HEADER IMMUNE SYSTEM 10-DEC-24 9MGB TITLE SCFV ANTIBODY CL33 BOUND TO R-PHYCOERYTHRIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: R-PHYCOERYTHRIN ALPHA CHAIN; COMPND 3 CHAIN: A, C, F, I, L, O; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: R-PHYCOERYTHRIN BETA CHAIN; COMPND 6 CHAIN: B, D, G, J, M, Q; COMPND 7 MOL_ID: 3; COMPND 8 MOLECULE: CL33 SCFV; COMPND 9 CHAIN: a, c, e, g, i, k; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NEOPYROPIA TENERA; SOURCE 3 ORGANISM_TAXID: 2785; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: NEOPYROPIA TENERA; SOURCE 6 ORGANISM_TAXID: 2785; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS PHYCOERYTHRIN, ANTIBODY, SCFV, IMMUNITY, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR L.RASHLEIGH,B.S.GULLY REVDAT 1 06-AUG-25 9MGB 0 JRNL AUTH L.RASHLEIGH,H.VENUGOPAL,M.T.RICE,S.D.GUNASINGHE,C.L.SOK, JRNL AUTH 2 N.A.GHERARDIN,C.F.ALMEIDA,I.VAN RHIJN,D.B.MOODY,D.I.GODFREY, JRNL AUTH 3 J.ROSSJOHN,B.S.GULLY JRNL TITL ANTIBODY-LIKE RECOGNITION OF A GAMMA DELTA T CELL RECEPTOR JRNL TITL 2 TOWARD A FOREIGN ANTIGEN JRNL REF STRUCTURE 2025 JRNL REFN ISSN 0969-2126 JRNL DOI 10.1016/J.STR.2025.07.006 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 2.100 REMARK 3 NUMBER OF PARTICLES : 274000 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 9MGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290882. 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 : R-PHYCOERYTHRIN BOUND BY CL33 REMARK 245 SCFV; R-PHYCOERYTHRIN; CL33 SCFV 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 : 8.50 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 TALOS ARCTICA REMARK 245 DETECTOR TYPE : FEI FALCON III (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 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) : 5000.00 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) : 200 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: OCTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, F, G, I, J, L, M, REMARK 350 AND CHAINS: O, Q, a, c, e, g, i, k 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 VAL a 2 REMARK 465 HIS a 3 REMARK 465 SER a 4 REMARK 465 SER a 123 REMARK 465 ALA a 124 REMARK 465 ALA a 125 REMARK 465 ALA a 126 REMARK 465 GLY a 127 REMARK 465 GLY a 128 REMARK 465 GLY a 129 REMARK 465 GLY a 130 REMARK 465 SER a 131 REMARK 465 GLY a 132 REMARK 465 GLY a 133 REMARK 465 GLY a 134 REMARK 465 GLY a 135 REMARK 465 SER a 136 REMARK 465 GLY a 137 REMARK 465 GLY a 138 REMARK 465 GLY a 139 REMARK 465 GLY a 140 REMARK 465 SER a 141 REMARK 465 VAL a 142 REMARK 465 HIS a 143 REMARK 465 LYS a 251 REMARK 465 HIS a 252 REMARK 465 HIS a 253 REMARK 465 HIS a 254 REMARK 465 HIS a 255 REMARK 465 HIS a 256 REMARK 465 HIS a 257 REMARK 465 MET c 1 REMARK 465 VAL c 2 REMARK 465 HIS c 3 REMARK 465 SER c 4 REMARK 465 SER c 123 REMARK 465 ALA c 124 REMARK 465 ALA c 125 REMARK 465 ALA c 126 REMARK 465 GLY c 127 REMARK 465 GLY c 128 REMARK 465 GLY c 129 REMARK 465 GLY c 130 REMARK 465 SER c 131 REMARK 465 GLY c 132 REMARK 465 GLY c 133 REMARK 465 GLY c 134 REMARK 465 GLY c 135 REMARK 465 SER c 136 REMARK 465 GLY c 137 REMARK 465 GLY c 138 REMARK 465 GLY c 139 REMARK 465 GLY c 140 REMARK 465 SER c 141 REMARK 465 VAL c 142 REMARK 465 HIS c 143 REMARK 465 LYS c 251 REMARK 465 HIS c 252 REMARK 465 HIS c 253 REMARK 465 HIS c 254 REMARK 465 HIS c 255 REMARK 465 HIS c 256 REMARK 465 HIS c 257 REMARK 465 MET e 1 REMARK 465 VAL e 2 REMARK 465 HIS e 3 REMARK 465 SER e 4 REMARK 465 SER e 123 REMARK 465 ALA e 124 REMARK 465 ALA e 125 REMARK 465 ALA e 126 REMARK 465 GLY e 127 REMARK 465 GLY e 128 REMARK 465 GLY e 129 REMARK 465 GLY e 130 REMARK 465 SER e 131 REMARK 465 GLY e 132 REMARK 465 GLY e 133 REMARK 465 GLY e 134 REMARK 465 GLY e 135 REMARK 465 SER e 136 REMARK 465 GLY e 137 REMARK 465 GLY e 138 REMARK 465 GLY e 139 REMARK 465 GLY e 140 REMARK 465 SER e 141 REMARK 465 VAL e 142 REMARK 465 HIS e 143 REMARK 465 LYS e 251 REMARK 465 HIS e 252 REMARK 465 HIS e 253 REMARK 465 HIS e 254 REMARK 465 HIS e 255 REMARK 465 HIS e 256 REMARK 465 HIS e 257 REMARK 465 MET g 1 REMARK 465 VAL g 2 REMARK 465 HIS g 3 REMARK 465 SER g 4 REMARK 465 SER g 123 REMARK 465 ALA g 124 REMARK 465 ALA g 125 REMARK 465 ALA g 126 REMARK 465 GLY g 127 REMARK 465 GLY g 128 REMARK 465 GLY g 129 REMARK 465 GLY g 130 REMARK 465 SER g 131 REMARK 465 GLY g 132 REMARK 465 GLY g 133 REMARK 465 GLY g 134 REMARK 465 GLY g 135 REMARK 465 SER g 136 REMARK 465 GLY g 137 REMARK 465 GLY g 138 REMARK 465 GLY g 139 REMARK 465 GLY g 140 REMARK 465 SER g 141 REMARK 465 VAL g 142 REMARK 465 HIS g 143 REMARK 465 LYS g 251 REMARK 465 HIS g 252 REMARK 465 HIS g 253 REMARK 465 HIS g 254 REMARK 465 HIS g 255 REMARK 465 HIS g 256 REMARK 465 HIS g 257 REMARK 465 MET i 1 REMARK 465 VAL i 2 REMARK 465 HIS i 3 REMARK 465 SER i 4 REMARK 465 SER i 123 REMARK 465 ALA i 124 REMARK 465 ALA i 125 REMARK 465 ALA i 126 REMARK 465 GLY i 127 REMARK 465 GLY i 128 REMARK 465 GLY i 129 REMARK 465 GLY i 130 REMARK 465 SER i 131 REMARK 465 GLY i 132 REMARK 465 GLY i 133 REMARK 465 GLY i 134 REMARK 465 GLY i 135 REMARK 465 SER i 136 REMARK 465 GLY i 137 REMARK 465 GLY i 138 REMARK 465 GLY i 139 REMARK 465 GLY i 140 REMARK 465 SER i 141 REMARK 465 VAL i 142 REMARK 465 HIS i 143 REMARK 465 LYS i 251 REMARK 465 HIS i 252 REMARK 465 HIS i 253 REMARK 465 HIS i 254 REMARK 465 HIS i 255 REMARK 465 HIS i 256 REMARK 465 HIS i 257 REMARK 465 MET k 1 REMARK 465 VAL k 2 REMARK 465 HIS k 3 REMARK 465 SER k 4 REMARK 465 SER k 123 REMARK 465 ALA k 124 REMARK 465 ALA k 125 REMARK 465 ALA k 126 REMARK 465 GLY k 127 REMARK 465 GLY k 128 REMARK 465 GLY k 129 REMARK 465 GLY k 130 REMARK 465 SER k 131 REMARK 465 GLY k 132 REMARK 465 GLY k 133 REMARK 465 GLY k 134 REMARK 465 GLY k 135 REMARK 465 SER k 136 REMARK 465 GLY k 137 REMARK 465 GLY k 138 REMARK 465 GLY k 139 REMARK 465 GLY k 140 REMARK 465 SER k 141 REMARK 465 VAL k 142 REMARK 465 HIS k 143 REMARK 465 LYS k 251 REMARK 465 HIS k 252 REMARK 465 HIS k 253 REMARK 465 HIS k 254 REMARK 465 HIS k 255 REMARK 465 HIS k 256 REMARK 465 HIS k 257 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 OD2 ASP I 87 OH TYR g 106 2.04 REMARK 500 OD2 ASP F 87 OH TYR a 106 2.06 REMARK 500 OH TYR J 95 O ARG L 17 2.17 REMARK 500 O ARG C 17 OH TYR G 95 2.17 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 ALA B 16 54.70 38.59 REMARK 500 CYS G 109 -37.16 -130.53 REMARK 500 SER I 20 -168.26 -124.75 REMARK 500 CYS J 109 -36.94 -130.32 REMARK 500 CYS Q 109 -38.63 -130.16 REMARK 500 LEU a 191 -60.81 -94.19 REMARK 500 THR a 195 -17.08 72.98 REMARK 500 SER a 196 -3.73 -143.14 REMARK 500 SER a 211 -32.59 -130.05 REMARK 500 ASN c 108 30.53 -94.19 REMARK 500 ASN c 175 11.52 59.93 REMARK 500 THR c 195 -16.42 73.19 REMARK 500 SER c 196 -3.63 -143.00 REMARK 500 ASN e 108 52.86 -92.79 REMARK 500 SER e 109 35.44 -92.16 REMARK 500 THR e 195 -16.27 73.45 REMARK 500 SER e 196 -3.57 -142.95 REMARK 500 SER e 220 47.86 -82.73 REMARK 500 ASN e 221 174.60 179.19 REMARK 500 LEU g 191 -61.16 -94.41 REMARK 500 THR g 195 -16.65 72.89 REMARK 500 SER g 196 -15.07 -140.77 REMARK 500 SER g 211 -32.47 -130.41 REMARK 500 ASN i 175 11.19 59.62 REMARK 500 THR i 195 -16.37 73.40 REMARK 500 SER i 196 -15.07 -140.96 REMARK 500 VAL k 120 127.43 72.75 REMARK 500 LEU k 191 -61.87 -95.68 REMARK 500 THR k 195 -16.08 73.48 REMARK 500 SER k 196 -14.74 -140.87 REMARK 500 SER k 211 -31.34 -130.60 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48248 RELATED DB: EMDB REMARK 900 SCFV ANTIBODY CL33 BOUND TO R-PHYCOERYTHRIN DBREF 9MGB A 1 164 PDB 9MGB 9MGB 1 164 DBREF 9MGB B 1 176 PDB 9MGB 9MGB 1 176 DBREF 9MGB C 1 164 PDB 9MGB 9MGB 1 164 DBREF 9MGB D 1 176 PDB 9MGB 9MGB 1 176 DBREF 9MGB F 1 164 PDB 9MGB 9MGB 1 164 DBREF 9MGB G 1 176 PDB 9MGB 9MGB 1 176 DBREF 9MGB I 1 164 PDB 9MGB 9MGB 1 164 DBREF 9MGB J 1 176 PDB 9MGB 9MGB 1 176 DBREF 9MGB L 1 164 PDB 9MGB 9MGB 1 164 DBREF 9MGB M 1 176 PDB 9MGB 9MGB 1 176 DBREF 9MGB O 1 164 PDB 9MGB 9MGB 1 164 DBREF 9MGB Q 1 176 PDB 9MGB 9MGB 1 176 DBREF 9MGB a 1 257 PDB 9MGB 9MGB 1 257 DBREF 9MGB c 1 257 PDB 9MGB 9MGB 1 257 DBREF 9MGB e 1 257 PDB 9MGB 9MGB 1 257 DBREF 9MGB g 1 257 PDB 9MGB 9MGB 1 257 DBREF 9MGB i 1 257 PDB 9MGB 9MGB 1 257 DBREF 9MGB k 1 257 PDB 9MGB 9MGB 1 257 SEQRES 1 A 164 MET LYS SER VAL ILE THR THR THR ILE SER ALA ALA ASP SEQRES 2 A 164 ALA ALA GLY ARG PHE PRO SER SER SER ASP LEU GLU SER SEQRES 3 A 164 VAL GLN GLY ASN ILE GLN ARG ALA ALA SER ARG LEU GLU SEQRES 4 A 164 ALA ALA GLU LYS LEU ALA GLY ASN HIS GLU ALA VAL VAL SEQRES 5 A 164 LYS GLU ALA GLY ASP ALA CYS PHE ALA LYS TYR PRO TYR SEQRES 6 A 164 LEU LYS ASN PRO GLY GLU ALA GLY ASP SER GLN GLU LYS SEQRES 7 A 164 ILE ASN LYS CYS TYR ARG ASP ILE ASP HIS TYR MET ARG SEQRES 8 A 164 LEU ILE ASN TYR SER LEU VAL VAL GLY GLY THR GLY PRO SEQRES 9 A 164 LEU ASP GLU TRP GLY ILE ALA GLY ALA ARG GLU VAL TYR SEQRES 10 A 164 ARG ALA LEU ASN LEU PRO GLY SER SER TYR ILE ALA ALA SEQRES 11 A 164 PHE VAL PHE THR ARG ASP ARG LEU CYS VAL PRO ARG ASP SEQRES 12 A 164 MET SER ALA GLN ALA ALA VAL GLU PHE SER GLY ALA LEU SEQRES 13 A 164 ASP TYR VAL ILE ASN SER LEU CYS SEQRES 1 B 176 MET LEU ASP ALA PHE SER ARG VAL VAL VAL ASN SER ASP SEQRES 2 B 176 SER LYS ALA ALA TYR VAL SER GLY SER ASP LEU GLN ALA SEQRES 3 B 176 LEU LYS THR PHE ILE ALA ASP GLY ASN LYS ARG LEU ASP SEQRES 4 B 176 ALA VAL ASN SER ILE VAL SER ASN ALA SER CYS ILE VAL SEQRES 5 B 176 SER ASP ALA VAL SER GLY MET ILE CYS GLU ASN PRO GLY SEQRES 6 B 176 LEU ILE ALA PRO GLY GLY ASN CYS TYR THR ASN ARG ARG SEQRES 7 B 176 MET ALA ALA CYS LEU ARG ASP GLY GLU ILE ILE LEU ARG SEQRES 8 B 176 TYR THR SER TYR ALA LEU LEU ALA GLY ASP SER SER VAL SEQRES 9 B 176 LEU GLU ASP ARG CYS LEU ASN GLY LEU LYS GLU THR TYR SEQRES 10 B 176 ILE ALA LEU GLY VAL PRO THR ASN SER THR VAL ARG ALA SEQRES 11 B 176 VAL SER ILE MET LYS SER SER ALA VAL ALA PHE ILE SER SEQRES 12 B 176 ASN THR ALA SER GLN ARG LYS MET ALA THR ALA ASP GLY SEQRES 13 B 176 ASP CYS SER ALA LEU SER SER GLU VAL ALA SER TYR CYS SEQRES 14 B 176 ASP LYS VAL SER ALA ALA ILE SEQRES 1 C 164 MET LYS SER VAL ILE THR THR THR ILE SER ALA ALA ASP SEQRES 2 C 164 ALA ALA GLY ARG PHE PRO SER SER SER ASP LEU GLU SER SEQRES 3 C 164 VAL GLN GLY ASN ILE GLN ARG ALA ALA SER ARG LEU GLU SEQRES 4 C 164 ALA ALA GLU LYS LEU ALA GLY ASN HIS GLU ALA VAL VAL SEQRES 5 C 164 LYS GLU ALA GLY ASP ALA CYS PHE ALA LYS TYR PRO TYR SEQRES 6 C 164 LEU LYS ASN PRO GLY GLU ALA GLY ASP SER GLN GLU LYS SEQRES 7 C 164 ILE ASN LYS CYS TYR ARG ASP ILE ASP HIS TYR MET ARG SEQRES 8 C 164 LEU ILE ASN TYR SER LEU VAL VAL GLY GLY THR GLY PRO SEQRES 9 C 164 LEU ASP GLU TRP GLY ILE ALA GLY ALA ARG GLU VAL TYR SEQRES 10 C 164 ARG ALA LEU ASN LEU PRO GLY SER SER TYR ILE ALA ALA SEQRES 11 C 164 PHE VAL PHE THR ARG ASP ARG LEU CYS VAL PRO ARG ASP SEQRES 12 C 164 MET SER ALA GLN ALA ALA VAL GLU PHE SER GLY ALA LEU SEQRES 13 C 164 ASP TYR VAL ILE ASN SER LEU CYS SEQRES 1 D 176 MET LEU ASP ALA PHE SER ARG VAL VAL VAL ASN SER ASP SEQRES 2 D 176 SER LYS ALA ALA TYR VAL SER GLY SER ASP LEU GLN ALA SEQRES 3 D 176 LEU LYS THR PHE ILE ALA ASP GLY ASN LYS ARG LEU ASP SEQRES 4 D 176 ALA VAL ASN SER ILE VAL SER ASN ALA SER CYS ILE VAL SEQRES 5 D 176 SER ASP ALA VAL SER GLY MET ILE CYS GLU ASN PRO GLY SEQRES 6 D 176 LEU ILE ALA PRO GLY GLY ASN CYS TYR THR ASN ARG ARG SEQRES 7 D 176 MET ALA ALA CYS LEU ARG ASP GLY GLU ILE ILE LEU ARG SEQRES 8 D 176 TYR THR SER TYR ALA LEU LEU ALA GLY ASP SER SER VAL SEQRES 9 D 176 LEU GLU ASP ARG CYS LEU ASN GLY LEU LYS GLU THR TYR SEQRES 10 D 176 ILE ALA LEU GLY VAL PRO THR ASN SER THR VAL ARG ALA SEQRES 11 D 176 VAL SER ILE MET LYS SER SER ALA VAL ALA PHE ILE SER SEQRES 12 D 176 ASN THR ALA SER GLN ARG LYS MET ALA THR ALA ASP GLY SEQRES 13 D 176 ASP CYS SER ALA LEU SER SER GLU VAL ALA SER TYR CYS SEQRES 14 D 176 ASP LYS VAL SER ALA ALA ILE SEQRES 1 F 164 MET LYS SER VAL ILE THR THR THR ILE SER ALA ALA ASP SEQRES 2 F 164 ALA ALA GLY ARG PHE PRO SER SER SER ASP LEU GLU SER SEQRES 3 F 164 VAL GLN GLY ASN ILE GLN ARG ALA ALA SER ARG LEU GLU SEQRES 4 F 164 ALA ALA GLU LYS LEU ALA GLY ASN HIS GLU ALA VAL VAL SEQRES 5 F 164 LYS GLU ALA GLY ASP ALA CYS PHE ALA LYS TYR PRO TYR SEQRES 6 F 164 LEU LYS ASN PRO GLY GLU ALA GLY ASP SER GLN GLU LYS SEQRES 7 F 164 ILE ASN LYS CYS TYR ARG ASP ILE ASP HIS TYR MET ARG SEQRES 8 F 164 LEU ILE ASN TYR SER LEU VAL VAL GLY GLY THR GLY PRO SEQRES 9 F 164 LEU ASP GLU TRP GLY ILE ALA GLY ALA ARG GLU VAL TYR SEQRES 10 F 164 ARG ALA LEU ASN LEU PRO GLY SER SER TYR ILE ALA ALA SEQRES 11 F 164 PHE VAL PHE THR ARG ASP ARG LEU CYS VAL PRO ARG ASP SEQRES 12 F 164 MET SER ALA GLN ALA ALA VAL GLU PHE SER GLY ALA LEU SEQRES 13 F 164 ASP TYR VAL ILE ASN SER LEU CYS SEQRES 1 G 176 MET LEU ASP ALA PHE SER ARG VAL VAL VAL ASN SER ASP SEQRES 2 G 176 SER LYS ALA ALA TYR VAL SER GLY SER ASP LEU GLN ALA SEQRES 3 G 176 LEU LYS THR PHE ILE ALA ASP GLY ASN LYS ARG LEU ASP SEQRES 4 G 176 ALA VAL ASN SER ILE VAL SER ASN ALA SER CYS ILE VAL SEQRES 5 G 176 SER ASP ALA VAL SER GLY MET ILE CYS GLU ASN PRO GLY SEQRES 6 G 176 LEU ILE ALA PRO GLY GLY ASN CYS TYR THR ASN ARG ARG SEQRES 7 G 176 MET ALA ALA CYS LEU ARG ASP GLY GLU ILE ILE LEU ARG SEQRES 8 G 176 TYR THR SER TYR ALA LEU LEU ALA GLY ASP SER SER VAL SEQRES 9 G 176 LEU GLU ASP ARG CYS LEU ASN GLY LEU LYS GLU THR TYR SEQRES 10 G 176 ILE ALA LEU GLY VAL PRO THR ASN SER THR VAL ARG ALA SEQRES 11 G 176 VAL SER ILE MET LYS SER SER ALA VAL ALA PHE ILE SER SEQRES 12 G 176 ASN THR ALA SER GLN ARG LYS MET ALA THR ALA ASP GLY SEQRES 13 G 176 ASP CYS SER ALA LEU SER SER GLU VAL ALA SER TYR CYS SEQRES 14 G 176 ASP LYS VAL SER ALA ALA ILE SEQRES 1 I 164 MET LYS SER VAL ILE THR THR THR ILE SER ALA ALA ASP SEQRES 2 I 164 ALA ALA GLY ARG PHE PRO SER SER SER ASP LEU GLU SER SEQRES 3 I 164 VAL GLN GLY ASN ILE GLN ARG ALA ALA SER ARG LEU GLU SEQRES 4 I 164 ALA ALA GLU LYS LEU ALA GLY ASN HIS GLU ALA VAL VAL SEQRES 5 I 164 LYS GLU ALA GLY ASP ALA CYS PHE ALA LYS TYR PRO TYR SEQRES 6 I 164 LEU LYS ASN PRO GLY GLU ALA GLY ASP SER GLN GLU LYS SEQRES 7 I 164 ILE ASN LYS CYS TYR ARG ASP ILE ASP HIS TYR MET ARG SEQRES 8 I 164 LEU ILE ASN TYR SER LEU VAL VAL GLY GLY THR GLY PRO SEQRES 9 I 164 LEU ASP GLU TRP GLY ILE ALA GLY ALA ARG GLU VAL TYR SEQRES 10 I 164 ARG ALA LEU ASN LEU PRO GLY SER SER TYR ILE ALA ALA SEQRES 11 I 164 PHE VAL PHE THR ARG ASP ARG LEU CYS VAL PRO ARG ASP SEQRES 12 I 164 MET SER ALA GLN ALA ALA VAL GLU PHE SER GLY ALA LEU SEQRES 13 I 164 ASP TYR VAL ILE ASN SER LEU CYS SEQRES 1 J 176 MET LEU ASP ALA PHE SER ARG VAL VAL VAL ASN SER ASP SEQRES 2 J 176 SER LYS ALA ALA TYR VAL SER GLY SER ASP LEU GLN ALA SEQRES 3 J 176 LEU LYS THR PHE ILE ALA ASP GLY ASN LYS ARG LEU ASP SEQRES 4 J 176 ALA VAL ASN SER ILE VAL SER ASN ALA SER CYS ILE VAL SEQRES 5 J 176 SER ASP ALA VAL SER GLY MET ILE CYS GLU ASN PRO GLY SEQRES 6 J 176 LEU ILE ALA PRO GLY GLY ASN CYS TYR THR ASN ARG ARG SEQRES 7 J 176 MET ALA ALA CYS LEU ARG ASP GLY GLU ILE ILE LEU ARG SEQRES 8 J 176 TYR THR SER TYR ALA LEU LEU ALA GLY ASP SER SER VAL SEQRES 9 J 176 LEU GLU ASP ARG CYS LEU ASN GLY LEU LYS GLU THR TYR SEQRES 10 J 176 ILE ALA LEU GLY VAL PRO THR ASN SER THR VAL ARG ALA SEQRES 11 J 176 VAL SER ILE MET LYS SER SER ALA VAL ALA PHE ILE SER SEQRES 12 J 176 ASN THR ALA SER GLN ARG LYS MET ALA THR ALA ASP GLY SEQRES 13 J 176 ASP CYS SER ALA LEU SER SER GLU VAL ALA SER TYR CYS SEQRES 14 J 176 ASP LYS VAL SER ALA ALA ILE SEQRES 1 L 164 MET LYS SER VAL ILE THR THR THR ILE SER ALA ALA ASP SEQRES 2 L 164 ALA ALA GLY ARG PHE PRO SER SER SER ASP LEU GLU SER SEQRES 3 L 164 VAL GLN GLY ASN ILE GLN ARG ALA ALA SER ARG LEU GLU SEQRES 4 L 164 ALA ALA GLU LYS LEU ALA GLY ASN HIS GLU ALA VAL VAL SEQRES 5 L 164 LYS GLU ALA GLY ASP ALA CYS PHE ALA LYS TYR PRO TYR SEQRES 6 L 164 LEU LYS ASN PRO GLY GLU ALA GLY ASP SER GLN GLU LYS SEQRES 7 L 164 ILE ASN LYS CYS TYR ARG ASP ILE ASP HIS TYR MET ARG SEQRES 8 L 164 LEU ILE ASN TYR SER LEU VAL VAL GLY GLY THR GLY PRO SEQRES 9 L 164 LEU ASP GLU TRP GLY ILE ALA GLY ALA ARG GLU VAL TYR SEQRES 10 L 164 ARG ALA LEU ASN LEU PRO GLY SER SER TYR ILE ALA ALA SEQRES 11 L 164 PHE VAL PHE THR ARG ASP ARG LEU CYS VAL PRO ARG ASP SEQRES 12 L 164 MET SER ALA GLN ALA ALA VAL GLU PHE SER GLY ALA LEU SEQRES 13 L 164 ASP TYR VAL ILE ASN SER LEU CYS SEQRES 1 M 176 MET LEU ASP ALA PHE SER ARG VAL VAL VAL ASN SER ASP SEQRES 2 M 176 SER LYS ALA ALA TYR VAL SER GLY SER ASP LEU GLN ALA SEQRES 3 M 176 LEU LYS THR PHE ILE ALA ASP GLY ASN LYS ARG LEU ASP SEQRES 4 M 176 ALA VAL ASN SER ILE VAL SER ASN ALA SER CYS ILE VAL SEQRES 5 M 176 SER ASP ALA VAL SER GLY MET ILE CYS GLU ASN PRO GLY SEQRES 6 M 176 LEU ILE ALA PRO GLY GLY ASN CYS TYR THR ASN ARG ARG SEQRES 7 M 176 MET ALA ALA CYS LEU ARG ASP GLY GLU ILE ILE LEU ARG SEQRES 8 M 176 TYR THR SER TYR ALA LEU LEU ALA GLY ASP SER SER VAL SEQRES 9 M 176 LEU GLU ASP ARG CYS LEU ASN GLY LEU LYS GLU THR TYR SEQRES 10 M 176 ILE ALA LEU GLY VAL PRO THR ASN SER THR VAL ARG ALA SEQRES 11 M 176 VAL SER ILE MET LYS SER SER ALA VAL ALA PHE ILE SER SEQRES 12 M 176 ASN THR ALA SER GLN ARG LYS MET ALA THR ALA ASP GLY SEQRES 13 M 176 ASP CYS SER ALA LEU SER SER GLU VAL ALA SER TYR CYS SEQRES 14 M 176 ASP LYS VAL SER ALA ALA ILE SEQRES 1 O 164 MET LYS SER VAL ILE THR THR THR ILE SER ALA ALA ASP SEQRES 2 O 164 ALA ALA GLY ARG PHE PRO SER SER SER ASP LEU GLU SER SEQRES 3 O 164 VAL GLN GLY ASN ILE GLN ARG ALA ALA SER ARG LEU GLU SEQRES 4 O 164 ALA ALA GLU LYS LEU ALA GLY ASN HIS GLU ALA VAL VAL SEQRES 5 O 164 LYS GLU ALA GLY ASP ALA CYS PHE ALA LYS TYR PRO TYR SEQRES 6 O 164 LEU LYS ASN PRO GLY GLU ALA GLY ASP SER GLN GLU LYS SEQRES 7 O 164 ILE ASN LYS CYS TYR ARG ASP ILE ASP HIS TYR MET ARG SEQRES 8 O 164 LEU ILE ASN TYR SER LEU VAL VAL GLY GLY THR GLY PRO SEQRES 9 O 164 LEU ASP GLU TRP GLY ILE ALA GLY ALA ARG GLU VAL TYR SEQRES 10 O 164 ARG ALA LEU ASN LEU PRO GLY SER SER TYR ILE ALA ALA SEQRES 11 O 164 PHE VAL PHE THR ARG ASP ARG LEU CYS VAL PRO ARG ASP SEQRES 12 O 164 MET SER ALA GLN ALA ALA VAL GLU PHE SER GLY ALA LEU SEQRES 13 O 164 ASP TYR VAL ILE ASN SER LEU CYS SEQRES 1 Q 176 MET LEU ASP ALA PHE SER ARG VAL VAL VAL ASN SER ASP SEQRES 2 Q 176 SER LYS ALA ALA TYR VAL SER GLY SER ASP LEU GLN ALA SEQRES 3 Q 176 LEU LYS THR PHE ILE ALA ASP GLY ASN LYS ARG LEU ASP SEQRES 4 Q 176 ALA VAL ASN SER ILE VAL SER ASN ALA SER CYS ILE VAL SEQRES 5 Q 176 SER ASP ALA VAL SER GLY MET ILE CYS GLU ASN PRO GLY SEQRES 6 Q 176 LEU ILE ALA PRO GLY GLY ASN CYS TYR THR ASN ARG ARG SEQRES 7 Q 176 MET ALA ALA CYS LEU ARG ASP GLY GLU ILE ILE LEU ARG SEQRES 8 Q 176 TYR THR SER TYR ALA LEU LEU ALA GLY ASP SER SER VAL SEQRES 9 Q 176 LEU GLU ASP ARG CYS LEU ASN GLY LEU LYS GLU THR TYR SEQRES 10 Q 176 ILE ALA LEU GLY VAL PRO THR ASN SER THR VAL ARG ALA SEQRES 11 Q 176 VAL SER ILE MET LYS SER SER ALA VAL ALA PHE ILE SER SEQRES 12 Q 176 ASN THR ALA SER GLN ARG LYS MET ALA THR ALA ASP GLY SEQRES 13 Q 176 ASP CYS SER ALA LEU SER SER GLU VAL ALA SER TYR CYS SEQRES 14 Q 176 ASP LYS VAL SER ALA ALA ILE SEQRES 1 a 257 MET VAL HIS SER GLU VAL GLN LEU GLN GLN SER GLY ALA SEQRES 2 a 257 GLU LEU ALA ARG PRO GLY ALA SER VAL LYS LEU SER CYS SEQRES 3 a 257 LYS ALA SER GLY TYR THR PHE THR SER TYR GLY ILE SER SEQRES 4 a 257 TRP VAL LYS GLN ARG THR GLY GLN GLY LEU GLU TRP ILE SEQRES 5 a 257 GLY GLU ILE TYR PRO ARG SER GLY ASN THR TYR TYR ASN SEQRES 6 a 257 GLU LYS PHE LYS GLY LYS ALA THR LEU THR ALA ASP LYS SEQRES 7 a 257 SER SER SER THR ALA TYR MET GLU LEU ARG SER LEU THR SEQRES 8 a 257 SER GLU ASP SER ALA VAL TYR PHE CYS ALA ARG GLN GLY SEQRES 9 a 257 TYR TYR ALA ASN SER GLN PHE THR TYR TRP GLY GLN GLY SEQRES 10 a 257 THR LEU VAL THR VAL SER ALA ALA ALA GLY GLY GLY GLY SEQRES 11 a 257 SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER VAL HIS SEQRES 12 a 257 SER ASP ILE GLN MET THR GLN THR THR SER SER LEU SER SEQRES 13 a 257 ALA SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SEQRES 14 a 257 SER GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN SEQRES 15 a 257 LYS PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SEQRES 16 a 257 SER SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 17 a 257 SER GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN SEQRES 18 a 257 LEU GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN SEQRES 19 a 257 TYR SER LYS LEU PRO TRP THR PHE GLY GLY GLY THR ASN SEQRES 20 a 257 LEU GLU ILE LYS HIS HIS HIS HIS HIS HIS SEQRES 1 c 257 MET VAL HIS SER GLU VAL GLN LEU GLN GLN SER GLY ALA SEQRES 2 c 257 GLU LEU ALA ARG PRO GLY ALA SER VAL LYS LEU SER CYS SEQRES 3 c 257 LYS ALA SER GLY TYR THR PHE THR SER TYR GLY ILE SER SEQRES 4 c 257 TRP VAL LYS GLN ARG THR GLY GLN GLY LEU GLU TRP ILE SEQRES 5 c 257 GLY GLU ILE TYR PRO ARG SER GLY ASN THR TYR TYR ASN SEQRES 6 c 257 GLU LYS PHE LYS GLY LYS ALA THR LEU THR ALA ASP LYS SEQRES 7 c 257 SER SER SER THR ALA TYR MET GLU LEU ARG SER LEU THR SEQRES 8 c 257 SER GLU ASP SER ALA VAL TYR PHE CYS ALA ARG GLN GLY SEQRES 9 c 257 TYR TYR ALA ASN SER GLN PHE THR TYR TRP GLY GLN GLY SEQRES 10 c 257 THR LEU VAL THR VAL SER ALA ALA ALA GLY GLY GLY GLY SEQRES 11 c 257 SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER VAL HIS SEQRES 12 c 257 SER ASP ILE GLN MET THR GLN THR THR SER SER LEU SER SEQRES 13 c 257 ALA SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SEQRES 14 c 257 SER GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN SEQRES 15 c 257 LYS PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SEQRES 16 c 257 SER SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 17 c 257 SER GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN SEQRES 18 c 257 LEU GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN SEQRES 19 c 257 TYR SER LYS LEU PRO TRP THR PHE GLY GLY GLY THR ASN SEQRES 20 c 257 LEU GLU ILE LYS HIS HIS HIS HIS HIS HIS SEQRES 1 e 257 MET VAL HIS SER GLU VAL GLN LEU GLN GLN SER GLY ALA SEQRES 2 e 257 GLU LEU ALA ARG PRO GLY ALA SER VAL LYS LEU SER CYS SEQRES 3 e 257 LYS ALA SER GLY TYR THR PHE THR SER TYR GLY ILE SER SEQRES 4 e 257 TRP VAL LYS GLN ARG THR GLY GLN GLY LEU GLU TRP ILE SEQRES 5 e 257 GLY GLU ILE TYR PRO ARG SER GLY ASN THR TYR TYR ASN SEQRES 6 e 257 GLU LYS PHE LYS GLY LYS ALA THR LEU THR ALA ASP LYS SEQRES 7 e 257 SER SER SER THR ALA TYR MET GLU LEU ARG SER LEU THR SEQRES 8 e 257 SER GLU ASP SER ALA VAL TYR PHE CYS ALA ARG GLN GLY SEQRES 9 e 257 TYR TYR ALA ASN SER GLN PHE THR TYR TRP GLY GLN GLY SEQRES 10 e 257 THR LEU VAL THR VAL SER ALA ALA ALA GLY GLY GLY GLY SEQRES 11 e 257 SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER VAL HIS SEQRES 12 e 257 SER ASP ILE GLN MET THR GLN THR THR SER SER LEU SER SEQRES 13 e 257 ALA SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SEQRES 14 e 257 SER GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN SEQRES 15 e 257 LYS PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SEQRES 16 e 257 SER SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 17 e 257 SER GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN SEQRES 18 e 257 LEU GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN SEQRES 19 e 257 TYR SER LYS LEU PRO TRP THR PHE GLY GLY GLY THR ASN SEQRES 20 e 257 LEU GLU ILE LYS HIS HIS HIS HIS HIS HIS SEQRES 1 g 257 MET VAL HIS SER GLU VAL GLN LEU GLN GLN SER GLY ALA SEQRES 2 g 257 GLU LEU ALA ARG PRO GLY ALA SER VAL LYS LEU SER CYS SEQRES 3 g 257 LYS ALA SER GLY TYR THR PHE THR SER TYR GLY ILE SER SEQRES 4 g 257 TRP VAL LYS GLN ARG THR GLY GLN GLY LEU GLU TRP ILE SEQRES 5 g 257 GLY GLU ILE TYR PRO ARG SER GLY ASN THR TYR TYR ASN SEQRES 6 g 257 GLU LYS PHE LYS GLY LYS ALA THR LEU THR ALA ASP LYS SEQRES 7 g 257 SER SER SER THR ALA TYR MET GLU LEU ARG SER LEU THR SEQRES 8 g 257 SER GLU ASP SER ALA VAL TYR PHE CYS ALA ARG GLN GLY SEQRES 9 g 257 TYR TYR ALA ASN SER GLN PHE THR TYR TRP GLY GLN GLY SEQRES 10 g 257 THR LEU VAL THR VAL SER ALA ALA ALA GLY GLY GLY GLY SEQRES 11 g 257 SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER VAL HIS SEQRES 12 g 257 SER ASP ILE GLN MET THR GLN THR THR SER SER LEU SER SEQRES 13 g 257 ALA SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SEQRES 14 g 257 SER GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN SEQRES 15 g 257 LYS PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SEQRES 16 g 257 SER SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 17 g 257 SER GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN SEQRES 18 g 257 LEU GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN SEQRES 19 g 257 TYR SER LYS LEU PRO TRP THR PHE GLY GLY GLY THR ASN SEQRES 20 g 257 LEU GLU ILE LYS HIS HIS HIS HIS HIS HIS SEQRES 1 i 257 MET VAL HIS SER GLU VAL GLN LEU GLN GLN SER GLY ALA SEQRES 2 i 257 GLU LEU ALA ARG PRO GLY ALA SER VAL LYS LEU SER CYS SEQRES 3 i 257 LYS ALA SER GLY TYR THR PHE THR SER TYR GLY ILE SER SEQRES 4 i 257 TRP VAL LYS GLN ARG THR GLY GLN GLY LEU GLU TRP ILE SEQRES 5 i 257 GLY GLU ILE TYR PRO ARG SER GLY ASN THR TYR TYR ASN SEQRES 6 i 257 GLU LYS PHE LYS GLY LYS ALA THR LEU THR ALA ASP LYS SEQRES 7 i 257 SER SER SER THR ALA TYR MET GLU LEU ARG SER LEU THR SEQRES 8 i 257 SER GLU ASP SER ALA VAL TYR PHE CYS ALA ARG GLN GLY SEQRES 9 i 257 TYR TYR ALA ASN SER GLN PHE THR TYR TRP GLY GLN GLY SEQRES 10 i 257 THR LEU VAL THR VAL SER ALA ALA ALA GLY GLY GLY GLY SEQRES 11 i 257 SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER VAL HIS SEQRES 12 i 257 SER ASP ILE GLN MET THR GLN THR THR SER SER LEU SER SEQRES 13 i 257 ALA SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SEQRES 14 i 257 SER GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN SEQRES 15 i 257 LYS PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SEQRES 16 i 257 SER SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 17 i 257 SER GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN SEQRES 18 i 257 LEU GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN SEQRES 19 i 257 TYR SER LYS LEU PRO TRP THR PHE GLY GLY GLY THR ASN SEQRES 20 i 257 LEU GLU ILE LYS HIS HIS HIS HIS HIS HIS SEQRES 1 k 257 MET VAL HIS SER GLU VAL GLN LEU GLN GLN SER GLY ALA SEQRES 2 k 257 GLU LEU ALA ARG PRO GLY ALA SER VAL LYS LEU SER CYS SEQRES 3 k 257 LYS ALA SER GLY TYR THR PHE THR SER TYR GLY ILE SER SEQRES 4 k 257 TRP VAL LYS GLN ARG THR GLY GLN GLY LEU GLU TRP ILE SEQRES 5 k 257 GLY GLU ILE TYR PRO ARG SER GLY ASN THR TYR TYR ASN SEQRES 6 k 257 GLU LYS PHE LYS GLY LYS ALA THR LEU THR ALA ASP LYS SEQRES 7 k 257 SER SER SER THR ALA TYR MET GLU LEU ARG SER LEU THR SEQRES 8 k 257 SER GLU ASP SER ALA VAL TYR PHE CYS ALA ARG GLN GLY SEQRES 9 k 257 TYR TYR ALA ASN SER GLN PHE THR TYR TRP GLY GLN GLY SEQRES 10 k 257 THR LEU VAL THR VAL SER ALA ALA ALA GLY GLY GLY GLY SEQRES 11 k 257 SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER VAL HIS SEQRES 12 k 257 SER ASP ILE GLN MET THR GLN THR THR SER SER LEU SER SEQRES 13 k 257 ALA SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SEQRES 14 k 257 SER GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN SEQRES 15 k 257 LYS PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SEQRES 16 k 257 SER SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 17 k 257 SER GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN SEQRES 18 k 257 LEU GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN SEQRES 19 k 257 TYR SER LYS LEU PRO TRP THR PHE GLY GLY GLY THR ASN SEQRES 20 k 257 LEU GLU ILE LYS HIS HIS HIS HIS HIS HIS HET PEB A 201 43 HET PEB A 202 43 HET PUB B 201 43 HET PEB B 202 43 HET PEB B 203 43 HET PEB C 201 43 HET PEB C 202 43 HET PUB D 201 43 HET PEB D 202 43 HET PEB D 203 43 HET PEB F 201 43 HET PEB F 202 43 HET PUB G 201 43 HET PEB G 202 43 HET PEB G 203 43 HET PEB I 201 43 HET PEB I 202 43 HET PUB J 201 43 HET PEB J 202 43 HET PEB J 203 43 HET PEB L 201 43 HET PEB L 202 43 HET PUB M 201 43 HET PEB M 202 43 HET PEB M 203 43 HET PEB O 201 43 HET PEB O 202 43 HET PUB Q 201 43 HET PEB Q 202 43 HET PEB Q 203 43 HETNAM PEB PHYCOERYTHROBILIN HETNAM PUB PHYCOUROBILIN FORMUL 19 PEB 24(C33 H40 N4 O6) FORMUL 21 PUB 6(C33 H42 N4 O6) HELIX 1 AA1 SER A 3 ALA A 15 1 13 HELIX 2 AA2 SER A 20 ASN A 47 1 28 HELIX 3 AA3 ASN A 47 TYR A 63 1 17 HELIX 4 AA4 PRO A 64 ASN A 68 5 5 HELIX 5 AA5 SER A 75 GLY A 100 1 26 HELIX 6 AA6 THR A 102 GLY A 109 1 8 HELIX 7 AA7 GLY A 112 LEU A 120 1 9 HELIX 8 AA8 PRO A 123 LEU A 138 1 16 HELIX 9 AA9 SER A 145 CYS A 164 1 20 HELIX 10 AB1 ASP B 3 SER B 14 1 12 HELIX 11 AB2 SER B 20 ASP B 33 1 14 HELIX 12 AB3 ASP B 33 SER B 46 1 14 HELIX 13 AB4 ASN B 47 ASN B 63 1 17 HELIX 14 AB5 PRO B 64 ALA B 68 5 5 HELIX 15 AB6 THR B 75 GLY B 100 1 26 HELIX 16 AB7 SER B 102 CYS B 109 1 8 HELIX 17 AB8 GLY B 112 GLY B 121 1 10 HELIX 18 AB9 PRO B 123 SER B 143 1 21 HELIX 19 AC1 CYS B 158 ILE B 176 1 19 HELIX 20 AC2 SER C 3 ALA C 15 1 13 HELIX 21 AC3 SER C 20 ASN C 47 1 28 HELIX 22 AC4 ASN C 47 TYR C 63 1 17 HELIX 23 AC5 PRO C 64 ASN C 68 5 5 HELIX 24 AC6 SER C 75 GLY C 100 1 26 HELIX 25 AC7 THR C 102 GLY C 109 1 8 HELIX 26 AC8 GLY C 112 LEU C 120 1 9 HELIX 27 AC9 PRO C 123 LEU C 138 1 16 HELIX 28 AD1 SER C 145 CYS C 164 1 20 HELIX 29 AD2 ASP D 3 LYS D 15 1 13 HELIX 30 AD3 SER D 20 ASP D 33 1 14 HELIX 31 AD4 ASP D 33 SER D 46 1 14 HELIX 32 AD5 ASN D 47 ASN D 63 1 17 HELIX 33 AD6 PRO D 64 ILE D 67 5 4 HELIX 34 AD7 THR D 75 GLY D 100 1 26 HELIX 35 AD8 SER D 102 LEU D 110 1 9 HELIX 36 AD9 GLY D 112 GLY D 121 1 10 HELIX 37 AE1 PRO D 123 SER D 143 1 21 HELIX 38 AE2 CYS D 158 ILE D 176 1 19 HELIX 39 AE3 SER F 3 ALA F 15 1 13 HELIX 40 AE4 SER F 20 ASN F 47 1 28 HELIX 41 AE5 ASN F 47 TYR F 63 1 17 HELIX 42 AE6 PRO F 64 ASN F 68 5 5 HELIX 43 AE7 SER F 75 GLY F 100 1 26 HELIX 44 AE8 THR F 102 GLY F 109 1 8 HELIX 45 AE9 GLY F 112 LEU F 120 1 9 HELIX 46 AF1 PRO F 123 LEU F 138 1 16 HELIX 47 AF2 SER F 145 CYS F 164 1 20 HELIX 48 AF3 ASP G 3 SER G 14 1 12 HELIX 49 AF4 SER G 20 ASP G 33 1 14 HELIX 50 AF5 ASP G 33 ASN G 47 1 15 HELIX 51 AF6 ASN G 47 ASN G 63 1 17 HELIX 52 AF7 PRO G 64 ILE G 67 5 4 HELIX 53 AF8 THR G 75 GLY G 100 1 26 HELIX 54 AF9 SER G 102 LEU G 110 1 9 HELIX 55 AG1 GLY G 112 GLY G 121 1 10 HELIX 56 AG2 PRO G 123 SER G 143 1 21 HELIX 57 AG3 CYS G 158 ILE G 176 1 19 HELIX 58 AG4 SER I 3 ALA I 15 1 13 HELIX 59 AG5 SER I 20 ASN I 47 1 28 HELIX 60 AG6 ASN I 47 TYR I 63 1 17 HELIX 61 AG7 PRO I 64 ASN I 68 5 5 HELIX 62 AG8 SER I 75 GLY I 100 1 26 HELIX 63 AG9 THR I 102 GLY I 109 1 8 HELIX 64 AH1 GLY I 112 LEU I 120 1 9 HELIX 65 AH2 PRO I 123 LEU I 138 1 16 HELIX 66 AH3 SER I 145 CYS I 164 1 20 HELIX 67 AH4 ASP J 3 SER J 14 1 12 HELIX 68 AH5 SER J 20 ASP J 33 1 14 HELIX 69 AH6 ASP J 33 SER J 46 1 14 HELIX 70 AH7 ASN J 47 ASN J 63 1 17 HELIX 71 AH8 PRO J 64 ILE J 67 5 4 HELIX 72 AH9 THR J 75 GLY J 100 1 26 HELIX 73 AI1 SER J 102 LEU J 110 1 9 HELIX 74 AI2 GLY J 112 GLY J 121 1 10 HELIX 75 AI3 PRO J 123 SER J 143 1 21 HELIX 76 AI4 CYS J 158 ILE J 176 1 19 HELIX 77 AI5 SER L 3 ALA L 15 1 13 HELIX 78 AI6 SER L 20 ASN L 47 1 28 HELIX 79 AI7 ASN L 47 TYR L 63 1 17 HELIX 80 AI8 PRO L 64 ASN L 68 5 5 HELIX 81 AI9 SER L 75 GLY L 100 1 26 HELIX 82 AJ1 THR L 102 GLY L 109 1 8 HELIX 83 AJ2 GLY L 112 LEU L 120 1 9 HELIX 84 AJ3 PRO L 123 LEU L 138 1 16 HELIX 85 AJ4 SER L 145 CYS L 164 1 20 HELIX 86 AJ5 ASP M 3 LYS M 15 1 13 HELIX 87 AJ6 SER M 20 ASP M 33 1 14 HELIX 88 AJ7 ASP M 33 SER M 46 1 14 HELIX 89 AJ8 ASN M 47 ASN M 63 1 17 HELIX 90 AJ9 PRO M 64 ILE M 67 5 4 HELIX 91 AK1 THR M 75 GLY M 100 1 26 HELIX 92 AK2 SER M 102 LEU M 110 1 9 HELIX 93 AK3 GLY M 112 GLY M 121 1 10 HELIX 94 AK4 PRO M 123 SER M 143 1 21 HELIX 95 AK5 CYS M 158 ILE M 176 1 19 HELIX 96 AK6 SER O 3 ALA O 15 1 13 HELIX 97 AK7 SER O 20 ASN O 47 1 28 HELIX 98 AK8 ASN O 47 TYR O 63 1 17 HELIX 99 AK9 PRO O 64 ASN O 68 5 5 HELIX 100 AL1 SER O 75 GLY O 100 1 26 HELIX 101 AL2 THR O 102 GLY O 109 1 8 HELIX 102 AL3 GLY O 112 LEU O 120 1 9 HELIX 103 AL4 PRO O 123 LEU O 138 1 16 HELIX 104 AL5 SER O 145 CYS O 164 1 20 HELIX 105 AL6 ASP Q 3 SER Q 14 1 12 HELIX 106 AL7 SER Q 20 ASP Q 33 1 14 HELIX 107 AL8 ASP Q 33 SER Q 46 1 14 HELIX 108 AL9 ASN Q 47 ASN Q 63 1 17 HELIX 109 AM1 PRO Q 64 ALA Q 68 5 5 HELIX 110 AM2 THR Q 75 GLY Q 100 1 26 HELIX 111 AM3 SER Q 102 LEU Q 110 1 9 HELIX 112 AM4 GLY Q 112 GLY Q 121 1 10 HELIX 113 AM5 PRO Q 123 SER Q 143 1 21 HELIX 114 AM6 CYS Q 158 ILE Q 176 1 19 HELIX 115 AM7 THR a 32 TYR a 36 5 5 HELIX 116 AM8 GLU a 66 LYS a 69 5 4 HELIX 117 AM9 THR a 91 SER a 95 5 5 HELIX 118 AN1 GLU a 223 ILE a 227 5 5 HELIX 119 AN2 THR c 32 TYR c 36 5 5 HELIX 120 AN3 GLU c 223 ILE c 227 5 5 HELIX 121 AN4 THR e 32 TYR e 36 5 5 HELIX 122 AN5 GLU e 223 ILE e 227 5 5 HELIX 123 AN6 THR g 32 TYR g 36 5 5 HELIX 124 AN7 GLU g 223 ILE g 227 5 5 HELIX 125 AN8 THR i 32 TYR i 36 5 5 HELIX 126 AN9 THR i 91 SER i 95 5 5 HELIX 127 AO1 GLU i 223 ILE i 227 5 5 HELIX 128 AO2 THR k 32 TYR k 36 5 5 HELIX 129 AO3 THR k 91 SER k 95 5 5 HELIX 130 AO4 GLU k 223 ILE k 227 5 5 SHEET 1 AA1 4 GLN a 9 GLN a 10 0 SHEET 2 AA1 4 VAL a 22 LYS a 27 -1 O LYS a 27 N GLN a 9 SHEET 3 AA1 4 THR a 82 LEU a 87 -1 O MET a 85 N LEU a 24 SHEET 4 AA1 4 ALA a 72 ASP a 77 -1 N THR a 75 O TYR a 84 SHEET 1 AA2 6 GLU a 14 LEU a 15 0 SHEET 2 AA2 6 THR a 118 THR a 121 1 O THR a 121 N GLU a 14 SHEET 3 AA2 6 ALA a 96 GLN a 103 -1 N ALA a 96 O VAL a 120 SHEET 4 AA2 6 GLY a 37 GLN a 43 -1 N GLY a 37 O GLN a 103 SHEET 5 AA2 6 LEU a 49 ILE a 55 -1 O GLU a 50 N LYS a 42 SHEET 6 AA2 6 THR a 62 TYR a 64 -1 O TYR a 63 N GLU a 54 SHEET 1 AA3 4 GLU a 14 LEU a 15 0 SHEET 2 AA3 4 THR a 118 THR a 121 1 O THR a 121 N GLU a 14 SHEET 3 AA3 4 ALA a 96 GLN a 103 -1 N ALA a 96 O VAL a 120 SHEET 4 AA3 4 PHE a 111 TRP a 114 -1 O TYR a 113 N ARG a 102 SHEET 1 AA4 4 MET a 148 THR a 149 0 SHEET 2 AA4 4 VAL a 163 ALA a 169 -1 O SER a 168 N THR a 149 SHEET 3 AA4 4 ASP a 214 ILE a 219 -1 O LEU a 217 N ILE a 165 SHEET 4 AA4 4 PHE a 206 GLY a 210 -1 N SER a 207 O THR a 218 SHEET 1 AA5 6 SER a 154 SER a 156 0 SHEET 2 AA5 6 THR a 246 GLU a 249 1 O ASN a 247 N LEU a 155 SHEET 3 AA5 6 ALA a 228 GLN a 234 -1 N TYR a 230 O THR a 246 SHEET 4 AA5 6 LEU a 177 GLN a 182 -1 N GLN a 182 O THR a 229 SHEET 5 AA5 6 VAL a 188 TYR a 193 -1 O ILE a 192 N TRP a 179 SHEET 6 AA5 6 SER a 197 LEU a 198 -1 O SER a 197 N TYR a 193 SHEET 1 AA6 4 SER a 154 SER a 156 0 SHEET 2 AA6 4 THR a 246 GLU a 249 1 O ASN a 247 N LEU a 155 SHEET 3 AA6 4 ALA a 228 GLN a 234 -1 N TYR a 230 O THR a 246 SHEET 4 AA6 4 THR a 241 PHE a 242 -1 O THR a 241 N GLN a 234 SHEET 1 AA7 4 GLN c 9 GLN c 10 0 SHEET 2 AA7 4 VAL c 22 LYS c 27 -1 O LYS c 27 N GLN c 9 SHEET 3 AA7 4 THR c 82 LEU c 87 -1 O MET c 85 N LEU c 24 SHEET 4 AA7 4 ALA c 72 ASP c 77 -1 N THR c 75 O TYR c 84 SHEET 1 AA8 5 THR c 62 TYR c 64 0 SHEET 2 AA8 5 LEU c 49 ILE c 55 -1 N GLU c 54 O TYR c 63 SHEET 3 AA8 5 GLY c 37 GLN c 43 -1 N LYS c 42 O GLU c 50 SHEET 4 AA8 5 ALA c 96 GLN c 103 -1 O GLN c 103 N GLY c 37 SHEET 5 AA8 5 PHE c 111 TRP c 114 -1 O TYR c 113 N ARG c 102 SHEET 1 AA9 5 THR c 62 TYR c 64 0 SHEET 2 AA9 5 LEU c 49 ILE c 55 -1 N GLU c 54 O TYR c 63 SHEET 3 AA9 5 GLY c 37 GLN c 43 -1 N LYS c 42 O GLU c 50 SHEET 4 AA9 5 ALA c 96 GLN c 103 -1 O GLN c 103 N GLY c 37 SHEET 5 AA9 5 THR c 118 VAL c 120 -1 O THR c 118 N TYR c 98 SHEET 1 AB1 4 MET c 148 THR c 149 0 SHEET 2 AB1 4 VAL c 163 ALA c 169 -1 O SER c 168 N THR c 149 SHEET 3 AB1 4 ASP c 214 ILE c 219 -1 O LEU c 217 N ILE c 165 SHEET 4 AB1 4 PHE c 206 GLY c 210 -1 N SER c 207 O THR c 218 SHEET 1 AB2 6 SER c 154 SER c 156 0 SHEET 2 AB2 6 THR c 246 GLU c 249 1 O GLU c 249 N LEU c 155 SHEET 3 AB2 6 THR c 229 GLN c 234 -1 N TYR c 230 O THR c 246 SHEET 4 AB2 6 LEU c 177 GLN c 182 -1 N TYR c 180 O TYR c 231 SHEET 5 AB2 6 VAL c 188 TYR c 193 -1 O ILE c 192 N TRP c 179 SHEET 6 AB2 6 SER c 197 LEU c 198 -1 O SER c 197 N TYR c 193 SHEET 1 AB3 4 SER c 154 SER c 156 0 SHEET 2 AB3 4 THR c 246 GLU c 249 1 O GLU c 249 N LEU c 155 SHEET 3 AB3 4 THR c 229 GLN c 234 -1 N TYR c 230 O THR c 246 SHEET 4 AB3 4 THR c 241 PHE c 242 -1 O THR c 241 N GLN c 234 SHEET 1 AB4 4 GLN e 9 GLN e 10 0 SHEET 2 AB4 4 VAL e 22 LYS e 27 -1 O LYS e 27 N GLN e 9 SHEET 3 AB4 4 THR e 82 LEU e 87 -1 O MET e 85 N LEU e 24 SHEET 4 AB4 4 ALA e 72 ASP e 77 -1 N THR e 75 O TYR e 84 SHEET 1 AB5 6 GLU e 14 LEU e 15 0 SHEET 2 AB5 6 THR e 118 THR e 121 1 O THR e 121 N GLU e 14 SHEET 3 AB5 6 ALA e 96 GLN e 103 -1 N TYR e 98 O THR e 118 SHEET 4 AB5 6 GLY e 37 ARG e 44 -1 N GLY e 37 O GLN e 103 SHEET 5 AB5 6 LEU e 49 ILE e 55 -1 O GLU e 50 N LYS e 42 SHEET 6 AB5 6 THR e 62 TYR e 64 -1 O TYR e 63 N GLU e 54 SHEET 1 AB6 4 GLU e 14 LEU e 15 0 SHEET 2 AB6 4 THR e 118 THR e 121 1 O THR e 121 N GLU e 14 SHEET 3 AB6 4 ALA e 96 GLN e 103 -1 N TYR e 98 O THR e 118 SHEET 4 AB6 4 PHE e 111 TRP e 114 -1 O TYR e 113 N ARG e 102 SHEET 1 AB7 4 MET e 148 THR e 149 0 SHEET 2 AB7 4 VAL e 163 ALA e 169 -1 O SER e 168 N THR e 149 SHEET 3 AB7 4 ASP e 214 ILE e 219 -1 O LEU e 217 N ILE e 165 SHEET 4 AB7 4 PHE e 206 GLY e 210 -1 N SER e 207 O THR e 218 SHEET 1 AB8 5 SER e 197 LEU e 198 0 SHEET 2 AB8 5 VAL e 188 TYR e 193 -1 N TYR e 193 O SER e 197 SHEET 3 AB8 5 LEU e 177 GLN e 182 -1 N GLN e 181 O LYS e 189 SHEET 4 AB8 5 THR e 229 GLN e 234 -1 O TYR e 231 N TYR e 180 SHEET 5 AB8 5 THR e 241 PHE e 242 -1 O THR e 241 N GLN e 234 SHEET 1 AB9 5 SER e 197 LEU e 198 0 SHEET 2 AB9 5 VAL e 188 TYR e 193 -1 N TYR e 193 O SER e 197 SHEET 3 AB9 5 LEU e 177 GLN e 182 -1 N GLN e 181 O LYS e 189 SHEET 4 AB9 5 THR e 229 GLN e 234 -1 O TYR e 231 N TYR e 180 SHEET 5 AB9 5 THR e 246 ASN e 247 -1 O THR e 246 N TYR e 230 SHEET 1 AC1 4 GLN g 9 GLN g 10 0 SHEET 2 AC1 4 VAL g 22 LYS g 27 -1 O LYS g 27 N GLN g 9 SHEET 3 AC1 4 THR g 82 LEU g 87 -1 O MET g 85 N LEU g 24 SHEET 4 AC1 4 ALA g 72 ASP g 77 -1 N THR g 75 O TYR g 84 SHEET 1 AC2 6 GLU g 14 LEU g 15 0 SHEET 2 AC2 6 THR g 118 THR g 121 1 O THR g 121 N GLU g 14 SHEET 3 AC2 6 ALA g 96 GLN g 103 -1 N TYR g 98 O THR g 118 SHEET 4 AC2 6 GLY g 37 ARG g 44 -1 N GLY g 37 O GLN g 103 SHEET 5 AC2 6 LEU g 49 ILE g 55 -1 O GLU g 50 N LYS g 42 SHEET 6 AC2 6 THR g 62 TYR g 64 -1 O TYR g 63 N GLU g 54 SHEET 1 AC3 4 GLU g 14 LEU g 15 0 SHEET 2 AC3 4 THR g 118 THR g 121 1 O THR g 121 N GLU g 14 SHEET 3 AC3 4 ALA g 96 GLN g 103 -1 N TYR g 98 O THR g 118 SHEET 4 AC3 4 PHE g 111 TRP g 114 -1 O TYR g 113 N ARG g 102 SHEET 1 AC4 4 MET g 148 THR g 149 0 SHEET 2 AC4 4 VAL g 163 ALA g 169 -1 O SER g 168 N THR g 149 SHEET 3 AC4 4 ASP g 214 ILE g 219 -1 O LEU g 217 N ILE g 165 SHEET 4 AC4 4 PHE g 206 GLY g 210 -1 N SER g 207 O THR g 218 SHEET 1 AC5 6 SER g 154 SER g 156 0 SHEET 2 AC5 6 THR g 246 GLU g 249 1 O ASN g 247 N LEU g 155 SHEET 3 AC5 6 THR g 229 GLN g 234 -1 N TYR g 230 O THR g 246 SHEET 4 AC5 6 LEU g 177 GLN g 182 -1 N GLN g 182 O THR g 229 SHEET 5 AC5 6 VAL g 188 TYR g 193 -1 O ILE g 192 N TRP g 179 SHEET 6 AC5 6 SER g 197 LEU g 198 -1 O SER g 197 N TYR g 193 SHEET 1 AC6 4 SER g 154 SER g 156 0 SHEET 2 AC6 4 THR g 246 GLU g 249 1 O ASN g 247 N LEU g 155 SHEET 3 AC6 4 THR g 229 GLN g 234 -1 N TYR g 230 O THR g 246 SHEET 4 AC6 4 THR g 241 PHE g 242 -1 O THR g 241 N GLN g 234 SHEET 1 AC7 4 GLN i 9 GLN i 10 0 SHEET 2 AC7 4 VAL i 22 LYS i 27 -1 O LYS i 27 N GLN i 9 SHEET 3 AC7 4 THR i 82 LEU i 87 -1 O MET i 85 N LEU i 24 SHEET 4 AC7 4 ALA i 72 ASP i 77 -1 N ASP i 77 O THR i 82 SHEET 1 AC8 6 GLU i 14 LEU i 15 0 SHEET 2 AC8 6 THR i 118 THR i 121 1 O LEU i 119 N GLU i 14 SHEET 3 AC8 6 ALA i 96 GLN i 103 -1 N TYR i 98 O THR i 118 SHEET 4 AC8 6 GLY i 37 GLN i 43 -1 N GLY i 37 O GLN i 103 SHEET 5 AC8 6 GLU i 50 ILE i 55 -1 O GLU i 50 N LYS i 42 SHEET 6 AC8 6 THR i 62 TYR i 64 -1 O TYR i 63 N GLU i 54 SHEET 1 AC9 4 GLU i 14 LEU i 15 0 SHEET 2 AC9 4 THR i 118 THR i 121 1 O LEU i 119 N GLU i 14 SHEET 3 AC9 4 ALA i 96 GLN i 103 -1 N TYR i 98 O THR i 118 SHEET 4 AC9 4 PHE i 111 TRP i 114 -1 O TYR i 113 N ARG i 102 SHEET 1 AD1 4 MET i 148 THR i 149 0 SHEET 2 AD1 4 VAL i 163 ALA i 169 -1 O SER i 168 N THR i 149 SHEET 3 AD1 4 ASP i 214 ILE i 219 -1 O LEU i 217 N ILE i 165 SHEET 4 AD1 4 PHE i 206 GLY i 210 -1 N SER i 207 O THR i 218 SHEET 1 AD2 6 SER i 154 SER i 156 0 SHEET 2 AD2 6 THR i 246 GLU i 249 1 O ASN i 247 N LEU i 155 SHEET 3 AD2 6 THR i 229 GLN i 234 -1 N TYR i 230 O THR i 246 SHEET 4 AD2 6 LEU i 177 GLN i 182 -1 N ASN i 178 O GLN i 233 SHEET 5 AD2 6 VAL i 188 TYR i 193 -1 O ILE i 192 N TRP i 179 SHEET 6 AD2 6 SER i 197 LEU i 198 -1 O SER i 197 N TYR i 193 SHEET 1 AD3 4 SER i 154 SER i 156 0 SHEET 2 AD3 4 THR i 246 GLU i 249 1 O ASN i 247 N LEU i 155 SHEET 3 AD3 4 THR i 229 GLN i 234 -1 N TYR i 230 O THR i 246 SHEET 4 AD3 4 THR i 241 PHE i 242 -1 O THR i 241 N GLN i 234 SHEET 1 AD4 4 GLN k 9 GLN k 10 0 SHEET 2 AD4 4 VAL k 22 LYS k 27 -1 O LYS k 27 N GLN k 9 SHEET 3 AD4 4 THR k 82 LEU k 87 -1 O MET k 85 N LEU k 24 SHEET 4 AD4 4 ALA k 72 ASP k 77 -1 N THR k 73 O GLU k 86 SHEET 1 AD5 5 THR k 62 TYR k 64 0 SHEET 2 AD5 5 LEU k 49 ILE k 55 -1 N GLU k 54 O TYR k 63 SHEET 3 AD5 5 GLY k 37 GLN k 43 -1 N LYS k 42 O GLU k 50 SHEET 4 AD5 5 VAL k 97 GLN k 103 -1 O GLN k 103 N GLY k 37 SHEET 5 AD5 5 PHE k 111 TRP k 114 -1 O TYR k 113 N ARG k 102 SHEET 1 AD6 4 MET k 148 GLN k 150 0 SHEET 2 AD6 4 VAL k 163 ALA k 169 -1 O SER k 168 N THR k 149 SHEET 3 AD6 4 ASP k 214 ILE k 219 -1 O LEU k 217 N ILE k 165 SHEET 4 AD6 4 PHE k 206 GLY k 210 -1 N SER k 207 O THR k 218 SHEET 1 AD7 6 SER k 154 SER k 156 0 SHEET 2 AD7 6 THR k 246 GLU k 249 1 O ASN k 247 N LEU k 155 SHEET 3 AD7 6 THR k 229 GLN k 234 -1 N TYR k 230 O THR k 246 SHEET 4 AD7 6 LEU k 177 GLN k 182 -1 N ASN k 178 O GLN k 233 SHEET 5 AD7 6 VAL k 188 TYR k 193 -1 O ILE k 192 N TRP k 179 SHEET 6 AD7 6 SER k 197 LEU k 198 -1 O SER k 197 N TYR k 193 SHEET 1 AD8 4 SER k 154 SER k 156 0 SHEET 2 AD8 4 THR k 246 GLU k 249 1 O ASN k 247 N LEU k 155 SHEET 3 AD8 4 THR k 229 GLN k 234 -1 N TYR k 230 O THR k 246 SHEET 4 AD8 4 THR k 241 PHE k 242 -1 O THR k 241 N GLN k 234 SSBOND 1 CYS a 26 CYS a 100 1555 1555 2.03 SSBOND 2 CYS a 167 CYS a 232 1555 1555 2.03 SSBOND 3 CYS c 26 CYS c 100 1555 1555 2.03 SSBOND 4 CYS c 167 CYS c 232 1555 1555 2.03 SSBOND 5 CYS e 26 CYS e 100 1555 1555 2.03 SSBOND 6 CYS e 167 CYS e 232 1555 1555 2.03 SSBOND 7 CYS g 26 CYS g 100 1555 1555 2.03 SSBOND 8 CYS g 167 CYS g 232 1555 1555 2.04 SSBOND 9 CYS i 26 CYS i 100 1555 1555 2.03 SSBOND 10 CYS i 167 CYS i 232 1555 1555 2.04 SSBOND 11 CYS k 26 CYS k 100 1555 1555 2.03 SSBOND 12 CYS k 167 CYS k 232 1555 1555 2.03 LINK SG CYS B 158 CAA PEB B 203 1555 1555 1.83 LINK SG CYS C 139 CAA PEB C 202 1555 1555 1.84 LINK SG CYS D 158 CAA PEB D 203 1555 1555 1.83 LINK SG CYS F 139 CAA PEB F 202 1555 1555 1.84 LINK SG CYS G 158 CAA PEB G 203 1555 1555 1.83 LINK SG CYS I 139 CAA PEB I 202 1555 1555 1.84 LINK SG CYS J 158 CAA PEB J 203 1555 1555 1.83 LINK SG CYS M 158 CAA PEB M 203 1555 1555 1.83 LINK SG CYS O 139 CAA PEB O 202 1555 1555 1.84 LINK SG CYS Q 158 CAA PEB Q 203 1555 1555 1.83 CISPEP 1 VAL A 140 PRO A 141 0 -2.75 CISPEP 2 VAL C 140 PRO C 141 0 -1.82 CISPEP 3 VAL F 140 PRO F 141 0 -1.37 CISPEP 4 VAL I 140 PRO I 141 0 -2.11 CISPEP 5 VAL L 140 PRO L 141 0 -1.79 CISPEP 6 VAL O 140 PRO O 141 0 -0.44 CISPEP 7 LEU a 238 PRO a 239 0 -2.43 CISPEP 8 LEU c 238 PRO c 239 0 -2.12 CISPEP 9 LEU e 238 PRO e 239 0 -2.08 CISPEP 10 LEU g 238 PRO g 239 0 -2.40 CISPEP 11 LEU i 238 PRO i 239 0 -2.19 CISPEP 12 LEU k 238 PRO k 239 0 -1.16 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000