HEADER VIRUS/IMMUNE SYSTEM 18-MAR-21 7M3L TITLE CANINE PARVOVIRUS AND FAB14 AT PARTIAL OCCUPANCY COMPND MOL_ID: 1; COMPND 2 MOLECULE: CAPSID PROTEIN 2; COMPND 3 CHAIN: A1; COMPND 4 SYNONYM: VP2; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB14 LIGHT CHAIN; COMPND 7 CHAIN: L2; COMPND 8 MOL_ID: 3; COMPND 9 MOLECULE: FAB14 HEAVY CHAIN; COMPND 10 CHAIN: H2 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CANINE PARVOVIRUS TYPE 2; SOURCE 3 ORGANISM_COMMON: CPV-2; SOURCE 4 ORGANISM_TAXID: 10788; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 7 ORGANISM_TAXID: 10090; SOURCE 8 MOL_ID: 3; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_TAXID: 10090 KEYWDS CANINE PARVOVIRUS, CPV, FAB14, VIRUS, VIRUS-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR D.J.GOTESCHIUS,S.R.HARTMANN,S.L.HAFENSTEIN JRNL AUTH D.J.GOETSCHIUS,S.R.HARTMANN,L.J.ORGANTINI,H.CALLAWAY, JRNL AUTH 2 K.HUANG,C.M.BATOR,R.E.ASHLEY,A.M.MAKHOV,J.F.CONWAY, JRNL AUTH 3 C.R.PARRISH,S.L.HAFENSTEIN JRNL TITL HIGH-RESOLUTION ASYMMETRIC STRUCTURE OF A FAB-VIRUS COMPLEX JRNL TITL 2 REVEALS OVERLAP WITH THE RECEPTOR BINDING SITE. JRNL REF PROC.NATL.ACAD.SCI.USA V. 118 2021 JRNL REFN ESSN 1091-6490 JRNL PMID 34074770 JRNL DOI 10.1073/PNAS.2025452118 REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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 : 95353 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 7M3L 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_1000255548. 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 : CANINE PARVOVIRUS WITH FAB; REMARK 245 CANINE PARVOVIRUS; FAB14 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI POLARA 300 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) : 60.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM 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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR REMARK 300 ICOSAHEDRAL POINT SYMMETRY (SCHOENFLIES SYMBOL = I). 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A1, L2, H2 REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 ASP A 3 REMARK 465 GLY A 4 REMARK 465 ALA A 5 REMARK 465 VAL A 6 REMARK 465 GLN A 7 REMARK 465 PRO A 8 REMARK 465 ASP A 9 REMARK 465 GLY A 10 REMARK 465 GLY A 11 REMARK 465 GLN A 12 REMARK 465 PRO A 13 REMARK 465 ALA A 14 REMARK 465 VAL A 15 REMARK 465 ARG A 16 REMARK 465 ASN A 17 REMARK 465 GLU A 18 REMARK 465 ARG A 19 REMARK 465 ALA A 20 REMARK 465 THR A 21 REMARK 465 GLY A 22 REMARK 465 SER A 23 REMARK 465 GLY A 24 REMARK 465 ASN A 25 REMARK 465 GLY A 26 REMARK 465 SER A 27 REMARK 465 GLY A 28 REMARK 465 GLY A 29 REMARK 465 GLY A 30 REMARK 465 GLY A 31 REMARK 465 GLY A 32 REMARK 465 GLY A 33 REMARK 465 GLY A 34 REMARK 465 SER A 35 REMARK 465 GLY A 36 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 O GLYA1 227 CE1 HISH2 101 1.55 REMARK 500 OD1 ASNA1 93 O GLYH2 102 1.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARGA1 332 C - N - CA ANGL. DEV. = 15.9 DEGREES 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 ASNA1 47 44.69 -140.49 REMARK 500 ASNA1 56 108.78 -54.55 REMARK 500 META1 87 72.37 -118.71 REMARK 500 ASNA1 115 71.89 -100.20 REMARK 500 TRPA1 126 -81.98 -66.71 REMARK 500 GLNA1 127 -22.11 32.23 REMARK 500 LEUA1 128 -16.91 -140.16 REMARK 500 ALAA1 157 67.20 60.83 REMARK 500 GLNA1 159 55.94 -151.59 REMARK 500 PROA1 238 42.60 -82.52 REMARK 500 ASNA1 282 43.60 -85.56 REMARK 500 ASNA1 292 50.90 -98.83 REMARK 500 SERA1 348 -158.88 -157.94 REMARK 500 PROA1 423 128.79 -32.71 REMARK 500 ASPA1 475 50.22 -92.07 REMARK 500 PROA1 512 44.48 -89.47 REMARK 500 ASNA1 557 28.02 -142.01 REMARK 500 ASNA1 565 -14.45 69.90 REMARK 500 ALAL2 32 46.92 36.15 REMARK 500 ALAL2 51 -5.04 65.72 REMARK 500 ALAH2 14 49.60 -93.44 REMARK 500 SERH2 15 -37.61 -130.79 REMARK 500 ALAH2 16 -167.36 -128.76 REMARK 500 ASPH2 89 34.69 -93.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 TRPA1 126 GLNA1 127 133.14 REMARK 500 THRA1 158 GLNA1 159 143.99 REMARK 500 GLNA1 159 PROA1 160 140.03 REMARK 500 LEUA1 422 PROA1 423 -126.65 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-23656 RELATED DB: EMDB REMARK 900 CANINE PARVOVIRUS AND FAB14 AT PARTIAL OCCUPANCY DBREF 7M3LA1 1 584 UNP B2ZG07 B2ZG07_PAVC 1 584 DBREF 7M3LL2 1 108 PDB 7M3L 7M3L 1 108 DBREF 7M3LH2 1 119 PDB 7M3L 7M3L 1 119 SEQRES 1A1 584 MET SER ASP GLY ALA VAL GLN PRO ASP GLY GLY GLN PRO SEQRES 2A1 584 ALA VAL ARG ASN GLU ARG ALA THR GLY SER GLY ASN GLY SEQRES 3A1 584 SER GLY GLY GLY GLY GLY GLY GLY SER GLY GLY VAL GLY SEQRES 4A1 584 ILE SER THR GLY THR PHE ASN ASN GLN THR GLU PHE LYS SEQRES 5A1 584 PHE LEU GLU ASN GLY TRP VAL GLU ILE THR ALA ASN SER SEQRES 6A1 584 SER ARG LEU VAL HIS LEU ASN MET PRO GLU SER GLU ASN SEQRES 7A1 584 TYR ARG ARG VAL VAL VAL ASN ASN MET ASP LYS THR ALA SEQRES 8A1 584 VAL ASN GLY ASN MET ALA LEU ASP ASP ILE HIS ALA GLN SEQRES 9A1 584 ILE VAL THR PRO TRP SER LEU VAL ASP ALA ASN ALA TRP SEQRES 10A1 584 GLY VAL TRP PHE ASN PRO GLY ASP TRP GLN LEU ILE VAL SEQRES 11A1 584 ASN THR MET SER GLU LEU HIS LEU VAL SER PHE GLU GLN SEQRES 12A1 584 GLU ILE PHE ASN VAL VAL LEU LYS THR VAL SER GLU SER SEQRES 13A1 584 ALA THR GLN PRO PRO THR LYS VAL TYR ASN ASN ASP LEU SEQRES 14A1 584 THR ALA SER LEU MET VAL ALA LEU ASP SER ASN ASN THR SEQRES 15A1 584 MET PRO PHE THR PRO ALA ALA MET ARG SER GLU THR LEU SEQRES 16A1 584 GLY PHE TYR PRO TRP LYS PRO THR ILE PRO THR PRO TRP SEQRES 17A1 584 ARG TYR TYR PHE GLN TRP ASP ARG THR LEU ILE PRO SER SEQRES 18A1 584 HIS THR GLY THR SER GLY THR PRO THR ASN ILE TYR HIS SEQRES 19A1 584 GLY THR ASP PRO ASP ASP VAL GLN PHE TYR THR ILE GLU SEQRES 20A1 584 ASN SER VAL PRO VAL HIS LEU LEU ARG THR GLY ASP GLU SEQRES 21A1 584 PHE ALA THR GLY THR PHE PHE PHE ASP CYS LYS PRO CYS SEQRES 22A1 584 ARG LEU THR HIS THR TRP GLN THR ASN ARG ALA LEU GLY SEQRES 23A1 584 LEU PRO PRO PHE LEU ASN SER LEU PRO GLN SER GLU GLY SEQRES 24A1 584 ALA THR ASN PHE GLY ASP ILE GLY VAL GLN GLN ASP LYS SEQRES 25A1 584 ARG ARG GLY VAL THR GLN MET GLY ASN THR ASN TYR ILE SEQRES 26A1 584 THR GLU ALA THR ILE MET ARG PRO ALA GLU VAL GLY TYR SEQRES 27A1 584 SER ALA PRO TYR TYR SER PHE GLU ALA SER THR GLN GLY SEQRES 28A1 584 PRO PHE LYS THR PRO ILE ALA ALA GLY ARG GLY GLY ALA SEQRES 29A1 584 GLN THR ASP GLU ASN GLN ALA ALA ASP GLY ASN PRO ARG SEQRES 30A1 584 TYR ALA PHE GLY ARG GLN HIS GLY GLN LYS THR THR THR SEQRES 31A1 584 THR GLY GLU THR PRO GLU ARG PHE THR TYR ILE ALA HIS SEQRES 32A1 584 GLN ASP THR GLY ARG TYR PRO GLU GLY ASP TRP ILE GLN SEQRES 33A1 584 ASN ILE ASN PHE ASN LEU PRO VAL THR ASN ASP ASN VAL SEQRES 34A1 584 LEU LEU PRO THR ASP PRO ILE GLY GLY LYS THR GLY ILE SEQRES 35A1 584 ASN TYR THR ASN ILE PHE ASN THR TYR GLY PRO LEU THR SEQRES 36A1 584 ALA LEU ASN ASN VAL PRO PRO VAL TYR PRO ASN GLY GLN SEQRES 37A1 584 ILE TRP ASP LYS GLU PHE ASP THR ASP LEU LYS PRO ARG SEQRES 38A1 584 LEU HIS VAL ASN ALA PRO PHE VAL CYS GLN ASN ASN CYS SEQRES 39A1 584 PRO GLY GLN LEU PHE VAL LYS VAL ALA PRO ASN LEU THR SEQRES 40A1 584 ASN GLU TYR ASP PRO ASP ALA SER ALA ASN MET SER ARG SEQRES 41A1 584 ILE VAL THR TYR SER ASP PHE TRP TRP LYS GLY LYS LEU SEQRES 42A1 584 VAL PHE LYS ALA LYS LEU ARG ALA SER HIS THR TRP ASN SEQRES 43A1 584 PRO ILE GLN GLN MET SER ILE ASN VAL ASP ASN GLN PHE SEQRES 44A1 584 ASN TYR VAL PRO SER ASN ILE GLY GLY MET LYS ILE VAL SEQRES 45A1 584 TYR GLU LYS SER GLN LEU ALA PRO ARG LYS LEU TYR SEQRES 1L2 108 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2L2 108 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3L2 108 GLN ASP VAL ASN THR ALA LEU ALA TRP TYR GLN GLN ILE SEQRES 4L2 108 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5L2 108 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR ALA SER SEQRES 6L2 108 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER VAL SEQRES 7L2 108 GLN ALA GLU ASP LEU ALA LEU TYR TYR CYS GLN GLN HIS SEQRES 8L2 108 TYR THR THR PRO TRP THR PHE GLY GLY GLY THR LYS LEU SEQRES 9L2 108 GLU ILE LYS ARG SEQRES 1H2 119 ALA VAL HIS LEU GLN GLY THR GLU LEU VAL LYS PRO GLY SEQRES 2H2 119 ALA SER ALA GLY VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3H2 119 TYR THR PHE THR ASN TYR ASP MET ASN TRP VAL ARG GLN SEQRES 4H2 119 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY TRP ILE PHE SEQRES 5H2 119 PRO GLY ASP GLY SER THR ARG TYR ASN GLU LYS PHE LYS SEQRES 6H2 119 GLY LYS ALA THR LEU THR THR ASP LYS SER SER SER THR SEQRES 7H2 119 ALA TYR GLN LEU ASN ARG LEU THR SER GLU ASP SER ALA SEQRES 8H2 119 VAL TYR PHE CYS ALA ARG ARG GLY SER HIS GLY SER TYR SEQRES 9H2 119 SER PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10H2 119 SER GLY HELIX 1 AA1 ALAA1 116 TRPA1 120 5 5 HELIX 2 AA2 ASNA1 122 TRPA1 126 5 5 HELIX 3 AA3 GLNA1 309 ARGA1 313 5 5 HELIX 4 AA4 TYRA1 409 ASPA1 413 5 5 HELIX 5 AA5 THRA1 425 ASPA1 427 5 3 HELIX 6 AA6 ASNA1 443 ILEA1 447 5 5 HELIX 7 AA7 ASNA1 554 GLNA1 558 5 5 HELIX 8 AA8 GLNL2 79 LEUL2 83 5 5 HELIX 9 AA9 THRH2 28 TYRH2 32 5 5 HELIX 10 AB1 GLUH2 62 LYSH2 65 5 4 SHEET 1 AA1 5 THRA1 49 PHEA1 53 0 SHEET 2 AA1 5 TRPA1 58 ASNA1 72 -1 O THRA1 62 N GLUA1 50 SHEET 3 AA1 5 THRA1 523 LEUA1 539 -1 O SERA1 525 N LEUA1 71 SHEET 4 AA1 5 META1 133 PHEA1 146 -1 N SERA1 134 O LYSA1 538 SHEET 5 AA1 5 PHEA1 261 ALAA1 262 -1 O PHEA1 261 N ILEA1 145 SHEET 1 AA2 5 LYSA1 163 ASNA1 167 0 SHEET 2 AA2 5 LEUA1 150 GLUA1 155 -1 N THRA1 152 O ASNA1 166 SHEET 3 AA2 5 THRA1 523 LEUA1 539 -1 O TYRA1 524 N LYSA1 151 SHEET 4 AA2 5 META1 133 PHEA1 146 -1 N SERA1 134 O LYSA1 538 SHEET 5 AA2 5 CYSA1 273 ARGA1 274 -1 O CYSA1 273 N LEUA1 136 SHEET 1 AA3 3 VALA1 82 VALA1 84 0 SHEET 2 AA3 3 HISA1 102 LEUA1 111 -1 O GLNA1 104 N VALA1 82 SHEET 3 AA3 3 THRA1 206 PHEA1 212 -1 O THRA1 206 N LEUA1 111 SHEET 1 AA4 5 VALA1 82 VALA1 84 0 SHEET 2 AA4 5 HISA1 102 LEUA1 111 -1 O GLNA1 104 N VALA1 82 SHEET 3 AA4 5 LEUA1 498 VALA1 502 -1 O VALA1 500 N SERA1 110 SHEET 4 AA4 5 LEUA1 173 LEUA1 177 -1 N ALAA1 176 O PHEA1 499 SHEET 5 AA4 5 VALA1 252 LEUA1 255 -1 O LEUA1 255 N LEUA1 173 SHEET 1 AA5 2 ASPA1 215 LEUA1 218 0 SHEET 2 AA5 2 ASNA1 231 GLYA1 235 -1 O GLYA1 235 N ASPA1 215 SHEET 1 AA6 2 THRA1 276 THRA1 278 0 SHEET 2 AA6 2 ALAA1 579 ARGA1 581 1 O ALAA1 579 N HISA1 277 SHEET 1 AA7 2 GLUA1 335 VALA1 336 0 SHEET 2 AA7 2 THRA1 455 ALAA1 456 1 O ALAA1 456 N GLUA1 335 SHEET 1 AA8 2 PHEA1 345 GLUA1 346 0 SHEET 2 AA8 2 PHEA1 353 LYSA1 354 -1 O PHEA1 353 N GLUA1 346 SHEET 1 AA9 2 ARGA1 377 PHEA1 380 0 SHEET 2 AA9 2 GLUA1 396 THRA1 399 -1 O GLUA1 396 N PHEA1 380 SHEET 1 AB1 2 ILEA1 415 GLNA1 416 0 SHEET 2 AB1 2 VALA1 429 LEUA1 430 -1 O LEUA1 430 N ILEA1 415 SHEET 1 AB2 2 TRPA1 470 LYSA1 472 0 SHEET 2 AB2 2 PHEA1 488 CYSA1 490 1 O CYSA1 490 N ASPA1 471 SHEET 1 AB3 4 METL2 4 GLNL2 6 0 SHEET 2 AB3 4 VALL2 19 VALL2 29 -1 O LYSL2 24 N THRL2 5 SHEET 3 AB3 4 GLYL2 68 ILEL2 75 -1 O PHEL2 73 N ILEL2 21 SHEET 4 AB3 4 PHEL2 62 GLYL2 66 -1 N THRL2 63 O THRL2 74 SHEET 1 AB4 6 PHEL2 10 THRL2 13 0 SHEET 2 AB4 6 THRL2 102 ILEL2 106 1 O GLUL2 105 N THRL2 13 SHEET 3 AB4 6 LEUL2 85 GLNL2 90 -1 N TYRL2 86 O THRL2 102 SHEET 4 AB4 6 LEUL2 33 GLNL2 38 -1 N ALAL2 34 O GLNL2 89 SHEET 5 AB4 6 LYSL2 45 TYRL2 49 -1 O LEUL2 47 N TRPL2 35 SHEET 6 AB4 6 ASNL2 53 ARGL2 54 -1 O ASNL2 53 N TYRL2 49 SHEET 1 AB5 4 HISH2 3 GLYH2 6 0 SHEET 2 AB5 4 LEUH2 20 SERH2 25 -1 O SERH2 25 N HISH2 3 SHEET 3 AB5 4 THRH2 78 GLNH2 81 -1 O GLNH2 81 N LEUH2 20 SHEET 4 AB5 4 LEUH2 70 ASPH2 73 -1 N ASPH2 73 O THRH2 78 SHEET 1 AB6 5 SERH2 57 TYRH2 60 0 SHEET 2 AB6 5 GLYH2 44 PHEH2 52 -1 N PHEH2 52 O SERH2 57 SHEET 3 AB6 5 METH2 34 ARGH2 40 -1 N ARGH2 38 O GLUH2 46 SHEET 4 AB6 5 VALH2 92 ARGH2 97 -1 O PHEH2 94 N VALH2 37 SHEET 5 AB6 5 THRH2 113 LEUH2 114 -1 O THRH2 113 N TYRH2 93 SSBOND 1 CYSL2 23 CYSL2 88 1555 1555 2.03 SSBOND 2 CYSH2 22 CYSH2 95 1555 1555 2.02 CISPEP 1 TYRA1 464 PROA1 465 0 -7.51 CISPEP 2 THRL2 94 PROL2 95 0 3.84 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