135 N ASP A 130 SHEET 1 AA9 3 LYS A 197 LYS A 199 0 SHEET 2 AA9 3 ASP A 157 GLY A 160 -1 N LEU A 158 O ALA A 198 SHEET 3 AA9 3 TRP A 211 PRO A 213 -1 O HIS A 212 N GLN A 159 SHEET 1 AB1 5 VAL A 236 THR A 240 0 SHEET 2 AB1 5 THR B 221 THR B 228 -1 O TYR B 227 N LEU A 237 SHEET 3 AB1 5 GLN B 145 GLY B 152 -1 N HIS B 147 O ASN B 226 SHEET 4 AB1 5 GLY B 261 VAL B 274 -1 O ILE B 269 N TYR B 146 SHEET 5 AB1 5 SER B 83 GLN B 88 -1 N SER B 83 O CYS B 266 SHEET 1 AB2 5 VAL A 236 THR A 240 0 SHEET 2 AB2 5 THR B 221 THR B 228 -1 O TYR B 227 N LEU A 237 SHEET 3 AB2 5 GLN B 145 GLY B 152 -1 N HIS B 147 O ASN B 226 SHEET 4 AB2 5 GLY B 261 VAL B 274 -1 O ILE B 269 N TYR B 146 SHEET 5 AB2 5 HIS B 281 GLY B 285 -1 O ARG B 284 N MET B 270 SHEET 1 AB3 2 ARG A 352 VAL A 354 0 SHEET 2 AB3 2 LYS A 359 LYS A 361 -1 O THR A 360 N TYR A 353 SHEET 1 AB4 4 THR B 31 LEU B 37 0 SHEET 2 AB4 4 ARG B 288 LYS B 300 -1 O LEU B 294 N THR B 31 SHEET 3 AB4 4 THR B 100 VAL B 113 -1 N GLU B 105 O ARG B 295 SHEET 4 AB4 4 GLU B 94 ASP B 95 -1 N ASP B 95 O THR B 100 SHEET 1 AB5 4 THR B 31 LEU B 37 0 SHEET 2 AB5 4 ARG B 288 LYS B 300 -1 O LEU B 294 N THR B 31 SHEET 3 AB5 4 THR B 100 VAL B 113 -1 N GLU B 105 O ARG B 295 SHEET 4 AB5 4 THR B 245 VAL B 246 -1 O THR B 245 N VAL B 109 SHEET 1 AB6 2 PRO B 128 ASP B 130 0 SHEET 2 AB6 2 LYS B 135 SER B 138 -1 O LYS B 135 N ASP B 130 SHEET 1 AB7 3 LYS B 197 ALA B 198 0 SHEET 2 AB7 3 LEU B 158 GLY B 160 -1 N LEU B 158 O ALA B 198 SHEET 3 AB7 3 TRP B 211 PRO B 213 -1 O HIS B 212 N GLN B 159 SHEET 1 AB8 5 VAL B 236 THR B 240 0 SHEET 2 AB8 5 THR C 221 THR C 228 -1 O TYR C 227 N LEU B 237 SHEET 3 AB8 5 GLN C 145 GLY C 152 -1 N VAL C 151 O ARG C 222 SHEET 4 AB8 5 GLY C 261 VAL C 274 -1 O VAL C 267 N VAL C 148 SHEET 5 AB8 5 SER C 83 GLN C 88 -1 N ALA C 85 O LEU C 264 SHEET 1 AB9 5 VAL B 236 THR B 240 0 SHEET 2 AB9 5 THR C 221 THR C 228 -1 O TYR C 227 N LEU B 237 SHEET 3 AB9 5 GLN C 145 GLY C 152 -1 N VAL C 151 O ARG C 222 SHEET 4 AB9 5 GLY C 261 VAL C 274 -1 O VAL C 267 N VAL C 148 SHEET 5 AB9 5 HIS C 281 GLY C 285 -1 O ARG C 284 N MET C 270 SHEET 1 AC1 2 ARG B 352 ASP B 355 0 SHEET 2 AC1 2 GLY B 358 LYS B 361 -1 O THR B 360 N TYR B 353 SHEET 1 AC2 4 VAL C 30 LEU C 37 0 SHEET 2 AC2 4 ARG C 288 LYS C 300 -1 O ARG C 288 N LEU C 37 SHEET 3 AC2 4 THR C 100 VAL C 113 -1 N LEU C 101 O VAL C 299 SHEET 4 AC2 4 THR C 245 VAL C 246 -1 O THR C 245 N VAL C 109 SHEET 1 AC3 2 PRO C 128 ASP C 130 0 SHEET 2 AC3 2 LYS C 135 SER C 138 -1 O LYS C 135 N ASP C 130 SHEET 1 AC4 3 LYS C 197 LYS C 199 0 SHEET 2 AC4 3 ASP C 157 GLY C 160 -1 N LEU C 158 O ALA C 198 SHEET 3 AC4 3 TRP C 211 PRO C 213 -1 O HIS C 212 N GLN C 159 SHEET 1 AC5 5 VAL C 236 THR C 240 0 SHEET 2 AC5 5 THR D 221 THR D 228 -1 O GLY D 225 N PHE C 239 SHEET 3 AC5 5 GLN D 145 GLY D 152 -1 N VAL D 151 O ARG D 222 SHEET 4 AC5 5 GLY D 261 TRP D 272 -1 O VAL D 267 N VAL D 148 SHEET 5 AC5 5 SER D 83 GLN D 88 -1 N LEU D 87 O LEU D 262 SHEET 1 AC6 5 VAL C 236 THR C 240 0 SHEET 2 AC6 5 THR D 221 THR D 228 -1 O GLY D 225 N PHE C 239 SHEET 3 AC6 5 GLN D 145 GLY D 152 -1 N VAL D 151 O ARG D 222 SHEET 4 AC6 5 GLY D 261 TRP D 272 -1 O VAL D 267 N VAL D 148 SHEET 5 AC6 5 TRP D 283 GLY D 285 -1 O ARG D 284 N MET D 270 SHEET 1 AC7 4 VAL D 30 LEU D 37 0 SHEET 2 AC7 4 ARG D 288 LYS D 300 -1 O PHE D 290 N ALA D 35 SHEET 3 AC7 4 THR D 100 VAL D 113 -1 N LEU D 101 O VAL D 299 SHEET 4 AC7 4 GLU D 94 ASP D 95 -1 N ASP D 95 O THR D 100 SHEET 1 AC8 4 VAL D 30 LEU D 37 0 SHEET 2 AC8 4 ARG D 288 LYS D 300 -1 O PHE D 290 N ALA D 35 SHEET 3 AC8 4 THR D 100 VAL D 113 -1 N LEU D 101 O VAL D 299 SHEET 4 AC8 4 THR D 245 VAL D 246 -1 O THR D 245 N VAL D 109 SHEET 1 AC9 2 PRO D 128 ASP D 130 0 SHEET 2 AC9 2 LYS D 135 SER D 138 -1 O LYS D 135 N ASP D 130 SHEET 1 AD1 3 LYS D 197 LYS D 199 0 SHEET 2 AD1 3 ASP D 157 GLY D 160 -1 N LEU D 158 O ALA D 198 SHEET 3 AD1 3 TRP D 211 PRO D 213 -1 O HIS D 212 N GLN D 159 SHEET 1 AD2 5 VAL D 236 THR D 240 0 SHEET 2 AD2 5 THR E 221 THR E 228 -1 O TYR E 227 N LEU D 237 SHEET 3 AD2 5 GLN E 145 GLY E 152 -1 N VAL E 151 O ARG E 222 SHEET 4 AD2 5 GLY E 261 VAL E 274 -1 O VAL E 267 N VAL E 148 SHEET 5 AD2 5 SER E 83 GLN E 88 -1 N LEU E 87 O LEU E 262 SHEET 1 AD3 5 VAL D 236 THR D 240 0 SHEET 2 AD3 5 THR E 221 THR E 228 -1 O TYR E 227 N LEU D 237 SHEET 3 AD3 5 GLN E 145 GLY E 152 -1 N VAL E 151 O ARG E 222 SHEET 4 AD3 5 GLY E 261 VAL E 274 -1 O VAL E 267 N VAL E 148 SHEET 5 AD3 5 HIS E 281 GLY E 285 -1 O ARG E 284 N GLY E 271 SHEET 1 AD4 4 THR E 31 LEU E 37 0 SHEET 2 AD4 4 ARG E 288 LYS E 300 -1 O LEU E 294 N THR E 31 SHEET 3 AD4 4 THR E 100 VAL E 113 -1 N MET E 103 O ARG E 297 SHEET 4 AD4 4 THR E 245 VAL E 246 -1 O THR E 245 N VAL E 109 SHEET 1 AD5 2 PRO E 128 ASP E 130 0 SHEET 2 AD5 2 LYS E 135 SER E 138 -1 O LYS E 135 N ASP E 130 SHEET 1 AD6 3 LYS E 197 LYS E 199 0 SHEET 2 AD6 3 ASP E 157 GLY E 160 -1 N LEU E 158 O ALA E 198 SHEET 3 AD6 3 TRP E 211 PRO E 213 -1 O HIS E 212 N GLN E 159 SHEET 1 AD7 2 THR E 351 VAL E 354 0 SHEET 2 AD7 2 LYS E 359 THR E 362 -1 O THR E 362 N THR E 351 SHEET 1 AD8 4 METL3 4 GLNL3 6 0 SHEET 2 AD8 4 VALL3 19 VALL3 29 -1 O ARGL3 24 N THRL3 5 SHEET 3 AD8 4 GLYL3 68 ILEL3 75 -1 O PHEL3 71 N CYSL3 23 SHEET 4 AD8 4 PHEL3 62 GLYL3 66 -1 N THRL3 63 O THRL3 74 SHEET 1 AD9 3 LYSL3 45 ILEL3 48 0 SHEET 2 AD9 3 VALL3 33 GLNL3 38 -1 N GLNL3 37 O LYSL3 45 SHEET 3 AD9 3 VALL3 85 GLNL3 90 -1 O TYRL3 87 N TYRL3 36 SHEET 1 AE1 3 CYSH3 18 SERH3 19 0 SHEET 2 AE1 3 THRH3 73 ARGH3 77 -1 O LEUH3 74 N CYSH3 18 SHEET 3 AE1 3 THRH3 64 ASPH3 68 -1 N THRH3 64 O ARGH3 77 SHEET 1 AE2 5 THRH3 53 TYRH3 55 0 SHEET 2 AE2 5 GLYH3 40 ILEH3 47 -1 N TYRH3 46 O PHEH3 54 SHEET 3 AE2 5 METH3 30 VALH3 36 -1 N ARGH3 34 O ASPH3 42 SHEET 4 AE2 5 ILEH3 88 ARGH3 93 -1 O ILEH3 88 N GLNH3 35 SHEET 5 AE2 5 TYRH3 107 TRPH3 108 -1 O TYRH3 107 N ARGH3 93 SHEET 1 AE3 4 METL4 4 GLNL4 6 0 SHEET 2 AE3 4 VALL4 19 VALL4 29 -1 O ARGL4 24 N THRL4 5 SHEET 3 AE3 4 GLYL4 68 ILEL4 75 -1 O PHEL4 71 N CYSL4 23 SHEET 4 AE3 4 PHEL4 62 GLYL4 66 -1 N THRL4 63 O THRL4 74 SHEET 1 AE4 3 LYSL4 45 ILEL4 48 0 SHEET 2 AE4 3 VALL4 33 GLNL4 38 -1 N GLNL4 37 O LYSL4 45 SHEET 3 AE4 3 VALL4 85 GLNL4 90 -1 O TYRL4 87 N TYRL4 36 SHEET 1 AE5 3 CYSH4 18 SERH4 19 0 SHEET 2 AE5 3 THRH4 73 ARGH4 77 -1 O LEUH4 74 N CYSH4 18 SHEET 3 AE5 3 THRH4 64 ASPH4 68 -1 N THRH4 64 O ARGH4 77 SHEET 1 AE6 5 THRH4 53 TYRH4 55 0 SHEET 2 AE6 5 GLYH4 40 ILEH4 47 -1 N TYRH4 46 O PHEH4 54 SHEET 3 AE6 5 METH4 30 VALH4 36 -1 N ARGH4 34 O ASPH4 42 SHEET 4 AE6 5 ILEH4 88 ARGH4 93 -1 O ILEH4 88 N GLNH4 35 SHEET 5 AE6 5 TYRH4 107 TRPH4 108 -1 O TYRH4 107 N ARGH4 93 SHEET 1 AE7 4 METL5 4 GLNL5 6 0 SHEET 2 AE7 4 VALL5 19 VALL5 29 -1 O ARGL5 24 N THRL5 5 SHEET 3 AE7 4 GLYL5 68 ILEL5 75 -1 O PHEL5 71 N CYSL5 23 SHEET 4 AE7 4 PHEL5 62 GLYL5 66 -1 N THRL5 63 O THRL5 74 SHEET 1 AE8 3 LYSL5 45 ILEL5 48 0 SHEET 2 AE8 3 VALL5 33 GLNL5 38 -1 N GLNL5 37 O LYSL5 45 SHEET 3 AE8 3 VALL5 85 GLNL5 90 -1 O TYRL5 87 N TYRL5 36 SHEET 1 AE9 3 CYSH5 18 SERH5 19 0 SHEET 2 AE9 3 THRH5 73 ARGH5 77 -1 O LEUH5 74 N CYSH5 18 SHEET 3 AE9 3 THRH5 64 ASPH5 68 -1 N THRH5 64 O ARGH5 77 SHEET 1 AF1 5 THRH5 53 TYRH5 55 0 SHEET 2 AF1 5 GLYH5 40 ILEH5 47 -1 N TYRH5 46 O PHEH5 54 SHEET 3 AF1 5 METH5 30 VALH5 36 -1 N ARGH5 34 O ASPH5 42 SHEET 4 AF1 5 ILEH5 88 ARGH5 93 -1 O ILEH5 88 N GLNH5 35 SHEET 5 AF1 5 TYRH5 107 TRPH5 108 -1 O TYRH5 107 N ARGH5 93 SHEET 1 AF2 4 METL6 4 GLNL6 6 0 SHEET 2 AF2 4 VALL6 19 VALL6 29 -1 O ARGL6 24 N THRL6 5 SHEET 3 AF2 4 GLYL6 68 ILEL6 75 -1 O PHEL6 71 N CYSL6 23 SHEET 4 AF2 4 PHEL6 62 GLYL6 66 -1 N THRL6 63 O THRL6 74 SHEET 1 AF3 3 LYSL6 45 ILEL6 48 0 SHEET 2 AF3 3 VALL6 33 GLNL6 38 -1 N GLNL6 37 O LYSL6 45 SHEET 3 AF3 3 VALL6 85 GLNL6 90 -1 O TYRL6 87 N TYRL6 36 SHEET 1 AF4 3 CYSH6 18 SERH6 19 0 SHEET 2 AF4 3 THRH6 73 ARGH6 77 -1 O LEUH6 74 N CYSH6 18 SHEET 3 AF4 3 THRH6 64 ASPH6 68 -1 N THRH6 64 O ARGH6 77 SHEET 1 AF5 5 THRH6 53 TYRH6 55 0 SHEET 2 AF5 5 GLYH6 40 ILEH6 47 -1 N TYRH6 46 O PHEH6 54 SHEET 3 AF5 5 METH6 30 VALH6 36 -1 N ARGH6 34 O ASPH6 42 SHEET 4 AF5 5 ILEH6 88 ARGH6 93 -1 O ILEH6 88 N GLNH6 35 SHEET 5 AF5 5 TYRH6 107 TRPH6 108 -1 O TYRH6 107 N ARGH6 93 SSBOND 1 CYSL2 23 CYSL2 88 1555 1555 2.03 SSBOND 2 CYSH2 18 CYSH2 91 1555 1555 2.02 SSBOND 3 CYS A 3 CYS B 98 1555 1555 2.03 SSBOND 4 CYS A 98 CYS E 3 1555 1555 2.03 SSBOND 5 CYS B 3 CYS C 98 1555 1555 2.04 SSBOND 6 CYS C 3 CYS D 98 1555 1555 2.03 SSBOND 7 CYS D 3 CYS E 98 1555 1555 2.02 SSBOND 8 CYSL3 23 CYSL3 88 1555 1555 2.03 SSBOND 9 CYSH3 18 CYSH3 91 1555 1555 2.02 SSBOND 10 CYSL4 23 CYSL4 88 1555 1555 2.03 SSBOND 11 CYSH4 18 CYSH4 91 1555 1555 2.02 SSBOND 12 CYSL5 23 CYSL5 88 1555 1555 2.03 SSBOND 13 CYSH5 18 CYSH5 91 1555 1555 2.02 SSBOND 14 CYSL6 23 CYSL6 88 1555 1555 2.03 SSBOND 15 CYSH6 18 CYSH6 91 1555 1555 2.02 CISPEP 1 PHEL2 94 PROL2 95 0 5.39 CISPEP 2 PHEL3 94 PROL3 95 0 5.38 CISPEP 3 PHEL4 94 PROL4 95 0 5.31 CISPEP 4 PHEL5 94 PROL5 95 0 5.31 CISPEP 5 PHEL6 94 PROL6 95 0 5.35 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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