HEADER VIRAL PROTEIN/IMMUNE SYSTEM 25-JUL-24 9CU7 TITLE STRUCTURE OF 16.ND.92 FAB IN COMPLEX WITH A/SOLOMON TITLE 2 ISLANDS/3/2006(H1N1) INFLUENZA VIRUS HEMAGGLUTININ COMPND MOL_ID: 1; COMPND 2 MOLECULE: VARIABLE HEAVY CHAIN OF 16.ND.92 FAB; COMPND 3 CHAIN: H, I, J; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: VARIABLE LIGHT CHAIN OF 16.ND.92 FAB; COMPND 7 CHAIN: L, M, N; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HEMAGGLUTININ HA1; COMPND 11 CHAIN: A, C, E; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: HEMAGGLUTININ HA2; COMPND 15 CHAIN: B, D, F; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPI 293F; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: EXPI 293F; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/SOLOMON SOURCE 19 ISLANDS/3/2006(H1N1)); SOURCE 20 ORGANISM_TAXID: 464623; SOURCE 21 GENE: HA; SOURCE 22 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 23 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 25 EXPRESSION_SYSTEM_CELL_LINE: SF9; SOURCE 26 MOL_ID: 4; SOURCE 27 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/SOLOMON SOURCE 28 ISLANDS/3/2006(H1N1)); SOURCE 29 ORGANISM_TAXID: 464623; SOURCE 30 GENE: HA; SOURCE 31 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 32 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 34 EXPRESSION_SYSTEM_CELL_LINE: SF9 KEYWDS ANTIBODY, INFLUENZA, HEMAGGLUTININ, VIRAL PROTEIN-IMMUNE SYSTEM KEYWDS 2 COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR W.O.OUYANG,T.PHOLCHAREE,N.C.WU REVDAT 1 30-JUL-25 9CU7 0 JRNL AUTH W.O.OUYANG,T.PHOLCHAREE,N.C.WU JRNL TITL STRUCTURE OF 16.ND.92 FAB IN COMPLEX WITH A/SOLOMON JRNL TITL 2 ISLANDS/3/2006(H1N1) INFLUENZA VIRUS HEMAGGLUTININ JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.82 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.820 REMARK 3 NUMBER OF PARTICLES : 152449 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 9CU7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1000286293. 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 : 16.ND.92 FAB IN COMPLEX WITH REMARK 245 A/SOLOMON ISLANDS/3/2006 (H1N1) REMARK 245 HEMAGGLUTININ REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 3.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : BLOT FORCE: 0, BLOT TIME: 3 S, REMARK 245 HUMIDITY 90%, AND 4 C. REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : BOTH HEMAGGLUTININ AND FAB WERE REMARK 245 RECOMBINANTLY EXPRESSED AND PURIFIED. THE FAB WAS THEN MIXED REMARK 245 WITH HEMAGGLUTININ AT 3.5:1 RATIO. THE COMPLEX WERE THEN REMARK 245 ISOLATED USING SIZE EXCLUSION CHROMATOGRAPHY. REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 5000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5735.00 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 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I, J, L, M, N, A, C, E, B, REMARK 350 AND CHAINS: D, F 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 ASP H 61 CG OD1 OD2 REMARK 470 LYS H 64 CG CD CE NZ REMARK 470 LYS I 64 CG CD CE NZ REMARK 470 LYS J 64 CG CD CE NZ REMARK 470 GLU A 125B CG CD OE1 OE2 REMARK 470 GLU A 144 CG CD OE1 OE2 REMARK 470 ASP A 225 CG OD1 OD2 REMARK 470 ASP A 275 CG OD1 OD2 REMARK 470 GLU A 276 CG CD OE1 OE2 REMARK 470 GLU C 125B CG CD OE1 OE2 REMARK 470 GLU C 144 CG CD OE1 OE2 REMARK 470 ASP C 225 CG OD1 OD2 REMARK 470 ASP C 275 CG OD1 OD2 REMARK 470 GLU C 276 CG CD OE1 OE2 REMARK 470 GLU E 125B CG CD OE1 OE2 REMARK 470 GLU E 144 CG CD OE1 OE2 REMARK 470 ASP E 225 CG OD1 OD2 REMARK 470 ASP E 275 CG OD1 OD2 REMARK 470 GLU E 276 CG CD OE1 OE2 REMARK 470 ASN B 60 CG OD1 ND2 REMARK 470 THR B 61 OG1 CG2 REMARK 470 GLN B 62 CG CD OE1 NE2 REMARK 470 PHE B 63 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR B 64 OG1 CG2 REMARK 470 ASN D 60 CG OD1 ND2 REMARK 470 THR D 61 OG1 CG2 REMARK 470 GLN D 62 CG CD OE1 NE2 REMARK 470 PHE D 63 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR D 64 OG1 CG2 REMARK 470 ASN F 60 CG OD1 ND2 REMARK 470 THR F 61 OG1 CG2 REMARK 470 GLN F 62 CG CD OE1 NE2 REMARK 470 PHE F 63 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR F 64 OG1 CG2 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 PHE H 100A -118.82 50.08 REMARK 500 VAL I 48 -62.37 -105.43 REMARK 500 PHE I 100A -116.53 50.61 REMARK 500 PHE J 100A -116.11 47.17 REMARK 500 SER J 112 -178.33 -170.43 REMARK 500 GLN L 27 -168.65 -125.58 REMARK 500 SER L 30 -129.17 54.63 REMARK 500 TRP L 32 58.86 -95.95 REMARK 500 ALA L 51 -9.30 70.67 REMARK 500 ALA L 84 -168.39 -160.68 REMARK 500 SER L 95 -4.98 70.62 REMARK 500 SER M 30 -130.98 55.97 REMARK 500 ALA M 51 -6.83 68.35 REMARK 500 SER M 95 -6.39 72.10 REMARK 500 SER N 30 -120.19 51.69 REMARK 500 ALA N 51 -7.14 67.68 REMARK 500 SER N 67 145.83 -172.56 REMARK 500 SER N 95 -7.85 72.19 REMARK 500 GLU N 105 -169.91 -117.84 REMARK 500 ASN A 95 52.74 -94.77 REMARK 500 SER A 117 140.88 -170.35 REMARK 500 THR A 132 52.29 -95.80 REMARK 500 ASN C 95 53.01 -95.58 REMARK 500 GLU C 122 99.99 -69.94 REMARK 500 THR C 132 64.58 -100.35 REMARK 500 SER C 206 -168.16 -128.01 REMARK 500 LYS C 313 116.36 -160.36 REMARK 500 TYR E 17 -168.49 -127.28 REMARK 500 ASN E 95 58.92 -96.34 REMARK 500 THR E 132 56.03 -100.39 REMARK 500 GLU E 276 30.21 -92.64 REMARK 500 PRO E 284 2.60 -62.54 REMARK 500 LYS B 127 -123.06 57.25 REMARK 500 LYS D 127 -138.77 60.50 REMARK 500 ALA F 5 -60.53 -91.55 REMARK 500 ALA F 7 18.10 59.86 REMARK 500 LYS F 127 -132.60 60.00 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG I 71 0.22 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-45930 RELATED DB: EMDB REMARK 900 STRUCTURE OF 16.ND.92 FAB IN COMPLEX WITH A/SOLOMON ISLANDS/3/ REMARK 900 2006(H1N1) INFLUENZA VIRUS HEMAGGLUTININ DBREF 9CU7 H 2 113 PDB 9CU7 9CU7 2 113 DBREF 9CU7 I 2 113 PDB 9CU7 9CU7 2 113 DBREF 9CU7 J 2 113 PDB 9CU7 9CU7 2 113 DBREF 9CU7 L 2 106 PDB 9CU7 9CU7 2 106 DBREF 9CU7 M 2 106 PDB 9CU7 9CU7 2 106 DBREF 9CU7 N 2 106 PDB 9CU7 9CU7 2 106 DBREF1 9CU7 A 11 324 UNP A0A0G2RTI0_9INFA DBREF2 9CU7 A A0A0G2RTI0 18 338 DBREF1 9CU7 C 11 324 UNP A0A0G2RTI0_9INFA DBREF2 9CU7 C A0A0G2RTI0 18 338 DBREF1 9CU7 E 11 324 UNP A0A0G2RTI0_9INFA DBREF2 9CU7 E A0A0G2RTI0 18 338 DBREF 9CU7 B 2 170 UNP C8CQF2 C8CQF2_9INFA 345 513 DBREF 9CU7 D 2 170 UNP C8CQF2 C8CQF2_9INFA 345 513 DBREF 9CU7 F 2 170 UNP C8CQF2 C8CQF2_9INFA 345 513 SEQADV 9CU7 ARG A 53 UNP A0A0G2RTI LEU 60 CONFLICT SEQADV 9CU7 ARG C 53 UNP A0A0G2RTI LEU 60 CONFLICT SEQADV 9CU7 ARG E 53 UNP A0A0G2RTI LEU 60 CONFLICT SEQRES 1 H 127 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 H 127 GLY GLY SER LEU ARG LEU SER CYS GLU ALA SER GLY PHE SEQRES 3 H 127 THR LEU SER SER TYR TRP MET HIS TRP VAL ARG GLN ASP SEQRES 4 H 127 PRO GLY LYS GLY LEU VAL TRP VAL ALA VAL ILE ASN SER SEQRES 5 H 127 ASP GLY SER SER THR ASP TYR ALA ASP PHE VAL LYS GLY SEQRES 6 H 127 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 H 127 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 H 127 VAL TYR TYR CYS ALA ARG ALA PRO GLN GLY THR VAL PHE SEQRES 9 H 127 GLY VAL VAL ILE ILE GLY ALA ASP GLY PHE ASP ILE TRP SEQRES 10 H 127 GLY GLN GLY THR MET VAL THR VAL SER SER SEQRES 1 I 127 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 I 127 GLY GLY SER LEU ARG LEU SER CYS GLU ALA SER GLY PHE SEQRES 3 I 127 THR LEU SER SER TYR TRP MET HIS TRP VAL ARG GLN ASP SEQRES 4 I 127 PRO GLY LYS GLY LEU VAL TRP VAL ALA VAL ILE ASN SER SEQRES 5 I 127 ASP GLY SER SER THR ASP TYR ALA ASP PHE VAL LYS GLY SEQRES 6 I 127 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 I 127 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 I 127 VAL TYR TYR CYS ALA ARG ALA PRO GLN GLY THR VAL PHE SEQRES 9 I 127 GLY VAL VAL ILE ILE GLY ALA ASP GLY PHE ASP ILE TRP SEQRES 10 I 127 GLY GLN GLY THR MET VAL THR VAL SER SER SEQRES 1 J 127 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 J 127 GLY GLY SER LEU ARG LEU SER CYS GLU ALA SER GLY PHE SEQRES 3 J 127 THR LEU SER SER TYR TRP MET HIS TRP VAL ARG GLN ASP SEQRES 4 J 127 PRO GLY LYS GLY LEU VAL TRP VAL ALA VAL ILE ASN SER SEQRES 5 J 127 ASP GLY SER SER THR ASP TYR ALA ASP PHE VAL LYS GLY SEQRES 6 J 127 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 J 127 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 J 127 VAL TYR TYR CYS ALA ARG ALA PRO GLN GLY THR VAL PHE SEQRES 9 J 127 GLY VAL VAL ILE ILE GLY ALA ASP GLY PHE ASP ILE TRP SEQRES 10 J 127 GLY GLN GLY THR MET VAL THR VAL SER SER SEQRES 1 L 107 ILE GLN MET THR HIS ILE PRO VAL SER LEU SER ALA SER SEQRES 2 L 107 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 L 107 SER ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 4 L 107 GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER THR SEQRES 5 L 107 LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 L 107 SER GLY THR ASP PHE THR LEU THR ILE ASN SER LEU GLN SEQRES 7 L 107 PRO ASP ASP PHE ALA THR TYR TYR CYS GLN HIS TYR ASN SEQRES 8 L 107 THR TYR SER ARG ALA TRP THR PHE GLY GLN GLY THR LYS SEQRES 9 L 107 VAL GLU VAL SEQRES 1 M 107 ILE GLN MET THR HIS ILE PRO VAL SER LEU SER ALA SER SEQRES 2 M 107 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 M 107 SER ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 4 M 107 GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER THR SEQRES 5 M 107 LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 M 107 SER GLY THR ASP PHE THR LEU THR ILE ASN SER LEU GLN SEQRES 7 M 107 PRO ASP ASP PHE ALA THR TYR TYR CYS GLN HIS TYR ASN SEQRES 8 M 107 THR TYR SER ARG ALA TRP THR PHE GLY GLN GLY THR LYS SEQRES 9 M 107 VAL GLU VAL SEQRES 1 N 107 ILE GLN MET THR HIS ILE PRO VAL SER LEU SER ALA SER SEQRES 2 N 107 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 N 107 SER ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 4 N 107 GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER THR SEQRES 5 N 107 LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 N 107 SER GLY THR ASP PHE THR LEU THR ILE ASN SER LEU GLN SEQRES 7 N 107 PRO ASP ASP PHE ALA THR TYR TYR CYS GLN HIS TYR ASN SEQRES 8 N 107 THR TYR SER ARG ALA TRP THR PHE GLY GLN GLY THR LYS SEQRES 9 N 107 VAL GLU VAL SEQRES 1 A 321 ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 A 321 ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR VAL SEQRES 3 A 321 THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN GLY SEQRES 4 A 321 LYS LEU CYS ARG LEU LYS GLY ILE ALA PRO LEU GLN LEU SEQRES 5 A 321 GLY ASN CYS SER VAL ALA GLY TRP ILE LEU GLY ASN PRO SEQRES 6 A 321 GLU CYS GLU LEU LEU ILE SER ARG GLU SER TRP SER TYR SEQRES 7 A 321 ILE VAL GLU LYS PRO ASN PRO GLU ASN GLY THR CYS TYR SEQRES 8 A 321 PRO GLY HIS PHE ALA ASP TYR GLU GLU LEU ARG GLU GLN SEQRES 9 A 321 LEU SER SER VAL SER SER PHE GLU ARG PHE GLU ILE PHE SEQRES 10 A 321 PRO LYS GLU SER SER TRP PRO ASN HIS THR THR THR GLY SEQRES 11 A 321 VAL SER ALA SER CYS SER HIS ASN GLY GLU SER SER PHE SEQRES 12 A 321 TYR LYS ASN LEU LEU TRP LEU THR GLY LYS ASN GLY LEU SEQRES 13 A 321 TYR PRO ASN LEU SER LYS SER TYR ALA ASN ASN LYS GLU SEQRES 14 A 321 LYS GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO PRO SEQRES 15 A 321 ASN ILE GLY ASP GLN ARG ALA LEU TYR HIS LYS GLU ASN SEQRES 16 A 321 ALA TYR VAL SER VAL VAL SER SER HIS TYR SER ARG LYS SEQRES 17 A 321 PHE THR PRO GLU ILE ALA LYS ARG PRO LYS VAL ARG ASP SEQRES 18 A 321 GLN GLU GLY ARG ILE ASN TYR TYR TRP THR LEU LEU GLU SEQRES 19 A 321 PRO GLY ASP THR ILE ILE PHE GLU ALA ASN GLY ASN LEU SEQRES 20 A 321 ILE ALA PRO ARG TYR ALA PHE ALA LEU SER ARG GLY PHE SEQRES 21 A 321 GLY SER GLY ILE ILE ASN SER ASN ALA PRO MET ASP GLU SEQRES 22 A 321 CYS ASP ALA LYS CYS GLN THR PRO GLN GLY ALA ILE ASN SEQRES 23 A 321 SER SER LEU PRO PHE GLN ASN VAL HIS PRO VAL THR ILE SEQRES 24 A 321 GLY GLU CYS PRO LYS TYR VAL ARG SER ALA LYS LEU ARG SEQRES 25 A 321 MET VAL THR GLY LEU ARG ASN ILE PRO SEQRES 1 C 321 ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 C 321 ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR VAL SEQRES 3 C 321 THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN GLY SEQRES 4 C 321 LYS LEU CYS ARG LEU LYS GLY ILE ALA PRO LEU GLN LEU SEQRES 5 C 321 GLY ASN CYS SER VAL ALA GLY TRP ILE LEU GLY ASN PRO SEQRES 6 C 321 GLU CYS GLU LEU LEU ILE SER ARG GLU SER TRP SER TYR SEQRES 7 C 321 ILE VAL GLU LYS PRO ASN PRO GLU ASN GLY THR CYS TYR SEQRES 8 C 321 PRO GLY HIS PHE ALA ASP TYR GLU GLU LEU ARG GLU GLN SEQRES 9 C 321 LEU SER SER VAL SER SER PHE GLU ARG PHE GLU ILE PHE SEQRES 10 C 321 PRO LYS GLU SER SER TRP PRO ASN HIS THR THR THR GLY SEQRES 11 C 321 VAL SER ALA SER CYS SER HIS ASN GLY GLU SER SER PHE SEQRES 12 C 321 TYR LYS ASN LEU LEU TRP LEU THR GLY LYS ASN GLY LEU SEQRES 13 C 321 TYR PRO ASN LEU SER LYS SER TYR ALA ASN ASN LYS GLU SEQRES 14 C 321 LYS GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO PRO SEQRES 15 C 321 ASN ILE GLY ASP GLN ARG ALA LEU TYR HIS LYS GLU ASN SEQRES 16 C 321 ALA TYR VAL SER VAL VAL SER SER HIS TYR SER ARG LYS SEQRES 17 C 321 PHE THR PRO GLU ILE ALA LYS ARG PRO LYS VAL ARG ASP SEQRES 18 C 321 GLN GLU GLY ARG ILE ASN TYR TYR TRP THR LEU LEU GLU SEQRES 19 C 321 PRO GLY ASP THR ILE ILE PHE GLU ALA ASN GLY ASN LEU SEQRES 20 C 321 ILE ALA PRO ARG TYR ALA PHE ALA LEU SER ARG GLY PHE SEQRES 21 C 321 GLY SER GLY ILE ILE ASN SER ASN ALA PRO MET ASP GLU SEQRES 22 C 321 CYS ASP ALA LYS CYS GLN THR PRO GLN GLY ALA ILE ASN SEQRES 23 C 321 SER SER LEU PRO PHE GLN ASN VAL HIS PRO VAL THR ILE SEQRES 24 C 321 GLY GLU CYS PRO LYS TYR VAL ARG SER ALA LYS LEU ARG SEQRES 25 C 321 MET VAL THR GLY LEU ARG ASN ILE PRO SEQRES 1 E 321 ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 E 321 ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR VAL SEQRES 3 E 321 THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN GLY SEQRES 4 E 321 LYS LEU CYS ARG LEU LYS GLY ILE ALA PRO LEU GLN LEU SEQRES 5 E 321 GLY ASN CYS SER VAL ALA GLY TRP ILE LEU GLY ASN PRO SEQRES 6 E 321 GLU CYS GLU LEU LEU ILE SER ARG GLU SER TRP SER TYR SEQRES 7 E 321 ILE VAL GLU LYS PRO ASN PRO GLU ASN GLY THR CYS TYR SEQRES 8 E 321 PRO GLY HIS PHE ALA ASP TYR GLU GLU LEU ARG GLU GLN SEQRES 9 E 321 LEU SER SER VAL SER SER PHE GLU ARG PHE GLU ILE PHE SEQRES 10 E 321 PRO LYS GLU SER SER TRP PRO ASN HIS THR THR THR GLY SEQRES 11 E 321 VAL SER ALA SER CYS SER HIS ASN GLY GLU SER SER PHE SEQRES 12 E 321 TYR LYS ASN LEU LEU TRP LEU THR GLY LYS ASN GLY LEU SEQRES 13 E 321 TYR PRO ASN LEU SER LYS SER TYR ALA ASN ASN LYS GLU SEQRES 14 E 321 LYS GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO PRO SEQRES 15 E 321 ASN ILE GLY ASP GLN ARG ALA LEU TYR HIS LYS GLU ASN SEQRES 16 E 321 ALA TYR VAL SER VAL VAL SER SER HIS TYR SER ARG LYS SEQRES 17 E 321 PHE THR PRO GLU ILE ALA LYS ARG PRO LYS VAL ARG ASP SEQRES 18 E 321 GLN GLU GLY ARG ILE ASN TYR TYR TRP THR LEU LEU GLU SEQRES 19 E 321 PRO GLY ASP THR ILE ILE PHE GLU ALA ASN GLY ASN LEU SEQRES 20 E 321 ILE ALA PRO ARG TYR ALA PHE ALA LEU SER ARG GLY PHE SEQRES 21 E 321 GLY SER GLY ILE ILE ASN SER ASN ALA PRO MET ASP GLU SEQRES 22 E 321 CYS ASP ALA LYS CYS GLN THR PRO GLN GLY ALA ILE ASN SEQRES 23 E 321 SER SER LEU PRO PHE GLN ASN VAL HIS PRO VAL THR ILE SEQRES 24 E 321 GLY GLU CYS PRO LYS TYR VAL ARG SER ALA LYS LEU ARG SEQRES 25 E 321 MET VAL THR GLY LEU ARG ASN ILE PRO SEQRES 1 B 169 LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY TRP SEQRES 2 B 169 THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS GLN SEQRES 3 B 169 ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS SER SEQRES 4 B 169 THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL ASN SEQRES 5 B 169 SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA VAL SEQRES 6 B 169 GLY LYS GLU PHE ASN LYS LEU GLU ARG ARG MET GLU ASN SEQRES 7 B 169 LEU ASN LYS LYS VAL ASP ASP GLY PHE ILE ASP ILE TRP SEQRES 8 B 169 THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN GLU SEQRES 9 B 169 ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN LEU SEQRES 10 B 169 TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA LYS SEQRES 11 B 169 GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS CYS SEQRES 12 B 169 ASN ASP GLU CYS MET GLU SER VAL LYS ASN GLY THR TYR SEQRES 13 B 169 ASP TYR PRO LYS TYR SER GLU GLU SER LYS LEU ASN ARG SEQRES 1 D 169 LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY TRP SEQRES 2 D 169 THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS GLN SEQRES 3 D 169 ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS SER SEQRES 4 D 169 THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL ASN SEQRES 5 D 169 SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA VAL SEQRES 6 D 169 GLY LYS GLU PHE ASN LYS LEU GLU ARG ARG MET GLU ASN SEQRES 7 D 169 LEU ASN LYS LYS VAL ASP ASP GLY PHE ILE ASP ILE TRP SEQRES 8 D 169 THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN GLU SEQRES 9 D 169 ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN LEU SEQRES 10 D 169 TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA LYS SEQRES 11 D 169 GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS CYS SEQRES 12 D 169 ASN ASP GLU CYS MET GLU SER VAL LYS ASN GLY THR TYR SEQRES 13 D 169 ASP TYR PRO LYS TYR SER GLU GLU SER LYS LEU ASN ARG SEQRES 1 F 169 LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY TRP SEQRES 2 F 169 THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS GLN SEQRES 3 F 169 ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS SER SEQRES 4 F 169 THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL ASN SEQRES 5 F 169 SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA VAL SEQRES 6 F 169 GLY LYS GLU PHE ASN LYS LEU GLU ARG ARG MET GLU ASN SEQRES 7 F 169 LEU ASN LYS LYS VAL ASP ASP GLY PHE ILE ASP ILE TRP SEQRES 8 F 169 THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN GLU SEQRES 9 F 169 ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN LEU SEQRES 10 F 169 TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA LYS SEQRES 11 F 169 GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS CYS SEQRES 12 F 169 ASN ASP GLU CYS MET GLU SER VAL LYS ASN GLY THR TYR SEQRES 13 F 169 ASP TYR PRO LYS TYR SER GLU GLU SER LYS LEU ASN ARG HELIX 1 AA1 THR H 28 SER H 30 5 3 HELIX 2 AA2 THR I 28 SER I 30 5 3 HELIX 3 AA3 THR J 28 SER J 30 5 3 HELIX 4 AA4 GLN L 79 PHE L 83 5 5 HELIX 5 AA5 GLN M 79 PHE M 83 5 5 HELIX 6 AA6 GLN N 79 PHE N 83 5 5 HELIX 7 AA7 SER A 65 GLY A 72 1 8 HELIX 8 AA8 ASP A 104 SER A 113 1 10 HELIX 9 AA9 PRO A 125 SER A 126 5 5 HELIX 10 AB1 ASN A 187 TYR A 195 1 9 HELIX 11 AB2 SER C 65 GLY C 72 1 8 HELIX 12 AB3 ASP C 104 SER C 113 1 10 HELIX 13 AB4 ASN C 187 HIS C 196 1 10 HELIX 14 AB5 SER E 65 GLY E 72 1 8 HELIX 15 AB6 ASP E 104 SER E 113 1 10 HELIX 16 AB7 PRO E 125 SER E 126 5 5 HELIX 17 AB8 ASN E 187 HIS E 196 1 10 HELIX 18 AB9 ASP B 37 LYS B 58 1 22 HELIX 19 AC1 ASN B 71 LEU B 73 5 3 HELIX 20 AC2 GLU B 74 LYS B 127 1 54 HELIX 21 AC3 ASN B 145 GLY B 155 1 11 HELIX 22 AC4 ASP B 158 ARG B 170 1 13 HELIX 23 AC5 ASP D 37 LYS D 58 1 22 HELIX 24 AC6 ASN D 71 LEU D 73 5 3 HELIX 25 AC7 GLU D 74 LYS D 127 1 54 HELIX 26 AC8 ASN D 145 GLY D 155 1 11 HELIX 27 AC9 ASP D 158 ARG D 170 1 13 HELIX 28 AD1 ASP F 37 MET F 59 1 23 HELIX 29 AD2 GLU F 74 LYS F 127 1 54 HELIX 30 AD3 ASN F 145 GLY F 155 1 11 HELIX 31 AD4 ASP F 158 ARG F 170 1 13 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 SER H 17 SER H 25 -1 O GLU H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 ASN H 82A-1 O LEU H 80 N LEU H 20 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 PRO H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 TYR H 32 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O VAL H 46 N ARG H 38 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O ASP H 58 N VAL H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 PRO H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 ILE H 102 TRP H 103 -1 O ILE H 102 N ARG H 94 SHEET 1 AA4 4 GLN I 3 SER I 7 0 SHEET 2 AA4 4 SER I 17 SER I 25 -1 O SER I 25 N GLN I 3 SHEET 3 AA4 4 THR I 77 ASN I 82A-1 O LEU I 80 N LEU I 20 SHEET 4 AA4 4 PHE I 67 ASP I 72 -1 N THR I 68 O GLN I 81 SHEET 1 AA5 6 LEU I 11 VAL I 12 0 SHEET 2 AA5 6 THR I 107 VAL I 111 1 O THR I 110 N VAL I 12 SHEET 3 AA5 6 ALA I 88 PRO I 96 -1 N TYR I 90 O THR I 107 SHEET 4 AA5 6 TYR I 32 GLN I 39 -1 N HIS I 35 O ALA I 93 SHEET 5 AA5 6 LEU I 45 ILE I 51 -1 O VAL I 46 N ARG I 38 SHEET 6 AA5 6 THR I 57 TYR I 59 -1 O ASP I 58 N VAL I 50 SHEET 1 AA6 4 LEU I 11 VAL I 12 0 SHEET 2 AA6 4 THR I 107 VAL I 111 1 O THR I 110 N VAL I 12 SHEET 3 AA6 4 ALA I 88 PRO I 96 -1 N TYR I 90 O THR I 107 SHEET 4 AA6 4 ILE I 102 TRP I 103 -1 O ILE I 102 N ARG I 94 SHEET 1 AA7 4 GLN J 3 SER J 7 0 SHEET 2 AA7 4 LEU J 18 SER J 25 -1 O SER J 21 N SER J 7 SHEET 3 AA7 4 THR J 77 MET J 82 -1 O LEU J 80 N LEU J 20 SHEET 4 AA7 4 PHE J 67 ASP J 72 -1 N THR J 68 O GLN J 81 SHEET 1 AA8 6 LEU J 11 VAL J 12 0 SHEET 2 AA8 6 THR J 107 VAL J 111 1 O THR J 110 N VAL J 12 SHEET 3 AA8 6 ALA J 88 PRO J 96 -1 N TYR J 90 O THR J 107 SHEET 4 AA8 6 TYR J 32 GLN J 39 -1 N GLN J 39 O VAL J 89 SHEET 5 AA8 6 LEU J 45 ILE J 51 -1 O VAL J 46 N ARG J 38 SHEET 6 AA8 6 THR J 57 TYR J 59 -1 O ASP J 58 N VAL J 50 SHEET 1 AA9 4 LEU J 11 VAL J 12 0 SHEET 2 AA9 4 THR J 107 VAL J 111 1 O THR J 110 N VAL J 12 SHEET 3 AA9 4 ALA J 88 PRO J 96 -1 N TYR J 90 O THR J 107 SHEET 4 AA9 4 ILE J 102 TRP J 103 -1 O ILE J 102 N ARG J 94 SHEET 1 AB1 4 MET L 4 ILE L 7 0 SHEET 2 AB1 4 THR L 20 ALA L 25 -1 O THR L 22 N ILE L 7 SHEET 3 AB1 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AB1 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB2 6 SER L 10 SER L 12 0 SHEET 2 AB2 6 THR L 102 GLU L 105 1 O LYS L 103 N LEU L 11 SHEET 3 AB2 6 THR L 85 ASN L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AB2 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AB2 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB2 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AB3 4 SER L 10 SER L 12 0 SHEET 2 AB3 4 THR L 102 GLU L 105 1 O LYS L 103 N LEU L 11 SHEET 3 AB3 4 THR L 85 ASN L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AB3 4 ALA L 95B PHE L 98 -1 O ALA L 95B N ASN L 92 SHEET 1 AB4 4 MET M 4 ILE M 7 0 SHEET 2 AB4 4 VAL M 19 ALA M 25 -1 O THR M 22 N ILE M 7 SHEET 3 AB4 4 ASP M 70 ILE M 75 -1 O LEU M 73 N ILE M 21 SHEET 4 AB4 4 PHE M 62 SER M 67 -1 N SER M 65 O THR M 72 SHEET 1 AB5 6 SER M 10 SER M 12 0 SHEET 2 AB5 6 THR M 102 GLU M 105 1 O LYS M 103 N LEU M 11 SHEET 3 AB5 6 THR M 85 ASN M 92 -1 N TYR M 86 O THR M 102 SHEET 4 AB5 6 LEU M 33 GLN M 38 -1 N GLN M 38 O THR M 85 SHEET 5 AB5 6 LYS M 45 TYR M 49 -1 O LYS M 45 N GLN M 37 SHEET 6 AB5 6 THR M 53 LEU M 54 -1 O THR M 53 N TYR M 49 SHEET 1 AB6 4 SER M 10 SER M 12 0 SHEET 2 AB6 4 THR M 102 GLU M 105 1 O LYS M 103 N LEU M 11 SHEET 3 AB6 4 THR M 85 ASN M 92 -1 N TYR M 86 O THR M 102 SHEET 4 AB6 4 ALA M 95B PHE M 98 -1 O THR M 97 N HIS M 90 SHEET 1 AB7 4 MET N 4 ILE N 7 0 SHEET 2 AB7 4 VAL N 19 ALA N 25 -1 O THR N 22 N ILE N 7 SHEET 3 AB7 4 ASP N 70 ILE N 75 -1 O LEU N 73 N ILE N 21 SHEET 4 AB7 4 PHE N 62 SER N 67 -1 N SER N 65 O THR N 72 SHEET 1 AB8 6 SER N 10 SER N 12 0 SHEET 2 AB8 6 THR N 102 GLU N 105 1 O LYS N 103 N LEU N 11 SHEET 3 AB8 6 THR N 85 ASN N 92 -1 N TYR N 86 O THR N 102 SHEET 4 AB8 6 LEU N 33 GLN N 38 -1 N GLN N 38 O THR N 85 SHEET 5 AB8 6 LYS N 45 TYR N 49 -1 O LYS N 45 N GLN N 37 SHEET 6 AB8 6 THR N 53 LEU N 54 -1 O THR N 53 N TYR N 49 SHEET 1 AB9 4 SER N 10 SER N 12 0 SHEET 2 AB9 4 THR N 102 GLU N 105 1 O LYS N 103 N LEU N 11 SHEET 3 AB9 4 THR N 85 ASN N 92 -1 N TYR N 86 O THR N 102 SHEET 4 AB9 4 ALA N 95B PHE N 98 -1 O THR N 97 N HIS N 90 SHEET 1 AC1 5 GLY B 31 ALA B 36 0 SHEET 2 AC1 5 TYR B 22 ASN B 28 -1 N TYR B 24 O ALA B 35 SHEET 3 AC1 5 THR A 12 TYR A 17 -1 N CYS A 14 O HIS B 25 SHEET 4 AC1 5 CYS B 137 PHE B 140 -1 O PHE B 138 N ILE A 13 SHEET 5 AC1 5 ALA B 130 GLU B 132 -1 N LYS B 131 O GLU B 139 SHEET 1 AC2 2 THR A 25 VAL A 26 0 SHEET 2 AC2 2 VAL A 34 THR A 35 -1 O VAL A 34 N VAL A 26 SHEET 1 AC3 2 SER A 39 ASN A 41 0 SHEET 2 AC3 2 ARG A 315 VAL A 317 -1 O MET A 316 N VAL A 40 SHEET 1 AC4 3 LEU A 43 GLU A 44 0 SHEET 2 AC4 3 PHE A 294 GLN A 295 1 O PHE A 294 N GLU A 44 SHEET 3 AC4 3 LYS A 307 TYR A 308 1 O LYS A 307 N GLN A 295 SHEET 1 AC5 2 LEU A 51 LEU A 54 0 SHEET 2 AC5 2 MET A 274 ALA A 279 1 O CYS A 277 N ARG A 53 SHEET 1 AC6 3 LEU A 59 GLN A 60 0 SHEET 2 AC6 3 ILE A 87 GLU A 89 1 O VAL A 88 N LEU A 59 SHEET 3 AC6 3 ILE A 267 ASN A 269 1 O ILE A 268 N ILE A 87 SHEET 1 AC7 4 VAL A 115 GLU A 122 0 SHEET 2 AC7 4 TYR A 256 ARG A 262 -1 O ALA A 257 N PHE A 121 SHEET 3 AC7 4 VAL A 176 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 4 AC7 4 ARG A 229 LEU A 237 -1 O ASN A 231 N VAL A 182 SHEET 1 AC8 2 SER A 136 HIS A 141 0 SHEET 2 AC8 2 GLU A 144 SER A 146 -1 O SER A 146 N SER A 136 SHEET 1 AC9 2 LEU A 151 TRP A 153 0 SHEET 2 AC9 2 ILE A 252 PRO A 254 -1 O ALA A 253 N LEU A 152 SHEET 1 AD1 4 LEU A 164 ALA A 169 0 SHEET 2 AD1 4 THR A 242 ALA A 247 -1 O PHE A 245 N LYS A 166 SHEET 3 AD1 4 VAL A 202 VAL A 205 -1 N VAL A 205 O ILE A 244 SHEET 4 AD1 4 SER A 210 PHE A 213 -1 O PHE A 213 N VAL A 202 SHEET 1 AD2 3 GLY A 286 ALA A 287 0 SHEET 2 AD2 3 CYS A 281 THR A 283 -1 N THR A 283 O GLY A 286 SHEET 3 AD2 3 ILE A 302 GLY A 303 -1 O ILE A 302 N GLN A 282 SHEET 1 AD3 5 GLY D 31 ALA D 36 0 SHEET 2 AD3 5 TYR D 22 ASN D 28 -1 N ASN D 28 O GLY D 31 SHEET 3 AD3 5 THR C 12 TYR C 17 -1 N GLY C 16 O GLY D 23 SHEET 4 AD3 5 CYS D 137 PHE D 140 -1 O PHE D 138 N ILE C 13 SHEET 5 AD3 5 ALA D 130 GLU D 132 -1 N LYS D 131 O GLU D 139 SHEET 1 AD4 2 THR C 25 VAL C 26 0 SHEET 2 AD4 2 VAL C 34 THR C 35 -1 O VAL C 34 N VAL C 26 SHEET 1 AD5 2 SER C 39 ASN C 41 0 SHEET 2 AD5 2 ARG C 315 VAL C 317 -1 O MET C 316 N VAL C 40 SHEET 1 AD6 3 LEU C 43 GLU C 44 0 SHEET 2 AD6 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLU C 44 SHEET 3 AD6 3 LYS C 307 TYR C 308 1 O LYS C 307 N GLN C 295 SHEET 1 AD7 2 LEU C 51 LEU C 54 0 SHEET 2 AD7 2 MET C 274 ALA C 279 1 O ASP C 275 N LEU C 51 SHEET 1 AD8 3 LEU C 59 GLY C 62 0 SHEET 2 AD8 3 ILE C 87 GLU C 89 1 O VAL C 88 N LEU C 59 SHEET 3 AD8 3 ILE C 267 ASN C 269 1 O ILE C 268 N ILE C 87 SHEET 1 AD9 4 VAL C 115 GLU C 122 0 SHEET 2 AD9 4 TYR C 256 ARG C 262 -1 O SER C 261 N SER C 117 SHEET 3 AD9 4 VAL C 176 HIS C 184 -1 N LEU C 177 O PHE C 258 SHEET 4 AD9 4 ARG C 229 LEU C 237 -1 O LEU C 237 N VAL C 176 SHEET 1 AE1 2 HIS C 130 THR C 131 0 SHEET 2 AE1 2 THR C 155 GLY C 156 -1 O THR C 155 N THR C 131 SHEET 1 AE2 2 SER C 136 HIS C 141 0 SHEET 2 AE2 2 GLU C 144 SER C 146 -1 O SER C 146 N CYS C 139 SHEET 1 AE3 2 LEU C 151 TRP C 153 0 SHEET 2 AE3 2 ILE C 252 PRO C 254 -1 O ALA C 253 N LEU C 152 SHEET 1 AE4 4 LEU C 164 ALA C 169 0 SHEET 2 AE4 4 THR C 242 ALA C 247 -1 O ALA C 247 N LEU C 164 SHEET 3 AE4 4 VAL C 202 VAL C 205 -1 N SER C 203 O GLU C 246 SHEET 4 AE4 4 SER C 210 PHE C 213 -1 O PHE C 213 N VAL C 202 SHEET 1 AE5 3 GLY C 286 ILE C 288 0 SHEET 2 AE5 3 CYS C 281 THR C 283 -1 N THR C 283 O GLY C 286 SHEET 3 AE5 3 ILE C 302 GLY C 303 -1 O ILE C 302 N GLN C 282 SHEET 1 AE6 5 GLY F 31 ALA F 36 0 SHEET 2 AE6 5 TYR F 22 ASN F 28 -1 N TYR F 24 O ALA F 35 SHEET 3 AE6 5 THR E 12 TYR E 17 -1 N CYS E 14 O HIS F 25 SHEET 4 AE6 5 CYS F 137 PHE F 140 -1 O PHE F 138 N ILE E 13 SHEET 5 AE6 5 ALA F 130 GLU F 132 -1 N LYS F 131 O GLU F 139 SHEET 1 AE7 2 THR E 25 VAL E 26 0 SHEET 2 AE7 2 VAL E 34 THR E 35 -1 O VAL E 34 N VAL E 26 SHEET 1 AE8 2 SER E 39 ASN E 41 0 SHEET 2 AE8 2 ARG E 315 VAL E 317 -1 O MET E 316 N VAL E 40 SHEET 1 AE9 3 LEU E 43 GLU E 44 0 SHEET 2 AE9 3 PHE E 294 GLN E 295 1 O PHE E 294 N GLU E 44 SHEET 3 AE9 3 LYS E 307 TYR E 308 1 O LYS E 307 N GLN E 295 SHEET 1 AF1 2 LEU E 51 LEU E 54 0 SHEET 2 AF1 2 MET E 274 ALA E 279 1 O ASP E 275 N LEU E 51 SHEET 1 AF2 3 LEU E 59 GLN E 60 0 SHEET 2 AF2 3 ILE E 87 GLU E 89 1 O VAL E 88 N LEU E 59 SHEET 3 AF2 3 ILE E 267 ASN E 269 1 O ILE E 268 N ILE E 87 SHEET 1 AF3 4 VAL E 115 GLU E 122 0 SHEET 2 AF3 4 TYR E 256 ARG E 262 -1 O ALA E 257 N PHE E 121 SHEET 3 AF3 4 VAL E 176 HIS E 184 -1 N LEU E 177 O PHE E 258 SHEET 4 AF3 4 ARG E 229 LEU E 237 -1 O ASN E 231 N VAL E 182 SHEET 1 AF4 2 HIS E 130 THR E 131 0 SHEET 2 AF4 2 THR E 155 GLY E 156 -1 O THR E 155 N THR E 131 SHEET 1 AF5 2 SER E 136 HIS E 141 0 SHEET 2 AF5 2 GLU E 144 SER E 146 -1 O SER E 146 N CYS E 139 SHEET 1 AF6 2 LEU E 151 TRP E 153 0 SHEET 2 AF6 2 ILE E 252 PRO E 254 -1 O ALA E 253 N LEU E 152 SHEET 1 AF7 4 LEU E 164 ALA E 169 0 SHEET 2 AF7 4 THR E 242 ALA E 247 -1 O ILE E 243 N TYR E 168 SHEET 3 AF7 4 VAL E 202 VAL E 205 -1 N SER E 203 O GLU E 246 SHEET 4 AF7 4 SER E 210 PHE E 213 -1 O PHE E 213 N VAL E 202 SHEET 1 AF8 3 GLY E 286 ILE E 288 0 SHEET 2 AF8 3 CYS E 281 THR E 283 -1 N THR E 283 O GLY E 286 SHEET 3 AF8 3 ILE E 302 GLY E 303 -1 O ILE E 302 N GLN E 282 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 3 CYS J 22 CYS J 92 1555 1555 2.03 SSBOND 4 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 5 CYS M 23 CYS M 88 1555 1555 2.04 SSBOND 6 CYS N 23 CYS N 88 1555 1555 2.04 SSBOND 7 CYS A 14 CYS B 137 1555 1555 2.05 SSBOND 8 CYS A 52 CYS A 277 1555 1555 2.03 SSBOND 9 CYS A 64 CYS A 76 1555 1555 2.04 SSBOND 10 CYS A 97 CYS A 139 1555 1555 2.03 SSBOND 11 CYS A 281 CYS A 305 1555 1555 2.03 SSBOND 12 CYS C 14 CYS D 137 1555 1555 2.03 SSBOND 13 CYS C 52 CYS C 277 1555 1555 2.03 SSBOND 14 CYS C 64 CYS C 76 1555 1555 2.04 SSBOND 15 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 16 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 17 CYS E 14 CYS F 137 1555 1555 2.03 SSBOND 18 CYS E 52 CYS E 277 1555 1555 2.03 SSBOND 19 CYS E 64 CYS E 76 1555 1555 2.04 SSBOND 20 CYS E 97 CYS E 139 1555 1555 2.03 SSBOND 21 CYS E 281 CYS E 305 1555 1555 2.03 SSBOND 22 CYS B 144 CYS B 148 1555 1555 2.03 SSBOND 23 CYS D 144 CYS D 148 1555 1555 2.02 SSBOND 24 CYS F 144 CYS F 148 1555 1555 2.03 CISPEP 1 ILE L 7 PRO L 8 0 -5.63 CISPEP 2 ILE M 7 PRO M 8 0 -5.68 CISPEP 3 ILE N 7 PRO N 8 0 -7.52 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