HEADER MEMBRANE PROTEIN 03-AUG-21 7PC0 TITLE GABA-A RECEPTOR BOUND BY A-COBRATOXIN CAVEAT 7PC0 NAG G 1 HAS WRONG CHIRALITY AT ATOM C1 BMA G 3 HAS WRONG CAVEAT 2 7PC0 CHIRALITY AT ATOM C1 MAN G 4 HAS WRONG CHIRALITY AT ATOM C1 CAVEAT 3 7PC0 MAN G 5 HAS WRONG CHIRALITY AT ATOM C1 MAN G 6 HAS WRONG CAVEAT 4 7PC0 CHIRALITY AT ATOM C1 MAN I 5 HAS WRONG CHIRALITY AT ATOM C1 CAVEAT 5 7PC0 NAG J 1 HAS WRONG CHIRALITY AT ATOM C1 NAG J 2 HAS WRONG CAVEAT 6 7PC0 CHIRALITY AT ATOM C1 BMA J 3 HAS WRONG CHIRALITY AT ATOM C1 CAVEAT 7 7PC0 NAG C 501 HAS WRONG CHIRALITY AT ATOM C1 NAG E 501 HAS CAVEAT 8 7PC0 WRONG CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MEGABODY 25; COMPND 3 CHAIN: F; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GABA(A) RECEPTOR SUBUNIT ALPHA-1,GABA(A) RECEPTOR SUBUNIT COMPND 7 ALPHA-1,GABA(A) RECEPTOR SUBUNIT ALPHA-1,GAMMA-AMINOBUTYRIC ACID COMPND 8 RECEPTOR SUBUNIT ALPHA-1; COMPND 9 CHAIN: A; COMPND 10 SYNONYM: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-1; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT BETA-3; COMPND 14 CHAIN: B, C, E; COMPND 15 SYNONYM: GABA(A) RECEPTOR SUBUNIT BETA-3; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-1; COMPND 19 CHAIN: D; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: ALPHA-COBRATOXIN; COMPND 23 CHAIN: K; COMPND 24 SYNONYM: ALPHA-CT,ALPHA-CBT,ALPHA-CBTX,ALPHA-CTX,ALPHA-ELAPITOXIN- COMPND 25 NK2A,ALPHA-EPTX-NK2A,LONG NEUROTOXIN 1,SIAMENSIS 3; COMPND 26 MOL_ID: 6; COMPND 27 MOLECULE: ALPHA-COBRATOXIN; COMPND 28 CHAIN: L; COMPND 29 SYNONYM: ALPHA-CT,ALPHA-CBT,ALPHA-CBTX,ALPHA-CTX,ALPHA-ELAPITOXIN- COMPND 30 NK2A,ALPHA-EPTX-NK2A,LONG NEUROTOXIN 1,SIAMENSIS 3 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_TAXID: 9844; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN, HUMAN; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 GENE: GABRA1; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN, HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 GENE: GABRB3; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 GENE: GABRA1; SOURCE 25 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: NAJA KAOUTHIA; SOURCE 29 ORGANISM_COMMON: MONOCLED COBRA; SOURCE 30 ORGANISM_TAXID: 8649; SOURCE 31 MOL_ID: 6; SOURCE 32 ORGANISM_SCIENTIFIC: NAJA KAOUTHIA; SOURCE 33 ORGANISM_COMMON: MONOCLED COBRA; SOURCE 34 ORGANISM_TAXID: 8649 KEYWDS NEUROTRANSMISSION, TOXIN, GABA, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR V.B.KASARAGOD,P.S.MILLER JRNL AUTH V.B.KASARAGOD,M.MORTENSEN,S.W.HARDWICK,A.A.WAHID,V.DOROVYKH, JRNL AUTH 2 D.Y.CHIRGADZE,T.G.SMART,P.S.MILLER JRNL TITL MECHANISMS OF INHIBITION AND ACTIVATION OF EXTRASYNAPTIC JRNL TITL 2 ALPHA BETA GABAA RECEPTORS JRNL REF NATURE 2022 JRNL REFN ESSN 1476-4687 JRNL DOI 10.1038/S41586-022-04402-Z REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.000 REMARK 3 NUMBER OF PARTICLES : 78662 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 7PC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292116333. 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 : GABA-A RECEPTOR PENTAMER BOUND REMARK 245 BY COBRATOXIN; GABA-A RECEPTOR REMARK 245 PENTAMER; COBRATOXIN; MEGABODY REMARK 245 25 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.25 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : DIFFRACTION REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 50.69 REMARK 245 ILLUMINATION MODE : SPOT SCAN REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, A, B, C, E, D, K, L, G, H, REMARK 350 AND CHAINS: I, J REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ILE K 9 CB CG1 CG2 CD1 REMARK 470 ALA K 28 CB REMARK 470 ARG K 68 CB CG CD NE CZ NH1 NH2 REMARK 470 LYS K 69 CB CG CD CE NZ REMARK 470 ARG K 70 CG CD NE CZ NH1 NH2 REMARK 470 ILE L 9 CB CG1 CG2 CD1 REMARK 470 ALA L 28 CB 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 O6 BMA G 3 O5 MAN G 4 1.80 REMARK 500 O3 MAN I 4 O5 MAN I 5 1.90 REMARK 500 O4 NAG G 1 O5 NAG G 2 1.96 REMARK 500 O PHE B 221 OG1 THR B 225 2.00 REMARK 500 O PHE E 221 OG1 THR E 225 2.02 REMARK 500 OD2 ASP L 8 O3 MAN J 4 2.09 REMARK 500 OG SER F 7 OG SER F 21 2.09 REMARK 500 OG SER B 51 OD1 ASP B 56 2.09 REMARK 500 OD2 ASP B 101 OG1 THR B 132 2.10 REMARK 500 O6 BMA J 3 C2 MAN J 4 2.10 REMARK 500 OG SER C 46 OD1 ASP C 48 2.11 REMARK 500 OG1 THR C 110 O THR D 99 2.11 REMARK 500 O GLU A 174 OG SER A 178 2.15 REMARK 500 O6 BMA G 3 O2 MAN G 4 2.16 REMARK 500 O VAL D 238 OG SER D 241 2.17 REMARK 500 O6 BMA G 3 C2 MAN G 4 2.18 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 CYS K 62 CA - CB - SG ANGL. DEV. = 7.7 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 GLU F 44 -166.87 -74.65 REMARK 500 ASN F 85 63.46 60.06 REMARK 500 ALA F 92 -176.76 -170.04 REMARK 500 ASP F 113 -61.37 -92.46 REMARK 500 ASP A 98 33.89 -95.05 REMARK 500 LEU A 194 56.92 -96.19 REMARK 500 LEU A 247 -71.21 -64.66 REMARK 500 ASN A 248 -177.89 -179.17 REMARK 500 ALA A 285 -6.46 73.05 REMARK 500 THR B 110 -13.04 75.73 REMARK 500 ASN B 113 93.22 -68.92 REMARK 500 ASN B 243 -168.26 -170.15 REMARK 500 THR C 110 -12.88 73.87 REMARK 500 ASN C 243 -167.94 -168.92 REMARK 500 PRO C 273 43.99 -85.03 REMARK 500 PRO C 276 76.07 -66.60 REMARK 500 THR E 110 -13.82 74.62 REMARK 500 ASN E 113 97.37 -69.02 REMARK 500 ASN E 243 -170.93 -171.42 REMARK 500 PRO E 273 45.64 -85.02 REMARK 500 PRO E 276 77.92 -68.64 REMARK 500 ASP D 98 50.96 -92.56 REMARK 500 CYS D 153 77.92 43.17 REMARK 500 ASN D 248 -178.34 -178.70 REMARK 500 GLN D 314 69.71 38.75 REMARK 500 CYS K 20 148.23 -177.73 REMARK 500 PHE K 29 34.96 70.07 REMARK 500 SER K 31 -60.30 -94.02 REMARK 500 VAL K 52 148.62 -170.17 REMARK 500 SER K 58 -39.35 -130.08 REMARK 500 ASN K 61 -70.03 65.74 REMARK 500 CYS K 62 -62.68 85.47 REMARK 500 PRO L 7 48.37 -88.61 REMARK 500 ASP L 8 -0.78 74.42 REMARK 500 THR L 10 56.14 -91.03 REMARK 500 SER L 11 -35.09 -130.04 REMARK 500 CYS L 20 -178.50 -65.52 REMARK 500 ALA L 28 -119.21 69.40 REMARK 500 CYS L 56 -167.85 -79.88 REMARK 500 CYS L 62 -62.37 -95.20 REMARK 500 ASN L 63 82.42 -157.40 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 VAL K 19 CYS K 20 -139.51 REMARK 500 ASN K 61 CYS K 62 141.05 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG A 501 REMARK 610 NAG D 501 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B 602 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 267 NE2 REMARK 620 2 HIS C 267 NE2 86.3 REMARK 620 3 HIS E 267 NE2 127.3 139.8 REMARK 620 N 1 2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-13315 RELATED DB: EMDB REMARK 900 GABA-A RECEPTOR BOUND BY A-COBRATOXIN DBREF 7PC0 F 1 122 PDB 7PC0 7PC0 1 122 DBREF1 7PC0 A 12 312 UNP A0A1B0GV38_HUMAN DBREF2 7PC0 A A0A1B0GV38 54 354 DBREF 7PC0 A 313 416 PDB 7PC0 7PC0 313 416 DBREF 7PC0 B 8 419 UNP P28472 GBRB3_HUMAN 33 334 DBREF 7PC0 B 420 447 PDB 7PC0 7PC0 420 447 DBREF 7PC0 C 8 419 UNP P28472 GBRB3_HUMAN 33 334 DBREF 7PC0 C 420 447 PDB 7PC0 7PC0 420 447 DBREF 7PC0 E 8 419 UNP P28472 GBRB3_HUMAN 33 334 DBREF 7PC0 E 420 447 PDB 7PC0 7PC0 420 447 DBREF 7PC0 D 12 418 PDB 7PC0 7PC0 12 418 DBREF 7PC0 K 1 71 UNP P01391 3L21_NAJKA 1 71 DBREF 7PC0 L 1 67 UNP P01391 3L21_NAJKA 1 67 SEQADV 7PC0 SER B 308 UNP P28472 GLY 333 CONFLICT SEQADV 7PC0 SER C 308 UNP P28472 GLY 333 CONFLICT SEQADV 7PC0 SER E 308 UNP P28472 GLY 333 CONFLICT SEQRES 1 F 113 GLN VAL GLN LEU GLN GLU SER GLY LEU ARG LEU SER CYS SEQRES 2 F 113 ALA ALA SER GLY HIS THR PHE ASN TYR PRO ILE MET GLY SEQRES 3 F 113 TRP PHE ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL SEQRES 4 F 113 GLY ALA ILE SER TRP SER GLY GLY SER THR SER TYR ALA SEQRES 5 F 113 ASP SER VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASN SEQRES 6 F 113 ALA LYS ASN THR VAL TYR LEU GLU MET ASN ASN LEU LYS SEQRES 7 F 113 PRO GLU ASP THR ALA VAL TYR TYR CYS ALA ALA LYS GLY SEQRES 8 F 113 ARG TYR SER GLY GLY LEU TYR TYR PRO THR ASN TYR ASP SEQRES 9 F 113 TYR TRP GLY GLN GLY THR GLN VAL THR SEQRES 1 A 334 THR THR VAL PHE THR ARG ILE LEU ASP ARG LEU LEU ASP SEQRES 2 A 334 GLY TYR ASP ASN ARG LEU ARG PRO GLY LEU GLY GLU ARG SEQRES 3 A 334 VAL THR GLU VAL LYS THR ASP ILE PHE VAL THR SER PHE SEQRES 4 A 334 GLY PRO VAL SER ASP HIS ASP MET GLU TYR THR ILE ASP SEQRES 5 A 334 VAL PHE PHE ARG GLN SER TRP LYS ASP GLU ARG LEU LYS SEQRES 6 A 334 PHE LYS GLY PRO MET THR VAL LEU ARG LEU ASN ASN LEU SEQRES 7 A 334 MET ALA SER LYS ILE TRP THR PRO ASP THR PHE PHE HIS SEQRES 8 A 334 ASN GLY LYS LYS SER VAL ALA HIS ASN MET THR MET PRO SEQRES 9 A 334 ASN LYS LEU LEU ARG ILE THR GLU ASP GLY THR LEU LEU SEQRES 10 A 334 TYR THR MET ARG LEU THR VAL ARG ALA GLU CYS PRO MET SEQRES 11 A 334 HIS LEU GLU ASP PHE PRO MET ASP ALA HIS ALA CYS PRO SEQRES 12 A 334 LEU LYS PHE GLY SER TYR ALA TYR THR ARG ALA GLU VAL SEQRES 13 A 334 VAL TYR GLU TRP THR ARG GLU PRO ALA ARG SER VAL VAL SEQRES 14 A 334 VAL ALA GLU ASP GLY SER ARG LEU ASN GLN TYR ASP LEU SEQRES 15 A 334 LEU GLY GLN THR VAL ASP SER GLY ILE VAL GLN SER SER SEQRES 16 A 334 THR GLY GLU TYR VAL VAL MET THR THR HIS PHE HIS LEU SEQRES 17 A 334 LYS ARG LYS ILE GLY TYR PHE VAL ILE GLN THR TYR LEU SEQRES 18 A 334 PRO CYS ILE MET THR VAL ILE LEU SER GLN VAL SER PHE SEQRES 19 A 334 TRP LEU ASN ARG GLU SER VAL PRO ALA ARG THR VAL PHE SEQRES 20 A 334 GLY VAL THR THR VAL LEU THR MET THR THR LEU SER ILE SEQRES 21 A 334 SER ALA ARG ASN SER LEU PRO LYS VAL ALA TYR ALA THR SEQRES 22 A 334 ALA MET ASP TRP PHE ILE ALA VAL CYS TYR ALA PHE VAL SEQRES 23 A 334 PHE SER ALA LEU ILE GLU PHE ALA THR VAL ASN TYR PHE SEQRES 24 A 334 THR LYS SER GLN PRO ALA ARG ALA ALA LYS ILE ASP ARG SEQRES 25 A 334 LEU SER ARG ILE ALA PHE PRO LEU LEU PHE GLY ILE PHE SEQRES 26 A 334 ASN LEU VAL TYR TRP ALA THR TYR LEU SEQRES 1 B 330 ASN MET SER PHE VAL LYS GLU THR VAL ASP LYS LEU LEU SEQRES 2 B 330 LYS GLY TYR ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY SEQRES 3 B 330 PRO PRO VAL CYS VAL GLY MET ASN ILE ASP ILE ALA SER SEQRES 4 B 330 ILE ASP MET VAL SER GLU VAL ASN MET ASP TYR THR LEU SEQRES 5 B 330 THR MET TYR PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU SEQRES 6 B 330 ALA TYR SER GLY ILE PRO LEU ASN LEU THR LEU ASP ASN SEQRES 7 B 330 ARG VAL ALA ASP GLN LEU TRP VAL PRO ASP THR TYR PHE SEQRES 8 B 330 LEU ASN ASP LYS LYS SER PHE VAL HIS GLY VAL THR VAL SEQRES 9 B 330 LYS ASN ARG MET ILE ARG LEU HIS PRO ASP GLY THR VAL SEQRES 10 B 330 LEU TYR GLY LEU ARG ILE THR THR THR ALA ALA CYS MET SEQRES 11 B 330 MET ASP LEU ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS SEQRES 12 B 330 THR LEU GLU ILE GLU SER TYR GLY TYR THR THR ASP ASP SEQRES 13 B 330 ILE GLU PHE TYR TRP ARG GLY GLY ASP LYS ALA VAL THR SEQRES 14 B 330 GLY VAL GLU ARG ILE GLU LEU PRO GLN PHE SER ILE VAL SEQRES 15 B 330 GLU HIS ARG LEU VAL SER ARG ASN VAL VAL PHE ALA THR SEQRES 16 B 330 GLY ALA TYR PRO ARG LEU SER LEU SER PHE ARG LEU LYS SEQRES 17 B 330 ARG ASN ILE GLY TYR PHE ILE LEU GLN THR TYR MET PRO SEQRES 18 B 330 SER ILE LEU ILE THR ILE LEU SER TRP VAL SER PHE TRP SEQRES 19 B 330 ILE ASN TYR ASP ALA SER ALA ALA ARG VAL ALA LEU GLY SEQRES 20 B 330 ILE THR THR VAL LEU THR MET THR THR ILE ASN THR HIS SEQRES 21 B 330 LEU ARG GLU THR LEU PRO LYS ILE PRO TYR VAL LYS ALA SEQRES 22 B 330 ILE ASP MET TYR LEU MET GLY CYS PHE VAL PHE VAL PHE SEQRES 23 B 330 LEU ALA LEU LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE SEQRES 24 B 330 PHE SER ARG ALA ALA ALA ILE ASP ARG TRP SER ARG ILE SEQRES 25 B 330 VAL PHE PRO PHE THR PHE SER LEU PHE ASN LEU VAL TYR SEQRES 26 B 330 TRP LEU TYR TYR VAL SEQRES 1 C 330 ASN MET SER PHE VAL LYS GLU THR VAL ASP LYS LEU LEU SEQRES 2 C 330 LYS GLY TYR ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY SEQRES 3 C 330 PRO PRO VAL CYS VAL GLY MET ASN ILE ASP ILE ALA SER SEQRES 4 C 330 ILE ASP MET VAL SER GLU VAL ASN MET ASP TYR THR LEU SEQRES 5 C 330 THR MET TYR PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU SEQRES 6 C 330 ALA TYR SER GLY ILE PRO LEU ASN LEU THR LEU ASP ASN SEQRES 7 C 330 ARG VAL ALA ASP GLN LEU TRP VAL PRO ASP THR TYR PHE SEQRES 8 C 330 LEU ASN ASP LYS LYS SER PHE VAL HIS GLY VAL THR VAL SEQRES 9 C 330 LYS ASN ARG MET ILE ARG LEU HIS PRO ASP GLY THR VAL SEQRES 10 C 330 LEU TYR GLY LEU ARG ILE THR THR THR ALA ALA CYS MET SEQRES 11 C 330 MET ASP LEU ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS SEQRES 12 C 330 THR LEU GLU ILE GLU SER TYR GLY TYR THR THR ASP ASP SEQRES 13 C 330 ILE GLU PHE TYR TRP ARG GLY GLY ASP LYS ALA VAL THR SEQRES 14 C 330 GLY VAL GLU ARG ILE GLU LEU PRO GLN PHE SER ILE VAL SEQRES 15 C 330 GLU HIS ARG LEU VAL SER ARG ASN VAL VAL PHE ALA THR SEQRES 16 C 330 GLY ALA TYR PRO ARG LEU SER LEU SER PHE ARG LEU LYS SEQRES 17 C 330 ARG ASN ILE GLY TYR PHE ILE LEU GLN THR TYR MET PRO SEQRES 18 C 330 SER ILE LEU ILE THR ILE LEU SER TRP VAL SER PHE TRP SEQRES 19 C 330 ILE ASN TYR ASP ALA SER ALA ALA ARG VAL ALA LEU GLY SEQRES 20 C 330 ILE THR THR VAL LEU THR MET THR THR ILE ASN THR HIS SEQRES 21 C 330 LEU ARG GLU THR LEU PRO LYS ILE PRO TYR VAL LYS ALA SEQRES 22 C 330 ILE ASP MET TYR LEU MET GLY CYS PHE VAL PHE VAL PHE SEQRES 23 C 330 LEU ALA LEU LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE SEQRES 24 C 330 PHE SER ARG ALA ALA ALA ILE ASP ARG TRP SER ARG ILE SEQRES 25 C 330 VAL PHE PRO PHE THR PHE SER LEU PHE ASN LEU VAL TYR SEQRES 26 C 330 TRP LEU TYR TYR VAL SEQRES 1 E 330 ASN MET SER PHE VAL LYS GLU THR VAL ASP LYS LEU LEU SEQRES 2 E 330 LYS GLY TYR ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY SEQRES 3 E 330 PRO PRO VAL CYS VAL GLY MET ASN ILE ASP ILE ALA SER SEQRES 4 E 330 ILE ASP MET VAL SER GLU VAL ASN MET ASP TYR THR LEU SEQRES 5 E 330 THR MET TYR PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU SEQRES 6 E 330 ALA TYR SER GLY ILE PRO LEU ASN LEU THR LEU ASP ASN SEQRES 7 E 330 ARG VAL ALA ASP GLN LEU TRP VAL PRO ASP THR TYR PHE SEQRES 8 E 330 LEU ASN ASP LYS LYS SER PHE VAL HIS GLY VAL THR VAL SEQRES 9 E 330 LYS ASN ARG MET ILE ARG LEU HIS PRO ASP GLY THR VAL SEQRES 10 E 330 LEU TYR GLY LEU ARG ILE THR THR THR ALA ALA CYS MET SEQRES 11 E 330 MET ASP LEU ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS SEQRES 12 E 330 THR LEU GLU ILE GLU SER TYR GLY TYR THR THR ASP ASP SEQRES 13 E 330 ILE GLU PHE TYR TRP ARG GLY GLY ASP LYS ALA VAL THR SEQRES 14 E 330 GLY VAL GLU ARG ILE GLU LEU PRO GLN PHE SER ILE VAL SEQRES 15 E 330 GLU HIS ARG LEU VAL SER ARG ASN VAL VAL PHE ALA THR SEQRES 16 E 330 GLY ALA TYR PRO ARG LEU SER LEU SER PHE ARG LEU LYS SEQRES 17 E 330 ARG ASN ILE GLY TYR PHE ILE LEU GLN THR TYR MET PRO SEQRES 18 E 330 SER ILE LEU ILE THR ILE LEU SER TRP VAL SER PHE TRP SEQRES 19 E 330 ILE ASN TYR ASP ALA SER ALA ALA ARG VAL ALA LEU GLY SEQRES 20 E 330 ILE THR THR VAL LEU THR MET THR THR ILE ASN THR HIS SEQRES 21 E 330 LEU ARG GLU THR LEU PRO LYS ILE PRO TYR VAL LYS ALA SEQRES 22 E 330 ILE ASP MET TYR LEU MET GLY CYS PHE VAL PHE VAL PHE SEQRES 23 E 330 LEU ALA LEU LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE SEQRES 24 E 330 PHE SER ARG ALA ALA ALA ILE ASP ARG TRP SER ARG ILE SEQRES 25 E 330 VAL PHE PRO PHE THR PHE SER LEU PHE ASN LEU VAL TYR SEQRES 26 E 330 TRP LEU TYR TYR VAL SEQRES 1 D 336 THR THR VAL PHE THR ARG ILE LEU ASP ARG LEU LEU ASP SEQRES 2 D 336 GLY TYR ASP ASN ARG LEU ARG PRO GLY LEU GLY GLU ARG SEQRES 3 D 336 VAL THR GLU VAL LYS THR ASP ILE PHE VAL THR SER PHE SEQRES 4 D 336 GLY PRO VAL SER ASP HIS ASP MET GLU TYR THR ILE ASP SEQRES 5 D 336 VAL PHE PHE ARG GLN SER TRP LYS ASP GLU ARG LEU LYS SEQRES 6 D 336 PHE LYS GLY PRO MET THR VAL LEU ARG LEU ASN ASN LEU SEQRES 7 D 336 MET ALA SER LYS ILE TRP THR PRO ASP THR PHE PHE HIS SEQRES 8 D 336 ASN GLY LYS LYS SER VAL ALA HIS ASN MET THR MET PRO SEQRES 9 D 336 ASN LYS LEU LEU ARG ILE THR GLU ASP GLY THR LEU LEU SEQRES 10 D 336 TYR THR MET ARG LEU THR VAL ARG ALA GLU CYS PRO MET SEQRES 11 D 336 HIS LEU GLU ASP PHE PRO MET ASP ALA HIS ALA CYS PRO SEQRES 12 D 336 LEU LYS PHE GLY SER TYR ALA TYR THR ARG ALA GLU VAL SEQRES 13 D 336 VAL TYR GLU TRP THR ARG GLU PRO ALA ARG SER VAL VAL SEQRES 14 D 336 VAL ALA GLU ASP GLY SER ARG LEU ASN GLN TYR ASP LEU SEQRES 15 D 336 LEU GLY GLN THR VAL ASP SER GLY ILE VAL GLN SER SER SEQRES 16 D 336 THR GLY GLU TYR VAL VAL MET THR THR HIS PHE HIS LEU SEQRES 17 D 336 LYS ARG LYS ILE GLY TYR PHE VAL ILE GLN THR TYR LEU SEQRES 18 D 336 PRO CYS ILE MET THR VAL ILE LEU SER GLN VAL SER PHE SEQRES 19 D 336 TRP LEU ASN ARG GLU SER VAL PRO ALA ARG THR VAL PHE SEQRES 20 D 336 GLY VAL THR THR VAL LEU THR MET THR THR LEU SER ILE SEQRES 21 D 336 SER ALA ARG ASN SER LEU PRO LYS VAL ALA TYR ALA THR SEQRES 22 D 336 ALA MET ASP TRP PHE ILE ALA VAL CYS TYR ALA PHE VAL SEQRES 23 D 336 PHE SER ALA LEU ILE GLU PHE ALA THR VAL ASN TYR PHE SEQRES 24 D 336 THR LYS SER GLN PRO ALA ARG ALA ALA LYS ILE ASP ARG SEQRES 25 D 336 LEU SER ARG ILE ALA PHE PRO LEU LEU PHE GLY ILE PHE SEQRES 26 D 336 ASN LEU VAL TYR TRP ALA THR TYR LEU ASN ARG SEQRES 1 K 71 ILE ARG CYS PHE ILE THR PRO ASP ILE THR SER LYS ASP SEQRES 2 K 71 CYS PRO ASN GLY HIS VAL CYS TYR THR LYS THR TRP CYS SEQRES 3 K 71 ASP ALA PHE CYS SER ILE ARG GLY LYS ARG VAL ASP LEU SEQRES 4 K 71 GLY CYS ALA ALA THR CYS PRO THR VAL LYS THR GLY VAL SEQRES 5 K 71 ASP ILE GLN CYS CYS SER THR ASP ASN CYS ASN PRO PHE SEQRES 6 K 71 PRO THR ARG LYS ARG PRO SEQRES 1 L 67 ILE ARG CYS PHE ILE THR PRO ASP ILE THR SER LYS ASP SEQRES 2 L 67 CYS PRO ASN GLY HIS VAL CYS TYR THR LYS THR TRP CYS SEQRES 3 L 67 ASP ALA PHE CYS SER ILE ARG GLY LYS ARG VAL ASP LEU SEQRES 4 L 67 GLY CYS ALA ALA THR CYS PRO THR VAL LYS THR GLY VAL SEQRES 5 L 67 ASP ILE GLN CYS CYS SER THR ASP ASN CYS ASN PRO PHE SEQRES 6 L 67 PRO THR HET NAG A 501 14 HET HSM B 601 8 HET ZN B 602 1 HET NAG C 501 14 HET NAG E 501 14 HET NAG D 501 14 HET HEX D 502 6 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 MAN G 7 11 HET NAG H 1 14 HET NAG H 2 14 HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET MAN I 4 11 HET MAN I 5 11 HET MAN I 6 11 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET MAN J 4 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM HSM HISTAMINE HETNAM ZN ZINC ION HETNAM HEX HEXANE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 9 NAG 12(C8 H15 N O6) FORMUL 10 HSM C5 H9 N3 FORMUL 11 ZN ZN 2+ FORMUL 15 HEX C6 H14 FORMUL 16 BMA 3(C6 H12 O6) FORMUL 16 MAN 8(C6 H12 O6) HELIX 1 AA1 HIS F 27 TYR F 31 5 5 HELIX 2 AA2 ALA F 61 LYS F 65 5 5 HELIX 3 AA3 LYS F 87 THR F 91 5 5 HELIX 4 AA4 TYR F 108 TYR F 112 5 5 HELIX 5 AA5 THR A 13 LEU A 23 1 11 HELIX 6 AA6 GLU A 73 LYS A 76 5 4 HELIX 7 AA7 ASN A 87 SER A 92 1 6 HELIX 8 AA8 HIS A 142 PHE A 146 5 5 HELIX 9 AA9 GLU A 174 VAL A 179 1 6 HELIX 10 AB1 ILE A 223 ASN A 248 1 26 HELIX 11 AB2 SER A 251 LEU A 277 1 27 HELIX 12 AB3 MET A 286 PHE A 310 1 25 HELIX 13 AB4 GLN A 314 TYR A 415 1 31 HELIX 14 AB5 MET B 9 LYS B 21 1 13 HELIX 15 AB6 LYS B 70 ALA B 73 5 4 HELIX 16 AB7 ASP B 84 LEU B 91 5 8 HELIX 17 AB8 GLY B 170 LYS B 173 5 4 HELIX 18 AB9 TYR B 220 ILE B 242 1 23 HELIX 19 AC1 ALA B 246 LEU B 272 1 27 HELIX 20 AC2 LYS B 279 SER B 308 1 30 HELIX 21 AC3 ALA B 420 TYR B 446 1 27 HELIX 22 AC4 MET C 9 LYS C 21 1 13 HELIX 23 AC5 LYS C 70 ALA C 73 5 4 HELIX 24 AC6 ASP C 84 LEU C 91 5 8 HELIX 25 AC7 GLY C 170 LYS C 173 5 4 HELIX 26 AC8 THR C 225 ILE C 242 1 18 HELIX 27 AC9 ALA C 246 LEU C 272 1 27 HELIX 28 AD1 LYS C 279 SER C 308 1 30 HELIX 29 AD2 ALA C 420 TYR C 446 1 27 HELIX 30 AD3 MET E 9 LYS E 21 1 13 HELIX 31 AD4 LYS E 70 ALA E 73 5 4 HELIX 32 AD5 ASP E 84 LEU E 91 5 8 HELIX 33 AD6 GLY E 170 LYS E 173 5 4 HELIX 34 AD7 TYR E 220 SER E 239 1 20 HELIX 35 AD8 PHE E 240 ILE E 242 5 3 HELIX 36 AD9 ALA E 246 LEU E 272 1 27 HELIX 37 AE1 LYS E 279 SER E 308 1 30 HELIX 38 AE2 ALA E 420 TYR E 446 1 27 HELIX 39 AE3 THR D 13 LEU D 23 1 11 HELIX 40 AE4 GLU D 73 LYS D 76 5 4 HELIX 41 AE5 ASN D 87 LYS D 93 1 7 HELIX 42 AE6 HIS D 142 PHE D 146 5 5 HELIX 43 AE7 GLU D 174 VAL D 179 1 6 HELIX 44 AE8 ILE D 223 THR D 230 1 8 HELIX 45 AE9 THR D 230 SER D 244 1 15 HELIX 46 AF1 SER D 251 LEU D 277 1 27 HELIX 47 AF2 THR D 284 PHE D 310 1 27 HELIX 48 AF3 GLN D 314 ARG D 418 1 34 HELIX 49 AF4 PRO K 66 ARG K 70 5 5 SHEET 1 AA1 4 GLN F 5 SER F 7 0 SHEET 2 AA1 4 ARG F 19 ALA F 23 -1 O ALA F 23 N GLN F 5 SHEET 3 AA1 4 THR F 78 MET F 83 -1 O LEU F 81 N LEU F 20 SHEET 4 AA1 4 PHE F 68 ASP F 73 -1 N THR F 69 O GLU F 82 SHEET 1 AA2 6 ILE F 33 GLN F 39 0 SHEET 2 AA2 6 VAL F 48 SER F 52 -1 O ILE F 51 N MET F 34 SHEET 3 AA2 6 THR F 58 SER F 59 -1 O SER F 59 N ALA F 50 SHEET 4 AA2 6 ALA F 92 LYS F 99 -1 O ALA F 97 N GLY F 35 SHEET 5 AA2 6 TYR F 114 TRP F 115 -1 O TYR F 114 N ALA F 98 SHEET 6 AA2 6 THR F 119 VAL F 121 -1 O VAL F 121 N ALA F 92 SHEET 1 AA3 8 THR A 39 SER A 54 0 SHEET 2 AA3 8 GLU A 59 LYS A 71 -1 O SER A 69 N LYS A 42 SHEET 3 AA3 8 LEU A 84 LEU A 86 0 SHEET 4 AA3 8 VAL A 108 ALA A 109 0 SHEET 5 AA3 8 LYS A 117 ILE A 121 -1 O ILE A 121 N LEU A 84 SHEET 6 AA3 8 THR A 126 GLU A 138 -1 O LEU A 128 N ARG A 120 SHEET 7 AA3 8 VAL A 167 TRP A 171 1 O GLU A 170 N THR A 43 SHEET 8 AA3 8 VAL A 180 VAL A 181 1 O VAL A 180 N VAL A 47 SHEET 1 AA4 4 THR A 99 PHE A 101 0 SHEET 2 AA4 4 ALA A 150 SER A 159 -1 O GLY A 158 N PHE A 100 SHEET 3 AA4 4 GLU A 209 ARG A 221 -1 O MET A 213 N PHE A 157 SHEET 4 AA4 4 TYR A 191 GLN A 204 -1 N LEU A 194 O HIS A 218 SHEET 1 AA5 7 VAL B 36 SER B 51 0 SHEET 2 AA5 7 ASP B 56 ARG B 68 -1 O GLN B 64 N ASN B 41 SHEET 3 AA5 7 THR B 82 LEU B 83 0 SHEET 4 AA5 7 ARG B 114 LEU B 118 -1 O ILE B 116 N LEU B 83 SHEET 5 AA5 7 THR B 123 ALA B 135 -1 O GLY B 127 N MET B 115 SHEET 6 AA5 7 ILE B 164 TRP B 168 1 O GLU B 165 N VAL B 38 SHEET 7 AA5 7 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 LYS B 215 -1 O LEU B 208 N ILE B 154 SHEET 4 AA6 4 SER B 187 VAL B 199 -1 N ARG B 196 O ARG B 207 SHEET 1 AA7 8 VAL C 36 SER C 51 0 SHEET 2 AA7 8 ASP C 56 ARG C 68 -1 O TYR C 62 N ASP C 43 SHEET 3 AA7 8 THR C 82 LEU C 83 0 SHEET 4 AA7 8 PHE C 105 VAL C 106 0 SHEET 5 AA7 8 ARG C 114 LEU C 118 -1 O ILE C 116 N LEU C 83 SHEET 6 AA7 8 THR C 123 ALA C 135 -1 O GLY C 127 N MET C 115 SHEET 7 AA7 8 ILE C 164 TRP C 168 1 O GLU C 165 N VAL C 38 SHEET 8 AA7 8 VAL C 175 THR C 176 1 O THR C 176 N ILE C 44 SHEET 1 AA8 4 THR C 96 PHE C 98 0 SHEET 2 AA8 4 GLU C 147 SER C 156 -1 O GLU C 155 N TYR C 97 SHEET 3 AA8 4 ALA C 204 LYS C 215 -1 O PHE C 212 N CYS C 150 SHEET 4 AA8 4 SER C 187 VAL C 199 -1 N ARG C 196 O ARG C 207 SHEET 1 AA9 8 VAL E 36 SER E 51 0 SHEET 2 AA9 8 ASP E 56 ARG E 68 -1 O TYR E 66 N GLY E 39 SHEET 3 AA9 8 LEU E 81 LEU E 83 0 SHEET 4 AA9 8 ASP E 101 VAL E 106 0 SHEET 5 AA9 8 ARG E 114 LEU E 118 -1 O LEU E 118 N LEU E 81 SHEET 6 AA9 8 THR E 123 ALA E 135 -1 O GLY E 127 N MET E 115 SHEET 7 AA9 8 ILE E 164 TRP E 168 1 O GLU E 165 N VAL E 38 SHEET 8 AA9 8 VAL E 175 THR E 176 1 O THR E 176 N ILE E 44 SHEET 1 AB1 4 THR E 96 PHE E 98 0 SHEET 2 AB1 4 GLU E 147 SER E 156 -1 O GLU E 155 N TYR E 97 SHEET 3 AB1 4 ALA E 204 ARG E 216 -1 O PHE E 212 N CYS E 150 SHEET 4 AB1 4 PHE E 186 VAL E 199 -1 N VAL E 198 O TYR E 205 SHEET 1 AB2 9 THR D 39 VAL D 47 0 SHEET 2 AB2 9 VAL D 53 SER D 54 0 SHEET 3 AB2 9 GLU D 59 LYS D 71 -1 O GLU D 59 N SER D 54 SHEET 4 AB2 9 VAL D 83 LEU D 86 0 SHEET 5 AB2 9 VAL D 108 ALA D 109 0 SHEET 6 AB2 9 LYS D 117 THR D 122 -1 O ILE D 121 N LEU D 84 SHEET 7 AB2 9 THR D 126 GLU D 138 -1 O THR D 130 N LEU D 118 SHEET 8 AB2 9 VAL D 167 TRP D 171 1 O GLU D 170 N THR D 43 SHEET 9 AB2 9 VAL D 180 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 LEU D 155 SER D 159 -1 O GLY D 158 N PHE D 100 SHEET 3 AB3 4 TYR D 210 HIS D 218 -1 O MET D 213 N PHE D 157 SHEET 4 AB3 4 GLY D 195 VAL D 203 -1 N GLY D 201 O VAL D 212 SHEET 1 AB4 2 VAL L 19 TRP L 25 0 SHEET 2 AB4 2 ARG L 36 ALA L 42 -1 O ARG L 36 N TRP L 25 SSBOND 1 CYS F 22 CYS F 96 1555 1555 2.04 SSBOND 2 CYS A 139 CYS A 153 1555 1555 2.03 SSBOND 3 CYS B 136 CYS B 150 1555 1555 2.04 SSBOND 4 CYS C 136 CYS C 150 1555 1555 2.03 SSBOND 5 CYS E 136 CYS E 150 1555 1555 2.03 SSBOND 6 CYS D 139 CYS D 153 1555 1555 2.04 SSBOND 7 CYS K 3 CYS K 20 1555 1555 2.03 SSBOND 8 CYS K 3 CYS K 62 1555 1555 2.05 SSBOND 9 CYS K 14 CYS K 41 1555 1555 2.03 SSBOND 10 CYS K 20 CYS K 57 1555 1555 2.06 SSBOND 11 CYS K 20 CYS K 62 1555 1555 2.02 SSBOND 12 CYS K 26 CYS K 30 1555 1555 2.04 SSBOND 13 CYS K 45 CYS K 56 1555 1555 2.04 SSBOND 14 CYS K 57 CYS K 62 1555 1555 2.03 SSBOND 15 CYS L 3 CYS L 20 1555 1555 2.03 SSBOND 16 CYS L 14 CYS L 41 1555 1555 2.04 SSBOND 17 CYS L 20 CYS L 57 1555 1555 2.05 SSBOND 18 CYS L 20 CYS L 62 1555 1555 2.03 SSBOND 19 CYS L 26 CYS L 30 1555 1555 2.03 SSBOND 20 CYS L 45 CYS L 56 1555 1555 2.03 SSBOND 21 CYS L 57 CYS L 62 1555 1555 2.02 LINK ND2 ASN B 80 C1 NAG H 1 1555 1555 1.49 LINK ND2 ASN B 149 C1 NAG G 1 1555 1555 1.48 LINK ND2 ASN C 80 C1 NAG C 501 1555 1555 1.45 LINK ND2 ASN C 149 C1 NAG I 1 1555 1555 1.52 LINK ND2 ASN E 80 C1 NAG E 501 1555 1555 1.45 LINK ND2 ASN E 149 C1 NAG J 1 1555 1555 1.48 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.43 LINK O6 BMA G 3 C1 MAN G 4 1555 1555 1.45 LINK O3 BMA G 3 C1 MAN G 7 1555 1555 1.43 LINK O3 MAN G 4 C1 MAN G 5 1555 1555 1.44 LINK O6 MAN G 4 C1 MAN G 6 1555 1555 1.45 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.46 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.41 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.43 LINK O6 BMA I 3 C1 MAN I 4 1555 1555 1.44 LINK O3 BMA I 3 C1 MAN I 6 1555 1555 1.43 LINK O3 MAN I 4 C1 MAN I 5 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.43 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.43 LINK O6 BMA J 3 C1 MAN J 4 1555 1555 1.45 LINK NE2 HIS B 267 ZN ZN B 602 1555 1555 2.27 LINK ZN ZN B 602 NE2 HIS C 267 1555 1555 2.54 LINK ZN ZN B 602 NE2 HIS E 267 1555 1555 2.40 CISPEP 1 PHE A 146 PRO A 147 0 -5.19 CISPEP 2 TYR B 143 PRO B 144 0 1.25 CISPEP 3 TYR C 143 PRO C 144 0 0.64 CISPEP 4 TYR E 143 PRO E 144 0 3.94 CISPEP 5 PHE D 146 PRO D 147 0 -1.21 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