HEADER MEMBRANE PROTEIN 23-MAY-24 9FG0 TITLE CRYO-EM STRUCTURE OF THE ALPHA1BETA3GAMMA2 GABA(A) RECEPTOR IN COMPLEX TITLE 2 WITH GABA AND NB38 IN THE SHORT-LIVED ASYMMETRIC OPEN 2 STATE CAVEAT 9FG0 MAN A 5 HAS WRONG CHIRALITY AT ATOM C1 MAN A 6 HAS WRONG CAVEAT 2 9FG0 CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-1; COMPND 3 CHAIN: A, D; COMPND 4 SYNONYM: GABA(A) RECEPTOR SUBUNIT ALPHA-1,GABAAR SUBUNIT ALPHA-1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT BETA-3; COMPND 8 CHAIN: B, E; COMPND 9 SYNONYM: GABA(A) RECEPTOR SUBUNIT BETA-3,GABAAR SUBUNIT BETA-3; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT GAMMA-2; COMPND 13 CHAIN: C; COMPND 14 SYNONYM: GABA(A) RECEPTOR SUBUNIT GAMMA-2,GABAAR SUBUNIT GAMMA-2; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: NANOBODY38; COMPND 18 CHAIN: F; COMPND 19 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: GABRA1; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 GENE: GABRB3; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 GENE: GABRG2; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-; SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PHR-TETO2; SOURCE 28 MOL_ID: 4; SOURCE 29 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 30 ORGANISM_TAXID: 9844; SOURCE 31 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 33 EXPRESSION_SYSTEM_STRAIN: WK6 SU- KEYWDS GABA, NEUROTRANSMISSION, GATING CYCLE, TIME-RESOLVED CRYO-EM, KEYWDS 2 MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR D.B.MIHAYLOV,T.MALINAUSKAS,A.R.ARICESCU REVDAT 1 11-JUN-25 9FG0 0 JRNL AUTH D.B.MIHAYLOV,T.MALINAUSKAS,A.R.ARICESCU JRNL TITL CRYO-EM STRUCTURE OF THE ALPHA1BETA3GAMMA2 GABA(A) RECEPTOR JRNL TITL 2 IN COMPLEX WITH GABA AND NB38 IN THE SHORT-LIVED ASYMMETRIC JRNL TITL 3 OPEN 2 STATE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : TOPAZ, EPU, CTFFIND, PHENIX, PHENIX, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6HUK REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : OTHER REMARK 3 REFINEMENT TARGET : FSC AT 0.5 REMARK 3 OVERALL ANISOTROPIC B VALUE : 30.000 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) : 3.600 REMARK 3 NUMBER OF PARTICLES : 28000 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 9FG0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1292138692. 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 : CRYO-EM STRUCTURE OF THE REMARK 245 ALPHA1BETA3GAMMA2 GABA(A) REMARK 245 RECEPTOR IN COMPLEX WITH GABA REMARK 245 AND NB38 IN THE SHORT-LIVED REMARK 245 ASYMMETRIC OPEN 2 STATE REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 REMARK 245 SAMPLE SUPPORT DETAILS : CURRENT: 30MA REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 20929 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : TFS FALCON 4I (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1400.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2400.00 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 : 96000 REMARK 245 CALIBRATED MAGNIFICATION : 96000 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, a, b, G, c, REMARK 350 AND CHAINS: d, e, H 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 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 PRO A 147 31.25 -96.78 REMARK 500 ARG A 173 -166.72 -125.50 REMARK 500 LYS A 312 -2.87 70.86 REMARK 500 ASP C 110 57.82 -94.25 REMARK 500 SER C 195 49.69 -94.11 REMARK 500 VAL C 204 -60.50 -99.27 REMARK 500 ASN D 87 -79.71 -71.50 REMARK 500 ASN D 88 -25.26 -148.42 REMARK 500 ASP D 98 58.24 -94.93 REMARK 500 ARG D 173 -166.25 -125.64 REMARK 500 LYS D 312 -4.06 69.82 REMARK 500 ASP E 95 55.45 -91.33 REMARK 500 LEU E 145 59.61 -94.69 REMARK 500 CYS F 23 117.11 -161.00 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-50380 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE ALPHA1BETA3GAMMA2 GABA(A) RECEPTOR IN REMARK 900 COMPLEX WITH GABA AND NB38 IN THE SHORT-LIVED ASYMMETRIC OPEN 2 REMARK 900 STATE DBREF 9FG0 A 10 312 UNP P14867 GBRA1_HUMAN 37 339 DBREF 9FG0 A 391 418 UNP P14867 GBRA1_HUMAN 418 445 DBREF 9FG0 B 8 307 UNP P28472 GBRB3_HUMAN 33 332 DBREF 9FG0 B 422 447 UNP P28472 GBRB3_HUMAN 447 472 DBREF 9FG0 C 25 322 UNP P18507 GBRG2_HUMAN 64 361 DBREF 9FG0 C 400 428 UNP P18507 GBRG2_HUMAN 447 475 DBREF 9FG0 D 10 312 UNP P14867 GBRA1_HUMAN 37 339 DBREF 9FG0 D 391 418 UNP P14867 GBRA1_HUMAN 418 445 DBREF 9FG0 E 8 307 UNP P28472 GBRB3_HUMAN 33 332 DBREF 9FG0 E 422 447 UNP P28472 GBRB3_HUMAN 447 472 DBREF 9FG0 F 2 124 PDB 9FG0 9FG0 2 124 SEQADV 9FG0 SER A 313 UNP P14867 LINKER SEQADV 9FG0 GLN A 314 UNP P14867 LINKER SEQADV 9FG0 PRO A 315 UNP P14867 LINKER SEQADV 9FG0 ALA A 316 UNP P14867 LINKER SEQADV 9FG0 ARG A 317 UNP P14867 LINKER SEQADV 9FG0 ALA A 318 UNP P14867 LINKER SEQADV 9FG0 ALA A 319 UNP P14867 LINKER SEQADV 9FG0 SER B 308 UNP P28472 LINKER SEQADV 9FG0 GLN B 309 UNP P28472 LINKER SEQADV 9FG0 PRO B 310 UNP P28472 LINKER SEQADV 9FG0 ALA B 311 UNP P28472 LINKER SEQADV 9FG0 ARG B 312 UNP P28472 LINKER SEQADV 9FG0 ALA B 313 UNP P28472 LINKER SEQADV 9FG0 ALA B 314 UNP P28472 LINKER SEQADV 9FG0 SER C 323 UNP P18507 LINKER SEQADV 9FG0 GLN C 324 UNP P18507 LINKER SEQADV 9FG0 PRO C 325 UNP P18507 LINKER SEQADV 9FG0 ALA C 326 UNP P18507 LINKER SEQADV 9FG0 ARG C 327 UNP P18507 LINKER SEQADV 9FG0 ALA C 328 UNP P18507 LINKER SEQADV 9FG0 GLY C 429 UNP P18507 EXPRESSION TAG SEQADV 9FG0 SER D 313 UNP P14867 LINKER SEQADV 9FG0 GLN D 314 UNP P14867 LINKER SEQADV 9FG0 PRO D 315 UNP P14867 LINKER SEQADV 9FG0 ALA D 316 UNP P14867 LINKER SEQADV 9FG0 ARG D 317 UNP P14867 LINKER SEQADV 9FG0 ALA D 318 UNP P14867 LINKER SEQADV 9FG0 ALA D 319 UNP P14867 LINKER SEQADV 9FG0 SER E 308 UNP P28472 LINKER SEQADV 9FG0 GLN E 309 UNP P28472 LINKER SEQADV 9FG0 PRO E 310 UNP P28472 LINKER SEQADV 9FG0 ALA E 311 UNP P28472 LINKER SEQADV 9FG0 ARG E 312 UNP P28472 LINKER SEQADV 9FG0 ALA E 313 UNP P28472 LINKER SEQADV 9FG0 ALA E 314 UNP P28472 LINKER SEQRES 1 A 338 ASP ASN THR THR VAL PHE THR ARG ILE LEU ASP ARG LEU SEQRES 2 A 338 LEU ASP GLY TYR ASP ASN ARG LEU ARG PRO GLY LEU GLY SEQRES 3 A 338 GLU ARG VAL THR GLU VAL LYS THR ASP ILE PHE VAL THR SEQRES 4 A 338 SER PHE GLY PRO VAL SER ASP HIS ASP MET GLU TYR THR SEQRES 5 A 338 ILE ASP VAL PHE PHE ARG GLN SER TRP LYS ASP GLU ARG SEQRES 6 A 338 LEU LYS PHE LYS GLY PRO MET THR VAL LEU ARG LEU ASN SEQRES 7 A 338 ASN LEU MET ALA SER LYS ILE TRP THR PRO ASP THR PHE SEQRES 8 A 338 PHE HIS ASN GLY LYS LYS SER VAL ALA HIS ASN MET THR SEQRES 9 A 338 MET PRO ASN LYS LEU LEU ARG ILE THR GLU ASP GLY THR SEQRES 10 A 338 LEU LEU TYR THR MET ARG LEU THR VAL ARG ALA GLU CYS SEQRES 11 A 338 PRO MET HIS LEU GLU ASP PHE PRO MET ASP ALA HIS ALA SEQRES 12 A 338 CYS PRO LEU LYS PHE GLY SER TYR ALA TYR THR ARG ALA SEQRES 13 A 338 GLU VAL VAL TYR GLU TRP THR ARG GLU PRO ALA ARG SER SEQRES 14 A 338 VAL VAL VAL ALA GLU ASP GLY SER ARG LEU ASN GLN TYR SEQRES 15 A 338 ASP LEU LEU GLY GLN THR VAL ASP SER GLY ILE VAL GLN SEQRES 16 A 338 SER SER THR GLY GLU TYR VAL VAL MET THR THR HIS PHE SEQRES 17 A 338 HIS LEU LYS ARG LYS ILE GLY TYR PHE VAL ILE GLN THR SEQRES 18 A 338 TYR LEU PRO CYS ILE MET THR VAL ILE LEU SER GLN VAL SEQRES 19 A 338 SER PHE TRP LEU ASN ARG GLU SER VAL PRO ALA ARG THR SEQRES 20 A 338 VAL PHE GLY VAL THR THR VAL LEU THR MET THR THR LEU SEQRES 21 A 338 SER ILE SER ALA ARG ASN SER LEU PRO LYS VAL ALA TYR SEQRES 22 A 338 ALA THR ALA MET ASP TRP PHE ILE ALA VAL CYS TYR ALA SEQRES 23 A 338 PHE VAL PHE SER ALA LEU ILE GLU PHE ALA THR VAL ASN SEQRES 24 A 338 TYR PHE THR LYS SER GLN PRO ALA ARG ALA ALA LYS ILE SEQRES 25 A 338 ASP ARG LEU SER ARG ILE ALA PHE PRO LEU LEU PHE GLY SEQRES 26 A 338 ILE PHE ASN LEU VAL TYR TRP ALA THR TYR LEU ASN ARG SEQRES 1 B 333 ASN MET SER PHE VAL LYS GLU THR VAL ASP LYS LEU LEU SEQRES 2 B 333 LYS GLY TYR ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY SEQRES 3 B 333 PRO PRO VAL CYS VAL GLY MET ASN ILE ASP ILE ALA SER SEQRES 4 B 333 ILE ASP MET VAL SER GLU VAL ASN MET ASP TYR THR LEU SEQRES 5 B 333 THR MET TYR PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU SEQRES 6 B 333 ALA TYR SER GLY ILE PRO LEU ASN LEU THR LEU ASP ASN SEQRES 7 B 333 ARG VAL ALA ASP GLN LEU TRP VAL PRO ASP THR TYR PHE SEQRES 8 B 333 LEU ASN ASP LYS LYS SER PHE VAL HIS GLY VAL THR VAL SEQRES 9 B 333 LYS ASN ARG MET ILE ARG LEU HIS PRO ASP GLY THR VAL SEQRES 10 B 333 LEU TYR GLY LEU ARG ILE THR THR THR ALA ALA CYS MET SEQRES 11 B 333 MET ASP LEU ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS SEQRES 12 B 333 THR LEU GLU ILE GLU SER TYR GLY TYR THR THR ASP ASP SEQRES 13 B 333 ILE GLU PHE TYR TRP ARG GLY GLY ASP LYS ALA VAL THR SEQRES 14 B 333 GLY VAL GLU ARG ILE GLU LEU PRO GLN PHE SER ILE VAL SEQRES 15 B 333 GLU HIS ARG LEU VAL SER ARG ASN VAL VAL PHE ALA THR SEQRES 16 B 333 GLY ALA TYR PRO ARG LEU SER LEU SER PHE ARG LEU LYS SEQRES 17 B 333 ARG ASN ILE GLY TYR PHE ILE LEU GLN THR TYR MET PRO SEQRES 18 B 333 SER ILE LEU ILE THR ILE LEU SER TRP VAL SER PHE TRP SEQRES 19 B 333 ILE ASN TYR ASP ALA SER ALA ALA ARG VAL ALA LEU GLY SEQRES 20 B 333 ILE THR THR VAL LEU THR MET THR THR ILE ASN THR HIS SEQRES 21 B 333 LEU ARG GLU THR LEU PRO LYS ILE PRO TYR VAL LYS ALA SEQRES 22 B 333 ILE ASP MET TYR LEU MET GLY CYS PHE VAL PHE VAL PHE SEQRES 23 B 333 LEU ALA LEU LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE SEQRES 24 B 333 PHE SER GLN PRO ALA ARG ALA ALA ALA ILE ASP ARG TRP SEQRES 25 B 333 SER ARG ILE VAL PHE PRO PHE THR PHE SER LEU PHE ASN SEQRES 26 B 333 LEU VAL TYR TRP LEU TYR TYR VAL SEQRES 1 C 334 GLY ASP VAL THR VAL ILE LEU ASN ASN LEU LEU GLU GLY SEQRES 2 C 334 TYR ASP ASN LYS LEU ARG PRO ASP ILE GLY VAL LYS PRO SEQRES 3 C 334 THR LEU ILE HIS THR ASP MET TYR VAL ASN SER ILE GLY SEQRES 4 C 334 PRO VAL ASN ALA ILE ASN MET GLU TYR THR ILE ASP ILE SEQRES 5 C 334 PHE PHE ALA GLN THR TRP TYR ASP ARG ARG LEU LYS PHE SEQRES 6 C 334 ASN SER THR ILE LYS VAL LEU ARG LEU ASN SER ASN MET SEQRES 7 C 334 VAL GLY LYS ILE TRP ILE PRO ASP THR PHE PHE ARG ASN SEQRES 8 C 334 SER LYS LYS ALA ASP ALA HIS TRP ILE THR THR PRO ASN SEQRES 9 C 334 ARG MET LEU ARG ILE TRP ASN ASP GLY ARG VAL LEU TYR SEQRES 10 C 334 THR LEU ARG LEU THR ILE ASP ALA GLU CYS GLN LEU GLN SEQRES 11 C 334 LEU HIS ASN PHE PRO MET ASP GLU HIS SER CYS PRO LEU SEQRES 12 C 334 GLU PHE SER SER TYR GLY TYR PRO ARG GLU GLU ILE VAL SEQRES 13 C 334 TYR GLN TRP LYS ARG SER SER VAL GLU VAL GLY ASP THR SEQRES 14 C 334 ARG SER TRP ARG LEU TYR GLN PHE SER PHE VAL GLY LEU SEQRES 15 C 334 ARG ASN THR THR GLU VAL VAL LYS THR THR SER GLY ASP SEQRES 16 C 334 TYR VAL VAL MET SER VAL TYR PHE ASP LEU SER ARG ARG SEQRES 17 C 334 MET GLY TYR PHE THR ILE GLN THR TYR ILE PRO CYS THR SEQRES 18 C 334 LEU ILE VAL VAL LEU SER TRP VAL SER PHE TRP ILE ASN SEQRES 19 C 334 LYS ASP ALA VAL PRO ALA ARG THR SER LEU GLY ILE THR SEQRES 20 C 334 THR VAL LEU THR MET THR THR LEU SER THR ILE ALA ARG SEQRES 21 C 334 LYS SER LEU PRO LYS VAL SER TYR VAL THR ALA MET ASP SEQRES 22 C 334 LEU PHE VAL SER VAL CYS PHE ILE PHE VAL PHE SER ALA SEQRES 23 C 334 LEU VAL GLU TYR GLY THR LEU HIS TYR PHE VAL SER SER SEQRES 24 C 334 GLN PRO ALA ARG ALA ALA LYS MET ASP SER TYR ALA ARG SEQRES 25 C 334 ILE PHE PHE PRO THR ALA PHE CYS LEU PHE ASN LEU VAL SEQRES 26 C 334 TYR TRP VAL SER TYR LEU TYR LEU GLY SEQRES 1 D 338 ASP ASN THR THR VAL PHE THR ARG ILE LEU ASP ARG LEU SEQRES 2 D 338 LEU ASP GLY TYR ASP ASN ARG LEU ARG PRO GLY LEU GLY SEQRES 3 D 338 GLU ARG VAL THR GLU VAL LYS THR ASP ILE PHE VAL THR SEQRES 4 D 338 SER PHE GLY PRO VAL SER ASP HIS ASP MET GLU TYR THR SEQRES 5 D 338 ILE ASP VAL PHE PHE ARG GLN SER TRP LYS ASP GLU ARG SEQRES 6 D 338 LEU LYS PHE LYS GLY PRO MET THR VAL LEU ARG LEU ASN SEQRES 7 D 338 ASN LEU MET ALA SER LYS ILE TRP THR PRO ASP THR PHE SEQRES 8 D 338 PHE HIS ASN GLY LYS LYS SER VAL ALA HIS ASN MET THR SEQRES 9 D 338 MET PRO ASN LYS LEU LEU ARG ILE THR GLU ASP GLY THR SEQRES 10 D 338 LEU LEU TYR THR MET ARG LEU THR VAL ARG ALA GLU CYS SEQRES 11 D 338 PRO MET HIS LEU GLU ASP PHE PRO MET ASP ALA HIS ALA SEQRES 12 D 338 CYS PRO LEU LYS PHE GLY SER TYR ALA TYR THR ARG ALA SEQRES 13 D 338 GLU VAL VAL TYR GLU TRP THR ARG GLU PRO ALA ARG SER SEQRES 14 D 338 VAL VAL VAL ALA GLU ASP GLY SER ARG LEU ASN GLN TYR SEQRES 15 D 338 ASP LEU LEU GLY GLN THR VAL ASP SER GLY ILE VAL GLN SEQRES 16 D 338 SER SER THR GLY GLU TYR VAL VAL MET THR THR HIS PHE SEQRES 17 D 338 HIS LEU LYS ARG LYS ILE GLY TYR PHE VAL ILE GLN THR SEQRES 18 D 338 TYR LEU PRO CYS ILE MET THR VAL ILE LEU SER GLN VAL SEQRES 19 D 338 SER PHE TRP LEU ASN ARG GLU SER VAL PRO ALA ARG THR SEQRES 20 D 338 VAL PHE GLY VAL THR THR VAL LEU THR MET THR THR LEU SEQRES 21 D 338 SER ILE SER ALA ARG ASN SER LEU PRO LYS VAL ALA TYR SEQRES 22 D 338 ALA THR ALA MET ASP TRP PHE ILE ALA VAL CYS TYR ALA SEQRES 23 D 338 PHE VAL PHE SER ALA LEU ILE GLU PHE ALA THR VAL ASN SEQRES 24 D 338 TYR PHE THR LYS SER GLN PRO ALA ARG ALA ALA LYS ILE SEQRES 25 D 338 ASP ARG LEU SER ARG ILE ALA PHE PRO LEU LEU PHE GLY SEQRES 26 D 338 ILE PHE ASN LEU VAL TYR TRP ALA THR TYR LEU ASN ARG SEQRES 1 E 333 ASN MET SER PHE VAL LYS GLU THR VAL ASP LYS LEU LEU SEQRES 2 E 333 LYS GLY TYR ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY SEQRES 3 E 333 PRO PRO VAL CYS VAL GLY MET ASN ILE ASP ILE ALA SER SEQRES 4 E 333 ILE ASP MET VAL SER GLU VAL ASN MET ASP TYR THR LEU SEQRES 5 E 333 THR MET TYR PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU SEQRES 6 E 333 ALA TYR SER GLY ILE PRO LEU ASN LEU THR LEU ASP ASN SEQRES 7 E 333 ARG VAL ALA ASP GLN LEU TRP VAL PRO ASP THR TYR PHE SEQRES 8 E 333 LEU ASN ASP LYS LYS SER PHE VAL HIS GLY VAL THR VAL SEQRES 9 E 333 LYS ASN ARG MET ILE ARG LEU HIS PRO ASP GLY THR VAL SEQRES 10 E 333 LEU TYR GLY LEU ARG ILE THR THR THR ALA ALA CYS MET SEQRES 11 E 333 MET ASP LEU ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS SEQRES 12 E 333 THR LEU GLU ILE GLU SER TYR GLY TYR THR THR ASP ASP SEQRES 13 E 333 ILE GLU PHE TYR TRP ARG GLY GLY ASP LYS ALA VAL THR SEQRES 14 E 333 GLY VAL GLU ARG ILE GLU LEU PRO GLN PHE SER ILE VAL SEQRES 15 E 333 GLU HIS ARG LEU VAL SER ARG ASN VAL VAL PHE ALA THR SEQRES 16 E 333 GLY ALA TYR PRO ARG LEU SER LEU SER PHE ARG LEU LYS SEQRES 17 E 333 ARG ASN ILE GLY TYR PHE ILE LEU GLN THR TYR MET PRO SEQRES 18 E 333 SER ILE LEU ILE THR ILE LEU SER TRP VAL SER PHE TRP SEQRES 19 E 333 ILE ASN TYR ASP ALA SER ALA ALA ARG VAL ALA LEU GLY SEQRES 20 E 333 ILE THR THR VAL LEU THR MET THR THR ILE ASN THR HIS SEQRES 21 E 333 LEU ARG GLU THR LEU PRO LYS ILE PRO TYR VAL LYS ALA SEQRES 22 E 333 ILE ASP MET TYR LEU MET GLY CYS PHE VAL PHE VAL PHE SEQRES 23 E 333 LEU ALA LEU LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE SEQRES 24 E 333 PHE SER GLN PRO ALA ARG ALA ALA ALA ILE ASP ARG TRP SEQRES 25 E 333 SER ARG ILE VAL PHE PRO PHE THR PHE SER LEU PHE ASN SEQRES 26 E 333 LEU VAL TYR TRP LEU TYR TYR VAL SEQRES 1 F 123 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 123 ALA GLY GLY SER LEU ARG VAL SER CYS ALA ALA SER GLY SEQRES 3 F 123 ARG THR PHE THR THR TYR ILE MET ALA TRP PHE ARG GLN SEQRES 4 F 123 ALA PRO GLY LYS GLU ARG GLU PHE LEU ALA ALA MET ASP SEQRES 5 F 123 GLN GLY ARG ILE GLN TYR TYR GLY ASP SER VAL ARG GLY SEQRES 6 F 123 ARG PHE THR ILE SER ARG ASP TYR ALA LYS ASN SER VAL SEQRES 7 F 123 ASP LEU GLN LEU ASP GLY LEU ARG PRO GLU ASP THR ALA SEQRES 8 F 123 VAL TYR TYR CYS ALA ALA GLY ALA GLY PHE TRP GLY LEU SEQRES 9 F 123 ARG THR ALA SER SER TYR HIS TYR TRP GLY GLN GLY THR SEQRES 10 F 123 GLN VAL THR VAL SER SER HET NAG a 1 14 HET NAG a 2 14 HET BMA a 3 11 HET MAN a 4 11 HET MAN a 5 11 HET MAN a 6 11 HET MAN a 7 11 HET MAN a 8 11 HET MAN a 9 11 HET MAN a 10 11 HET NAG b 1 14 HET NAG b 2 14 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET MAN G 4 11 HET MAN G 5 11 HET MAN G 6 11 HET NAG c 1 14 HET NAG c 2 14 HET NAG d 1 14 HET NAG d 2 14 HET BMA d 3 11 HET MAN d 4 11 HET MAN d 5 11 HET NAG e 1 14 HET NAG e 2 14 HET NAG H 1 14 HET NAG H 2 14 HET BMA H 3 11 HET MAN H 4 11 HET MAN H 5 11 HET MAN H 6 11 HET ABU B 501 7 HET ABU E 501 7 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM ABU GAMMA-AMINO-BUTANOIC ACID HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN ABU GAMMA(AMINO)-BUTYRIC ACID FORMUL 7 NAG 14(C8 H15 N O6) FORMUL 7 BMA 4(C6 H12 O6) FORMUL 7 MAN 15(C6 H12 O6) FORMUL 14 ABU 2(C4 H9 N O2) HELIX 1 AA1 ASP A 10 LEU A 23 1 14 HELIX 2 AA2 GLU A 73 LYS A 76 5 4 HELIX 3 AA3 ASN A 87 SER A 92 1 6 HELIX 4 AA4 GLU A 174 ARG A 177 5 4 HELIX 5 AA5 ILE A 223 THR A 230 1 8 HELIX 6 AA6 THR A 230 SER A 244 1 15 HELIX 7 AA7 PHE A 245 LEU A 247 5 3 HELIX 8 AA8 SER A 251 LEU A 277 1 27 HELIX 9 AA9 THR A 284 THR A 311 1 28 HELIX 10 AB1 GLN A 314 TYR A 415 1 31 HELIX 11 AB2 MET B 9 LYS B 21 1 13 HELIX 12 AB3 LYS B 70 ALA B 73 5 4 HELIX 13 AB4 ASP B 84 LEU B 91 5 8 HELIX 14 AB5 GLY B 170 LYS B 173 5 4 HELIX 15 AB6 GLY B 177 ILE B 181 5 5 HELIX 16 AB7 ILE B 218 THR B 225 1 8 HELIX 17 AB8 THR B 225 SER B 236 1 12 HELIX 18 AB9 TRP B 237 ILE B 242 5 6 HELIX 19 AC1 ALA B 246 LEU B 272 1 27 HELIX 20 AC2 LYS B 279 PHE B 306 1 28 HELIX 21 AC3 GLN B 309 TYR B 446 1 31 HELIX 22 AC4 ASP C 26 GLU C 36 1 11 HELIX 23 AC5 ARG C 85 LYS C 88 5 4 HELIX 24 AC6 ASN C 99 ILE C 106 5 8 HELIX 25 AC7 MET C 233 THR C 240 1 8 HELIX 26 AC8 THR C 240 SER C 254 1 15 HELIX 27 AC9 PHE C 255 ILE C 257 5 3 HELIX 28 AD1 ALA C 261 ILE C 282 1 22 HELIX 29 AD2 THR C 294 GLN C 324 1 31 HELIX 30 AD3 GLN C 324 LEU C 428 1 34 HELIX 31 AD4 ASN D 11 LEU D 23 1 13 HELIX 32 AD5 GLU D 73 LYS D 76 5 4 HELIX 33 AD6 MET D 90 ILE D 94 5 5 HELIX 34 AD7 HIS D 142 PHE D 146 5 5 HELIX 35 AD8 GLU D 174 ARG D 177 5 4 HELIX 36 AD9 ILE D 223 THR D 230 1 8 HELIX 37 AE1 THR D 230 SER D 244 1 15 HELIX 38 AE2 PHE D 245 LEU D 247 5 3 HELIX 39 AE3 SER D 251 ASN D 275 1 25 HELIX 40 AE4 THR D 284 THR D 311 1 28 HELIX 41 AE5 GLN D 314 ARG D 418 1 34 HELIX 42 AE6 MET E 9 LYS E 21 1 13 HELIX 43 AE7 LYS E 70 ALA E 73 5 4 HELIX 44 AE8 ASP E 84 LEU E 91 5 8 HELIX 45 AE9 GLY E 170 LYS E 173 5 4 HELIX 46 AF1 GLY E 177 ILE E 181 5 5 HELIX 47 AF2 ILE E 218 THR E 225 1 8 HELIX 48 AF3 THR E 225 SER E 236 1 12 HELIX 49 AF4 TRP E 237 ILE E 242 5 6 HELIX 50 AF5 ALA E 246 LEU E 272 1 27 HELIX 51 AF6 LYS E 279 PHE E 306 1 28 HELIX 52 AF7 GLN E 309 VAL E 447 1 32 HELIX 53 AF8 ARG F 87 THR F 91 5 5 HELIX 54 AF9 THR F 107 TYR F 111 5 5 SHEET 1 AA1 6 VAL A 83 LEU A 86 0 SHEET 2 AA1 6 LYS A 117 THR A 122 -1 O ILE A 121 N LEU A 84 SHEET 3 AA1 6 THR A 126 GLU A 138 -1 O THR A 130 N LEU A 118 SHEET 4 AA1 6 GLU A 59 LYS A 71 -1 N TRP A 70 O LEU A 127 SHEET 5 AA1 6 THR A 39 SER A 54 -1 N PHE A 46 O PHE A 65 SHEET 6 AA1 6 VAL A 167 TRP A 171 1 O GLU A 170 N THR A 43 SHEET 1 AA2 5 VAL A 108 ALA A 109 0 SHEET 2 AA2 5 THR A 126 GLU A 138 -1 O THR A 134 N VAL A 108 SHEET 3 AA2 5 GLU A 59 LYS A 71 -1 N TRP A 70 O LEU A 127 SHEET 4 AA2 5 THR A 39 SER A 54 -1 N PHE A 46 O PHE A 65 SHEET 5 AA2 5 VAL A 179 VAL A 181 1 O VAL A 180 N VAL A 47 SHEET 1 AA3 4 THR A 99 PHE A 101 0 SHEET 2 AA3 4 ALA A 150 SER A 159 -1 O GLY A 158 N PHE A 100 SHEET 3 AA3 4 GLU A 209 ARG A 221 -1 O MET A 213 N PHE A 157 SHEET 4 AA3 4 TYR A 191 GLN A 204 -1 N THR A 197 O HIS A 216 SHEET 1 AA4 6 LEU B 81 LEU B 83 0 SHEET 2 AA4 6 ARG B 114 LEU B 118 -1 O LEU B 118 N LEU B 81 SHEET 3 AA4 6 THR B 123 ALA B 135 -1 O LEU B 125 N ARG B 117 SHEET 4 AA4 6 ASP B 56 ARG B 68 -1 N TRP B 67 O VAL B 124 SHEET 5 AA4 6 VAL B 36 SER B 51 -1 N ASN B 41 O GLN B 64 SHEET 6 AA4 6 ILE B 164 TRP B 168 1 O GLU B 165 N VAL B 38 SHEET 1 AA5 5 ASP B 101 VAL B 106 0 SHEET 2 AA5 5 THR B 123 ALA B 135 -1 O THR B 133 N LYS B 102 SHEET 3 AA5 5 ASP B 56 ARG B 68 -1 N TRP B 67 O VAL B 124 SHEET 4 AA5 5 VAL B 36 SER B 51 -1 N ASN B 41 O GLN B 64 SHEET 5 AA5 5 VAL B 175 THR B 176 1 O THR B 176 N ILE B 44 SHEET 1 AA6 4 THR B 96 PHE B 98 0 SHEET 2 AA6 4 GLU B 147 SER B 156 -1 O GLU B 155 N TYR B 97 SHEET 3 AA6 4 ALA B 204 ARG B 216 -1 O PHE B 212 N CYS B 150 SHEET 4 AA6 4 PHE B 186 VAL B 199 -1 N VAL B 194 O SER B 209 SHEET 1 AA7 4 VAL C 95 LEU C 98 0 SHEET 2 AA7 4 ARG C 129 TRP C 134 -1 O LEU C 131 N LEU C 98 SHEET 3 AA7 4 ARG C 138 GLU C 150 -1 O LEU C 140 N ARG C 132 SHEET 4 AA7 4 SER C 116 ALA C 121 -1 N LYS C 117 O ASP C 148 SHEET 1 AA8 6 VAL C 95 LEU C 98 0 SHEET 2 AA8 6 ARG C 129 TRP C 134 -1 O LEU C 131 N LEU C 98 SHEET 3 AA8 6 ARG C 138 GLU C 150 -1 O LEU C 140 N ARG C 132 SHEET 4 AA8 6 GLU C 71 TYR C 83 -1 N PHE C 78 O LEU C 143 SHEET 5 AA8 6 THR C 51 ASN C 66 -1 N ASN C 66 O GLU C 71 SHEET 6 AA8 6 ILE C 179 VAL C 190 1 O GLU C 189 N VAL C 59 SHEET 1 AA9 4 THR C 111 PHE C 113 0 SHEET 2 AA9 4 GLU C 162 SER C 171 -1 O SER C 170 N PHE C 112 SHEET 3 AA9 4 ASP C 219 ARG C 231 -1 O LEU C 229 N HIS C 163 SHEET 4 AA9 4 PHE C 201 LYS C 214 -1 N GLU C 211 O VAL C 222 SHEET 1 AB1 6 VAL D 83 LEU D 86 0 SHEET 2 AB1 6 LYS D 117 THR D 122 -1 O LEU D 119 N LEU D 86 SHEET 3 AB1 6 THR D 126 GLU D 138 -1 O LEU D 128 N ARG D 120 SHEET 4 AB1 6 GLU D 59 LYS D 71 -1 N PHE D 66 O MET D 131 SHEET 5 AB1 6 THR D 39 SER D 54 -1 N LYS D 42 O SER D 69 SHEET 6 AB1 6 VAL D 167 TRP D 171 1 O GLU D 170 N VAL D 41 SHEET 1 AB2 5 VAL D 108 ALA D 109 0 SHEET 2 AB2 5 THR D 126 GLU D 138 -1 O THR D 134 N VAL D 108 SHEET 3 AB2 5 GLU D 59 LYS D 71 -1 N PHE D 66 O MET D 131 SHEET 4 AB2 5 THR D 39 SER D 54 -1 N LYS D 42 O SER D 69 SHEET 5 AB2 5 VAL D 179 VAL D 181 1 O VAL D 180 N VAL D 47 SHEET 1 AB3 4 THR D 99 PHE D 101 0 SHEET 2 AB3 4 ALA D 150 SER D 159 -1 O GLY D 158 N PHE D 100 SHEET 3 AB3 4 GLU D 209 ARG D 221 -1 O LEU D 219 N HIS D 151 SHEET 4 AB3 4 TYR D 191 GLN D 204 -1 N ASP D 199 O THR D 214 SHEET 1 AB4 6 LEU E 81 LEU E 83 0 SHEET 2 AB4 6 ARG E 114 LEU E 118 -1 O LEU E 118 N LEU E 81 SHEET 3 AB4 6 THR E 123 ALA E 135 -1 O LEU E 125 N ARG E 117 SHEET 4 AB4 6 ASP E 56 ARG E 68 -1 N TRP E 67 O VAL E 124 SHEET 5 AB4 6 VAL E 36 SER E 51 -1 N ASN E 41 O GLN E 64 SHEET 6 AB4 6 ILE E 164 TRP E 168 1 O GLU E 165 N VAL E 38 SHEET 1 AB5 5 ASP E 101 VAL E 106 0 SHEET 2 AB5 5 THR E 123 ALA E 135 -1 O THR E 133 N LYS E 103 SHEET 3 AB5 5 ASP E 56 ARG E 68 -1 N TRP E 67 O VAL E 124 SHEET 4 AB5 5 VAL E 36 SER E 51 -1 N ASN E 41 O GLN E 64 SHEET 5 AB5 5 VAL E 175 THR E 176 1 O THR E 176 N ILE E 44 SHEET 1 AB6 4 THR E 96 PHE E 98 0 SHEET 2 AB6 4 GLU E 147 SER E 156 -1 O GLU E 155 N TYR E 97 SHEET 3 AB6 4 GLY E 203 ARG E 216 -1 O LEU E 208 N ILE E 154 SHEET 4 AB6 4 PHE E 186 PHE E 200 -1 N VAL E 189 O ARG E 213 SHEET 1 AB7 4 GLN F 4 GLU F 7 0 SHEET 2 AB7 4 LEU F 19 SER F 26 -1 O ALA F 24 N GLN F 6 SHEET 3 AB7 4 SER F 78 LEU F 83 -1 O LEU F 81 N VAL F 21 SHEET 4 AB7 4 PHE F 68 ASP F 73 -1 N THR F 69 O GLN F 82 SHEET 1 AB8 6 GLY F 11 VAL F 13 0 SHEET 2 AB8 6 THR F 118 VAL F 122 1 O THR F 121 N GLY F 11 SHEET 3 AB8 6 ALA F 92 GLY F 99 -1 N ALA F 92 O VAL F 120 SHEET 4 AB8 6 ILE F 34 GLN F 40 -1 N ILE F 34 O GLY F 99 SHEET 5 AB8 6 ARG F 46 MET F 52 -1 O GLU F 47 N ARG F 39 SHEET 6 AB8 6 GLN F 58 TYR F 60 -1 O TYR F 59 N ALA F 51 SHEET 1 AB9 4 GLY F 11 VAL F 13 0 SHEET 2 AB9 4 THR F 118 VAL F 122 1 O THR F 121 N GLY F 11 SHEET 3 AB9 4 ALA F 92 GLY F 99 -1 N ALA F 92 O VAL F 120 SHEET 4 AB9 4 TYR F 113 TRP F 114 -1 O TYR F 113 N ALA F 98 SSBOND 1 CYS A 139 CYS A 153 1555 1555 2.03 SSBOND 2 CYS B 136 CYS B 150 1555 1555 2.04 SSBOND 3 CYS C 151 CYS C 165 1555 1555 2.03 SSBOND 4 CYS D 139 CYS D 153 1555 1555 2.03 SSBOND 5 CYS E 136 CYS E 150 1555 1555 2.03 SSBOND 6 CYS F 23 CYS F 96 1555 1555 2.03 LINK ND2 ASN A 111 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN B 80 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN B 149 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN C 208 C1 NAG c 1 1555 1555 1.45 LINK ND2 ASN D 111 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN E 80 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN E 149 C1 NAG H 1 1555 1555 1.44 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.44 LINK O3 BMA a 3 C1 MAN a 4 1555 1555 1.44 LINK O6 BMA a 3 C1 MAN a 7 1555 1555 1.45 LINK O2 MAN a 4 C1 MAN a 5 1555 1555 1.44 LINK O2 MAN a 5 C1 MAN a 6 1555 1555 1.44 LINK O6 MAN a 7 C1 MAN a 8 1555 1555 1.44 LINK O3 MAN a 7 C1 MAN a 10 1555 1555 1.44 LINK O2 MAN a 8 C1 MAN a 9 1555 1555 1.44 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.43 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.44 LINK O6 BMA G 3 C1 MAN G 4 1555 1555 1.44 LINK O3 BMA G 3 C1 MAN G 6 1555 1555 1.44 LINK O3 MAN G 4 C1 MAN G 5 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.44 LINK O3 BMA d 3 C1 MAN d 4 1555 1555 1.44 LINK O6 BMA d 3 C1 MAN d 5 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.44 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.43 LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.45 LINK O6 BMA H 3 C1 MAN H 4 1555 1555 1.44 LINK O3 BMA H 3 C1 MAN H 6 1555 1555 1.44 LINK O3 MAN H 4 C1 MAN H 5 1555 1555 1.44 CISPEP 1 MET A 112 THR A 113 0 -0.09 CISPEP 2 PHE A 146 PRO A 147 0 2.55 CISPEP 3 VAL B 109 THR B 110 0 0.77 CISPEP 4 TYR B 143 PRO B 144 0 2.88 CISPEP 5 ILE C 124 THR C 125 0 -1.47 CISPEP 6 PHE C 158 PRO C 159 0 3.07 CISPEP 7 MET D 112 THR D 113 0 -3.60 CISPEP 8 PHE D 146 PRO D 147 0 0.64 CISPEP 9 VAL E 109 THR E 110 0 0.05 CISPEP 10 TYR E 143 PRO E 144 0 0.47 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