HEADER MEMBRANE PROTEIN 02-AUG-21 7PBD TITLE A1B3 GABA-A RECEPTOR + GABA CAVEAT 7PBD MAN H 5 HAS WRONG CHIRALITY AT ATOM C1 BMA I 3 HAS WRONG CAVEAT 2 7PBD CHIRALITY AT ATOM C1 NAG J 2 HAS WRONG CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GABA(A) RECEPTOR SUBUNIT ALPHA-1; COMPND 3 CHAIN: A, D; COMPND 4 SYNONYM: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT BETA-3,GAMMA- COMPND 8 AMINOBUTYRIC ACID RECEPTOR SUBUNIT BETA-3; COMPND 9 CHAIN: B, C, E; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: MEGABODY 25; COMPND 13 CHAIN: F; COMPND 14 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_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: GABRB3; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 19 ORGANISM_TAXID: 9844; SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS PLGIC GABA NEUROTRANSMISSION, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR P.S.MILLER,V.B.KASARAGOD 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. 3.04 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) : 3.040 REMARK 3 NUMBER OF PARTICLES : 139537 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 7PBD 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_1292116250. 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 - MEGABODY 25 REMARK 245 COMPLEX; GABA-A RECEPTOR; REMARK 245 MEGABODY 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 K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 54.70 REMARK 245 ILLUMINATION MODE : SPOT SCAN REMARK 245 NOMINAL MAGNIFICATION : 130000 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, D, F, G, H, I, J, REMARK 350 AND CHAINS: K REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLN B 1 REMARK 465 SER B 2 REMARK 465 VAL B 3 REMARK 465 ASN B 4 REMARK 465 ASP B 5 REMARK 465 PRO B 6 REMARK 465 GLY B 7 REMARK 465 GLN B 308A REMARK 465 PRO B 308B REMARK 465 ALA B 308C REMARK 465 GLY B 308D REMARK 465 THR B 308E REMARK 465 ALA B 308F REMARK 465 ASP B 308G REMARK 465 LEU B 308H REMARK 465 GLU B 308I REMARK 465 ASP B 308J REMARK 465 ASN B 308K REMARK 465 TRP B 308L REMARK 465 GLU B 308M REMARK 465 THR B 308N REMARK 465 LEU B 308O REMARK 465 ASN B 308P REMARK 465 ASP B 308Q REMARK 465 ASN B 308R REMARK 465 LEU B 308S REMARK 465 LYS B 308T REMARK 465 VAL B 308U REMARK 465 ILE B 308V REMARK 465 GLU B 308W REMARK 465 LYS B 308X REMARK 465 ALA B 308Y REMARK 465 ASP B 308Z REMARK 465 ASN B 309A REMARK 465 ALA B 309B REMARK 465 ALA B 309C REMARK 465 GLN B 309D REMARK 465 VAL B 309E REMARK 465 LYS B 309F REMARK 465 ASP B 309G REMARK 465 ALA B 309H REMARK 465 LEU B 309I REMARK 465 THR B 309J REMARK 465 LYS B 309K REMARK 465 MET B 309L REMARK 465 ARG B 309M REMARK 465 ALA B 309N REMARK 465 ALA B 309O REMARK 465 ALA B 309P REMARK 465 LEU B 309Q REMARK 465 ASP B 309R REMARK 465 ALA B 309S REMARK 465 GLN B 309T REMARK 465 LYS B 309U REMARK 465 ALA B 309V REMARK 465 THR B 309W REMARK 465 PRO B 309X REMARK 465 PRO B 309Y REMARK 465 LYS B 309Z REMARK 465 LEU B 310A REMARK 465 GLU B 310B REMARK 465 ASP B 310C REMARK 465 LYS B 310D REMARK 465 SER B 310E REMARK 465 PRO B 310F REMARK 465 ASP B 310G REMARK 465 SER B 310H REMARK 465 PRO B 310I REMARK 465 GLU B 310J REMARK 465 MET B 310K REMARK 465 LYS B 310L REMARK 465 ASP B 310M REMARK 465 PHE B 310N REMARK 465 ARG B 310O REMARK 465 HIS B 310P REMARK 465 GLY B 310Q REMARK 465 PHE B 310R REMARK 465 ASP B 310S REMARK 465 ILE B 310T REMARK 465 LEU B 310U REMARK 465 VAL B 310V REMARK 465 GLY B 310W REMARK 465 GLN B 310X REMARK 465 ILE B 310Y REMARK 465 ASP B 310Z REMARK 465 ASP B 311A REMARK 465 ALA B 311B REMARK 465 LEU B 311C REMARK 465 LYS B 311D REMARK 465 LEU B 311E REMARK 465 ALA B 311F REMARK 465 ASN B 311G REMARK 465 GLU B 311H REMARK 465 GLY B 311I REMARK 465 LYS B 311J REMARK 465 VAL B 311K REMARK 465 LYS B 311L REMARK 465 GLU B 311M REMARK 465 ALA B 311N REMARK 465 GLN B 311O REMARK 465 ALA B 311P REMARK 465 ALA B 311Q REMARK 465 ALA B 311R REMARK 465 GLU B 311S REMARK 465 GLN B 311T REMARK 465 LEU B 311U REMARK 465 LYS B 311V REMARK 465 THR B 311W REMARK 465 THR B 311X REMARK 465 ARG B 311Y REMARK 465 ASN B 311Z REMARK 465 ALA B 312A REMARK 465 TYR B 312B REMARK 465 ILE B 312C REMARK 465 GLN B 312D REMARK 465 ASN B 448 REMARK 465 GLN C 1 REMARK 465 SER C 2 REMARK 465 VAL C 3 REMARK 465 ASN C 4 REMARK 465 ASP C 5 REMARK 465 PRO C 6 REMARK 465 GLY C 7 REMARK 465 GLN C 308A REMARK 465 PRO C 308B REMARK 465 ALA C 308C REMARK 465 GLY C 308D REMARK 465 THR C 308E REMARK 465 ALA C 308F REMARK 465 ASP C 308G REMARK 465 LEU C 308H REMARK 465 GLU C 308I REMARK 465 ASP C 308J REMARK 465 ASN C 308K REMARK 465 TRP C 308L REMARK 465 GLU C 308M REMARK 465 THR C 308N REMARK 465 LEU C 308O REMARK 465 ASN C 308P REMARK 465 ASP C 308Q REMARK 465 ASN C 308R REMARK 465 LEU C 308S REMARK 465 LYS C 308T REMARK 465 VAL C 308U REMARK 465 ILE C 308V REMARK 465 GLU C 308W REMARK 465 LYS C 308X REMARK 465 ALA C 308Y REMARK 465 ASP C 308Z REMARK 465 ASN C 309A REMARK 465 ALA C 309B REMARK 465 ALA C 309C REMARK 465 GLN C 309D REMARK 465 VAL C 309E REMARK 465 LYS C 309F REMARK 465 ASP C 309G REMARK 465 ALA C 309H REMARK 465 LEU C 309I REMARK 465 THR C 309J REMARK 465 LYS C 309K REMARK 465 MET C 309L REMARK 465 ARG C 309M REMARK 465 ALA C 309N REMARK 465 ALA C 309O REMARK 465 ALA C 309P REMARK 465 LEU C 309Q REMARK 465 ASP C 309R REMARK 465 ALA C 309S REMARK 465 GLN C 309T REMARK 465 LYS C 309U REMARK 465 ALA C 309V REMARK 465 THR C 309W REMARK 465 PRO C 309X REMARK 465 PRO C 309Y REMARK 465 LYS C 309Z REMARK 465 LEU C 310A REMARK 465 GLU C 310B REMARK 465 ASP C 310C REMARK 465 LYS C 310D REMARK 465 SER C 310E REMARK 465 PRO C 310F REMARK 465 ASP C 310G REMARK 465 SER C 310H REMARK 465 PRO C 310I REMARK 465 GLU C 310J REMARK 465 MET C 310K REMARK 465 LYS C 310L REMARK 465 ASP C 310M REMARK 465 PHE C 310N REMARK 465 ARG C 310O REMARK 465 HIS C 310P REMARK 465 GLY C 310Q REMARK 465 PHE C 310R REMARK 465 ASP C 310S REMARK 465 ILE C 310T REMARK 465 LEU C 310U REMARK 465 VAL C 310V REMARK 465 GLY C 310W REMARK 465 GLN C 310X REMARK 465 ILE C 310Y REMARK 465 ASP C 310Z REMARK 465 ASP C 311A REMARK 465 ALA C 311B REMARK 465 LEU C 311C REMARK 465 LYS C 311D REMARK 465 LEU C 311E REMARK 465 ALA C 311F REMARK 465 ASN C 311G REMARK 465 GLU C 311H REMARK 465 GLY C 311I REMARK 465 LYS C 311J REMARK 465 VAL C 311K REMARK 465 LYS C 311L REMARK 465 GLU C 311M REMARK 465 ALA C 311N REMARK 465 GLN C 311O REMARK 465 ALA C 311P REMARK 465 ALA C 311Q REMARK 465 ALA C 311R REMARK 465 GLU C 311S REMARK 465 GLN C 311T REMARK 465 LEU C 311U REMARK 465 LYS C 311V REMARK 465 THR C 311W REMARK 465 THR C 311X REMARK 465 ARG C 311Y REMARK 465 ASN C 311Z REMARK 465 ALA C 312A REMARK 465 TYR C 312B REMARK 465 ILE C 312C REMARK 465 GLN C 312D REMARK 465 LYS C 312E REMARK 465 TYR C 312F REMARK 465 LEU C 312G REMARK 465 THR C 312H REMARK 465 GLY C 312I REMARK 465 ASN C 448 REMARK 465 GLN E 1 REMARK 465 SER E 2 REMARK 465 VAL E 3 REMARK 465 ASN E 4 REMARK 465 ASP E 5 REMARK 465 PRO E 6 REMARK 465 GLY E 7 REMARK 465 GLN E 308A REMARK 465 PRO E 308B REMARK 465 ALA E 308C REMARK 465 GLY E 308D REMARK 465 THR E 308E REMARK 465 ALA E 308F REMARK 465 ASP E 308G REMARK 465 LEU E 308H REMARK 465 GLU E 308I REMARK 465 ASP E 308J REMARK 465 ASN E 308K REMARK 465 TRP E 308L REMARK 465 GLU E 308M REMARK 465 THR E 308N REMARK 465 LEU E 308O REMARK 465 ASN E 308P REMARK 465 ASP E 308Q REMARK 465 ASN E 308R REMARK 465 LEU E 308S REMARK 465 LYS E 308T REMARK 465 VAL E 308U REMARK 465 ILE E 308V REMARK 465 GLU E 308W REMARK 465 LYS E 308X REMARK 465 ALA E 308Y REMARK 465 ASP E 308Z REMARK 465 ASN E 309A REMARK 465 ALA E 309B REMARK 465 ALA E 309C REMARK 465 GLN E 309D REMARK 465 VAL E 309E REMARK 465 LYS E 309F REMARK 465 ASP E 309G REMARK 465 ALA E 309H REMARK 465 LEU E 309I REMARK 465 THR E 309J REMARK 465 LYS E 309K REMARK 465 MET E 309L REMARK 465 ARG E 309M REMARK 465 ALA E 309N REMARK 465 ALA E 309O REMARK 465 ALA E 309P REMARK 465 LEU E 309Q REMARK 465 ASP E 309R REMARK 465 ALA E 309S REMARK 465 GLN E 309T REMARK 465 LYS E 309U REMARK 465 ALA E 309V REMARK 465 THR E 309W REMARK 465 PRO E 309X REMARK 465 PRO E 309Y REMARK 465 LYS E 309Z REMARK 465 LEU E 310A REMARK 465 GLU E 310B REMARK 465 ASP E 310C REMARK 465 LYS E 310D REMARK 465 SER E 310E REMARK 465 PRO E 310F REMARK 465 ASP E 310G REMARK 465 SER E 310H REMARK 465 PRO E 310I REMARK 465 GLU E 310J REMARK 465 MET E 310K REMARK 465 LYS E 310L REMARK 465 ASP E 310M REMARK 465 PHE E 310N REMARK 465 ARG E 310O REMARK 465 HIS E 310P REMARK 465 GLY E 310Q REMARK 465 PHE E 310R REMARK 465 ASP E 310S REMARK 465 ILE E 310T REMARK 465 LEU E 310U REMARK 465 VAL E 310V REMARK 465 GLY E 310W REMARK 465 GLN E 310X REMARK 465 ILE E 310Y REMARK 465 ASP E 310Z REMARK 465 ASP E 311A REMARK 465 ALA E 311B REMARK 465 LEU E 311C REMARK 465 LYS E 311D REMARK 465 LEU E 311E REMARK 465 ALA E 311F REMARK 465 ASN E 311G REMARK 465 GLU E 311H REMARK 465 GLY E 311I REMARK 465 LYS E 311J REMARK 465 VAL E 311K REMARK 465 LYS E 311L REMARK 465 GLU E 311M REMARK 465 ALA E 311N REMARK 465 GLN E 311O REMARK 465 ALA E 311P REMARK 465 ALA E 311Q REMARK 465 ALA E 311R REMARK 465 GLU E 311S REMARK 465 GLN E 311T REMARK 465 LEU E 311U REMARK 465 LYS E 311V REMARK 465 THR E 311W REMARK 465 THR E 311X REMARK 465 ARG E 311Y REMARK 465 ASN E 311Z REMARK 465 ALA E 312A REMARK 465 TYR E 312B REMARK 465 ILE E 312C REMARK 465 GLN E 312D REMARK 465 LYS E 312E REMARK 465 ASN E 448 REMARK 465 GLY F 9 REMARK 465 GLY F 10 REMARK 465 LEU F 11 REMARK 465 VAL F 12 REMARK 465 GLN F 13 REMARK 465 THR F 14 REMARK 465 LYS F 15 REMARK 465 THR F 16 REMARK 465 THR F 17 REMARK 465 THR F 18 REMARK 465 SER F 19 REMARK 465 VAL F 20 REMARK 465 ILE F 21 REMARK 465 ASP F 22 REMARK 465 THR F 23 REMARK 465 THR F 24 REMARK 465 ASN F 25 REMARK 465 ASP F 26 REMARK 465 ALA F 27 REMARK 465 GLN F 28 REMARK 465 ASN F 29 REMARK 465 LEU F 30 REMARK 465 LEU F 31 REMARK 465 THR F 32 REMARK 465 GLN F 33 REMARK 465 ALA F 34 REMARK 465 GLN F 35 REMARK 465 THR F 36 REMARK 465 ILE F 37 REMARK 465 VAL F 38 REMARK 465 ASN F 39 REMARK 465 THR F 40 REMARK 465 LEU F 41 REMARK 465 LYS F 42 REMARK 465 ASP F 43 REMARK 465 TYR F 44 REMARK 465 CYS F 45 REMARK 465 PRO F 46 REMARK 465 ILE F 47 REMARK 465 LEU F 48 REMARK 465 ILE F 49 REMARK 465 ALA F 50 REMARK 465 LYS F 51 REMARK 465 SER F 52 REMARK 465 SER F 53 REMARK 465 SER F 54 REMARK 465 SER F 55 REMARK 465 ASN F 56 REMARK 465 GLY F 57 REMARK 465 GLY F 58 REMARK 465 THR F 59 REMARK 465 ASN F 60 REMARK 465 ASN F 61 REMARK 465 ALA F 62 REMARK 465 ASN F 63 REMARK 465 THR F 64 REMARK 465 PRO F 65 REMARK 465 SER F 66 REMARK 465 TRP F 67 REMARK 465 GLN F 68 REMARK 465 THR F 69 REMARK 465 ALA F 70 REMARK 465 GLY F 71 REMARK 465 GLY F 72 REMARK 465 GLY F 73 REMARK 465 LYS F 74 REMARK 465 ASN F 75 REMARK 465 SER F 76 REMARK 465 CYS F 77 REMARK 465 ALA F 78 REMARK 465 THR F 79 REMARK 465 PHE F 80 REMARK 465 GLY F 81 REMARK 465 ALA F 82 REMARK 465 GLU F 83 REMARK 465 PHE F 84 REMARK 465 SER F 85 REMARK 465 ALA F 86 REMARK 465 ALA F 87 REMARK 465 SER F 88 REMARK 465 ASP F 89 REMARK 465 MET F 90 REMARK 465 ILE F 91 REMARK 465 ASN F 92 REMARK 465 ASN F 93 REMARK 465 ALA F 94 REMARK 465 GLN F 95 REMARK 465 LYS F 96 REMARK 465 ILE F 97 REMARK 465 VAL F 98 REMARK 465 GLN F 99 REMARK 465 GLU F 100 REMARK 465 THR F 101 REMARK 465 GLN F 102 REMARK 465 GLN F 103 REMARK 465 LEU F 104 REMARK 465 SER F 105 REMARK 465 ALA F 106 REMARK 465 ASN F 107 REMARK 465 GLN F 108 REMARK 465 PRO F 109 REMARK 465 LYS F 110 REMARK 465 ASN F 111 REMARK 465 ILE F 112 REMARK 465 THR F 113 REMARK 465 GLN F 114 REMARK 465 PRO F 115 REMARK 465 HIS F 116 REMARK 465 ASN F 117 REMARK 465 LEU F 118 REMARK 465 ASN F 119 REMARK 465 LEU F 120 REMARK 465 ASN F 121 REMARK 465 SER F 122 REMARK 465 PRO F 123 REMARK 465 SER F 124 REMARK 465 SER F 125 REMARK 465 LEU F 126 REMARK 465 THR F 127 REMARK 465 ALA F 128 REMARK 465 LEU F 129 REMARK 465 ALA F 130 REMARK 465 GLN F 131 REMARK 465 LYS F 132 REMARK 465 MET F 133 REMARK 465 LEU F 134 REMARK 465 LYS F 135 REMARK 465 ASN F 136 REMARK 465 ALA F 137 REMARK 465 GLN F 138 REMARK 465 SER F 139 REMARK 465 GLN F 140 REMARK 465 ALA F 141 REMARK 465 GLU F 142 REMARK 465 ILE F 143 REMARK 465 LEU F 144 REMARK 465 LYS F 145 REMARK 465 LEU F 146 REMARK 465 ALA F 147 REMARK 465 ASN F 148 REMARK 465 GLN F 149 REMARK 465 VAL F 150 REMARK 465 GLU F 151 REMARK 465 SER F 152 REMARK 465 ASP F 153 REMARK 465 PHE F 154 REMARK 465 ASN F 155 REMARK 465 LYS F 156 REMARK 465 LEU F 157 REMARK 465 SER F 158 REMARK 465 SER F 159 REMARK 465 GLY F 160 REMARK 465 HIS F 161 REMARK 465 LEU F 162 REMARK 465 LYS F 163 REMARK 465 ASP F 164 REMARK 465 TYR F 165 REMARK 465 ILE F 166 REMARK 465 GLY F 167 REMARK 465 LYS F 168 REMARK 465 CYS F 169 REMARK 465 ASP F 170 REMARK 465 ALA F 171 REMARK 465 SER F 172 REMARK 465 ALA F 173 REMARK 465 ILE F 174 REMARK 465 SER F 175 REMARK 465 SER F 176 REMARK 465 ALA F 177 REMARK 465 ASN F 178 REMARK 465 MET F 179 REMARK 465 THR F 180 REMARK 465 MET F 181 REMARK 465 GLN F 182 REMARK 465 ASN F 183 REMARK 465 GLN F 184 REMARK 465 LYS F 185 REMARK 465 ASN F 186 REMARK 465 ASN F 187 REMARK 465 TRP F 188 REMARK 465 GLY F 189 REMARK 465 ASN F 190 REMARK 465 GLY F 191 REMARK 465 CYS F 192 REMARK 465 ALA F 193 REMARK 465 GLY F 194 REMARK 465 VAL F 195 REMARK 465 GLU F 196 REMARK 465 GLU F 197 REMARK 465 THR F 198 REMARK 465 GLN F 199 REMARK 465 SER F 200 REMARK 465 LEU F 201 REMARK 465 LEU F 202 REMARK 465 LYS F 203 REMARK 465 THR F 204 REMARK 465 SER F 205 REMARK 465 ALA F 206 REMARK 465 ALA F 207 REMARK 465 ASP F 208 REMARK 465 PHE F 209 REMARK 465 ASN F 210 REMARK 465 ASN F 211 REMARK 465 GLN F 212 REMARK 465 THR F 213 REMARK 465 PRO F 214 REMARK 465 GLN F 215 REMARK 465 ILE F 216 REMARK 465 ASN F 217 REMARK 465 GLN F 218 REMARK 465 ALA F 219 REMARK 465 GLN F 220 REMARK 465 ASN F 221 REMARK 465 LEU F 222 REMARK 465 ALA F 223 REMARK 465 ASN F 224 REMARK 465 THR F 225 REMARK 465 LEU F 226 REMARK 465 ILE F 227 REMARK 465 GLN F 228 REMARK 465 GLU F 229 REMARK 465 LEU F 230 REMARK 465 GLY F 231 REMARK 465 ASN F 232 REMARK 465 ASN F 233 REMARK 465 THR F 234 REMARK 465 TYR F 235 REMARK 465 GLU F 236 REMARK 465 GLN F 237 REMARK 465 LEU F 238 REMARK 465 SER F 239 REMARK 465 ARG F 240 REMARK 465 LEU F 241 REMARK 465 LEU F 242 REMARK 465 THR F 243 REMARK 465 ASN F 244 REMARK 465 ASP F 245 REMARK 465 ASN F 246 REMARK 465 GLY F 247 REMARK 465 THR F 248 REMARK 465 ASN F 249 REMARK 465 SER F 250 REMARK 465 LYS F 251 REMARK 465 THR F 252 REMARK 465 SER F 253 REMARK 465 ALA F 254 REMARK 465 GLN F 255 REMARK 465 ALA F 256 REMARK 465 ILE F 257 REMARK 465 ASN F 258 REMARK 465 GLN F 259 REMARK 465 ALA F 260 REMARK 465 VAL F 261 REMARK 465 ASN F 262 REMARK 465 ASN F 263 REMARK 465 LEU F 264 REMARK 465 ASN F 265 REMARK 465 GLU F 266 REMARK 465 ARG F 267 REMARK 465 ALA F 268 REMARK 465 LYS F 269 REMARK 465 THR F 270 REMARK 465 LEU F 271 REMARK 465 ALA F 272 REMARK 465 GLY F 273 REMARK 465 GLY F 274 REMARK 465 THR F 275 REMARK 465 THR F 276 REMARK 465 ASN F 277 REMARK 465 SER F 278 REMARK 465 PRO F 279 REMARK 465 ALA F 280 REMARK 465 TYR F 281 REMARK 465 GLN F 282 REMARK 465 ALA F 283 REMARK 465 THR F 284 REMARK 465 LEU F 285 REMARK 465 LEU F 286 REMARK 465 ALA F 287 REMARK 465 LEU F 288 REMARK 465 ARG F 289 REMARK 465 SER F 290 REMARK 465 VAL F 291 REMARK 465 LEU F 292 REMARK 465 GLY F 293 REMARK 465 LEU F 294 REMARK 465 TRP F 295 REMARK 465 ASN F 296 REMARK 465 SER F 297 REMARK 465 MET F 298 REMARK 465 GLY F 299 REMARK 465 TYR F 300 REMARK 465 ALA F 301 REMARK 465 VAL F 302 REMARK 465 ILE F 303 REMARK 465 CYS F 304 REMARK 465 GLY F 305 REMARK 465 GLY F 306 REMARK 465 TYR F 307 REMARK 465 THR F 308 REMARK 465 LYS F 309 REMARK 465 SER F 310 REMARK 465 PRO F 311 REMARK 465 GLY F 312 REMARK 465 GLU F 313 REMARK 465 ASN F 314 REMARK 465 ASN F 315 REMARK 465 GLN F 316 REMARK 465 LYS F 317 REMARK 465 ASP F 318 REMARK 465 PHE F 319 REMARK 465 HIS F 320 REMARK 465 TYR F 321 REMARK 465 THR F 322 REMARK 465 ASP F 323 REMARK 465 GLU F 324 REMARK 465 ASN F 325 REMARK 465 GLY F 326 REMARK 465 ASN F 327 REMARK 465 GLY F 328 REMARK 465 THR F 329 REMARK 465 THR F 330 REMARK 465 ILE F 331 REMARK 465 ASN F 332 REMARK 465 CYS F 333 REMARK 465 GLY F 334 REMARK 465 GLY F 335 REMARK 465 SER F 336 REMARK 465 THR F 337 REMARK 465 ASN F 338 REMARK 465 SER F 339 REMARK 465 ASN F 340 REMARK 465 GLY F 341 REMARK 465 THR F 342 REMARK 465 HIS F 343 REMARK 465 SER F 344 REMARK 465 TYR F 345 REMARK 465 ASN F 346 REMARK 465 GLY F 347 REMARK 465 THR F 348 REMARK 465 ASN F 349 REMARK 465 THR F 350 REMARK 465 LEU F 351 REMARK 465 LYS F 352 REMARK 465 ALA F 353 REMARK 465 ASP F 354 REMARK 465 LYS F 355 REMARK 465 ASN F 356 REMARK 465 VAL F 357 REMARK 465 SER F 358 REMARK 465 LEU F 359 REMARK 465 SER F 360 REMARK 465 ILE F 361 REMARK 465 GLU F 362 REMARK 465 GLN F 363 REMARK 465 TYR F 364 REMARK 465 GLU F 365 REMARK 465 LYS F 366 REMARK 465 ILE F 367 REMARK 465 HIS F 368 REMARK 465 GLU F 369 REMARK 465 ALA F 370 REMARK 465 TYR F 371 REMARK 465 GLN F 372 REMARK 465 ILE F 373 REMARK 465 LEU F 374 REMARK 465 SER F 375 REMARK 465 LYS F 376 REMARK 465 ALA F 377 REMARK 465 LEU F 378 REMARK 465 LYS F 379 REMARK 465 GLN F 380 REMARK 465 ALA F 381 REMARK 465 GLY F 382 REMARK 465 LEU F 383 REMARK 465 ALA F 384 REMARK 465 PRO F 385 REMARK 465 LEU F 386 REMARK 465 ASN F 387 REMARK 465 SER F 388 REMARK 465 LYS F 389 REMARK 465 GLY F 390 REMARK 465 GLU F 391 REMARK 465 LYS F 392 REMARK 465 LEU F 393 REMARK 465 GLU F 394 REMARK 465 ALA F 395 REMARK 465 HIS F 396 REMARK 465 VAL F 397 REMARK 465 THR F 398 REMARK 465 THR F 399 REMARK 465 SER F 400 REMARK 465 LYS F 401 REMARK 465 TYR F 402 REMARK 465 GLY F 403 REMARK 465 SER F 404 REMARK 465 VAL F 510 REMARK 465 SER F 511 REMARK 465 SER F 512 REMARK 465 HIS F 513 REMARK 465 HIS F 514 REMARK 465 HIS F 515 REMARK 465 HIS F 516 REMARK 465 HIS F 517 REMARK 465 HIS F 518 REMARK 465 GLU F 519 REMARK 465 PRO F 520 REMARK 465 GLU F 521 REMARK 465 ALA F 522 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 ND2 ASN D 111 O5 NAG D 502 1.61 REMARK 500 O4 NAG H 2 C2 BMA H 3 1.90 REMARK 500 ND2 ASN A 111 O5 NAG A 502 1.92 REMARK 500 O6 BMA K 3 O5 MAN K 5 1.96 REMARK 500 C6 BMA H 3 C1 MAN H 5 2.00 REMARK 500 OE2 GLU B 179 OG SER F 446 2.06 REMARK 500 O4 NAG H 1 O5 NAG H 2 2.07 REMARK 500 OH TYR B 97 OE2 GLU B 155 2.09 REMARK 500 O4 NAG I 1 O5 NAG I 2 2.12 REMARK 500 O6 BMA I 3 O5 MAN I 5 2.13 REMARK 500 ND2 ASN C 80 O5 NAG J 1 2.16 REMARK 500 O TYR B 304 OG SER B 308 2.18 REMARK 500 O6 BMA H 3 C2 MAN H 5 2.19 REMARK 500 O3 BMA K 3 O5 MAN K 4 2.19 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 453 CB - CG - OD1 ANGL. DEV. = 6.5 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 LEU A 75 52.09 -92.50 REMARK 500 ASP A 98 36.66 -98.28 REMARK 500 THR A 113 -74.31 65.00 REMARK 500 ASP A 145 32.07 -97.38 REMARK 500 LEU A 194 37.02 -99.48 REMARK 500 ALA A 281 58.11 -96.24 REMARK 500 TYR A 282 140.58 -170.31 REMARK 500 THR A 284 -75.54 -94.95 REMARK 500 ALA A 285 -26.33 -144.37 REMARK 500 PRO A 315 44.07 -82.24 REMARK 500 THR B 110 -21.50 73.98 REMARK 500 ARG B 207 118.35 -161.06 REMARK 500 SER C 46 135.93 -171.11 REMARK 500 ASP C 48 -164.36 -79.42 REMARK 500 ASP C 95 47.12 -87.84 REMARK 500 THR C 110 -11.76 73.96 REMARK 500 THR E 110 -12.95 74.08 REMARK 500 LEU E 145 30.99 -96.08 REMARK 500 ALA E 280 -6.93 74.96 REMARK 500 ASN D 87 -169.80 -78.24 REMARK 500 THR D 113 -70.78 63.46 REMARK 500 ARG D 173 -165.01 -126.48 REMARK 500 ASP F 453 39.34 35.63 REMARK 500 ARG F 454 -36.01 -131.90 REMARK 500 SER F 490 17.14 -141.45 REMARK 500 ASP F 500 -60.71 -92.65 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-13290 RELATED DB: EMDB REMARK 900 A1B3 GABA-A RECEPTOR + GABA DBREF1 7PBD A 12 312 UNP A0A1B0GV38_HUMAN DBREF2 7PBD A A0A1B0GV38 54 354 DBREF1 7PBD A 401 418 UNP A0A1B0GV38_HUMAN DBREF2 7PBD A A0A1B0GV38 443 460 DBREF 7PBD B 1 448 PDB 7PBD 7PBD 1 448 DBREF 7PBD C 1 448 PDB 7PBD 7PBD 1 448 DBREF 7PBD E 1 448 PDB 7PBD 7PBD 1 448 DBREF1 7PBD D 12 312 UNP A0A1B0GV38_HUMAN DBREF2 7PBD D A0A1B0GV38 54 354 DBREF1 7PBD D 401 418 UNP A0A1B0GV38_HUMAN DBREF2 7PBD D A0A1B0GV38 443 460 DBREF 7PBD F 1 522 PDB 7PBD 7PBD 1 522 SEQADV 7PBD SER A 313 UNP A0A1B0GV3 LINKER SEQADV 7PBD GLN A 314 UNP A0A1B0GV3 LINKER SEQADV 7PBD PRO A 315 UNP A0A1B0GV3 LINKER SEQADV 7PBD ALA A 316 UNP A0A1B0GV3 LINKER SEQADV 7PBD ARG A 317 UNP A0A1B0GV3 LINKER SEQADV 7PBD ALA A 318 UNP A0A1B0GV3 LINKER SEQADV 7PBD ALA A 319 UNP A0A1B0GV3 LINKER SEQADV 7PBD LYS A 391 UNP A0A1B0GV3 LINKER SEQADV 7PBD ILE A 392 UNP A0A1B0GV3 LINKER SEQADV 7PBD ASP A 393 UNP A0A1B0GV3 LINKER SEQADV 7PBD ARG A 394 UNP A0A1B0GV3 LINKER SEQADV 7PBD LEU A 395 UNP A0A1B0GV3 LINKER SEQADV 7PBD SER A 396 UNP A0A1B0GV3 LINKER SEQADV 7PBD ARG A 397 UNP A0A1B0GV3 LINKER SEQADV 7PBD ILE A 398 UNP A0A1B0GV3 LINKER SEQADV 7PBD ALA A 399 UNP A0A1B0GV3 LINKER SEQADV 7PBD PHE A 400 UNP A0A1B0GV3 LINKER SEQADV 7PBD SER D 313 UNP A0A1B0GV3 LINKER SEQADV 7PBD GLN D 314 UNP A0A1B0GV3 LINKER SEQADV 7PBD PRO D 315 UNP A0A1B0GV3 LINKER SEQADV 7PBD ALA D 316 UNP A0A1B0GV3 LINKER SEQADV 7PBD ARG D 317 UNP A0A1B0GV3 LINKER SEQADV 7PBD ALA D 318 UNP A0A1B0GV3 LINKER SEQADV 7PBD ALA D 319 UNP A0A1B0GV3 LINKER SEQADV 7PBD LYS D 391 UNP A0A1B0GV3 LINKER SEQADV 7PBD ILE D 392 UNP A0A1B0GV3 LINKER SEQADV 7PBD ASP D 393 UNP A0A1B0GV3 LINKER SEQADV 7PBD ARG D 394 UNP A0A1B0GV3 LINKER SEQADV 7PBD LEU D 395 UNP A0A1B0GV3 LINKER SEQADV 7PBD SER D 396 UNP A0A1B0GV3 LINKER SEQADV 7PBD ARG D 397 UNP A0A1B0GV3 LINKER SEQADV 7PBD ILE D 398 UNP A0A1B0GV3 LINKER SEQADV 7PBD ALA D 399 UNP A0A1B0GV3 LINKER SEQADV 7PBD PHE D 400 UNP A0A1B0GV3 LINKER SEQRES 1 A 336 THR THR VAL PHE THR ARG ILE LEU ASP ARG LEU LEU ASP SEQRES 2 A 336 GLY TYR ASP ASN ARG LEU ARG PRO GLY LEU GLY GLU ARG SEQRES 3 A 336 VAL THR GLU VAL LYS THR ASP ILE PHE VAL THR SER PHE SEQRES 4 A 336 GLY PRO VAL SER ASP HIS ASP MET GLU TYR THR ILE ASP SEQRES 5 A 336 VAL PHE PHE ARG GLN SER TRP LYS ASP GLU ARG LEU LYS SEQRES 6 A 336 PHE LYS GLY PRO MET THR VAL LEU ARG LEU ASN ASN LEU SEQRES 7 A 336 MET ALA SER LYS ILE TRP THR PRO ASP THR PHE PHE HIS SEQRES 8 A 336 ASN GLY LYS LYS SER VAL ALA HIS ASN MET THR MET PRO SEQRES 9 A 336 ASN LYS LEU LEU ARG ILE THR GLU ASP GLY THR LEU LEU SEQRES 10 A 336 TYR THR MET ARG LEU THR VAL ARG ALA GLU CYS PRO MET SEQRES 11 A 336 HIS LEU GLU ASP PHE PRO MET ASP ALA HIS ALA CYS PRO SEQRES 12 A 336 LEU LYS PHE GLY SER TYR ALA TYR THR ARG ALA GLU VAL SEQRES 13 A 336 VAL TYR GLU TRP THR ARG GLU PRO ALA ARG SER VAL VAL SEQRES 14 A 336 VAL ALA GLU ASP GLY SER ARG LEU ASN GLN TYR ASP LEU SEQRES 15 A 336 LEU GLY GLN THR VAL ASP SER GLY ILE VAL GLN SER SER SEQRES 16 A 336 THR GLY GLU TYR VAL VAL MET THR THR HIS PHE HIS LEU SEQRES 17 A 336 LYS ARG LYS ILE GLY TYR PHE VAL ILE GLN THR TYR LEU SEQRES 18 A 336 PRO CYS ILE MET THR VAL ILE LEU SER GLN VAL SER PHE SEQRES 19 A 336 TRP LEU ASN ARG GLU SER VAL PRO ALA ARG THR VAL PHE SEQRES 20 A 336 GLY VAL THR THR VAL LEU THR MET THR THR LEU SER ILE SEQRES 21 A 336 SER ALA ARG ASN SER LEU PRO LYS VAL ALA TYR ALA THR SEQRES 22 A 336 ALA MET ASP TRP PHE ILE ALA VAL CYS TYR ALA PHE VAL SEQRES 23 A 336 PHE SER ALA LEU ILE GLU PHE ALA THR VAL ASN TYR PHE SEQRES 24 A 336 THR LYS SER GLN PRO ALA ARG ALA ALA LYS ILE ASP ARG SEQRES 25 A 336 LEU SER ARG ILE ALA PHE PRO LEU LEU PHE GLY ILE PHE SEQRES 26 A 336 ASN LEU VAL TYR TRP ALA THR TYR LEU ASN ARG SEQRES 1 B 451 GLN SER VAL ASN ASP PRO GLY ASN MET SER PHE VAL LYS SEQRES 2 B 451 GLU THR VAL ASP LYS LEU LEU LYS GLY TYR ASP ILE ARG SEQRES 3 B 451 LEU ARG PRO ASP PHE GLY GLY PRO PRO VAL CYS VAL GLY SEQRES 4 B 451 MET ASN ILE ASP ILE ALA SER ILE ASP MET VAL SER GLU SEQRES 5 B 451 VAL ASN MET ASP TYR THR LEU THR MET TYR PHE GLN GLN SEQRES 6 B 451 TYR TRP ARG ASP LYS ARG LEU ALA TYR SER GLY ILE PRO SEQRES 7 B 451 LEU ASN LEU THR LEU ASP ASN ARG VAL ALA ASP GLN LEU SEQRES 8 B 451 TRP VAL PRO ASP THR TYR PHE LEU ASN ASP LYS LYS SER SEQRES 9 B 451 PHE VAL HIS GLY VAL THR VAL LYS ASN ARG MET ILE ARG SEQRES 10 B 451 LEU HIS PRO ASP GLY THR VAL LEU TYR GLY LEU ARG ILE SEQRES 11 B 451 THR THR THR ALA ALA CYS MET MET ASP LEU ARG ARG TYR SEQRES 12 B 451 PRO LEU ASP GLU GLN ASN CYS THR LEU GLU ILE GLU SER SEQRES 13 B 451 TYR GLY TYR THR THR ASP ASP ILE GLU PHE TYR TRP ARG SEQRES 14 B 451 GLY GLY ASP LYS ALA VAL THR GLY VAL GLU ARG ILE GLU SEQRES 15 B 451 LEU PRO GLN PHE SER ILE VAL GLU HIS ARG LEU VAL SER SEQRES 16 B 451 ARG ASN VAL VAL PHE ALA THR GLY ALA TYR PRO ARG LEU SEQRES 17 B 451 SER LEU SER PHE ARG LEU LYS ARG ASN ILE GLY TYR PHE SEQRES 18 B 451 ILE LEU GLN THR TYR MET PRO SER ILE LEU ILE THR ILE SEQRES 19 B 451 LEU SER TRP VAL SER PHE TRP ILE ASN TYR ASP ALA SER SEQRES 20 B 451 ALA ALA ARG VAL ALA LEU GLY ILE THR THR VAL LEU THR SEQRES 21 B 451 MET THR THR ILE ASN THR HIS LEU ARG GLU THR LEU PRO SEQRES 22 B 451 LYS ILE PRO TYR VAL LYS ALA ILE ASP MET TYR LEU MET SEQRES 23 B 451 GLY CYS PHE VAL PHE VAL PHE LEU ALA LEU LEU GLU TYR SEQRES 24 B 451 ALA PHE VAL ASN TYR ILE PHE PHE SER GLN PRO ALA GLY SEQRES 25 B 451 THR ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP SEQRES 26 B 451 ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN SEQRES 27 B 451 VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU SEQRES 28 B 451 ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SEQRES 29 B 451 SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY SEQRES 30 B 451 PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS SEQRES 31 B 451 LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA SEQRES 32 B 451 ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN SEQRES 33 B 451 LYS TYR LEU THR GLY ARG ALA ALA ALA ILE ASP ARG TRP SEQRES 34 B 451 SER ARG ILE VAL PHE PRO PHE THR PHE SER LEU PHE ASN SEQRES 35 B 451 LEU VAL TYR TRP LEU TYR TYR VAL ASN SEQRES 1 C 451 GLN SER VAL ASN ASP PRO GLY ASN MET SER PHE VAL LYS SEQRES 2 C 451 GLU THR VAL ASP LYS LEU LEU LYS GLY TYR ASP ILE ARG SEQRES 3 C 451 LEU ARG PRO ASP PHE GLY GLY PRO PRO VAL CYS VAL GLY SEQRES 4 C 451 MET ASN ILE ASP ILE ALA SER ILE ASP MET VAL SER GLU SEQRES 5 C 451 VAL ASN MET ASP TYR THR LEU THR MET TYR PHE GLN GLN SEQRES 6 C 451 TYR TRP ARG ASP LYS ARG LEU ALA TYR SER GLY ILE PRO SEQRES 7 C 451 LEU ASN LEU THR LEU ASP ASN ARG VAL ALA ASP GLN LEU SEQRES 8 C 451 TRP VAL PRO ASP THR TYR PHE LEU ASN ASP LYS LYS SER SEQRES 9 C 451 PHE VAL HIS GLY VAL THR VAL LYS ASN ARG MET ILE ARG SEQRES 10 C 451 LEU HIS PRO ASP GLY THR VAL LEU TYR GLY LEU ARG ILE SEQRES 11 C 451 THR THR THR ALA ALA CYS MET MET ASP LEU ARG ARG TYR SEQRES 12 C 451 PRO LEU ASP GLU GLN ASN CYS THR LEU GLU ILE GLU SER SEQRES 13 C 451 TYR GLY TYR THR THR ASP ASP ILE GLU PHE TYR TRP ARG SEQRES 14 C 451 GLY GLY ASP LYS ALA VAL THR GLY VAL GLU ARG ILE GLU SEQRES 15 C 451 LEU PRO GLN PHE SER ILE VAL GLU HIS ARG LEU VAL SER SEQRES 16 C 451 ARG ASN VAL VAL PHE ALA THR GLY ALA TYR PRO ARG LEU SEQRES 17 C 451 SER LEU SER PHE ARG LEU LYS ARG ASN ILE GLY TYR PHE SEQRES 18 C 451 ILE LEU GLN THR TYR MET PRO SER ILE LEU ILE THR ILE SEQRES 19 C 451 LEU SER TRP VAL SER PHE TRP ILE ASN TYR ASP ALA SER SEQRES 20 C 451 ALA ALA ARG VAL ALA LEU GLY ILE THR THR VAL LEU THR SEQRES 21 C 451 MET THR THR ILE ASN THR HIS LEU ARG GLU THR LEU PRO SEQRES 22 C 451 LYS ILE PRO TYR VAL LYS ALA ILE ASP MET TYR LEU MET SEQRES 23 C 451 GLY CYS PHE VAL PHE VAL PHE LEU ALA LEU LEU GLU TYR SEQRES 24 C 451 ALA PHE VAL ASN TYR ILE PHE PHE SER GLN PRO ALA GLY SEQRES 25 C 451 THR ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP SEQRES 26 C 451 ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN SEQRES 27 C 451 VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU SEQRES 28 C 451 ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SEQRES 29 C 451 SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY SEQRES 30 C 451 PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS SEQRES 31 C 451 LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA SEQRES 32 C 451 ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN SEQRES 33 C 451 LYS TYR LEU THR GLY ARG ALA ALA ALA ILE ASP ARG TRP SEQRES 34 C 451 SER ARG ILE VAL PHE PRO PHE THR PHE SER LEU PHE ASN SEQRES 35 C 451 LEU VAL TYR TRP LEU TYR TYR VAL ASN SEQRES 1 E 451 GLN SER VAL ASN ASP PRO GLY ASN MET SER PHE VAL LYS SEQRES 2 E 451 GLU THR VAL ASP LYS LEU LEU LYS GLY TYR ASP ILE ARG SEQRES 3 E 451 LEU ARG PRO ASP PHE GLY GLY PRO PRO VAL CYS VAL GLY SEQRES 4 E 451 MET ASN ILE ASP ILE ALA SER ILE ASP MET VAL SER GLU SEQRES 5 E 451 VAL ASN MET ASP TYR THR LEU THR MET TYR PHE GLN GLN SEQRES 6 E 451 TYR TRP ARG ASP LYS ARG LEU ALA TYR SER GLY ILE PRO SEQRES 7 E 451 LEU ASN LEU THR LEU ASP ASN ARG VAL ALA ASP GLN LEU SEQRES 8 E 451 TRP VAL PRO ASP THR TYR PHE LEU ASN ASP LYS LYS SER SEQRES 9 E 451 PHE VAL HIS GLY VAL THR VAL LYS ASN ARG MET ILE ARG SEQRES 10 E 451 LEU HIS PRO ASP GLY THR VAL LEU TYR GLY LEU ARG ILE SEQRES 11 E 451 THR THR THR ALA ALA CYS MET MET ASP LEU ARG ARG TYR SEQRES 12 E 451 PRO LEU ASP GLU GLN ASN CYS THR LEU GLU ILE GLU SER SEQRES 13 E 451 TYR GLY TYR THR THR ASP ASP ILE GLU PHE TYR TRP ARG SEQRES 14 E 451 GLY GLY ASP LYS ALA VAL THR GLY VAL GLU ARG ILE GLU SEQRES 15 E 451 LEU PRO GLN PHE SER ILE VAL GLU HIS ARG LEU VAL SER SEQRES 16 E 451 ARG ASN VAL VAL PHE ALA THR GLY ALA TYR PRO ARG LEU SEQRES 17 E 451 SER LEU SER PHE ARG LEU LYS ARG ASN ILE GLY TYR PHE SEQRES 18 E 451 ILE LEU GLN THR TYR MET PRO SER ILE LEU ILE THR ILE SEQRES 19 E 451 LEU SER TRP VAL SER PHE TRP ILE ASN TYR ASP ALA SER SEQRES 20 E 451 ALA ALA ARG VAL ALA LEU GLY ILE THR THR VAL LEU THR SEQRES 21 E 451 MET THR THR ILE ASN THR HIS LEU ARG GLU THR LEU PRO SEQRES 22 E 451 LYS ILE PRO TYR VAL LYS ALA ILE ASP MET TYR LEU MET SEQRES 23 E 451 GLY CYS PHE VAL PHE VAL PHE LEU ALA LEU LEU GLU TYR SEQRES 24 E 451 ALA PHE VAL ASN TYR ILE PHE PHE SER GLN PRO ALA GLY SEQRES 25 E 451 THR ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP SEQRES 26 E 451 ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN SEQRES 27 E 451 VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU SEQRES 28 E 451 ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SEQRES 29 E 451 SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY SEQRES 30 E 451 PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS SEQRES 31 E 451 LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA SEQRES 32 E 451 ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN SEQRES 33 E 451 LYS TYR LEU THR GLY ARG ALA ALA ALA ILE ASP ARG TRP SEQRES 34 E 451 SER ARG ILE VAL PHE PRO PHE THR PHE SER LEU PHE ASN SEQRES 35 E 451 LEU VAL TYR TRP LEU TYR TYR VAL ASN 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 F 522 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 522 THR LYS THR THR THR SER VAL ILE ASP THR THR ASN ASP SEQRES 3 F 522 ALA GLN ASN LEU LEU THR GLN ALA GLN THR ILE VAL ASN SEQRES 4 F 522 THR LEU LYS ASP TYR CYS PRO ILE LEU ILE ALA LYS SER SEQRES 5 F 522 SER SER SER ASN GLY GLY THR ASN ASN ALA ASN THR PRO SEQRES 6 F 522 SER TRP GLN THR ALA GLY GLY GLY LYS ASN SER CYS ALA SEQRES 7 F 522 THR PHE GLY ALA GLU PHE SER ALA ALA SER ASP MET ILE SEQRES 8 F 522 ASN ASN ALA GLN LYS ILE VAL GLN GLU THR GLN GLN LEU SEQRES 9 F 522 SER ALA ASN GLN PRO LYS ASN ILE THR GLN PRO HIS ASN SEQRES 10 F 522 LEU ASN LEU ASN SER PRO SER SER LEU THR ALA LEU ALA SEQRES 11 F 522 GLN LYS MET LEU LYS ASN ALA GLN SER GLN ALA GLU ILE SEQRES 12 F 522 LEU LYS LEU ALA ASN GLN VAL GLU SER ASP PHE ASN LYS SEQRES 13 F 522 LEU SER SER GLY HIS LEU LYS ASP TYR ILE GLY LYS CYS SEQRES 14 F 522 ASP ALA SER ALA ILE SER SER ALA ASN MET THR MET GLN SEQRES 15 F 522 ASN GLN LYS ASN ASN TRP GLY ASN GLY CYS ALA GLY VAL SEQRES 16 F 522 GLU GLU THR GLN SER LEU LEU LYS THR SER ALA ALA ASP SEQRES 17 F 522 PHE ASN ASN GLN THR PRO GLN ILE ASN GLN ALA GLN ASN SEQRES 18 F 522 LEU ALA ASN THR LEU ILE GLN GLU LEU GLY ASN ASN THR SEQRES 19 F 522 TYR GLU GLN LEU SER ARG LEU LEU THR ASN ASP ASN GLY SEQRES 20 F 522 THR ASN SER LYS THR SER ALA GLN ALA ILE ASN GLN ALA SEQRES 21 F 522 VAL ASN ASN LEU ASN GLU ARG ALA LYS THR LEU ALA GLY SEQRES 22 F 522 GLY THR THR ASN SER PRO ALA TYR GLN ALA THR LEU LEU SEQRES 23 F 522 ALA LEU ARG SER VAL LEU GLY LEU TRP ASN SER MET GLY SEQRES 24 F 522 TYR ALA VAL ILE CYS GLY GLY TYR THR LYS SER PRO GLY SEQRES 25 F 522 GLU ASN ASN GLN LYS ASP PHE HIS TYR THR ASP GLU ASN SEQRES 26 F 522 GLY ASN GLY THR THR ILE ASN CYS GLY GLY SER THR ASN SEQRES 27 F 522 SER ASN GLY THR HIS SER TYR ASN GLY THR ASN THR LEU SEQRES 28 F 522 LYS ALA ASP LYS ASN VAL SER LEU SER ILE GLU GLN TYR SEQRES 29 F 522 GLU LYS ILE HIS GLU ALA TYR GLN ILE LEU SER LYS ALA SEQRES 30 F 522 LEU LYS GLN ALA GLY LEU ALA PRO LEU ASN SER LYS GLY SEQRES 31 F 522 GLU LYS LEU GLU ALA HIS VAL THR THR SER LYS TYR GLY SEQRES 32 F 522 SER LEU ARG LEU SER CYS ALA ALA SER GLY HIS THR PHE SEQRES 33 F 522 ASN TYR PRO ILE MET GLY TRP PHE ARG GLN ALA PRO GLY SEQRES 34 F 522 LYS GLU ARG GLU PHE VAL GLY ALA ILE SER TRP SER GLY SEQRES 35 F 522 GLY SER THR SER TYR ALA ASP SER VAL LYS ASP ARG PHE SEQRES 36 F 522 THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL TYR LEU SEQRES 37 F 522 GLU MET ASN ASN LEU LYS PRO GLU ASP THR ALA VAL TYR SEQRES 38 F 522 TYR CYS ALA ALA LYS GLY ARG TYR SER GLY GLY LEU TYR SEQRES 39 F 522 TYR PRO THR ASN TYR ASP TYR TRP GLY GLN GLY THR GLN SEQRES 40 F 522 VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS GLU PRO SEQRES 41 F 522 GLU ALA HET ABU A 501 7 HET NAG A 502 14 HET HSM B 601 8 HET NAG E 501 14 HET ABU D 501 7 HET NAG D 502 14 HET NAG G 1 14 HET NAG G 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 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 NAG J 1 14 HET NAG J 2 14 HET NAG K 1 14 HET NAG K 2 14 HET BMA K 3 11 HET MAN K 4 11 HET MAN K 5 11 HETNAM ABU GAMMA-AMINO-BUTANOIC ACID HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM HSM HISTAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETSYN ABU GAMMA(AMINO)-BUTYRIC ACID FORMUL 7 ABU 2(C4 H9 N O2) FORMUL 8 NAG 13(C8 H15 N O6) FORMUL 9 HSM C5 H9 N3 FORMUL 14 BMA 3(C6 H12 O6) FORMUL 14 MAN 6(C6 H12 O6) HELIX 1 AA1 THR A 13 LEU A 23 1 11 HELIX 2 AA2 GLU A 73 LYS A 76 5 4 HELIX 3 AA3 ASN A 88 LYS A 93 1 6 HELIX 4 AA4 HIS A 142 PHE A 146 5 5 HELIX 5 AA5 GLU A 174 VAL A 179 1 6 HELIX 6 AA6 ILE A 223 THR A 230 1 8 HELIX 7 AA7 THR A 230 SER A 244 1 15 HELIX 8 AA8 SER A 251 LEU A 277 1 27 HELIX 9 AA9 ALA A 285 GLN A 314 1 30 HELIX 10 AB1 ALA A 316 ARG A 418 1 32 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 SER B 239 1 22 HELIX 17 AB8 PHE B 240 ILE B 242 5 3 HELIX 18 AB9 ALA B 246 ARG B 269 1 24 HELIX 19 AC1 GLU B 270 LEU B 272 5 3 HELIX 20 AC2 LYS B 279 SER B 308 1 30 HELIX 21 AC3 TYR B 415 VAL B 447 1 33 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 TYR C 220 THR C 225 1 6 HELIX 27 AC9 THR C 225 ILE C 242 1 18 HELIX 28 AD1 ALA C 246 LEU C 268 1 23 HELIX 29 AD2 ARG C 269 THR C 271 5 3 HELIX 30 AD3 LYS C 279 SER C 308 1 30 HELIX 31 AD4 ALA C 420 VAL C 447 1 28 HELIX 32 AD5 MET E 9 LEU E 20 1 12 HELIX 33 AD6 LYS E 70 ALA E 73 5 4 HELIX 34 AD7 ARG E 86 LEU E 91 1 6 HELIX 35 AD8 ASP E 139 TYR E 143 5 5 HELIX 36 AD9 GLY E 170 LYS E 173 5 4 HELIX 37 AE1 ILE E 218 ASN E 243 1 26 HELIX 38 AE2 ALA E 246 GLU E 270 1 25 HELIX 39 AE3 ILE E 281 SER E 308 1 28 HELIX 40 AE4 LEU E 416 VAL E 447 1 32 HELIX 41 AE5 THR D 13 LEU D 23 1 11 HELIX 42 AE6 ASN D 88 LYS D 93 1 6 HELIX 43 AE7 HIS D 142 PHE D 146 5 5 HELIX 44 AE8 GLU D 174 SER D 178 1 5 HELIX 45 AE9 ILE D 223 THR D 230 1 8 HELIX 46 AF1 THR D 230 LEU D 247 1 18 HELIX 47 AF2 SER D 251 SER D 276 1 26 HELIX 48 AF3 THR D 284 THR D 311 1 28 HELIX 49 AF4 GLN D 314 ASN D 417 1 33 HELIX 50 AF5 THR F 415 TYR F 418 5 4 HELIX 51 AF6 ASP F 449 LYS F 452 5 4 HELIX 52 AF7 LYS F 474 THR F 478 5 5 SHEET 1 AA1 9 THR A 39 ASP A 44 0 SHEET 2 AA1 9 PHE A 46 SER A 54 0 SHEET 3 AA1 9 GLU A 59 LYS A 71 -1 O ASP A 63 N SER A 49 SHEET 4 AA1 9 VAL A 83 LEU A 86 0 SHEET 5 AA1 9 VAL A 108 ALA A 109 0 SHEET 6 AA1 9 LYS A 117 THR A 122 -1 O ILE A 121 N LEU A 84 SHEET 7 AA1 9 THR A 126 GLU A 138 -1 O THR A 126 N THR A 122 SHEET 8 AA1 9 VAL A 167 TRP A 171 1 O VAL A 168 N THR A 39 SHEET 9 AA1 9 VAL A 180 VAL A 181 1 O VAL A 180 N VAL A 47 SHEET 1 AA2 4 THR A 99 PHE A 101 0 SHEET 2 AA2 4 ALA A 150 SER A 159 -1 O GLY A 158 N PHE A 100 SHEET 3 AA2 4 GLU A 209 ARG A 221 -1 O MET A 213 N PHE A 157 SHEET 4 AA2 4 TYR A 191 GLN A 204 -1 N THR A 197 O HIS A 216 SHEET 1 AA3 9 VAL B 36 SER B 46 0 SHEET 2 AA3 9 VAL B 50 SER B 51 0 SHEET 3 AA3 9 ASP B 56 ARG B 68 -1 O ASP B 56 N SER B 51 SHEET 4 AA3 9 LEU B 81 LEU B 83 0 SHEET 5 AA3 9 ASP B 101 VAL B 106 0 SHEET 6 AA3 9 ARG B 114 LEU B 118 -1 O LEU B 118 N LEU B 81 SHEET 7 AA3 9 THR B 123 ALA B 135 -1 O LEU B 125 N ARG B 117 SHEET 8 AA3 9 ILE B 164 TRP B 168 1 O GLU B 165 N VAL B 38 SHEET 9 AA3 9 VAL B 175 THR B 176 1 O THR B 176 N ILE B 42 SHEET 1 AA4 4 THR B 96 PHE B 98 0 SHEET 2 AA4 4 GLU B 147 SER B 156 -1 O GLU B 155 N TYR B 97 SHEET 3 AA4 4 ALA B 204 ARG B 216 -1 O LEU B 210 N LEU B 152 SHEET 4 AA4 4 PHE B 186 VAL B 199 -1 N VAL B 189 O ARG B 213 SHEET 1 AA5 8 VAL C 36 SER C 51 0 SHEET 2 AA5 8 ASP C 56 ARG C 68 -1 O TYR C 66 N GLY C 39 SHEET 3 AA5 8 THR C 82 LEU C 83 0 SHEET 4 AA5 8 PHE C 105 VAL C 106 0 SHEET 5 AA5 8 ARG C 114 LEU C 118 -1 O ILE C 116 N LEU C 83 SHEET 6 AA5 8 THR C 123 ALA C 135 -1 O LEU C 125 N ARG C 117 SHEET 7 AA5 8 ILE C 164 TRP C 168 1 O GLU C 165 N VAL C 38 SHEET 8 AA5 8 VAL C 175 THR C 176 1 O THR C 176 N ILE C 44 SHEET 1 AA6 4 THR C 96 PHE C 98 0 SHEET 2 AA6 4 GLU C 147 SER C 156 -1 O GLU C 155 N TYR C 97 SHEET 3 AA6 4 ALA C 204 ARG C 216 -1 O PHE C 212 N CYS C 150 SHEET 4 AA6 4 PHE C 186 VAL C 199 -1 N SER C 187 O LYS C 215 SHEET 1 AA7 9 VAL E 36 SER E 46 0 SHEET 2 AA7 9 VAL E 50 SER E 51 0 SHEET 3 AA7 9 ASP E 56 ARG E 68 -1 O ASP E 56 N SER E 51 SHEET 4 AA7 9 LEU E 81 LEU E 83 0 SHEET 5 AA7 9 ASP E 101 VAL E 106 0 SHEET 6 AA7 9 ARG E 114 LEU E 118 -1 O LEU E 118 N LEU E 81 SHEET 7 AA7 9 THR E 123 ALA E 135 -1 O LEU E 125 N ARG E 117 SHEET 8 AA7 9 ILE E 164 TRP E 168 1 O GLU E 165 N VAL E 38 SHEET 9 AA7 9 VAL E 175 THR E 176 1 O THR E 176 N ILE E 44 SHEET 1 AA8 4 THR E 96 PHE E 98 0 SHEET 2 AA8 4 GLU E 147 SER E 156 -1 O GLU E 155 N TYR E 97 SHEET 3 AA8 4 ALA E 204 ARG E 216 -1 O LEU E 208 N ILE E 154 SHEET 4 AA8 4 PHE E 186 VAL E 199 -1 N GLU E 190 O ARG E 213 SHEET 1 AA9 8 THR D 39 SER D 54 0 SHEET 2 AA9 8 GLU D 59 LYS D 71 -1 O ARG D 67 N ASP D 44 SHEET 3 AA9 8 VAL D 83 LEU D 86 0 SHEET 4 AA9 8 VAL D 108 ALA D 109 0 SHEET 5 AA9 8 LYS D 117 THR D 122 -1 O ILE D 121 N LEU D 84 SHEET 6 AA9 8 THR D 126 GLU D 138 -1 O LEU D 128 N ARG D 120 SHEET 7 AA9 8 VAL D 167 TRP D 171 1 O GLU D 170 N THR D 43 SHEET 8 AA9 8 VAL D 179 VAL D 181 1 O VAL D 180 N VAL D 47 SHEET 1 AB1 4 THR D 99 PHE D 101 0 SHEET 2 AB1 4 ALA D 150 SER D 159 -1 O GLY D 158 N PHE D 100 SHEET 3 AB1 4 GLU D 209 ARG D 221 -1 O PHE D 217 N CYS D 153 SHEET 4 AB1 4 TYR D 191 GLN D 204 -1 N VAL D 203 O TYR D 210 SHEET 1 AB2 2 VAL F 2 GLN F 3 0 SHEET 2 AB2 2 SER F 412 GLY F 413 -1 O SER F 412 N GLN F 3 SHEET 1 AB3 4 GLU F 6 SER F 7 0 SHEET 2 AB3 4 ARG F 406 ALA F 410 -1 O SER F 408 N SER F 7 SHEET 3 AB3 4 THR F 465 MET F 470 -1 O VAL F 466 N CYS F 409 SHEET 4 AB3 4 PHE F 455 ASP F 460 -1 N ASP F 460 O THR F 465 SHEET 1 AB4 6 MET F 421 GLN F 426 0 SHEET 2 AB4 6 GLU F 433 ILE F 438 -1 O ILE F 438 N MET F 421 SHEET 3 AB4 6 THR F 445 TYR F 447 -1 O SER F 446 N ALA F 437 SHEET 4 AB4 6 ALA F 479 ALA F 485 -1 O VAL F 480 N GLN F 426 SHEET 5 AB4 6 TYR F 501 TRP F 502 -1 O TYR F 501 N ALA F 485 SHEET 6 AB4 6 THR F 506 VAL F 508 -1 O THR F 506 N TYR F 481 SSBOND 1 CYS A 139 CYS A 153 1555 1555 2.03 SSBOND 2 CYS B 136 CYS B 150 1555 1555 2.03 SSBOND 3 CYS C 136 CYS C 150 1555 1555 2.04 SSBOND 4 CYS E 136 CYS E 150 1555 1555 2.03 SSBOND 5 CYS D 139 CYS D 153 1555 1555 2.04 SSBOND 6 CYS F 409 CYS F 483 1555 1555 2.03 LINK ND2 ASN A 111 C1 NAG A 502 1555 1555 1.45 LINK ND2 ASN B 80 C1 NAG G 1 1555 1555 1.54 LINK ND2 ASN B 149 C1 NAG H 1 1555 1555 1.48 LINK ND2 ASN C 80 C1 NAG J 1 1555 1555 1.46 LINK ND2 ASN C 149 C1 NAG I 1 1555 1555 1.47 LINK ND2 ASN E 80 C1 NAG E 501 1555 1555 1.52 LINK ND2 ASN E 149 C1 NAG K 1 1555 1555 1.50 LINK ND2 ASN D 111 C1 NAG D 502 1555 1555 1.46 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.46 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.41 LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.43 LINK O3 BMA H 3 C1 MAN H 4 1555 1555 1.43 LINK O6 BMA H 3 C1 MAN H 5 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.44 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.43 LINK O6 BMA I 3 C1 MAN I 5 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.43 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44 LINK O3 BMA K 3 C1 MAN K 4 1555 1555 1.43 LINK O6 BMA K 3 C1 MAN K 5 1555 1555 1.45 CISPEP 1 PHE A 146 PRO A 147 0 -1.61 CISPEP 2 TYR B 143 PRO B 144 0 -1.57 CISPEP 3 TYR C 143 PRO C 144 0 -0.22 CISPEP 4 TYR E 143 PRO E 144 0 -2.16 CISPEP 5 PHE D 146 PRO D 147 0 -2.87 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