HEADER IMMUNE SYSTEM 20-JUN-22 8DE6 TITLE OLIGOMERIC C9 IN COMPLEX WITH AE11 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: AE11 FAB VH; COMPND 3 CHAIN: E, B; COMPND 4 OTHER_DETAILS: PAPAIN-TREATED IGG; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: AE11 FAB VL; COMPND 7 CHAIN: F, I; COMPND 8 OTHER_DETAILS: PAPAIN-DIGESTED IGG; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: COMPLEMENT COMPONENT C9; COMPND 11 CHAIN: A, C, G; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 7 ORGANISM_COMMON: MOUSE; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 MOL_ID: 3; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 CELL_LINE: HEPATOCYTES; SOURCE 14 GENE: C9; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293 EXPI KEYWDS MEMBRANE ATTACK COMPLEX, COMPLEMENT COMPONENT 9, POLYC9, AE11, IMMUNE KEYWDS 2 SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR C.BAYLY-JONES JRNL AUTH C.BAYLY-JONES,B.H.T.HO,C.LAU,E.W.W.LEUNG,L.D'ANDREA, JRNL AUTH 2 C.J.LUPTON,S.M.EKKEL,H.VENUGOPAL,J.C.WHISSTOCK,T.E.MOLLNES, JRNL AUTH 3 B.A.SPICER,M.A.DUNSTONE JRNL TITL THE NEOEPITOPE OF THE COMPLEMENT C5B-9 MEMBRANE ATTACK JRNL TITL 2 COMPLEX IS FORMED BY PROXIMITY OF ADJACENT ANCILLARY REGIONS JRNL TITL 3 OF C9. JRNL REF COMMUN BIOL V. 6 42 2023 JRNL REFN ESSN 2399-3642 JRNL PMID 36639734 JRNL DOI 10.1038/S42003-023-04431-Y REMARK 2 REMARK 2 RESOLUTION. 3.20 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 : 6DLW REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : 163.000 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) : 3.200 REMARK 3 NUMBER OF PARTICLES : 10061 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 8DE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000266499. 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 : QUATERNARY COMPLEX OF AE11 FAB REMARK 245 AND POLYC9 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : FAB FRAGMENT OF AE11 GENERATED REMARK 245 BY PROTEOLYTIC CLEAVAGE OF AE11 IGG ANTIBODY, IN COMPLEX WITH REMARK 245 RECOMBINANT HUMAN C9 INCUBATED AT 37 DEGREES CELSIUS TO FORM REMARK 245 HOMO-OLIGOMERIC C9. 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) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 52.40 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 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: HEPTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, A, B, I, C, G REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET E 1 REMARK 465 ALA E 2 REMARK 465 VAL E 3 REMARK 465 LEU E 4 REMARK 465 ALA E 5 REMARK 465 LEU E 6 REMARK 465 LEU E 7 REMARK 465 PHE E 8 REMARK 465 CYS E 9 REMARK 465 LEU E 10 REMARK 465 VAL E 11 REMARK 465 THR E 12 REMARK 465 PHE E 13 REMARK 465 PRO E 14 REMARK 465 SER E 15 REMARK 465 CYS E 16 REMARK 465 ILE E 17 REMARK 465 LEU E 18 REMARK 465 SER E 19 REMARK 465 MET F 1 REMARK 465 SER F 2 REMARK 465 SER F 3 REMARK 465 ALA F 4 REMARK 465 GLN F 5 REMARK 465 PHE F 6 REMARK 465 LEU F 7 REMARK 465 GLY F 8 REMARK 465 LEU F 9 REMARK 465 LEU F 10 REMARK 465 LEU F 11 REMARK 465 LEU F 12 REMARK 465 CYS F 13 REMARK 465 PHE F 14 REMARK 465 GLN F 15 REMARK 465 GLY F 16 REMARK 465 THR F 17 REMARK 465 ARG F 18 REMARK 465 CYS F 19 REMARK 465 MET A -25 REMARK 465 GLU A -24 REMARK 465 THR A -23 REMARK 465 ASP A -22 REMARK 465 THR A -21 REMARK 465 LEU A -20 REMARK 465 LEU A -19 REMARK 465 LEU A -18 REMARK 465 TRP A -17 REMARK 465 VAL A -16 REMARK 465 LEU A -15 REMARK 465 LEU A -14 REMARK 465 LEU A -13 REMARK 465 TRP A -12 REMARK 465 VAL A -11 REMARK 465 PRO A -10 REMARK 465 GLY A -9 REMARK 465 SER A -8 REMARK 465 THR A -7 REMARK 465 GLY A -6 REMARK 465 ASP A -5 REMARK 465 ALA A -4 REMARK 465 ALA A -3 REMARK 465 GLN A -2 REMARK 465 PRO A -1 REMARK 465 ALA A 0 REMARK 465 GLN A 1 REMARK 465 TYR A 2 REMARK 465 THR A 3 REMARK 465 THR A 4 REMARK 465 SER A 5 REMARK 465 TYR A 6 REMARK 465 ASP A 7 REMARK 465 PRO A 8 REMARK 465 GLU A 9 REMARK 465 LEU A 10 REMARK 465 THR A 11 REMARK 465 GLU A 12 REMARK 465 SER A 13 REMARK 465 SER A 14 REMARK 465 GLY A 15 REMARK 465 SER A 16 REMARK 465 ALA A 17 REMARK 465 PHE A 202A REMARK 465 LYS A 202B REMARK 465 SER A 202C REMARK 465 ILE A 202D REMARK 465 ILE A 202E REMARK 465 GLN A 202F REMARK 465 GLU A 202G REMARK 465 LYS A 202H REMARK 465 THR A 202I REMARK 465 SER A 202J REMARK 465 ASN A 202K REMARK 465 PHE A 202L REMARK 465 ASN A 202M REMARK 465 ALA A 202N REMARK 465 ALA A 202O REMARK 465 ILE A 202P REMARK 465 SER A 202Q REMARK 465 LEU A 202R REMARK 465 LYS A 202S REMARK 465 PHE A 202T REMARK 465 THR A 202U REMARK 465 PRO A 202V REMARK 465 THR A 202W REMARK 465 GLU A 202X REMARK 465 THR A 202Y REMARK 465 ASN A 202Z REMARK 465 LYS A 203A REMARK 465 ALA A 203B REMARK 465 GLU A 203C REMARK 465 GLN A 203D REMARK 465 CYS A 203E REMARK 465 CYS A 203F REMARK 465 GLU A 203G REMARK 465 GLU A 203H REMARK 465 THR A 203I REMARK 465 ALA A 203J REMARK 465 SER A 203K REMARK 465 SER A 203L REMARK 465 ILE A 203M REMARK 465 SER A 203N REMARK 465 LEU A 203O REMARK 465 HIS A 203P REMARK 465 GLY A 203Q REMARK 465 LYS A 203R REMARK 465 GLY A 203S REMARK 465 SER A 203T REMARK 465 PHE A 203U REMARK 465 ARG A 203V REMARK 465 PHE A 203W REMARK 465 SER A 203X REMARK 465 TYR A 203Y REMARK 465 SER A 203Z REMARK 465 LYS A 204A REMARK 465 ASN A 204B REMARK 465 GLU A 204C REMARK 465 THR A 204D REMARK 465 TYR A 204E REMARK 465 GLN A 204F REMARK 465 LEU A 204G REMARK 465 PHE A 204H REMARK 465 LEU A 204I REMARK 465 GLY A 318A REMARK 465 VAL A 318B REMARK 465 GLU A 318C REMARK 465 LEU A 318D REMARK 465 LYS A 318E REMARK 465 ASP A 318F REMARK 465 ILE A 318G REMARK 465 LYS A 318H REMARK 465 ARG A 318I REMARK 465 CYS A 318J REMARK 465 LEU A 318K REMARK 465 GLY A 318L REMARK 465 TYR A 318M REMARK 465 HIS A 318N REMARK 465 LEU A 318O REMARK 465 ASP A 318P REMARK 465 VAL A 318Q REMARK 465 SER A 318R REMARK 465 LEU A 318S REMARK 465 ALA A 318T REMARK 465 PHE A 318U REMARK 465 SER A 318V REMARK 465 GLU A 318W REMARK 465 ILE A 318X REMARK 465 SER A 318Y REMARK 465 VAL A 318Z REMARK 465 GLY A 319A REMARK 465 ALA A 319B REMARK 465 GLU A 319C REMARK 465 PHE A 319D REMARK 465 ASN A 319E REMARK 465 LYS A 319F REMARK 465 ASP A 319G REMARK 465 ASP A 319H REMARK 465 CYS A 319I REMARK 465 VAL A 319J REMARK 465 LYS A 319K REMARK 465 ARG A 319L REMARK 465 GLY A 319M REMARK 465 GLU A 319N REMARK 465 GLY A 319O REMARK 465 ARG A 319P REMARK 465 ALA A 319Q REMARK 465 GLN A 478 REMARK 465 LYS A 479 REMARK 465 ILE A 480 REMARK 465 SER A 481 REMARK 465 GLU A 482 REMARK 465 GLY A 483 REMARK 465 LEU A 484 REMARK 465 PRO A 485 REMARK 465 ALA A 486 REMARK 465 LEU A 487 REMARK 465 GLU A 488 REMARK 465 PHE A 489 REMARK 465 PRO A 490 REMARK 465 ASN A 491 REMARK 465 GLU A 492 REMARK 465 LYS A 493 REMARK 465 MET B 1 REMARK 465 ALA B 2 REMARK 465 VAL B 3 REMARK 465 LEU B 4 REMARK 465 ALA B 5 REMARK 465 LEU B 6 REMARK 465 LEU B 7 REMARK 465 PHE B 8 REMARK 465 CYS B 9 REMARK 465 LEU B 10 REMARK 465 VAL B 11 REMARK 465 THR B 12 REMARK 465 PHE B 13 REMARK 465 PRO B 14 REMARK 465 SER B 15 REMARK 465 CYS B 16 REMARK 465 ILE B 17 REMARK 465 LEU B 18 REMARK 465 SER B 19 REMARK 465 MET I 1 REMARK 465 SER I 2 REMARK 465 SER I 3 REMARK 465 ALA I 4 REMARK 465 GLN I 5 REMARK 465 PHE I 6 REMARK 465 LEU I 7 REMARK 465 GLY I 8 REMARK 465 LEU I 9 REMARK 465 LEU I 10 REMARK 465 LEU I 11 REMARK 465 LEU I 12 REMARK 465 CYS I 13 REMARK 465 PHE I 14 REMARK 465 GLN I 15 REMARK 465 GLY I 16 REMARK 465 THR I 17 REMARK 465 ARG I 18 REMARK 465 CYS I 19 REMARK 465 MET C -25 REMARK 465 GLU C -24 REMARK 465 THR C -23 REMARK 465 ASP C -22 REMARK 465 THR C -21 REMARK 465 LEU C -20 REMARK 465 LEU C -19 REMARK 465 LEU C -18 REMARK 465 TRP C -17 REMARK 465 VAL C -16 REMARK 465 LEU C -15 REMARK 465 LEU C -14 REMARK 465 LEU C -13 REMARK 465 TRP C -12 REMARK 465 VAL C -11 REMARK 465 PRO C -10 REMARK 465 GLY C -9 REMARK 465 SER C -8 REMARK 465 THR C -7 REMARK 465 GLY C -6 REMARK 465 ASP C -5 REMARK 465 ALA C -4 REMARK 465 ALA C -3 REMARK 465 GLN C -2 REMARK 465 PRO C -1 REMARK 465 ALA C 0 REMARK 465 GLN C 1 REMARK 465 TYR C 2 REMARK 465 THR C 3 REMARK 465 THR C 4 REMARK 465 SER C 5 REMARK 465 TYR C 6 REMARK 465 ASP C 7 REMARK 465 PRO C 8 REMARK 465 GLU C 9 REMARK 465 LEU C 10 REMARK 465 THR C 11 REMARK 465 GLU C 12 REMARK 465 SER C 13 REMARK 465 SER C 14 REMARK 465 GLY C 15 REMARK 465 SER C 16 REMARK 465 ALA C 17 REMARK 465 PHE C 202A REMARK 465 LYS C 202B REMARK 465 SER C 202C REMARK 465 ILE C 202D REMARK 465 ILE C 202E REMARK 465 GLN C 202F REMARK 465 GLU C 202G REMARK 465 LYS C 202H REMARK 465 THR C 202I REMARK 465 SER C 202J REMARK 465 ASN C 202K REMARK 465 PHE C 202L REMARK 465 ASN C 202M REMARK 465 ALA C 202N REMARK 465 ALA C 202O REMARK 465 ILE C 202P REMARK 465 SER C 202Q REMARK 465 LEU C 202R REMARK 465 LYS C 202S REMARK 465 PHE C 202T REMARK 465 THR C 202U REMARK 465 PRO C 202V REMARK 465 THR C 202W REMARK 465 GLU C 202X REMARK 465 THR C 202Y REMARK 465 ASN C 202Z REMARK 465 LYS C 203A REMARK 465 ALA C 203B REMARK 465 GLU C 203C REMARK 465 GLN C 203D REMARK 465 CYS C 203E REMARK 465 CYS C 203F REMARK 465 GLU C 203G REMARK 465 GLU C 203H REMARK 465 THR C 203I REMARK 465 ALA C 203J REMARK 465 SER C 203K REMARK 465 SER C 203L REMARK 465 ILE C 203M REMARK 465 SER C 203N REMARK 465 LEU C 203O REMARK 465 HIS C 203P REMARK 465 GLY C 203Q REMARK 465 LYS C 203R REMARK 465 GLY C 203S REMARK 465 SER C 203T REMARK 465 PHE C 203U REMARK 465 ARG C 203V REMARK 465 PHE C 203W REMARK 465 SER C 203X REMARK 465 TYR C 203Y REMARK 465 SER C 203Z REMARK 465 LYS C 204A REMARK 465 ASN C 204B REMARK 465 GLU C 204C REMARK 465 THR C 204D REMARK 465 TYR C 204E REMARK 465 GLN C 204F REMARK 465 LEU C 204G REMARK 465 PHE C 204H REMARK 465 LEU C 204I REMARK 465 GLY C 318A REMARK 465 VAL C 318B REMARK 465 GLU C 318C REMARK 465 LEU C 318D REMARK 465 LYS C 318E REMARK 465 ASP C 318F REMARK 465 ILE C 318G REMARK 465 LYS C 318H REMARK 465 ARG C 318I REMARK 465 CYS C 318J REMARK 465 LEU C 318K REMARK 465 GLY C 318L REMARK 465 TYR C 318M REMARK 465 HIS C 318N REMARK 465 LEU C 318O REMARK 465 ASP C 318P REMARK 465 VAL C 318Q REMARK 465 SER C 318R REMARK 465 LEU C 318S REMARK 465 ALA C 318T REMARK 465 PHE C 318U REMARK 465 SER C 318V REMARK 465 GLU C 318W REMARK 465 ILE C 318X REMARK 465 SER C 318Y REMARK 465 VAL C 318Z REMARK 465 GLY C 319A REMARK 465 ALA C 319B REMARK 465 GLU C 319C REMARK 465 PHE C 319D REMARK 465 ASN C 319E REMARK 465 LYS C 319F REMARK 465 ASP C 319G REMARK 465 ASP C 319H REMARK 465 CYS C 319I REMARK 465 VAL C 319J REMARK 465 LYS C 319K REMARK 465 ARG C 319L REMARK 465 GLY C 319M REMARK 465 GLU C 319N REMARK 465 GLY C 319O REMARK 465 ARG C 319P REMARK 465 ALA C 319Q REMARK 465 GLN C 478 REMARK 465 LYS C 479 REMARK 465 ILE C 480 REMARK 465 SER C 481 REMARK 465 GLU C 482 REMARK 465 GLY C 483 REMARK 465 LEU C 484 REMARK 465 PRO C 485 REMARK 465 ALA C 486 REMARK 465 LEU C 487 REMARK 465 GLU C 488 REMARK 465 PHE C 489 REMARK 465 PRO C 490 REMARK 465 ASN C 491 REMARK 465 GLU C 492 REMARK 465 LYS C 493 REMARK 465 MET G -25 REMARK 465 GLU G -24 REMARK 465 THR G -23 REMARK 465 ASP G -22 REMARK 465 THR G -21 REMARK 465 LEU G -20 REMARK 465 LEU G -19 REMARK 465 LEU G -18 REMARK 465 TRP G -17 REMARK 465 VAL G -16 REMARK 465 LEU G -15 REMARK 465 LEU G -14 REMARK 465 LEU G -13 REMARK 465 TRP G -12 REMARK 465 VAL G -11 REMARK 465 PRO G -10 REMARK 465 GLY G -9 REMARK 465 SER G -8 REMARK 465 THR G -7 REMARK 465 GLY G -6 REMARK 465 ASP G -5 REMARK 465 ALA G -4 REMARK 465 ALA G -3 REMARK 465 GLN G -2 REMARK 465 PRO G -1 REMARK 465 ALA G 0 REMARK 465 GLN G 1 REMARK 465 TYR G 2 REMARK 465 THR G 3 REMARK 465 THR G 4 REMARK 465 SER G 5 REMARK 465 TYR G 6 REMARK 465 ASP G 7 REMARK 465 PRO G 8 REMARK 465 GLU G 9 REMARK 465 LEU G 10 REMARK 465 THR G 11 REMARK 465 GLU G 12 REMARK 465 SER G 13 REMARK 465 SER G 14 REMARK 465 GLY G 15 REMARK 465 SER G 16 REMARK 465 ALA G 17 REMARK 465 PHE G 202A REMARK 465 LYS G 202B REMARK 465 SER G 202C REMARK 465 ILE G 202D REMARK 465 ILE G 202E REMARK 465 GLN G 202F REMARK 465 GLU G 202G REMARK 465 LYS G 202H REMARK 465 THR G 202I REMARK 465 SER G 202J REMARK 465 ASN G 202K REMARK 465 PHE G 202L REMARK 465 ASN G 202M REMARK 465 ALA G 202N REMARK 465 ALA G 202O REMARK 465 ILE G 202P REMARK 465 SER G 202Q REMARK 465 LEU G 202R REMARK 465 LYS G 202S REMARK 465 PHE G 202T REMARK 465 THR G 202U REMARK 465 PRO G 202V REMARK 465 THR G 202W REMARK 465 GLU G 202X REMARK 465 THR G 202Y REMARK 465 ASN G 202Z REMARK 465 LYS G 203A REMARK 465 ALA G 203B REMARK 465 GLU G 203C REMARK 465 GLN G 203D REMARK 465 CYS G 203E REMARK 465 CYS G 203F REMARK 465 GLU G 203G REMARK 465 GLU G 203H REMARK 465 THR G 203I REMARK 465 ALA G 203J REMARK 465 SER G 203K REMARK 465 SER G 203L REMARK 465 ILE G 203M REMARK 465 SER G 203N REMARK 465 LEU G 203O REMARK 465 HIS G 203P REMARK 465 GLY G 203Q REMARK 465 LYS G 203R REMARK 465 GLY G 203S REMARK 465 SER G 203T REMARK 465 PHE G 203U REMARK 465 ARG G 203V REMARK 465 PHE G 203W REMARK 465 SER G 203X REMARK 465 TYR G 203Y REMARK 465 SER G 203Z REMARK 465 LYS G 204A REMARK 465 ASN G 204B REMARK 465 GLU G 204C REMARK 465 THR G 204D REMARK 465 TYR G 204E REMARK 465 GLN G 204F REMARK 465 LEU G 204G REMARK 465 PHE G 204H REMARK 465 LEU G 204I REMARK 465 GLY G 318A REMARK 465 VAL G 318B REMARK 465 GLU G 318C REMARK 465 LEU G 318D REMARK 465 LYS G 318E REMARK 465 ASP G 318F REMARK 465 ILE G 318G REMARK 465 LYS G 318H REMARK 465 ARG G 318I REMARK 465 CYS G 318J REMARK 465 LEU G 318K REMARK 465 GLY G 318L REMARK 465 TYR G 318M REMARK 465 HIS G 318N REMARK 465 LEU G 318O REMARK 465 ASP G 318P REMARK 465 VAL G 318Q REMARK 465 SER G 318R REMARK 465 LEU G 318S REMARK 465 ALA G 318T REMARK 465 PHE G 318U REMARK 465 SER G 318V REMARK 465 GLU G 318W REMARK 465 ILE G 318X REMARK 465 SER G 318Y REMARK 465 VAL G 318Z REMARK 465 GLY G 319A REMARK 465 ALA G 319B REMARK 465 GLU G 319C REMARK 465 PHE G 319D REMARK 465 ASN G 319E REMARK 465 LYS G 319F REMARK 465 ASP G 319G REMARK 465 ASP G 319H REMARK 465 CYS G 319I REMARK 465 VAL G 319J REMARK 465 LYS G 319K REMARK 465 ARG G 319L REMARK 465 GLY G 319M REMARK 465 GLU G 319N REMARK 465 GLY G 319O REMARK 465 ARG G 319P REMARK 465 ALA G 319Q REMARK 465 GLN G 478 REMARK 465 LYS G 479 REMARK 465 ILE G 480 REMARK 465 SER G 481 REMARK 465 GLU G 482 REMARK 465 GLY G 483 REMARK 465 LEU G 484 REMARK 465 PRO G 485 REMARK 465 ALA G 486 REMARK 465 LEU G 487 REMARK 465 GLU G 488 REMARK 465 PHE G 489 REMARK 465 PRO G 490 REMARK 465 ASN G 491 REMARK 465 GLU G 492 REMARK 465 LYS G 493 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 CD1 TRP A 30 O5 BMA A 603 1.41 REMARK 500 CD1 TRP C 30 C1 BMA C 603 1.48 REMARK 500 CD1 TRP C 27 C1 BMA C 602 1.49 REMARK 500 CD1 TRP G 27 C1 BMA G 602 1.49 REMARK 500 CD1 TRP G 30 C1 BMA G 603 1.49 REMARK 500 CD1 TRP A 30 C1 BMA A 603 1.49 REMARK 500 CD1 TRP A 27 C1 BMA A 602 1.49 REMARK 500 NE1 TRP A 30 C1 BMA A 603 1.66 REMARK 500 OG1 THR A 452 C2 NAG A 601 1.75 REMARK 500 OG1 THR G 452 C2 NAG G 601 1.79 REMARK 500 NE1 TRP C 30 C1 BMA C 603 1.91 REMARK 500 NE1 TRP G 27 C1 BMA G 602 1.93 REMARK 500 CD1 TRP G 27 O5 BMA G 602 1.97 REMARK 500 NE1 TRP G 30 C1 BMA G 603 2.01 REMARK 500 CD1 TRP C 30 O5 BMA C 603 2.04 REMARK 500 NE1 TRP A 27 C1 BMA A 602 2.04 REMARK 500 CD1 TRP G 30 O5 BMA G 603 2.13 REMARK 500 NE1 TRP C 27 C1 BMA C 602 2.16 REMARK 500 OD2 ASP G 270 OH TYR G 290 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU E 82 30.82 -98.80 REMARK 500 THR F 70 -14.17 75.48 REMARK 500 ARG F 72 121.32 -172.51 REMARK 500 THR F 88 -33.70 -133.98 REMARK 500 GLU A 116 75.25 54.24 REMARK 500 ASP A 123 -1.26 74.94 REMARK 500 GLU A 197 119.46 -160.16 REMARK 500 SER A 236 138.94 -170.51 REMARK 500 HIS A 244 117.56 -160.06 REMARK 500 ARG A 368 2.56 -67.93 REMARK 500 LYS A 369 -62.43 -97.66 REMARK 500 ALA A 399 74.28 -150.38 REMARK 500 SER B 26 -139.60 61.88 REMARK 500 SER B 95 61.91 60.36 REMARK 500 THR I 70 -10.68 70.42 REMARK 500 ALA I 103 -167.06 -161.85 REMARK 500 ASP C 106 23.16 -143.14 REMARK 500 GLU C 116 70.36 53.04 REMARK 500 ASP C 123 -5.80 67.45 REMARK 500 SER C 236 143.04 -170.41 REMARK 500 ARG C 368 2.50 -65.55 REMARK 500 LYS C 369 -60.60 -97.45 REMARK 500 ALA C 399 74.78 -153.17 REMARK 500 ASP G 106 24.84 -140.72 REMARK 500 GLU G 116 70.24 52.11 REMARK 500 ASP G 123 -6.04 78.68 REMARK 500 SER G 236 139.31 -171.97 REMARK 500 THR G 277 -168.84 -79.88 REMARK 500 MET G 315 111.83 -161.52 REMARK 500 ARG G 368 4.58 -67.28 REMARK 500 ALA G 399 82.96 -152.11 REMARK 500 LYS G 406 88.48 -152.13 REMARK 500 PRO G 465 -167.48 -77.29 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 BMA A 602 REMARK 610 BMA A 603 REMARK 610 BMA C 602 REMARK 610 BMA C 603 REMARK 610 BMA G 602 REMARK 610 BMA G 603 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 CA A 604 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN A 99 OD1 REMARK 620 2 ASP A 101 O 102.6 REMARK 620 3 ASP A 103 OD2 102.2 107.5 REMARK 620 4 ASP A 109 OD2 130.1 114.0 98.0 REMARK 620 5 GLU A 110 OE2 82.3 65.2 172.3 83.5 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 604 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 LEU C 96 O REMARK 620 2 ASN C 99 OD1 65.7 REMARK 620 3 ASP C 101 O 164.4 124.3 REMARK 620 4 ASP C 103 OD2 81.1 101.4 106.4 REMARK 620 5 ASP C 109 OD2 77.3 134.7 88.1 97.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA G 604 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 LEU G 96 O REMARK 620 2 ASN G 99 OD1 82.1 REMARK 620 3 ASP G 101 O 155.5 74.5 REMARK 620 4 ASP G 103 OD2 66.7 87.2 104.6 REMARK 620 5 ASP G 109 OD2 68.0 141.7 136.2 101.5 REMARK 620 6 GLU G 110 OE2 106.7 82.6 77.6 168.7 83.6 REMARK 620 N 1 2 3 4 5 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-27385 RELATED DB: EMDB REMARK 900 OLIGOMERIC C9 IN COMPLEX WITH AE11 FAB DBREF 8DE6 E 1 140 PDB 8DE6 8DE6 1 140 DBREF 8DE6 F 1 126 PDB 8DE6 8DE6 1 126 DBREF 8DE6 A 0 493 UNP P02748 CO9_HUMAN 21 559 DBREF 8DE6 B 1 140 PDB 8DE6 8DE6 1 140 DBREF 8DE6 I 1 126 PDB 8DE6 8DE6 1 126 DBREF 8DE6 C 0 493 UNP P02748 CO9_HUMAN 21 559 DBREF 8DE6 G 0 493 UNP P02748 CO9_HUMAN 21 559 SEQADV 8DE6 MET A -25 UNP P02748 INITIATING METHIONINE SEQADV 8DE6 GLU A -24 UNP P02748 EXPRESSION TAG SEQADV 8DE6 THR A -23 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ASP A -22 UNP P02748 EXPRESSION TAG SEQADV 8DE6 THR A -21 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU A -20 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU A -19 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU A -18 UNP P02748 EXPRESSION TAG SEQADV 8DE6 TRP A -17 UNP P02748 EXPRESSION TAG SEQADV 8DE6 VAL A -16 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU A -15 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU A -14 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU A -13 UNP P02748 EXPRESSION TAG SEQADV 8DE6 TRP A -12 UNP P02748 EXPRESSION TAG SEQADV 8DE6 VAL A -11 UNP P02748 EXPRESSION TAG SEQADV 8DE6 PRO A -10 UNP P02748 EXPRESSION TAG SEQADV 8DE6 GLY A -9 UNP P02748 EXPRESSION TAG SEQADV 8DE6 SER A -8 UNP P02748 EXPRESSION TAG SEQADV 8DE6 THR A -7 UNP P02748 EXPRESSION TAG SEQADV 8DE6 GLY A -6 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ASP A -5 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ALA A -4 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ALA A -3 UNP P02748 EXPRESSION TAG SEQADV 8DE6 GLN A -2 UNP P02748 EXPRESSION TAG SEQADV 8DE6 PRO A -1 UNP P02748 EXPRESSION TAG SEQADV 8DE6 MET C -25 UNP P02748 INITIATING METHIONINE SEQADV 8DE6 GLU C -24 UNP P02748 EXPRESSION TAG SEQADV 8DE6 THR C -23 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ASP C -22 UNP P02748 EXPRESSION TAG SEQADV 8DE6 THR C -21 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU C -20 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU C -19 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU C -18 UNP P02748 EXPRESSION TAG SEQADV 8DE6 TRP C -17 UNP P02748 EXPRESSION TAG SEQADV 8DE6 VAL C -16 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU C -15 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU C -14 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU C -13 UNP P02748 EXPRESSION TAG SEQADV 8DE6 TRP C -12 UNP P02748 EXPRESSION TAG SEQADV 8DE6 VAL C -11 UNP P02748 EXPRESSION TAG SEQADV 8DE6 PRO C -10 UNP P02748 EXPRESSION TAG SEQADV 8DE6 GLY C -9 UNP P02748 EXPRESSION TAG SEQADV 8DE6 SER C -8 UNP P02748 EXPRESSION TAG SEQADV 8DE6 THR C -7 UNP P02748 EXPRESSION TAG SEQADV 8DE6 GLY C -6 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ASP C -5 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ALA C -4 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ALA C -3 UNP P02748 EXPRESSION TAG SEQADV 8DE6 GLN C -2 UNP P02748 EXPRESSION TAG SEQADV 8DE6 PRO C -1 UNP P02748 EXPRESSION TAG SEQADV 8DE6 MET G -25 UNP P02748 INITIATING METHIONINE SEQADV 8DE6 GLU G -24 UNP P02748 EXPRESSION TAG SEQADV 8DE6 THR G -23 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ASP G -22 UNP P02748 EXPRESSION TAG SEQADV 8DE6 THR G -21 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU G -20 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU G -19 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU G -18 UNP P02748 EXPRESSION TAG SEQADV 8DE6 TRP G -17 UNP P02748 EXPRESSION TAG SEQADV 8DE6 VAL G -16 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU G -15 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU G -14 UNP P02748 EXPRESSION TAG SEQADV 8DE6 LEU G -13 UNP P02748 EXPRESSION TAG SEQADV 8DE6 TRP G -12 UNP P02748 EXPRESSION TAG SEQADV 8DE6 VAL G -11 UNP P02748 EXPRESSION TAG SEQADV 8DE6 PRO G -10 UNP P02748 EXPRESSION TAG SEQADV 8DE6 GLY G -9 UNP P02748 EXPRESSION TAG SEQADV 8DE6 SER G -8 UNP P02748 EXPRESSION TAG SEQADV 8DE6 THR G -7 UNP P02748 EXPRESSION TAG SEQADV 8DE6 GLY G -6 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ASP G -5 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ALA G -4 UNP P02748 EXPRESSION TAG SEQADV 8DE6 ALA G -3 UNP P02748 EXPRESSION TAG SEQADV 8DE6 GLN G -2 UNP P02748 EXPRESSION TAG SEQADV 8DE6 PRO G -1 UNP P02748 EXPRESSION TAG SEQRES 1 E 140 MET ALA VAL LEU ALA LEU LEU PHE CYS LEU VAL THR PHE SEQRES 2 E 140 PRO SER CYS ILE LEU SER GLN VAL GLN LEU LYS GLU SER SEQRES 3 E 140 GLY PRO GLY LEU VAL ALA PRO SER GLN SER LEU SER ILE SEQRES 4 E 140 THR CYS THR VAL SER GLY PHE SER LEU THR VAL TYR GLY SEQRES 5 E 140 VAL ASN TRP ILE ARG GLN PRO PRO GLY LYS GLY LEU GLU SEQRES 6 E 140 TRP LEU GLY MET ILE TRP GLY ASP GLY SER THR ASP TYR SEQRES 7 E 140 ASN SER ALA LEU LYS SER ARG LEU SER ILE THR LYS ASP SEQRES 8 E 140 ASN SER LYS SER GLN VAL PHE LEU LYS MET ASN SER LEU SEQRES 9 E 140 GLN THR ASP ASP THR ALA ARG TYR TYR CYS ALA ARG ASP SEQRES 10 E 140 ARG SER TYR GLY GLY SER SER ALA TRP PHE GLY TYR TRP SEQRES 11 E 140 GLY GLN GLY THR LEU VAL THR VAL SER ALA SEQRES 1 F 126 MET SER SER ALA GLN PHE LEU GLY LEU LEU LEU LEU CYS SEQRES 2 F 126 PHE GLN GLY THR ARG CYS ASP ILE GLN MET THR GLN THR SEQRES 3 F 126 THR SER SER LEU SER ALA SER LEU GLY ASP ARG VAL THR SEQRES 4 F 126 ILE SER CYS ARG ALA SER HIS ASP ILE SER ASN TYR LEU SEQRES 5 F 126 ASN TRP TYR GLN GLN LYS PRO ASP GLY THR LEU LYS LEU SEQRES 6 F 126 LEU ILE TYR TYR THR SER ARG LEU HIS SER GLY VAL PRO SEQRES 7 F 126 SER ARG PHE SER GLY SER GLY SER GLY THR ASP TYR SER SEQRES 8 F 126 LEU THR ILE SER ASN LEU GLU GLN GLU ASP VAL ALA THR SEQRES 9 F 126 TYR PHE CYS GLN GLN GLY ASN TYR LEU PRO TYR THR PHE SEQRES 10 F 126 GLY GLY GLY THR LYS LEU GLU ILE LYS SEQRES 1 A 564 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 A 564 TRP VAL PRO GLY SER THR GLY ASP ALA ALA GLN PRO ALA SEQRES 3 A 564 GLN TYR THR THR SER TYR ASP PRO GLU LEU THR GLU SER SEQRES 4 A 564 SER GLY SER ALA SER HIS ILE ASP CYS ARG MET SER PRO SEQRES 5 A 564 TRP SER GLU TRP SER GLN CYS ASP PRO CYS LEU ARG GLN SEQRES 6 A 564 MET PHE ARG SER ARG SER ILE GLU VAL PHE GLY GLN PHE SEQRES 7 A 564 ASN GLY LYS ARG CYS THR ASP ALA VAL GLY ASP ARG ARG SEQRES 8 A 564 GLN CYS VAL PRO THR GLU PRO CYS GLU ASP ALA GLU ASP SEQRES 9 A 564 ASP CYS GLY ASN ASP PHE GLN CYS SER THR GLY ARG CYS SEQRES 10 A 564 ILE LYS MET ARG LEU ARG CYS ASN GLY ASP ASN ASP CYS SEQRES 11 A 564 GLY ASP PHE SER ASP GLU ASP ASP CYS GLU SER GLU PRO SEQRES 12 A 564 ARG PRO PRO CYS ARG ASP ARG VAL VAL GLU GLU SER GLU SEQRES 13 A 564 LEU ALA ARG THR ALA GLY TYR GLY ILE ASN ILE LEU GLY SEQRES 14 A 564 MET ASP PRO LEU SER THR PRO PHE ASP ASN GLU PHE TYR SEQRES 15 A 564 ASN GLY LEU CYS ASN ARG ASP ARG ASP GLY ASN THR LEU SEQRES 16 A 564 THR TYR TYR ARG ARG PRO TRP ASN VAL ALA SER LEU ILE SEQRES 17 A 564 TYR GLU THR LYS GLY GLU LYS ASN PHE ARG THR GLU HIS SEQRES 18 A 564 TYR GLU GLU GLN ILE GLU ALA PHE LYS SER ILE ILE GLN SEQRES 19 A 564 GLU LYS THR SER ASN PHE ASN ALA ALA ILE SER LEU LYS SEQRES 20 A 564 PHE THR PRO THR GLU THR ASN LYS ALA GLU GLN CYS CYS SEQRES 21 A 564 GLU GLU THR ALA SER SER ILE SER LEU HIS GLY LYS GLY SEQRES 22 A 564 SER PHE ARG PHE SER TYR SER LYS ASN GLU THR TYR GLN SEQRES 23 A 564 LEU PHE LEU SER TYR SER SER LYS LYS GLU LYS MET PHE SEQRES 24 A 564 LEU HIS VAL LYS GLY GLU ILE HIS LEU GLY ARG PHE VAL SEQRES 25 A 564 MET ARG ASN ARG ASP VAL VAL LEU THR THR THR PHE VAL SEQRES 26 A 564 ASP ASP ILE LYS ALA LEU PRO THR THR TYR GLU LYS GLY SEQRES 27 A 564 GLU TYR PHE ALA PHE LEU GLU THR TYR GLY THR HIS TYR SEQRES 28 A 564 SER SER SER GLY SER LEU GLY GLY LEU TYR GLU LEU ILE SEQRES 29 A 564 TYR VAL LEU ASP LYS ALA SER MET LYS ARG LYS GLY VAL SEQRES 30 A 564 GLU LEU LYS ASP ILE LYS ARG CYS LEU GLY TYR HIS LEU SEQRES 31 A 564 ASP VAL SER LEU ALA PHE SER GLU ILE SER VAL GLY ALA SEQRES 32 A 564 GLU PHE ASN LYS ASP ASP CYS VAL LYS ARG GLY GLU GLY SEQRES 33 A 564 ARG ALA VAL ASN ILE THR SER GLU ASN LEU ILE ASP ASP SEQRES 34 A 564 VAL VAL SER LEU ILE ARG GLY GLY THR ARG LYS TYR ALA SEQRES 35 A 564 PHE GLU LEU LYS GLU LYS LEU LEU ARG GLY THR VAL ILE SEQRES 36 A 564 ASP VAL THR ASP PHE VAL ASN TRP ALA SER SER ILE ASN SEQRES 37 A 564 ASP ALA PRO VAL LEU ILE SER GLN LYS LEU SER PRO ILE SEQRES 38 A 564 TYR ASN LEU VAL PRO VAL LYS MET LYS ASN ALA HIS LEU SEQRES 39 A 564 LYS LYS GLN ASN LEU GLU ARG ALA ILE GLU ASP TYR ILE SEQRES 40 A 564 ASN GLU PHE SER VAL ARG LYS CYS HIS THR CYS GLN ASN SEQRES 41 A 564 GLY GLY THR VAL ILE LEU MET ASP GLY LYS CYS LEU CYS SEQRES 42 A 564 ALA CYS PRO PHE LYS PHE GLU GLY ILE ALA CYS GLU ILE SEQRES 43 A 564 SER LYS GLN LYS ILE SER GLU GLY LEU PRO ALA LEU GLU SEQRES 44 A 564 PHE PRO ASN GLU LYS SEQRES 1 B 140 MET ALA VAL LEU ALA LEU LEU PHE CYS LEU VAL THR PHE SEQRES 2 B 140 PRO SER CYS ILE LEU SER GLN VAL GLN LEU LYS GLU SER SEQRES 3 B 140 GLY PRO GLY LEU VAL ALA PRO SER GLN SER LEU SER ILE SEQRES 4 B 140 THR CYS THR VAL SER GLY PHE SER LEU THR VAL TYR GLY SEQRES 5 B 140 VAL ASN TRP ILE ARG GLN PRO PRO GLY LYS GLY LEU GLU SEQRES 6 B 140 TRP LEU GLY MET ILE TRP GLY ASP GLY SER THR ASP TYR SEQRES 7 B 140 ASN SER ALA LEU LYS SER ARG LEU SER ILE THR LYS ASP SEQRES 8 B 140 ASN SER LYS SER GLN VAL PHE LEU LYS MET ASN SER LEU SEQRES 9 B 140 GLN THR ASP ASP THR ALA ARG TYR TYR CYS ALA ARG ASP SEQRES 10 B 140 ARG SER TYR GLY GLY SER SER ALA TRP PHE GLY TYR TRP SEQRES 11 B 140 GLY GLN GLY THR LEU VAL THR VAL SER ALA SEQRES 1 I 126 MET SER SER ALA GLN PHE LEU GLY LEU LEU LEU LEU CYS SEQRES 2 I 126 PHE GLN GLY THR ARG CYS ASP ILE GLN MET THR GLN THR SEQRES 3 I 126 THR SER SER LEU SER ALA SER LEU GLY ASP ARG VAL THR SEQRES 4 I 126 ILE SER CYS ARG ALA SER HIS ASP ILE SER ASN TYR LEU SEQRES 5 I 126 ASN TRP TYR GLN GLN LYS PRO ASP GLY THR LEU LYS LEU SEQRES 6 I 126 LEU ILE TYR TYR THR SER ARG LEU HIS SER GLY VAL PRO SEQRES 7 I 126 SER ARG PHE SER GLY SER GLY SER GLY THR ASP TYR SER SEQRES 8 I 126 LEU THR ILE SER ASN LEU GLU GLN GLU ASP VAL ALA THR SEQRES 9 I 126 TYR PHE CYS GLN GLN GLY ASN TYR LEU PRO TYR THR PHE SEQRES 10 I 126 GLY GLY GLY THR LYS LEU GLU ILE LYS SEQRES 1 C 564 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 C 564 TRP VAL PRO GLY SER THR GLY ASP ALA ALA GLN PRO ALA SEQRES 3 C 564 GLN TYR THR THR SER TYR ASP PRO GLU LEU THR GLU SER SEQRES 4 C 564 SER GLY SER ALA SER HIS ILE ASP CYS ARG MET SER PRO SEQRES 5 C 564 TRP SER GLU TRP SER GLN CYS ASP PRO CYS LEU ARG GLN SEQRES 6 C 564 MET PHE ARG SER ARG SER ILE GLU VAL PHE GLY GLN PHE SEQRES 7 C 564 ASN GLY LYS ARG CYS THR ASP ALA VAL GLY ASP ARG ARG SEQRES 8 C 564 GLN CYS VAL PRO THR GLU PRO CYS GLU ASP ALA GLU ASP SEQRES 9 C 564 ASP CYS GLY ASN ASP PHE GLN CYS SER THR GLY ARG CYS SEQRES 10 C 564 ILE LYS MET ARG LEU ARG CYS ASN GLY ASP ASN ASP CYS SEQRES 11 C 564 GLY ASP PHE SER ASP GLU ASP ASP CYS GLU SER GLU PRO SEQRES 12 C 564 ARG PRO PRO CYS ARG ASP ARG VAL VAL GLU GLU SER GLU SEQRES 13 C 564 LEU ALA ARG THR ALA GLY TYR GLY ILE ASN ILE LEU GLY SEQRES 14 C 564 MET ASP PRO LEU SER THR PRO PHE ASP ASN GLU PHE TYR SEQRES 15 C 564 ASN GLY LEU CYS ASN ARG ASP ARG ASP GLY ASN THR LEU SEQRES 16 C 564 THR TYR TYR ARG ARG PRO TRP ASN VAL ALA SER LEU ILE SEQRES 17 C 564 TYR GLU THR LYS GLY GLU LYS ASN PHE ARG THR GLU HIS SEQRES 18 C 564 TYR GLU GLU GLN ILE GLU ALA PHE LYS SER ILE ILE GLN SEQRES 19 C 564 GLU LYS THR SER ASN PHE ASN ALA ALA ILE SER LEU LYS SEQRES 20 C 564 PHE THR PRO THR GLU THR ASN LYS ALA GLU GLN CYS CYS SEQRES 21 C 564 GLU GLU THR ALA SER SER ILE SER LEU HIS GLY LYS GLY SEQRES 22 C 564 SER PHE ARG PHE SER TYR SER LYS ASN GLU THR TYR GLN SEQRES 23 C 564 LEU PHE LEU SER TYR SER SER LYS LYS GLU LYS MET PHE SEQRES 24 C 564 LEU HIS VAL LYS GLY GLU ILE HIS LEU GLY ARG PHE VAL SEQRES 25 C 564 MET ARG ASN ARG ASP VAL VAL LEU THR THR THR PHE VAL SEQRES 26 C 564 ASP ASP ILE LYS ALA LEU PRO THR THR TYR GLU LYS GLY SEQRES 27 C 564 GLU TYR PHE ALA PHE LEU GLU THR TYR GLY THR HIS TYR SEQRES 28 C 564 SER SER SER GLY SER LEU GLY GLY LEU TYR GLU LEU ILE SEQRES 29 C 564 TYR VAL LEU ASP LYS ALA SER MET LYS ARG LYS GLY VAL SEQRES 30 C 564 GLU LEU LYS ASP ILE LYS ARG CYS LEU GLY TYR HIS LEU SEQRES 31 C 564 ASP VAL SER LEU ALA PHE SER GLU ILE SER VAL GLY ALA SEQRES 32 C 564 GLU PHE ASN LYS ASP ASP CYS VAL LYS ARG GLY GLU GLY SEQRES 33 C 564 ARG ALA VAL ASN ILE THR SER GLU ASN LEU ILE ASP ASP SEQRES 34 C 564 VAL VAL SER LEU ILE ARG GLY GLY THR ARG LYS TYR ALA SEQRES 35 C 564 PHE GLU LEU LYS GLU LYS LEU LEU ARG GLY THR VAL ILE SEQRES 36 C 564 ASP VAL THR ASP PHE VAL ASN TRP ALA SER SER ILE ASN SEQRES 37 C 564 ASP ALA PRO VAL LEU ILE SER GLN LYS LEU SER PRO ILE SEQRES 38 C 564 TYR ASN LEU VAL PRO VAL LYS MET LYS ASN ALA HIS LEU SEQRES 39 C 564 LYS LYS GLN ASN LEU GLU ARG ALA ILE GLU ASP TYR ILE SEQRES 40 C 564 ASN GLU PHE SER VAL ARG LYS CYS HIS THR CYS GLN ASN SEQRES 41 C 564 GLY GLY THR VAL ILE LEU MET ASP GLY LYS CYS LEU CYS SEQRES 42 C 564 ALA CYS PRO PHE LYS PHE GLU GLY ILE ALA CYS GLU ILE SEQRES 43 C 564 SER LYS GLN LYS ILE SER GLU GLY LEU PRO ALA LEU GLU SEQRES 44 C 564 PHE PRO ASN GLU LYS SEQRES 1 G 564 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 G 564 TRP VAL PRO GLY SER THR GLY ASP ALA ALA GLN PRO ALA SEQRES 3 G 564 GLN TYR THR THR SER TYR ASP PRO GLU LEU THR GLU SER SEQRES 4 G 564 SER GLY SER ALA SER HIS ILE ASP CYS ARG MET SER PRO SEQRES 5 G 564 TRP SER GLU TRP SER GLN CYS ASP PRO CYS LEU ARG GLN SEQRES 6 G 564 MET PHE ARG SER ARG SER ILE GLU VAL PHE GLY GLN PHE SEQRES 7 G 564 ASN GLY LYS ARG CYS THR ASP ALA VAL GLY ASP ARG ARG SEQRES 8 G 564 GLN CYS VAL PRO THR GLU PRO CYS GLU ASP ALA GLU ASP SEQRES 9 G 564 ASP CYS GLY ASN ASP PHE GLN CYS SER THR GLY ARG CYS SEQRES 10 G 564 ILE LYS MET ARG LEU ARG CYS ASN GLY ASP ASN ASP CYS SEQRES 11 G 564 GLY ASP PHE SER ASP GLU ASP ASP CYS GLU SER GLU PRO SEQRES 12 G 564 ARG PRO PRO CYS ARG ASP ARG VAL VAL GLU GLU SER GLU SEQRES 13 G 564 LEU ALA ARG THR ALA GLY TYR GLY ILE ASN ILE LEU GLY SEQRES 14 G 564 MET ASP PRO LEU SER THR PRO PHE ASP ASN GLU PHE TYR SEQRES 15 G 564 ASN GLY LEU CYS ASN ARG ASP ARG ASP GLY ASN THR LEU SEQRES 16 G 564 THR TYR TYR ARG ARG PRO TRP ASN VAL ALA SER LEU ILE SEQRES 17 G 564 TYR GLU THR LYS GLY GLU LYS ASN PHE ARG THR GLU HIS SEQRES 18 G 564 TYR GLU GLU GLN ILE GLU ALA PHE LYS SER ILE ILE GLN SEQRES 19 G 564 GLU LYS THR SER ASN PHE ASN ALA ALA ILE SER LEU LYS SEQRES 20 G 564 PHE THR PRO THR GLU THR ASN LYS ALA GLU GLN CYS CYS SEQRES 21 G 564 GLU GLU THR ALA SER SER ILE SER LEU HIS GLY LYS GLY SEQRES 22 G 564 SER PHE ARG PHE SER TYR SER LYS ASN GLU THR TYR GLN SEQRES 23 G 564 LEU PHE LEU SER TYR SER SER LYS LYS GLU LYS MET PHE SEQRES 24 G 564 LEU HIS VAL LYS GLY GLU ILE HIS LEU GLY ARG PHE VAL SEQRES 25 G 564 MET ARG ASN ARG ASP VAL VAL LEU THR THR THR PHE VAL SEQRES 26 G 564 ASP ASP ILE LYS ALA LEU PRO THR THR TYR GLU LYS GLY SEQRES 27 G 564 GLU TYR PHE ALA PHE LEU GLU THR TYR GLY THR HIS TYR SEQRES 28 G 564 SER SER SER GLY SER LEU GLY GLY LEU TYR GLU LEU ILE SEQRES 29 G 564 TYR VAL LEU ASP LYS ALA SER MET LYS ARG LYS GLY VAL SEQRES 30 G 564 GLU LEU LYS ASP ILE LYS ARG CYS LEU GLY TYR HIS LEU SEQRES 31 G 564 ASP VAL SER LEU ALA PHE SER GLU ILE SER VAL GLY ALA SEQRES 32 G 564 GLU PHE ASN LYS ASP ASP CYS VAL LYS ARG GLY GLU GLY SEQRES 33 G 564 ARG ALA VAL ASN ILE THR SER GLU ASN LEU ILE ASP ASP SEQRES 34 G 564 VAL VAL SER LEU ILE ARG GLY GLY THR ARG LYS TYR ALA SEQRES 35 G 564 PHE GLU LEU LYS GLU LYS LEU LEU ARG GLY THR VAL ILE SEQRES 36 G 564 ASP VAL THR ASP PHE VAL ASN TRP ALA SER SER ILE ASN SEQRES 37 G 564 ASP ALA PRO VAL LEU ILE SER GLN LYS LEU SER PRO ILE SEQRES 38 G 564 TYR ASN LEU VAL PRO VAL LYS MET LYS ASN ALA HIS LEU SEQRES 39 G 564 LYS LYS GLN ASN LEU GLU ARG ALA ILE GLU ASP TYR ILE SEQRES 40 G 564 ASN GLU PHE SER VAL ARG LYS CYS HIS THR CYS GLN ASN SEQRES 41 G 564 GLY GLY THR VAL ILE LEU MET ASP GLY LYS CYS LEU CYS SEQRES 42 G 564 ALA CYS PRO PHE LYS PHE GLU GLY ILE ALA CYS GLU ILE SEQRES 43 G 564 SER LYS GLN LYS ILE SER GLU GLY LEU PRO ALA LEU GLU SEQRES 44 G 564 PHE PRO ASN GLU LYS HET NAG A 601 14 HET BMA A 602 11 HET BMA A 603 11 HET CA A 604 1 HET NAG C 601 14 HET BMA C 602 11 HET BMA C 603 11 HET CA C 604 1 HET NAG G 601 14 HET BMA G 602 11 HET BMA G 603 11 HET CA G 604 1 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM CA CALCIUM ION FORMUL 8 NAG 3(C8 H15 N O6) FORMUL 9 BMA 6(C6 H12 O6) FORMUL 11 CA 3(CA 2+) HELIX 1 AA1 SER E 47 TYR E 51 5 5 HELIX 2 AA2 GLN E 105 THR E 109 5 5 HELIX 3 AA3 LYS A 93 ARG A 97 5 5 HELIX 4 AA4 ASP A 109 CYS A 113 5 5 HELIX 5 AA5 THR A 264 ALA A 273 1 10 HELIX 6 AA6 GLU A 279 GLY A 291 1 13 HELIX 7 AA7 LYS A 369 GLY A 381 1 13 HELIX 8 AA8 ASP A 385 ILE A 396 1 12 HELIX 9 AA9 ASN A 397 ALA A 399 5 3 HELIX 10 AB1 TYR A 411 VAL A 414 5 4 HELIX 11 AB2 ASN A 420 GLU A 438 1 19 HELIX 12 AB3 SER A 440 CYS A 444 5 5 HELIX 13 AB4 SER B 47 TYR B 51 5 5 HELIX 14 AB5 SER B 80 LYS B 83 5 4 HELIX 15 AB6 GLU I 98 VAL I 102 5 5 HELIX 16 AB7 LYS C 93 ARG C 97 5 5 HELIX 17 AB8 ASP C 109 CYS C 113 5 5 HELIX 18 AB9 SER C 129 THR C 134 1 6 HELIX 19 AC1 THR C 264 ALA C 273 1 10 HELIX 20 AC2 GLU C 279 GLY C 291 1 13 HELIX 21 AC3 LYS C 369 GLY C 381 1 13 HELIX 22 AC4 ASP C 385 ILE C 396 1 12 HELIX 23 AC5 ASN C 397 ALA C 399 5 3 HELIX 24 AC6 TYR C 411 VAL C 414 5 4 HELIX 25 AC7 ASN C 420 GLU C 438 1 19 HELIX 26 AC8 SER C 440 CYS C 444 5 5 HELIX 27 AC9 LYS G 93 ARG G 97 5 5 HELIX 28 AD1 ASP G 109 CYS G 113 5 5 HELIX 29 AD2 GLU G 130 THR G 134 5 5 HELIX 30 AD3 THR G 264 ALA G 273 1 10 HELIX 31 AD4 GLU G 279 GLY G 291 1 13 HELIX 32 AD5 LYS G 369 GLY G 381 1 13 HELIX 33 AD6 ASP G 385 ILE G 396 1 12 HELIX 34 AD7 ASN G 397 ALA G 399 5 3 HELIX 35 AD8 TYR G 411 VAL G 414 5 4 HELIX 36 AD9 ASN G 420 GLU G 438 1 19 HELIX 37 AE1 SER G 440 CYS G 444 5 5 SHEET 1 AA1 4 GLN E 22 SER E 26 0 SHEET 2 AA1 4 ILE E 39 SER E 44 -1 O THR E 42 N LYS E 24 SHEET 3 AA1 4 GLN E 96 LEU E 99 -1 O VAL E 97 N CYS E 41 SHEET 4 AA1 4 ILE E 88 ASP E 91 -1 N THR E 89 O PHE E 98 SHEET 1 AA2 6 LEU E 30 VAL E 31 0 SHEET 2 AA2 6 THR E 134 VAL E 138 1 O THR E 137 N VAL E 31 SHEET 3 AA2 6 ALA E 110 ARG E 116 -1 N TYR E 112 O THR E 134 SHEET 4 AA2 6 VAL E 53 GLN E 58 -1 N ILE E 56 O TYR E 113 SHEET 5 AA2 6 GLU E 65 ILE E 70 -1 O LEU E 67 N TRP E 55 SHEET 6 AA2 6 THR E 76 TYR E 78 -1 O ASP E 77 N MET E 69 SHEET 1 AA3 5 SER F 29 ALA F 32 0 SHEET 2 AA3 5 THR F 121 ILE F 125 1 O GLU F 124 N LEU F 30 SHEET 3 AA3 5 THR F 104 GLN F 109 -1 N TYR F 105 O THR F 121 SHEET 4 AA3 5 LEU F 52 LYS F 58 -1 N TYR F 55 O PHE F 106 SHEET 5 AA3 5 THR F 62 TYR F 68 -1 O ILE F 67 N TRP F 54 SHEET 1 AA4 3 VAL F 38 ARG F 43 0 SHEET 2 AA4 3 ASP F 89 ILE F 94 -1 O ILE F 94 N VAL F 38 SHEET 3 AA4 3 PHE F 81 SER F 86 -1 N SER F 84 O SER F 91 SHEET 1 AA5 2 ARG A 23 MET A 24 0 SHEET 2 AA5 2 ILE A 46 VAL A 48 -1 O GLU A 47 N ARG A 23 SHEET 1 AA6 2 GLN A 39 SER A 43 0 SHEET 2 AA6 2 GLY A 62 GLN A 66 -1 O ARG A 65 N MET A 40 SHEET 1 AA7 2 PHE A 84 GLN A 85 0 SHEET 2 AA7 2 CYS A 91 ILE A 92 -1 O ILE A 92 N PHE A 84 SHEET 1 AA8 3 GLU A 127 GLU A 128 0 SHEET 2 AA8 3 THR A 170 ARG A 173 1 O ARG A 173 N GLU A 127 SHEET 3 AA8 3 ARG A 162 ASP A 165 -1 N ASP A 163 O TYR A 172 SHEET 1 AA9 3 GLY A 138 ILE A 139 0 SHEET 2 AA9 3 HIS A 293 SER A 295 -1 O HIS A 293 N ILE A 139 SHEET 3 AA9 3 LEU A 407 PRO A 409 -1 O SER A 408 N TYR A 294 SHEET 1 AB116 VAL A 178 GLN A 199 0 SHEET 2 AB116 LYS A 237 MET A 256 -1 O VAL A 255 N ALA A 179 SHEET 3 AB116 SER A 297 ARG A 317 -1 O LEU A 300 N LEU A 251 SHEET 4 AB116 ASN A 349 ARG A 364 -1 O VAL A 360 N ILE A 307 SHEET 5 AB116 VAL A 401 SER A 404 -1 O ILE A 403 N SER A 299 SHEET 6 AB116 VAL C 178 GLY C 187 0 SHEET 7 AB116 ASN C 190 GLN C 199 0 SHEET 8 AB116 TYR C 234 MET C 256 -1 O LYS C 238 N GLU C 198 SHEET 9 AB116 SER C 297 ARG C 317 -1 O LEU C 300 N LEU C 251 SHEET 10 AB116 THR C 351 ARG C 364 -1 O ARG C 364 N LEU C 303 SHEET 11 AB116 VAL C 401 SER C 404 -1 O SER C 404 N SER C 299 SHEET 12 AB116 VAL G 178 GLU G 201 -1 O THR G 193 N ASP A 357 SHEET 13 AB116 LYS G 237 MET G 256 -1 O VAL G 255 N ALA G 179 SHEET 14 AB116 SER G 297 ARG G 317 -1 O LEU G 300 N LEU G 251 SHEET 15 AB116 ILE G 350 ARG G 364 -1 O ILE G 356 N ASP G 311 SHEET 16 AB116 VAL G 401 SER G 404 -1 O ILE G 403 N SER G 299 SHEET 1 AB2 2 THR A 452 LEU A 455 0 SHEET 2 AB2 2 CYS A 460 ALA A 463 -1 O LEU A 461 N ILE A 454 SHEET 1 AB3 4 GLN B 22 LYS B 24 0 SHEET 2 AB3 4 LEU B 37 SER B 44 -1 O SER B 44 N GLN B 22 SHEET 3 AB3 4 GLN B 96 MET B 101 -1 O VAL B 97 N CYS B 41 SHEET 4 AB3 4 LEU B 86 ASP B 91 -1 N THR B 89 O PHE B 98 SHEET 1 AB4 6 LEU B 30 VAL B 31 0 SHEET 2 AB4 6 THR B 134 VAL B 138 1 O THR B 137 N VAL B 31 SHEET 3 AB4 6 ALA B 110 ARG B 116 -1 N TYR B 112 O THR B 134 SHEET 4 AB4 6 VAL B 53 GLN B 58 -1 N ILE B 56 O TYR B 113 SHEET 5 AB4 6 GLU B 65 ILE B 70 -1 O LEU B 67 N TRP B 55 SHEET 6 AB4 6 THR B 76 TYR B 78 -1 O ASP B 77 N MET B 69 SHEET 1 AB5 3 SER I 29 ALA I 32 0 SHEET 2 AB5 3 THR I 121 ILE I 125 1 O GLU I 124 N LEU I 30 SHEET 3 AB5 3 THR I 104 TYR I 105 -1 N TYR I 105 O THR I 121 SHEET 1 AB6 3 VAL I 38 ARG I 43 0 SHEET 2 AB6 3 ASP I 89 ILE I 94 -1 O LEU I 92 N ILE I 40 SHEET 3 AB6 3 SER I 82 SER I 86 -1 N SER I 82 O THR I 93 SHEET 1 AB7 4 ARG I 72 LEU I 73 0 SHEET 2 AB7 4 THR I 62 TYR I 68 -1 N TYR I 68 O ARG I 72 SHEET 3 AB7 4 LEU I 52 LYS I 58 -1 N TRP I 54 O LEU I 66 SHEET 4 AB7 4 CYS I 107 GLN I 109 -1 O GLN I 108 N ASN I 53 SHEET 1 AB8 2 ARG C 23 MET C 24 0 SHEET 2 AB8 2 ILE C 46 VAL C 48 -1 O GLU C 47 N ARG C 23 SHEET 1 AB9 2 GLN C 39 SER C 43 0 SHEET 2 AB9 2 GLY C 62 GLN C 66 -1 O ARG C 65 N MET C 40 SHEET 1 AC1 3 GLY C 50 GLN C 51 0 SHEET 2 AC1 3 LYS C 459 ALA C 463 1 O CYS C 460 N GLY C 50 SHEET 3 AC1 3 THR C 452 LEU C 455 -1 N ILE C 454 O LEU C 461 SHEET 1 AC2 2 PHE C 84 GLN C 85 0 SHEET 2 AC2 2 CYS C 91 ILE C 92 -1 O ILE C 92 N PHE C 84 SHEET 1 AC3 3 GLU C 127 GLU C 128 0 SHEET 2 AC3 3 THR C 170 ARG C 173 1 O ARG C 173 N GLU C 127 SHEET 3 AC3 3 ARG C 164 ASP C 165 -1 N ASP C 165 O THR C 170 SHEET 1 AC4 3 GLY C 138 ILE C 139 0 SHEET 2 AC4 3 HIS C 293 SER C 295 -1 O HIS C 293 N ILE C 139 SHEET 3 AC4 3 LEU C 407 PRO C 409 -1 O SER C 408 N TYR C 294 SHEET 1 AC5 2 ARG G 23 MET G 24 0 SHEET 2 AC5 2 ILE G 46 VAL G 48 -1 O GLU G 47 N ARG G 23 SHEET 1 AC6 2 GLN G 39 SER G 43 0 SHEET 2 AC6 2 GLY G 62 GLN G 66 -1 O ARG G 65 N MET G 40 SHEET 1 AC7 2 PHE G 84 GLN G 85 0 SHEET 2 AC7 2 CYS G 91 ILE G 92 -1 O ILE G 92 N PHE G 84 SHEET 1 AC8 3 GLU G 127 GLU G 128 0 SHEET 2 AC8 3 THR G 170 ARG G 173 1 O ARG G 173 N GLU G 127 SHEET 3 AC8 3 ARG G 162 ASP G 165 -1 N ASP G 163 O TYR G 172 SHEET 1 AC9 3 GLY G 138 ILE G 139 0 SHEET 2 AC9 3 HIS G 293 SER G 295 -1 O HIS G 293 N ILE G 139 SHEET 3 AC9 3 LEU G 407 PRO G 409 -1 O SER G 408 N TYR G 294 SHEET 1 AD1 2 THR G 452 LEU G 455 0 SHEET 2 AD1 2 CYS G 460 ALA G 463 -1 O ALA G 463 N THR G 452 SSBOND 1 CYS E 41 CYS E 114 1555 1555 2.02 SSBOND 2 CYS F 42 CYS F 107 1555 1555 2.04 SSBOND 3 CYS A 22 CYS A 57 1555 1555 2.05 SSBOND 4 CYS A 33 CYS A 67 1555 1555 2.05 SSBOND 5 CYS A 36 CYS A 73 1555 1555 2.02 SSBOND 6 CYS A 80 CYS A 91 1555 1555 2.04 SSBOND 7 CYS A 86 CYS A 104 1555 1555 2.05 SSBOND 8 CYS A 98 CYS A 113 1555 1555 2.02 SSBOND 9 CYS A 121 CYS A 160 1555 1555 2.03 SSBOND 10 CYS A 444 CYS A 460 1555 1555 2.03 SSBOND 11 CYS A 447 CYS A 462 1555 1555 2.02 SSBOND 12 CYS A 464 CYS A 473 1555 1555 2.00 SSBOND 13 CYS B 41 CYS B 114 1555 1555 2.05 SSBOND 14 CYS I 42 CYS I 107 1555 1555 2.06 SSBOND 15 CYS C 22 CYS C 57 1555 1555 2.04 SSBOND 16 CYS C 33 CYS C 67 1555 1555 2.03 SSBOND 17 CYS C 36 CYS C 73 1555 1555 2.03 SSBOND 18 CYS C 80 CYS C 91 1555 1555 2.06 SSBOND 19 CYS C 86 CYS C 104 1555 1555 2.03 SSBOND 20 CYS C 98 CYS C 113 1555 1555 2.05 SSBOND 21 CYS C 121 CYS C 160 1555 1555 2.02 SSBOND 22 CYS C 444 CYS C 460 1555 1555 2.04 SSBOND 23 CYS C 447 CYS C 462 1555 1555 2.01 SSBOND 24 CYS C 464 CYS C 473 1555 1555 2.02 SSBOND 25 CYS G 22 CYS G 57 1555 1555 2.04 SSBOND 26 CYS G 33 CYS G 67 1555 1555 2.04 SSBOND 27 CYS G 36 CYS G 73 1555 1555 2.02 SSBOND 28 CYS G 80 CYS G 91 1555 1555 2.04 SSBOND 29 CYS G 86 CYS G 104 1555 1555 2.03 SSBOND 30 CYS G 98 CYS G 113 1555 1555 2.04 SSBOND 31 CYS G 121 CYS G 160 1555 1555 2.03 SSBOND 32 CYS G 444 CYS G 460 1555 1555 2.02 SSBOND 33 CYS G 447 CYS G 462 1555 1555 2.02 SSBOND 34 CYS G 464 CYS G 473 1555 1555 2.03 LINK OG1 THR A 452 C1 NAG A 601 1555 1555 1.45 LINK OG1 THR C 452 C1 NAG C 601 1555 1555 1.46 LINK OG1 THR G 452 C1 NAG G 601 1555 1555 1.44 LINK OD1 ASN A 99 CA CA A 604 1555 1555 2.32 LINK O ASP A 101 CA CA A 604 1555 1555 2.48 LINK OD2 ASP A 103 CA CA A 604 1555 1555 2.78 LINK OD2 ASP A 109 CA CA A 604 1555 1555 2.33 LINK OE2 GLU A 110 CA CA A 604 1555 1555 2.67 LINK O LEU C 96 CA CA C 604 1555 1555 2.94 LINK OD1 ASN C 99 CA CA C 604 1555 1555 2.27 LINK O ASP C 101 CA CA C 604 1555 1555 2.47 LINK OD2 ASP C 103 CA CA C 604 1555 1555 2.95 LINK OD2 ASP C 109 CA CA C 604 1555 1555 2.47 LINK O LEU G 96 CA CA G 604 1555 1555 3.14 LINK OD1 ASN G 99 CA CA G 604 1555 1555 2.83 LINK O ASP G 101 CA CA G 604 1555 1555 2.48 LINK OD2 ASP G 103 CA CA G 604 1555 1555 2.99 LINK OD2 ASP G 109 CA CA G 604 1555 1555 2.20 LINK OE2 GLU G 110 CA CA G 604 1555 1555 2.39 CISPEP 1 LEU F 113 PRO F 114 0 0.29 CISPEP 2 LEU I 113 PRO I 114 0 -7.69 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