HEADER BIOSYNTHETIC PROTEIN 03-MAR-25 9QBJ TITLE LEGOBODY DIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: NANOBODY ALFA-H6; COMPND 3 CHAIN: C, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB ANTIBODY 8D3_2_H-H6; COMPND 7 CHAIN: E, G; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: FA ANTIBODY 8D3_2_L; COMPND 11 CHAIN: F, H; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: MALTOSE/MALTODEXTRIN-BINDING PERIPLASMIC PROTEIN, COMPND 15 IMMUNOGLOBULIN G-BINDING PROTEIN A,IMMUNOGLOBULIN G-BINDING PROTEIN COMPND 16 G; COMPND 17 CHAIN: I; COMPND 18 SYNONYM: MMBP,MALTODEXTRIN-BINDING PROTEIN,MALTOSE-BINDING PROTEIN, COMPND 19 MBP,IGG-BINDING PROTEIN A,STAPHYLOCOCCAL PROTEIN A,SPA,IGG-BINDING COMPND 20 PROTEIN G; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: MALTOSE/MALTODEXTRIN-BINDING PERIPLASMIC PROTEIN, COMPND 24 IMMUNOGLOBULIN G-BINDING PROTEIN A,IMMUNOGLOBULIN G-BINDING PROTEIN COMPND 25 G; COMPND 26 CHAIN: J; COMPND 27 SYNONYM: MMBP,MALTODEXTRIN-BINDING PROTEIN,MALTOSE-BINDING PROTEIN, COMPND 28 MBP,IGG-BINDING PROTEIN A,STAPHYLOCOCCAL PROTEIN A,SPA,IGG-BINDING COMPND 29 PROTEIN G; COMPND 30 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 3 ORGANISM_TAXID: 30538; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 13 ORGANISM_TAXID: 10090; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 MOL_ID: 4; SOURCE 17 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, STAPHYLOCOCCUS AUREUS SUBSP. SOURCE 18 AUREUS N315, STREPTOCOCCUS SP. 'GROUP G'; SOURCE 19 ORGANISM_TAXID: 562, 158879, 1320; SOURCE 20 GENE: MALE, Z5632, ECS5017, SPA, SAOUHSC_00069, SPA, SA0107, SPG; SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 23 MOL_ID: 5; SOURCE 24 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, STAPHYLOCOCCUS AUREUS SUBSP. SOURCE 25 AUREUS N315, STREPTOCOCCUS SP. 'GROUP G'; SOURCE 26 ORGANISM_TAXID: 562, 158879, 1320; SOURCE 27 GENE: MALE, Z5632, ECS5017, SPA, SAOUHSC_00069, SPA, SA0107, SPG; SOURCE 28 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS LEGOBODY, DIMER, ANTI-ALFA, BIOSYNTHETIC PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR M.PACESA,A.VAN HALL-BEAUVAIS,A.MARCHAND,S.GEORGEON,B.E.CORREIA REVDAT 1 11-JUN-25 9QBJ 0 JRNL AUTH M.PACESA,A.VAN HALL-BEAUVAIS,A.MARCHAND,S.GEORGEON, JRNL AUTH 2 B.E.CORREIA JRNL TITL STRUCTURE OF A CRYOEM SCAFFOLD JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.20 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) : 3.200 REMARK 3 NUMBER OF PARTICLES : 114803 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 9QBJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1292146018. 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 : LEGOBODY DIMER 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 : 7.50 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 : TFS GLACIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (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 : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4000.00 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: OCTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F, G, H, I, J, A, B 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 GLU C 3 REMARK 465 HIS C 135 REMARK 465 GLU D 3 REMARK 465 SER E 137 REMARK 465 SER E 138 REMARK 465 LYS E 139 REMARK 465 SER E 140 REMARK 465 THR E 141 REMARK 465 SER E 142 REMARK 465 GLY E 143 REMARK 465 GLY E 144 REMARK 465 THR E 145 REMARK 465 SER E 196 REMARK 465 SER E 197 REMARK 465 SER E 198 REMARK 465 LEU E 199 REMARK 465 GLY E 200 REMARK 465 THR E 201 REMARK 465 GLN E 202 REMARK 465 LYS E 224 REMARK 465 SER E 225 REMARK 465 CYS E 226 REMARK 465 GLY E 227 REMARK 465 SER E 228 REMARK 465 GLY E 229 REMARK 465 THR E 230 REMARK 465 LYS E 231 REMARK 465 HIS E 232 REMARK 465 HIS E 233 REMARK 465 HIS E 234 REMARK 465 HIS E 235 REMARK 465 HIS E 236 REMARK 465 HIS E 237 REMARK 465 ASP F 156 REMARK 465 ASN F 157 REMARK 465 ALA F 158 REMARK 465 LEU F 159 REMARK 465 GLN F 160 REMARK 465 SER F 161 REMARK 465 GLY F 162 REMARK 465 LEU F 206 REMARK 465 SER F 207 REMARK 465 SER F 208 REMARK 465 PRO F 209 REMARK 465 ARG F 216 REMARK 465 GLY F 217 REMARK 465 GLU F 218 REMARK 465 CYS F 219 REMARK 465 SER G 137 REMARK 465 SER G 138 REMARK 465 LYS G 139 REMARK 465 SER G 140 REMARK 465 THR G 141 REMARK 465 SER G 142 REMARK 465 GLY G 143 REMARK 465 GLY G 144 REMARK 465 THR G 145 REMARK 465 SER G 196 REMARK 465 SER G 197 REMARK 465 SER G 198 REMARK 465 LEU G 199 REMARK 465 GLY G 200 REMARK 465 THR G 201 REMARK 465 GLN G 202 REMARK 465 LYS G 224 REMARK 465 SER G 225 REMARK 465 CYS G 226 REMARK 465 GLY G 227 REMARK 465 SER G 228 REMARK 465 GLY G 229 REMARK 465 THR G 230 REMARK 465 LYS G 231 REMARK 465 HIS G 232 REMARK 465 HIS G 233 REMARK 465 HIS G 234 REMARK 465 HIS G 235 REMARK 465 HIS G 236 REMARK 465 HIS G 237 REMARK 465 ASP H 156 REMARK 465 ASN H 157 REMARK 465 ALA H 158 REMARK 465 LEU H 159 REMARK 465 GLN H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 LEU H 206 REMARK 465 SER H 207 REMARK 465 SER H 208 REMARK 465 PRO H 209 REMARK 465 ARG H 216 REMARK 465 GLY H 217 REMARK 465 GLU H 218 REMARK 465 CYS H 219 REMARK 465 MET I 1 REMARK 465 HIS I 2 REMARK 465 HIS I 3 REMARK 465 HIS I 4 REMARK 465 HIS I 5 REMARK 465 HIS I 6 REMARK 465 HIS I 7 REMARK 465 GLY I 8 REMARK 465 SER I 9 REMARK 465 LYS I 10 REMARK 465 ILE I 11 REMARK 465 GLU I 12 REMARK 465 GLU I 13 REMARK 465 GLY I 14 REMARK 465 LYS I 15 REMARK 465 GLU I 37 REMARK 465 LYS I 38 REMARK 465 ASP I 39 REMARK 465 THR I 40 REMARK 465 GLY I 41 REMARK 465 ILE I 42 REMARK 465 ALA I 61 REMARK 465 THR I 62 REMARK 465 GLY I 63 REMARK 465 ASP I 64 REMARK 465 GLY I 65 REMARK 465 ALA I 150 REMARK 465 LYS I 151 REMARK 465 GLY I 152 REMARK 465 LYS I 153 REMARK 465 SER I 154 REMARK 465 ALA I 155 REMARK 465 LYS I 417 REMARK 465 GLY I 418 REMARK 465 GLY I 419 REMARK 465 SER I 420 REMARK 465 GLY I 421 REMARK 465 GLY I 422 REMARK 465 ALA I 423 REMARK 465 GLY I 476 REMARK 465 GLY I 477 REMARK 465 GLY I 478 REMARK 465 SER I 479 REMARK 465 GLY I 480 REMARK 465 GLY I 481 REMARK 465 GLY I 482 REMARK 465 SER I 483 REMARK 465 GLY I 484 REMARK 465 GLY I 485 REMARK 465 SER I 486 REMARK 465 ALA I 487 REMARK 465 ILE I 495 REMARK 465 ASN I 496 REMARK 465 GLY I 497 REMARK 465 LYS I 498 REMARK 465 THR I 499 REMARK 465 ASP I 528 REMARK 465 GLY I 529 REMARK 465 VAL I 530 REMARK 465 MET J 1 REMARK 465 HIS J 2 REMARK 465 HIS J 3 REMARK 465 HIS J 4 REMARK 465 HIS J 5 REMARK 465 HIS J 6 REMARK 465 HIS J 7 REMARK 465 GLY J 8 REMARK 465 SER J 9 REMARK 465 LYS J 10 REMARK 465 ILE J 11 REMARK 465 GLU J 12 REMARK 465 GLU J 13 REMARK 465 GLY J 14 REMARK 465 LYS J 15 REMARK 465 LEU J 16 REMARK 465 VAL J 17 REMARK 465 ILE J 18 REMARK 465 TRP J 19 REMARK 465 ILE J 20 REMARK 465 ASN J 21 REMARK 465 GLY J 22 REMARK 465 ASP J 23 REMARK 465 LYS J 24 REMARK 465 GLY J 25 REMARK 465 TYR J 26 REMARK 465 ASN J 27 REMARK 465 GLY J 28 REMARK 465 LEU J 29 REMARK 465 ALA J 30 REMARK 465 GLU J 31 REMARK 465 VAL J 32 REMARK 465 GLY J 33 REMARK 465 LYS J 34 REMARK 465 LYS J 35 REMARK 465 PHE J 36 REMARK 465 GLU J 37 REMARK 465 LYS J 38 REMARK 465 ASP J 39 REMARK 465 THR J 40 REMARK 465 GLY J 41 REMARK 465 ILE J 42 REMARK 465 LYS J 43 REMARK 465 VAL J 44 REMARK 465 THR J 45 REMARK 465 VAL J 46 REMARK 465 GLU J 47 REMARK 465 HIS J 48 REMARK 465 PRO J 49 REMARK 465 ASP J 50 REMARK 465 LYS J 51 REMARK 465 LEU J 52 REMARK 465 GLU J 53 REMARK 465 GLU J 54 REMARK 465 LYS J 55 REMARK 465 PHE J 56 REMARK 465 PRO J 57 REMARK 465 GLN J 58 REMARK 465 VAL J 59 REMARK 465 ALA J 60 REMARK 465 ALA J 61 REMARK 465 THR J 62 REMARK 465 GLY J 63 REMARK 465 ASP J 64 REMARK 465 GLY J 65 REMARK 465 LEU J 84 REMARK 465 LEU J 85 REMARK 465 ALA J 86 REMARK 465 GLU J 87 REMARK 465 ILE J 88 REMARK 465 THR J 89 REMARK 465 PRO J 90 REMARK 465 ASP J 91 REMARK 465 LYS J 92 REMARK 465 TYR J 108 REMARK 465 ASN J 109 REMARK 465 GLY J 110 REMARK 465 LYS J 111 REMARK 465 ALA J 150 REMARK 465 LYS J 151 REMARK 465 GLY J 152 REMARK 465 LYS J 153 REMARK 465 SER J 154 REMARK 465 ALA J 155 REMARK 465 ALA J 277 REMARK 465 ALA J 278 REMARK 465 SER J 279 REMARK 465 PRO J 280 REMARK 465 ASN J 281 REMARK 465 LYS J 282 REMARK 465 LYS J 417 REMARK 465 GLY J 418 REMARK 465 GLY J 419 REMARK 465 SER J 420 REMARK 465 GLY J 421 REMARK 465 GLY J 422 REMARK 465 ALA J 423 REMARK 465 GLY J 424 REMARK 465 SER J 425 REMARK 465 GLY J 426 REMARK 465 ASP J 427 REMARK 465 GLY J 476 REMARK 465 GLY J 477 REMARK 465 GLY J 478 REMARK 465 SER J 479 REMARK 465 GLY J 480 REMARK 465 GLY J 481 REMARK 465 GLY J 482 REMARK 465 SER J 483 REMARK 465 GLY J 484 REMARK 465 GLY J 485 REMARK 465 SER J 486 REMARK 465 ALA J 487 REMARK 465 VAL J 527 REMARK 465 ASP J 528 REMARK 465 GLY J 529 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 OE1 GLU J 443 ND2 ASN J 447 2.17 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 ASP F 175 CB - CG - OD2 ANGL. DEV. = 6.8 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 ASN C 89 70.51 57.37 REMARK 500 VAL C 107 -66.84 62.94 REMARK 500 HIS C 133 -30.27 -130.19 REMARK 500 ARG D 106 32.20 -96.61 REMARK 500 VAL D 107 -59.99 63.36 REMARK 500 SER F 9 -130.76 58.39 REMARK 500 ALA F 57 -8.21 70.00 REMARK 500 SER F 58 -37.30 -130.61 REMARK 500 ALA F 100 -149.25 56.02 REMARK 500 ARG F 113 -169.76 -161.68 REMARK 500 ASN F 143 64.21 62.39 REMARK 500 SER F 176 37.31 70.53 REMARK 500 ALA H 57 -8.71 70.12 REMARK 500 SER H 58 -37.42 -131.31 REMARK 500 ALA H 100 -151.49 55.98 REMARK 500 LEU I 294 50.75 -91.71 REMARK 500 ASP J 173 34.62 -98.78 REMARK 500 ASN J 182 45.52 39.77 REMARK 500 LYS J 248 12.11 54.76 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-53000 RELATED DB: EMDB REMARK 900 LEGOBODY DIMER DBREF 9QBJ C 3 135 PDB 9QBJ 9QBJ 3 135 DBREF 9QBJ D 3 135 PDB 9QBJ 9QBJ 3 135 DBREF 9QBJ E 1 237 PDB 9QBJ 9QBJ 1 237 DBREF 9QBJ F 1 219 PDB 9QBJ 9QBJ 1 219 DBREF 9QBJ G 1 237 PDB 9QBJ 9QBJ 1 237 DBREF 9QBJ H 1 219 PDB 9QBJ 9QBJ 1 219 DBREF 9QBJ I 10 367 UNP P0AEY0 MALE_ECO57 27 384 DBREF 9QBJ I 385 411 UNP P02976 SPA_STAA8 295 321 DBREF 9QBJ I 427 475 UNP P99134 SPA_STAAN 103 151 DBREF 9QBJ I 487 543 UNP P19909 SPG2_STRSG 440 496 DBREF 9QBJ J 10 367 UNP P0AEY0 MALE_ECO57 27 384 DBREF 9QBJ J 385 411 UNP P02976 SPA_STAA8 295 321 DBREF 9QBJ J 427 475 UNP P99134 SPA_STAAN 103 151 DBREF 9QBJ J 487 544 UNP P19909 SPG2_STRSG 440 497 SEQADV 9QBJ MET I 1 UNP P0AEY0 INITIATING METHIONINE SEQADV 9QBJ HIS I 2 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ HIS I 3 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ HIS I 4 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ HIS I 5 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ HIS I 6 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ HIS I 7 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ GLY I 8 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ SER I 9 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ GLN I 368 UNP P0AEY0 LINKER SEQADV 9QBJ ALA I 369 UNP P0AEY0 LINKER SEQADV 9QBJ LEU I 370 UNP P0AEY0 LINKER SEQADV 9QBJ ALA I 371 UNP P0AEY0 LINKER SEQADV 9QBJ PHE I 372 UNP P0AEY0 LINKER SEQADV 9QBJ ALA I 373 UNP P0AEY0 LINKER SEQADV 9QBJ GLN I 374 UNP P0AEY0 LINKER SEQADV 9QBJ ILE I 375 UNP P0AEY0 LINKER SEQADV 9QBJ LEU I 376 UNP P0AEY0 LINKER SEQADV 9QBJ ILE I 377 UNP P0AEY0 LINKER SEQADV 9QBJ MET I 378 UNP P0AEY0 LINKER SEQADV 9QBJ PRO I 379 UNP P0AEY0 LINKER SEQADV 9QBJ ASN I 380 UNP P0AEY0 LINKER SEQADV 9QBJ LEU I 381 UNP P0AEY0 LINKER SEQADV 9QBJ THR I 382 UNP P0AEY0 LINKER SEQADV 9QBJ GLU I 383 UNP P0AEY0 LINKER SEQADV 9QBJ GLU I 384 UNP P0AEY0 LINKER SEQADV 9QBJ GLU I 412 UNP P02976 LINKER SEQADV 9QBJ HIS I 413 UNP P02976 LINKER SEQADV 9QBJ GLN I 414 UNP P02976 LINKER SEQADV 9QBJ ALA I 415 UNP P02976 LINKER SEQADV 9QBJ PRO I 416 UNP P02976 LINKER SEQADV 9QBJ LYS I 417 UNP P02976 LINKER SEQADV 9QBJ GLY I 418 UNP P02976 LINKER SEQADV 9QBJ GLY I 419 UNP P02976 LINKER SEQADV 9QBJ SER I 420 UNP P02976 LINKER SEQADV 9QBJ GLY I 421 UNP P02976 LINKER SEQADV 9QBJ GLY I 422 UNP P02976 LINKER SEQADV 9QBJ ALA I 423 UNP P02976 LINKER SEQADV 9QBJ GLY I 424 UNP P02976 LINKER SEQADV 9QBJ SER I 425 UNP P02976 LINKER SEQADV 9QBJ GLY I 426 UNP P02976 LINKER SEQADV 9QBJ GLY I 476 UNP P99134 LINKER SEQADV 9QBJ GLY I 477 UNP P99134 LINKER SEQADV 9QBJ GLY I 478 UNP P99134 LINKER SEQADV 9QBJ SER I 479 UNP P99134 LINKER SEQADV 9QBJ GLY I 480 UNP P99134 LINKER SEQADV 9QBJ GLY I 481 UNP P99134 LINKER SEQADV 9QBJ GLY I 482 UNP P99134 LINKER SEQADV 9QBJ SER I 483 UNP P99134 LINKER SEQADV 9QBJ GLY I 484 UNP P99134 LINKER SEQADV 9QBJ GLY I 485 UNP P99134 LINKER SEQADV 9QBJ SER I 486 UNP P99134 LINKER SEQADV 9QBJ MET J 1 UNP P0AEY0 INITIATING METHIONINE SEQADV 9QBJ HIS J 2 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ HIS J 3 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ HIS J 4 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ HIS J 5 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ HIS J 6 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ HIS J 7 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ GLY J 8 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ SER J 9 UNP P0AEY0 EXPRESSION TAG SEQADV 9QBJ GLN J 368 UNP P0AEY0 LINKER SEQADV 9QBJ ALA J 369 UNP P0AEY0 LINKER SEQADV 9QBJ LEU J 370 UNP P0AEY0 LINKER SEQADV 9QBJ ALA J 371 UNP P0AEY0 LINKER SEQADV 9QBJ PHE J 372 UNP P0AEY0 LINKER SEQADV 9QBJ ALA J 373 UNP P0AEY0 LINKER SEQADV 9QBJ GLN J 374 UNP P0AEY0 LINKER SEQADV 9QBJ ILE J 375 UNP P0AEY0 LINKER SEQADV 9QBJ LEU J 376 UNP P0AEY0 LINKER SEQADV 9QBJ ILE J 377 UNP P0AEY0 LINKER SEQADV 9QBJ MET J 378 UNP P0AEY0 LINKER SEQADV 9QBJ PRO J 379 UNP P0AEY0 LINKER SEQADV 9QBJ ASN J 380 UNP P0AEY0 LINKER SEQADV 9QBJ LEU J 381 UNP P0AEY0 LINKER SEQADV 9QBJ THR J 382 UNP P0AEY0 LINKER SEQADV 9QBJ GLU J 383 UNP P0AEY0 LINKER SEQADV 9QBJ GLU J 384 UNP P0AEY0 LINKER SEQADV 9QBJ GLU J 412 UNP P02976 LINKER SEQADV 9QBJ HIS J 413 UNP P02976 LINKER SEQADV 9QBJ GLN J 414 UNP P02976 LINKER SEQADV 9QBJ ALA J 415 UNP P02976 LINKER SEQADV 9QBJ PRO J 416 UNP P02976 LINKER SEQADV 9QBJ LYS J 417 UNP P02976 LINKER SEQADV 9QBJ GLY J 418 UNP P02976 LINKER SEQADV 9QBJ GLY J 419 UNP P02976 LINKER SEQADV 9QBJ SER J 420 UNP P02976 LINKER SEQADV 9QBJ GLY J 421 UNP P02976 LINKER SEQADV 9QBJ GLY J 422 UNP P02976 LINKER SEQADV 9QBJ ALA J 423 UNP P02976 LINKER SEQADV 9QBJ GLY J 424 UNP P02976 LINKER SEQADV 9QBJ SER J 425 UNP P02976 LINKER SEQADV 9QBJ GLY J 426 UNP P02976 LINKER SEQADV 9QBJ GLY J 476 UNP P99134 LINKER SEQADV 9QBJ GLY J 477 UNP P99134 LINKER SEQADV 9QBJ GLY J 478 UNP P99134 LINKER SEQADV 9QBJ SER J 479 UNP P99134 LINKER SEQADV 9QBJ GLY J 480 UNP P99134 LINKER SEQADV 9QBJ GLY J 481 UNP P99134 LINKER SEQADV 9QBJ GLY J 482 UNP P99134 LINKER SEQADV 9QBJ SER J 483 UNP P99134 LINKER SEQADV 9QBJ GLY J 484 UNP P99134 LINKER SEQADV 9QBJ GLY J 485 UNP P99134 LINKER SEQADV 9QBJ SER J 486 UNP P99134 LINKER SEQRES 1 C 133 GLU VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 133 PRO GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 C 133 VAL THR ILE SER ALA LEU ASN ALA MET ALA MET GLY TRP SEQRES 4 C 133 TYR ARG GLN ALA PRO GLY GLU ARG ARG VAL MET VAL ALA SEQRES 5 C 133 ALA VAL SER GLU ARG GLY ASN ALA MET TYR ARG GLU SER SEQRES 6 C 133 VAL GLN GLY ARG PHE THR VAL THR ARG ASP PHE THR ASN SEQRES 7 C 133 LYS MET VAL SER LEU GLN MET ASP ASN LEU LYS PRO GLU SEQRES 8 C 133 ASP THR ALA VAL TYR TYR CYS HIS VAL LEU GLU ASP ARG SEQRES 9 C 133 VAL ASP SER PHE HIS ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 C 133 VAL THR VAL SER SER LEU GLU GLY THR LYS HIS HIS HIS SEQRES 11 C 133 HIS HIS HIS SEQRES 1 D 133 GLU VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 133 PRO GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 D 133 VAL THR ILE SER ALA LEU ASN ALA MET ALA MET GLY TRP SEQRES 4 D 133 TYR ARG GLN ALA PRO GLY GLU ARG ARG VAL MET VAL ALA SEQRES 5 D 133 ALA VAL SER GLU ARG GLY ASN ALA MET TYR ARG GLU SER SEQRES 6 D 133 VAL GLN GLY ARG PHE THR VAL THR ARG ASP PHE THR ASN SEQRES 7 D 133 LYS MET VAL SER LEU GLN MET ASP ASN LEU LYS PRO GLU SEQRES 8 D 133 ASP THR ALA VAL TYR TYR CYS HIS VAL LEU GLU ASP ARG SEQRES 9 D 133 VAL ASP SER PHE HIS ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 D 133 VAL THR VAL SER SER LEU GLU GLY THR LYS HIS HIS HIS SEQRES 11 D 133 HIS HIS HIS SEQRES 1 E 237 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 237 PRO GLY LYS SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 237 PHE THR PHE SER ASN PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 E 237 ALA PRO GLU MET GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 E 237 SER GLY SER THR THR LYS TYR TYR GLY ASP THR VAL LYS SEQRES 6 E 237 GLY ARG PHE THR ILE SER ARG ASP ASN PRO LYS ASN THR SEQRES 7 E 237 LEU TYR LEU GLN MET ASN SER LEU ARG SER GLU ASP THR SEQRES 8 E 237 ALA MET TYR TYR CYS ALA ARG ARG PRO LEU TYR ASP GLY SEQRES 9 E 237 ASP TYR GLY TYR PRO MET ASP TYR TRP GLY GLN GLY THR SEQRES 10 E 237 SER VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 E 237 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 E 237 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 E 237 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 E 237 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 E 237 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 E 237 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 E 237 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 E 237 GLU PRO LYS SER CYS GLY SER GLY THR LYS HIS HIS HIS SEQRES 19 E 237 HIS HIS HIS SEQRES 1 F 219 ASN ILE MET LEU THR GLN SER PRO SER SER LEU ALA VAL SEQRES 2 F 219 SER ALA GLY GLU ARG VAL THR MET SER CYS LYS SER THR SEQRES 3 F 219 GLN SER ILE LEU TYR ASN SER ASN GLN LYS THR TYR LEU SEQRES 4 F 219 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU SEQRES 5 F 219 LEU ILE TYR TRP ALA SER THR ARG ALA SER GLY VAL PRO SEQRES 6 F 219 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 F 219 LEU THR ILE ASN SER VAL GLN PRO GLU ASP LEU ALA VAL SEQRES 8 F 219 TYR TYR CYS HIS GLN TYR LEU SER ALA TRP THR PHE GLY SEQRES 9 F 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 F 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 F 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 F 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 F 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 F 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 F 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 F 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 F 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 G 237 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 237 PRO GLY LYS SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 237 PHE THR PHE SER ASN PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 G 237 ALA PRO GLU MET GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 G 237 SER GLY SER THR THR LYS TYR TYR GLY ASP THR VAL LYS SEQRES 6 G 237 GLY ARG PHE THR ILE SER ARG ASP ASN PRO LYS ASN THR SEQRES 7 G 237 LEU TYR LEU GLN MET ASN SER LEU ARG SER GLU ASP THR SEQRES 8 G 237 ALA MET TYR TYR CYS ALA ARG ARG PRO LEU TYR ASP GLY SEQRES 9 G 237 ASP TYR GLY TYR PRO MET ASP TYR TRP GLY GLN GLY THR SEQRES 10 G 237 SER VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 G 237 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 G 237 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 G 237 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 G 237 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 G 237 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 G 237 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 G 237 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 G 237 GLU PRO LYS SER CYS GLY SER GLY THR LYS HIS HIS HIS SEQRES 19 G 237 HIS HIS HIS SEQRES 1 H 219 ASN ILE MET LEU THR GLN SER PRO SER SER LEU ALA VAL SEQRES 2 H 219 SER ALA GLY GLU ARG VAL THR MET SER CYS LYS SER THR SEQRES 3 H 219 GLN SER ILE LEU TYR ASN SER ASN GLN LYS THR TYR LEU SEQRES 4 H 219 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU SEQRES 5 H 219 LEU ILE TYR TRP ALA SER THR ARG ALA SER GLY VAL PRO SEQRES 6 H 219 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 H 219 LEU THR ILE ASN SER VAL GLN PRO GLU ASP LEU ALA VAL SEQRES 8 H 219 TYR TYR CYS HIS GLN TYR LEU SER ALA TRP THR PHE GLY SEQRES 9 H 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 H 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 H 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 H 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 H 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 H 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 H 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 H 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 H 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 I 543 MET HIS HIS HIS HIS HIS HIS GLY SER LYS ILE GLU GLU SEQRES 2 I 543 GLY LYS LEU VAL ILE TRP ILE ASN GLY ASP LYS GLY TYR SEQRES 3 I 543 ASN GLY LEU ALA GLU VAL GLY LYS LYS PHE GLU LYS ASP SEQRES 4 I 543 THR GLY ILE LYS VAL THR VAL GLU HIS PRO ASP LYS LEU SEQRES 5 I 543 GLU GLU LYS PHE PRO GLN VAL ALA ALA THR GLY ASP GLY SEQRES 6 I 543 PRO ASP ILE ILE PHE TRP ALA HIS ASP ARG PHE GLY GLY SEQRES 7 I 543 TYR ALA GLN SER GLY LEU LEU ALA GLU ILE THR PRO ASP SEQRES 8 I 543 LYS ALA PHE GLN ASP LYS LEU TYR PRO PHE THR TRP ASP SEQRES 9 I 543 ALA VAL ARG TYR ASN GLY LYS LEU ILE ALA TYR PRO ILE SEQRES 10 I 543 ALA VAL GLU ALA LEU SER LEU ILE TYR ASN LYS ASP LEU SEQRES 11 I 543 LEU PRO ASN PRO PRO LYS THR TRP GLU GLU ILE PRO ALA SEQRES 12 I 543 LEU ASP LYS GLU LEU LYS ALA LYS GLY LYS SER ALA LEU SEQRES 13 I 543 MET PHE ASN LEU GLN GLU PRO TYR PHE THR TRP PRO LEU SEQRES 14 I 543 ILE ALA ALA ASP GLY GLY TYR ALA PHE LYS TYR GLU ASN SEQRES 15 I 543 GLY LYS TYR ASP ILE LYS ASP VAL GLY VAL ASP ASN ALA SEQRES 16 I 543 GLY ALA LYS ALA GLY LEU THR PHE LEU VAL ASP LEU ILE SEQRES 17 I 543 LYS ASN LYS HIS MET ASN ALA ASP THR ASP TYR SER ILE SEQRES 18 I 543 ALA GLU ALA ALA PHE ASN LYS GLY GLU THR ALA MET THR SEQRES 19 I 543 ILE ASN GLY PRO TRP ALA TRP SER ASN ILE ASP THR SER SEQRES 20 I 543 LYS VAL ASN TYR GLY VAL THR VAL LEU PRO THR PHE LYS SEQRES 21 I 543 GLY GLN PRO SER LYS PRO PHE VAL GLY VAL LEU SER ALA SEQRES 22 I 543 GLY ILE ASN ALA ALA SER PRO ASN LYS GLU LEU ALA LYS SEQRES 23 I 543 GLU PHE LEU GLU ASN TYR LEU LEU THR ASP GLU GLY LEU SEQRES 24 I 543 GLU ALA VAL ASN LYS ASP LYS PRO LEU GLY ALA VAL ALA SEQRES 25 I 543 LEU LYS SER TYR GLU GLU GLU LEU ALA LYS ASP PRO ARG SEQRES 26 I 543 ILE ALA ALA THR MET GLU ASN ALA GLN LYS GLY GLU ILE SEQRES 27 I 543 MET PRO ASN ILE PRO GLN MET SER ALA PHE TRP TYR ALA SEQRES 28 I 543 VAL ARG THR ALA VAL ILE ASN ALA ALA SER GLY ARG GLN SEQRES 29 I 543 THR VAL ASP GLN ALA LEU ALA PHE ALA GLN ILE LEU ILE SEQRES 30 I 543 MET PRO ASN LEU THR GLU GLU GLN ARG ASN GLY PHE ILE SEQRES 31 I 543 GLN SER LEU LYS ASP ASP PRO SER VAL SER LYS GLU ILE SEQRES 32 I 543 LEU ALA GLU ALA LYS LYS LEU ASN GLU HIS GLN ALA PRO SEQRES 33 I 543 LYS GLY GLY SER GLY GLY ALA GLY SER GLY ASP GLN GLN SEQRES 34 I 543 SER ALA PHE TYR GLU ILE LEU ASN MET PRO ASN LEU ASN SEQRES 35 I 543 GLU ALA GLN ARG ASN GLY PHE ILE GLN SER LEU LYS ASP SEQRES 36 I 543 ASP PRO SER GLN SER THR ASN VAL LEU GLY GLU ALA LYS SEQRES 37 I 543 LYS LEU ASN GLU SER GLN ALA GLY GLY GLY SER GLY GLY SEQRES 38 I 543 GLY SER GLY GLY SER ALA VAL THR THR TYR LYS LEU VAL SEQRES 39 I 543 ILE ASN GLY LYS THR LEU LYS GLY GLU THR THR THR LYS SEQRES 40 I 543 ALA VAL ASP ALA GLU THR ALA GLU LYS ALA PHE LYS GLN SEQRES 41 I 543 TYR ALA ASN ASP ASN GLY VAL ASP GLY VAL TRP THR TYR SEQRES 42 I 543 ASP ASP ALA THR LYS THR PHE THR VAL THR SEQRES 1 J 544 MET HIS HIS HIS HIS HIS HIS GLY SER LYS ILE GLU GLU SEQRES 2 J 544 GLY LYS LEU VAL ILE TRP ILE ASN GLY ASP LYS GLY TYR SEQRES 3 J 544 ASN GLY LEU ALA GLU VAL GLY LYS LYS PHE GLU LYS ASP SEQRES 4 J 544 THR GLY ILE LYS VAL THR VAL GLU HIS PRO ASP LYS LEU SEQRES 5 J 544 GLU GLU LYS PHE PRO GLN VAL ALA ALA THR GLY ASP GLY SEQRES 6 J 544 PRO ASP ILE ILE PHE TRP ALA HIS ASP ARG PHE GLY GLY SEQRES 7 J 544 TYR ALA GLN SER GLY LEU LEU ALA GLU ILE THR PRO ASP SEQRES 8 J 544 LYS ALA PHE GLN ASP LYS LEU TYR PRO PHE THR TRP ASP SEQRES 9 J 544 ALA VAL ARG TYR ASN GLY LYS LEU ILE ALA TYR PRO ILE SEQRES 10 J 544 ALA VAL GLU ALA LEU SER LEU ILE TYR ASN LYS ASP LEU SEQRES 11 J 544 LEU PRO ASN PRO PRO LYS THR TRP GLU GLU ILE PRO ALA SEQRES 12 J 544 LEU ASP LYS GLU LEU LYS ALA LYS GLY LYS SER ALA LEU SEQRES 13 J 544 MET PHE ASN LEU GLN GLU PRO TYR PHE THR TRP PRO LEU SEQRES 14 J 544 ILE ALA ALA ASP GLY GLY TYR ALA PHE LYS TYR GLU ASN SEQRES 15 J 544 GLY LYS TYR ASP ILE LYS ASP VAL GLY VAL ASP ASN ALA SEQRES 16 J 544 GLY ALA LYS ALA GLY LEU THR PHE LEU VAL ASP LEU ILE SEQRES 17 J 544 LYS ASN LYS HIS MET ASN ALA ASP THR ASP TYR SER ILE SEQRES 18 J 544 ALA GLU ALA ALA PHE ASN LYS GLY GLU THR ALA MET THR SEQRES 19 J 544 ILE ASN GLY PRO TRP ALA TRP SER ASN ILE ASP THR SER SEQRES 20 J 544 LYS VAL ASN TYR GLY VAL THR VAL LEU PRO THR PHE LYS SEQRES 21 J 544 GLY GLN PRO SER LYS PRO PHE VAL GLY VAL LEU SER ALA SEQRES 22 J 544 GLY ILE ASN ALA ALA SER PRO ASN LYS GLU LEU ALA LYS SEQRES 23 J 544 GLU PHE LEU GLU ASN TYR LEU LEU THR ASP GLU GLY LEU SEQRES 24 J 544 GLU ALA VAL ASN LYS ASP LYS PRO LEU GLY ALA VAL ALA SEQRES 25 J 544 LEU LYS SER TYR GLU GLU GLU LEU ALA LYS ASP PRO ARG SEQRES 26 J 544 ILE ALA ALA THR MET GLU ASN ALA GLN LYS GLY GLU ILE SEQRES 27 J 544 MET PRO ASN ILE PRO GLN MET SER ALA PHE TRP TYR ALA SEQRES 28 J 544 VAL ARG THR ALA VAL ILE ASN ALA ALA SER GLY ARG GLN SEQRES 29 J 544 THR VAL ASP GLN ALA LEU ALA PHE ALA GLN ILE LEU ILE SEQRES 30 J 544 MET PRO ASN LEU THR GLU GLU GLN ARG ASN GLY PHE ILE SEQRES 31 J 544 GLN SER LEU LYS ASP ASP PRO SER VAL SER LYS GLU ILE SEQRES 32 J 544 LEU ALA GLU ALA LYS LYS LEU ASN GLU HIS GLN ALA PRO SEQRES 33 J 544 LYS GLY GLY SER GLY GLY ALA GLY SER GLY ASP GLN GLN SEQRES 34 J 544 SER ALA PHE TYR GLU ILE LEU ASN MET PRO ASN LEU ASN SEQRES 35 J 544 GLU ALA GLN ARG ASN GLY PHE ILE GLN SER LEU LYS ASP SEQRES 36 J 544 ASP PRO SER GLN SER THR ASN VAL LEU GLY GLU ALA LYS SEQRES 37 J 544 LYS LEU ASN GLU SER GLN ALA GLY GLY GLY SER GLY GLY SEQRES 38 J 544 GLY SER GLY GLY SER ALA VAL THR THR TYR LYS LEU VAL SEQRES 39 J 544 ILE ASN GLY LYS THR LEU LYS GLY GLU THR THR THR LYS SEQRES 40 J 544 ALA VAL ASP ALA GLU THR ALA GLU LYS ALA PHE LYS GLN SEQRES 41 J 544 TYR ALA ASN ASP ASN GLY VAL ASP GLY VAL TRP THR TYR SEQRES 42 J 544 ASP ASP ALA THR LYS THR PHE THR VAL THR GLU HET BGC A 1 12 HET GLC A 2 11 HET BGC B 1 12 HET GLC B 2 11 HETNAM BGC BETA-D-GLUCOPYRANOSE HETNAM GLC ALPHA-D-GLUCOPYRANOSE HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE FORMUL 9 BGC 2(C6 H12 O6) FORMUL 9 GLC 2(C6 H12 O6) HELIX 1 AA1 THR C 30 ALA C 36 1 7 HELIX 2 AA2 GLU C 66 GLN C 69 5 4 HELIX 3 AA3 LYS C 91 THR C 95 5 5 HELIX 4 AA4 THR D 30 ALA D 36 1 7 HELIX 5 AA5 LYS D 91 THR D 95 5 5 HELIX 6 AA6 THR E 28 PHE E 32 5 5 HELIX 7 AA7 ARG E 87 THR E 91 5 5 HELIX 8 AA8 TYR E 102 GLY E 107 1 6 HELIX 9 AA9 SER F 126 SER F 132 1 7 HELIX 10 AB1 LYS F 188 HIS F 194 1 7 HELIX 11 AB2 THR G 28 PHE G 32 5 5 HELIX 12 AB3 ARG G 87 THR G 91 5 5 HELIX 13 AB4 TYR G 102 GLY G 107 1 6 HELIX 14 AB5 SER G 166 ALA G 168 5 3 HELIX 15 AB6 GLN H 85 LEU H 89 5 5 HELIX 16 AB7 SER H 126 GLY H 133 1 8 HELIX 17 AB8 LYS H 188 HIS H 194 1 7 HELIX 18 AB9 GLY I 25 PHE I 36 1 12 HELIX 19 AC1 LYS I 51 ALA I 60 1 10 HELIX 20 AC2 HIS I 73 SER I 82 1 10 HELIX 21 AC3 ASP I 91 LEU I 98 1 8 HELIX 22 AC4 TYR I 99 VAL I 106 1 8 HELIX 23 AC5 GLU I 140 LYS I 149 1 10 HELIX 24 AC6 GLU I 162 ASP I 173 1 12 HELIX 25 AC7 ASN I 194 ASN I 210 1 17 HELIX 26 AC8 ASP I 218 LYS I 228 1 11 HELIX 27 AC9 TRP I 239 THR I 246 1 8 HELIX 28 AD1 ASN I 281 TYR I 292 1 12 HELIX 29 AD2 THR I 295 LYS I 306 1 12 HELIX 30 AD3 LEU I 313 ALA I 321 1 9 HELIX 31 AD4 ASP I 323 GLY I 336 1 14 HELIX 32 AD5 GLN I 344 SER I 361 1 18 HELIX 33 AD6 THR I 365 MET I 378 1 14 HELIX 34 AD7 THR I 382 ASP I 396 1 15 HELIX 35 AD8 VAL I 399 GLN I 414 1 16 HELIX 36 AD9 SER I 425 ASN I 437 1 13 HELIX 37 AE1 ASN I 442 ASP I 456 1 15 HELIX 38 AE2 GLN I 459 GLN I 474 1 16 HELIX 39 AE3 ASP I 510 ASN I 525 1 16 HELIX 40 AE4 HIS J 73 GLY J 83 1 11 HELIX 41 AE5 PHE J 94 LEU J 98 5 5 HELIX 42 AE6 TYR J 99 VAL J 106 1 8 HELIX 43 AE7 GLU J 139 LYS J 149 1 11 HELIX 44 AE8 GLU J 162 ASP J 173 1 12 HELIX 45 AE9 ASN J 194 ASN J 210 1 17 HELIX 46 AF1 ASP J 218 LYS J 228 1 11 HELIX 47 AF2 TRP J 239 SER J 247 1 9 HELIX 48 AF3 LEU J 284 TYR J 292 1 9 HELIX 49 AF4 THR J 295 LYS J 306 1 12 HELIX 50 AF5 LEU J 313 ALA J 321 1 9 HELIX 51 AF6 ASP J 323 GLY J 336 1 14 HELIX 52 AF7 MET J 345 GLY J 362 1 18 HELIX 53 AF8 THR J 365 MET J 378 1 14 HELIX 54 AF9 THR J 382 ASP J 396 1 15 HELIX 55 AG1 VAL J 399 GLN J 414 1 16 HELIX 56 AG2 GLN J 429 LEU J 436 1 8 HELIX 57 AG3 ASN J 442 ASP J 456 1 15 HELIX 58 AG4 GLN J 459 ALA J 475 1 17 HELIX 59 AG5 ASP J 510 ASN J 525 1 16 SHEET 1 AA1 4 GLN C 5 SER C 9 0 SHEET 2 AA1 4 SER C 19 SER C 27 -1 O SER C 23 N SER C 9 SHEET 3 AA1 4 MET C 82 ASP C 88 -1 O MET C 87 N LEU C 20 SHEET 4 AA1 4 PHE C 72 ASP C 77 -1 N ASP C 77 O MET C 82 SHEET 1 AA2 6 GLY C 12 VAL C 14 0 SHEET 2 AA2 6 THR C 118 VAL C 122 1 O THR C 121 N GLY C 12 SHEET 3 AA2 6 ALA C 96 ASP C 105 -1 N TYR C 98 O THR C 118 SHEET 4 AA2 6 ALA C 38 GLN C 44 -1 N ALA C 38 O LEU C 103 SHEET 5 AA2 6 VAL C 51 VAL C 56 -1 O VAL C 51 N ARG C 43 SHEET 6 AA2 6 ALA C 62 TYR C 64 -1 O MET C 63 N ALA C 55 SHEET 1 AA3 4 GLY C 12 VAL C 14 0 SHEET 2 AA3 4 THR C 118 VAL C 122 1 O THR C 121 N GLY C 12 SHEET 3 AA3 4 ALA C 96 ASP C 105 -1 N TYR C 98 O THR C 118 SHEET 4 AA3 4 PHE C 110 TRP C 114 -1 O HIS C 111 N GLU C 104 SHEET 1 AA4 4 GLN D 5 SER D 9 0 SHEET 2 AA4 4 SER D 19 SER D 27 -1 O SER D 23 N SER D 9 SHEET 3 AA4 4 MET D 82 ASP D 88 -1 O MET D 87 N LEU D 20 SHEET 4 AA4 4 PHE D 72 ASP D 77 -1 N ASP D 77 O MET D 82 SHEET 1 AA5 6 GLY D 12 VAL D 14 0 SHEET 2 AA5 6 THR D 118 VAL D 122 1 O GLN D 119 N GLY D 12 SHEET 3 AA5 6 ALA D 96 ASP D 105 -1 N TYR D 98 O THR D 118 SHEET 4 AA5 6 ALA D 38 GLN D 44 -1 N GLN D 44 O VAL D 97 SHEET 5 AA5 6 VAL D 51 VAL D 56 -1 O VAL D 56 N MET D 39 SHEET 6 AA5 6 ALA D 62 TYR D 64 -1 O MET D 63 N ALA D 55 SHEET 1 AA6 4 GLY D 12 VAL D 14 0 SHEET 2 AA6 4 THR D 118 VAL D 122 1 O GLN D 119 N GLY D 12 SHEET 3 AA6 4 ALA D 96 ASP D 105 -1 N TYR D 98 O THR D 118 SHEET 4 AA6 4 PHE D 110 TRP D 114 -1 O HIS D 111 N GLU D 104 SHEET 1 AA7 4 GLN E 3 SER E 7 0 SHEET 2 AA7 4 SER E 17 SER E 25 -1 O SER E 25 N GLN E 3 SHEET 3 AA7 4 THR E 78 ASN E 84 -1 O LEU E 81 N LEU E 20 SHEET 4 AA7 4 PHE E 68 ASP E 73 -1 N ASP E 73 O THR E 78 SHEET 1 AA8 6 LEU E 11 VAL E 12 0 SHEET 2 AA8 6 THR E 117 VAL E 121 1 O THR E 120 N VAL E 12 SHEET 3 AA8 6 ALA E 92 ARG E 99 -1 N TYR E 94 O THR E 117 SHEET 4 AA8 6 GLY E 33 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AA8 6 GLU E 46 ILE E 51 -1 O ILE E 51 N MET E 34 SHEET 6 AA8 6 LYS E 58 TYR E 60 -1 O TYR E 59 N TYR E 50 SHEET 1 AA9 4 LEU E 11 VAL E 12 0 SHEET 2 AA9 4 THR E 117 VAL E 121 1 O THR E 120 N VAL E 12 SHEET 3 AA9 4 ALA E 92 ARG E 99 -1 N TYR E 94 O THR E 117 SHEET 4 AA9 4 TYR E 112 TRP E 113 -1 O TYR E 112 N ARG E 98 SHEET 1 AB1 4 SER E 130 LEU E 134 0 SHEET 2 AB1 4 ALA E 147 TYR E 155 -1 O LEU E 151 N PHE E 132 SHEET 3 AB1 4 TYR E 186 THR E 193 -1 O LEU E 188 N VAL E 152 SHEET 4 AB1 4 VAL E 173 THR E 175 -1 N HIS E 174 O VAL E 191 SHEET 1 AB2 4 SER E 130 LEU E 134 0 SHEET 2 AB2 4 ALA E 147 TYR E 155 -1 O LEU E 151 N PHE E 132 SHEET 3 AB2 4 TYR E 186 THR E 193 -1 O LEU E 188 N VAL E 152 SHEET 4 AB2 4 VAL E 179 LEU E 180 -1 N VAL E 179 O SER E 187 SHEET 1 AB3 7 THR E 161 TRP E 164 0 SHEET 2 AB3 7 ILE E 205 HIS E 210 -1 O ASN E 207 N SER E 163 SHEET 3 AB3 7 THR E 215 LYS E 220 -1 O LYS E 219 N CYS E 206 SHEET 4 AB3 7 LYS I 501 ALA I 508 -1 O LYS I 501 N ASP E 218 SHEET 5 AB3 7 THR I 489 VAL I 494 -1 N TYR I 491 O THR I 506 SHEET 6 AB3 7 THR I 539 THR I 541 1 O PHE I 540 N LYS I 492 SHEET 7 AB3 7 THR I 532 ASP I 534 -1 N THR I 532 O THR I 541 SHEET 1 AB4 4 LEU F 4 GLN F 6 0 SHEET 2 AB4 4 VAL F 19 SER F 25 -1 O LYS F 24 N THR F 5 SHEET 3 AB4 4 ASP F 76 ILE F 81 -1 O LEU F 79 N MET F 21 SHEET 4 AB4 4 PHE F 68 SER F 73 -1 N THR F 69 O THR F 80 SHEET 1 AB5 6 LEU F 11 SER F 14 0 SHEET 2 AB5 6 THR F 107 LYS F 112 1 O GLU F 110 N LEU F 11 SHEET 3 AB5 6 VAL F 91 GLN F 96 -1 N TYR F 92 O THR F 107 SHEET 4 AB5 6 ALA F 40 GLN F 44 -1 N TYR F 42 O TYR F 93 SHEET 5 AB5 6 LYS F 51 TYR F 55 -1 O LYS F 51 N GLN F 43 SHEET 6 AB5 6 THR F 59 ARG F 60 -1 O THR F 59 N TYR F 55 SHEET 1 AB6 4 LEU F 11 SER F 14 0 SHEET 2 AB6 4 THR F 107 LYS F 112 1 O GLU F 110 N LEU F 11 SHEET 3 AB6 4 VAL F 91 GLN F 96 -1 N TYR F 92 O THR F 107 SHEET 4 AB6 4 THR F 102 PHE F 103 -1 O THR F 102 N GLN F 96 SHEET 1 AB7 2 LEU F 30 TYR F 31 0 SHEET 2 AB7 2 LYS F 36 THR F 37 -1 O LYS F 36 N TYR F 31 SHEET 1 AB8 4 SER F 119 PHE F 123 0 SHEET 2 AB8 4 THR F 134 PHE F 144 -1 O VAL F 138 N PHE F 123 SHEET 3 AB8 4 TYR F 178 SER F 187 -1 O LEU F 180 N LEU F 141 SHEET 4 AB8 4 SER F 164 VAL F 168 -1 N GLN F 165 O THR F 183 SHEET 1 AB9 3 LYS F 150 LYS F 154 0 SHEET 2 AB9 3 TYR F 197 THR F 202 -1 O GLU F 200 N GLN F 152 SHEET 3 AB9 3 THR F 211 PHE F 214 -1 O LYS F 212 N CYS F 199 SHEET 1 AC1 4 GLN G 3 SER G 7 0 SHEET 2 AC1 4 SER G 17 SER G 25 -1 O ALA G 23 N VAL G 5 SHEET 3 AC1 4 THR G 78 ASN G 84 -1 O MET G 83 N LEU G 18 SHEET 4 AC1 4 PHE G 68 ASP G 73 -1 N THR G 69 O GLN G 82 SHEET 1 AC2 6 LEU G 11 VAL G 12 0 SHEET 2 AC2 6 THR G 117 VAL G 121 1 O THR G 120 N VAL G 12 SHEET 3 AC2 6 ALA G 92 ARG G 99 -1 N ALA G 92 O VAL G 119 SHEET 4 AC2 6 GLY G 33 ALA G 40 -1 N GLN G 39 O MET G 93 SHEET 5 AC2 6 GLY G 44 ILE G 51 -1 O ILE G 51 N MET G 34 SHEET 6 AC2 6 LYS G 58 TYR G 60 -1 O TYR G 59 N TYR G 50 SHEET 1 AC3 4 SER G 130 LEU G 134 0 SHEET 2 AC3 4 ALA G 147 LYS G 153 -1 O LYS G 153 N SER G 130 SHEET 3 AC3 4 TYR G 186 THR G 193 -1 O SER G 190 N CYS G 150 SHEET 4 AC3 4 VAL G 173 THR G 175 -1 N HIS G 174 O VAL G 191 SHEET 1 AC4 4 SER G 130 LEU G 134 0 SHEET 2 AC4 4 ALA G 147 LYS G 153 -1 O LYS G 153 N SER G 130 SHEET 3 AC4 4 TYR G 186 THR G 193 -1 O SER G 190 N CYS G 150 SHEET 4 AC4 4 VAL G 179 LEU G 180 -1 N VAL G 179 O SER G 187 SHEET 1 AC5 7 THR G 161 TRP G 164 0 SHEET 2 AC5 7 ILE G 205 HIS G 210 -1 O ASN G 207 N SER G 163 SHEET 3 AC5 7 THR G 215 LYS G 220 -1 O LYS G 219 N CYS G 206 SHEET 4 AC5 7 LYS J 501 ALA J 508 -1 O GLU J 503 N LYS G 216 SHEET 5 AC5 7 THR J 489 ASN J 496 -1 N TYR J 491 O THR J 506 SHEET 6 AC5 7 THR J 539 THR J 543 1 O VAL J 542 N VAL J 494 SHEET 7 AC5 7 TRP J 531 ASP J 534 -1 N ASP J 534 O THR J 539 SHEET 1 AC6 4 LEU H 4 GLN H 6 0 SHEET 2 AC6 4 VAL H 19 SER H 25 -1 O LYS H 24 N THR H 5 SHEET 3 AC6 4 ASP H 76 ILE H 81 -1 O LEU H 79 N MET H 21 SHEET 4 AC6 4 PHE H 68 SER H 73 -1 N THR H 69 O THR H 80 SHEET 1 AC7 6 SER H 10 SER H 14 0 SHEET 2 AC7 6 THR H 107 LYS H 112 1 O LYS H 112 N VAL H 13 SHEET 3 AC7 6 VAL H 91 GLN H 96 -1 N TYR H 92 O THR H 107 SHEET 4 AC7 6 LEU H 39 GLN H 44 -1 N TYR H 42 O TYR H 93 SHEET 5 AC7 6 LYS H 51 TYR H 55 -1 O LYS H 51 N GLN H 43 SHEET 6 AC7 6 THR H 59 ARG H 60 -1 O THR H 59 N TYR H 55 SHEET 1 AC8 4 SER H 10 SER H 14 0 SHEET 2 AC8 4 THR H 107 LYS H 112 1 O LYS H 112 N VAL H 13 SHEET 3 AC8 4 VAL H 91 GLN H 96 -1 N TYR H 92 O THR H 107 SHEET 4 AC8 4 THR H 102 PHE H 103 -1 O THR H 102 N GLN H 96 SHEET 1 AC9 2 LEU H 30 TYR H 31 0 SHEET 2 AC9 2 LYS H 36 THR H 37 -1 O LYS H 36 N TYR H 31 SHEET 1 AD1 4 SER H 119 PHE H 123 0 SHEET 2 AD1 4 THR H 134 PHE H 144 -1 O VAL H 138 N PHE H 123 SHEET 3 AD1 4 TYR H 178 SER H 187 -1 O LEU H 180 N LEU H 141 SHEET 4 AD1 4 SER H 164 VAL H 168 -1 N GLN H 165 O THR H 183 SHEET 1 AD2 3 ALA H 149 LYS H 154 0 SHEET 2 AD2 3 TYR H 197 HIS H 203 -1 O ALA H 198 N LYS H 154 SHEET 3 AD2 3 THR H 211 PHE H 214 -1 O PHE H 214 N TYR H 197 SHEET 1 AD3 6 THR I 45 GLU I 47 0 SHEET 2 AD3 6 VAL I 17 TRP I 19 1 N ILE I 18 O GLU I 47 SHEET 3 AD3 6 ILE I 68 ALA I 72 1 O PHE I 70 N TRP I 19 SHEET 4 AD3 6 PHE I 267 ILE I 275 -1 O SER I 272 N TRP I 71 SHEET 5 AD3 6 ALA I 114 GLU I 120 -1 N ALA I 118 O LEU I 271 SHEET 6 AD3 6 ALA I 310 VAL I 311 -1 O ALA I 310 N VAL I 119 SHEET 1 AD4 5 THR I 45 GLU I 47 0 SHEET 2 AD4 5 VAL I 17 TRP I 19 1 N ILE I 18 O GLU I 47 SHEET 3 AD4 5 ILE I 68 ALA I 72 1 O PHE I 70 N TRP I 19 SHEET 4 AD4 5 PHE I 267 ILE I 275 -1 O SER I 272 N TRP I 71 SHEET 5 AD4 5 GLU I 337 ILE I 338 1 O GLU I 337 N VAL I 268 SHEET 1 AD5 2 ARG I 107 TYR I 108 0 SHEET 2 AD5 2 LYS I 111 LEU I 112 -1 O LYS I 111 N TYR I 108 SHEET 1 AD6 3 MET I 233 ASN I 236 0 SHEET 2 AD6 3 SER I 123 ASN I 127 -1 N SER I 123 O ASN I 236 SHEET 3 AD6 3 TYR I 251 THR I 254 -1 O GLY I 252 N TYR I 126 SHEET 1 AD7 2 LYS I 179 GLU I 181 0 SHEET 2 AD7 2 LYS I 184 ASP I 186 -1 O LYS I 184 N GLU I 181 SHEET 1 AD8 4 ILE J 68 ALA J 72 0 SHEET 2 AD8 4 PHE J 267 ILE J 275 -1 O SER J 272 N TRP J 71 SHEET 3 AD8 4 TYR J 115 ALA J 121 -1 N ALA J 118 O LEU J 271 SHEET 4 AD8 4 ALA J 310 VAL J 311 -1 O ALA J 310 N VAL J 119 SHEET 1 AD9 3 ILE J 68 ALA J 72 0 SHEET 2 AD9 3 PHE J 267 ILE J 275 -1 O SER J 272 N TRP J 71 SHEET 3 AD9 3 GLU J 337 ILE J 338 1 O GLU J 337 N VAL J 268 SHEET 1 AE1 3 MET J 233 ASN J 236 0 SHEET 2 AE1 3 SER J 123 ASN J 127 -1 N SER J 123 O ASN J 236 SHEET 3 AE1 3 TYR J 251 THR J 254 -1 O GLY J 252 N TYR J 126 SHEET 1 AE2 2 LYS J 179 GLU J 181 0 SHEET 2 AE2 2 LYS J 184 ASP J 186 -1 O ASP J 186 N LYS J 179 SSBOND 1 CYS C 24 CYS C 100 1555 1555 2.03 SSBOND 2 CYS D 24 CYS D 100 1555 1555 2.03 SSBOND 3 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 4 CYS E 150 CYS E 206 1555 1555 2.03 SSBOND 5 CYS F 23 CYS F 94 1555 1555 2.04 SSBOND 6 CYS F 139 CYS F 199 1555 1555 2.03 SSBOND 7 CYS G 22 CYS G 96 1555 1555 2.04 SSBOND 8 CYS G 150 CYS G 206 1555 1555 2.04 SSBOND 9 CYS H 23 CYS H 94 1555 1555 2.04 SSBOND 10 CYS H 139 CYS H 199 1555 1555 2.03 LINK O4 BGC A 1 C1 GLC A 2 1555 1555 1.45 LINK O4 BGC B 1 C1 GLC B 2 1555 1555 1.45 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