HEADER VIRAL PROTEIN/IMMUNE SYSTEM 23-AUG-24 9DBX TITLE STRUCTURE OF AG11-2F01 FAB IN COMPLEX WITH A/SOLOMON ISLANDS/3/2006 TITLE 2 (H1N1) INFLUENZA VIRUS HEMAGGLUTININ COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ HA1 CHAIN; COMPND 3 CHAIN: A, C, E; COMPND 4 FRAGMENT: UNP RESIDUES 18-339; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEMAGGLUTININ HA2 CHAIN; COMPND 8 CHAIN: B, D, F; COMPND 9 FRAGMENT: UNP RESIDUES 349-516; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: HEAVY CHAIN OF INFLUENZA VIRUS HEMAGGLUTININ ANTIBODY AG11- COMPND 13 2F01; COMPND 14 CHAIN: H, W, Y; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: LIGHT CHAIN OF INFLUENZA VIRUS HEMAGGLUTININ ANTIBODY AG11- COMPND 18 2F01; COMPND 19 CHAIN: L, X, Z; COMPND 20 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 464623; SOURCE 4 STRAIN: A/SOLOMON ISLANDS/3/2006(H1N1); SOURCE 5 GENE: HA; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 11 ORGANISM_TAXID: 464623; SOURCE 12 STRAIN: A/SOLOMON ISLANDS/3/2006(H1N1); SOURCE 13 GENE: HA; SOURCE 14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 15 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 17 EXPRESSION_SYSTEM_CELL: SF9; SOURCE 18 MOL_ID: 3; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_COMMON: HUMAN; SOURCE 21 ORGANISM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 23 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM_CELL: EXPI293F; SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PHCMV3; SOURCE 28 MOL_ID: 4; SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 30 ORGANISM_COMMON: HUMAN; SOURCE 31 ORGANISM_TAXID: 9606; SOURCE 32 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 33 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 35 EXPRESSION_SYSTEM_CELL: EXPI293F; SOURCE 36 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 37 EXPRESSION_SYSTEM_PLASMID: PHCMV3 KEYWDS ANTIBODY-ANTIGEN COMPLEX, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Z.MOU,R.LEI,X.DAI,N.WU REVDAT 1 03-SEP-25 9DBX 0 JRNL AUTH Z.MOU,R.LEI,W.OUYANG,X.DAI,N.WU JRNL TITL STRUCTURE OF AG11-2F01 FAB IN COMPLEX WITH A/SOLOMON JRNL TITL 2 ISLANDS/3/2006 (H1N1) INFLUENZA VIRUS HEMAGGLUTININ JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : SERIALEM, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.900 REMARK 3 NUMBER OF PARTICLES : 359720 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 9DBX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1000286369. 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 : STRUCTURE OF AG11-2F01 FAB IN REMARK 245 COMPLEX WITH A/SOLOMON ISLANDS/ REMARK 245 3/2006 (H1N1) INFLUENZA VIRUS REMARK 245 HEMAGGLUTININ 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 : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, L, W, X, REMARK 350 AND CHAINS: Y, Z REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 PRO H 44 CG CD REMARK 470 PRO W 44 CG CD REMARK 470 PRO Y 44 CG CD 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 CYS A 52 -159.39 -81.82 REMARK 500 ILE A 56 -158.25 -114.77 REMARK 500 GLU A 75 30.81 -95.40 REMARK 500 LEU A 79 31.91 -99.30 REMARK 500 SER A 114 118.34 -160.38 REMARK 500 THR A 132 41.73 38.21 REMARK 500 ASN A 171 28.89 -140.58 REMARK 500 SER A 265 -152.96 -89.15 REMARK 500 PRO A 284 -2.72 -58.36 REMARK 500 ARG A 310 35.84 -98.90 REMARK 500 ALA B 7 18.33 -140.31 REMARK 500 LEU C 79 34.36 -98.88 REMARK 500 SER C 114 118.45 -160.35 REMARK 500 THR C 132 41.54 38.21 REMARK 500 ASN C 171 29.93 -140.69 REMARK 500 SER C 265 -130.78 -97.09 REMARK 500 PRO C 284 -2.81 -58.53 REMARK 500 ARG C 310 35.95 -99.02 REMARK 500 GLU E 75 30.69 -95.51 REMARK 500 LEU E 79 33.97 -98.77 REMARK 500 SER E 114 118.58 -160.21 REMARK 500 THR E 132 41.55 38.28 REMARK 500 ASN E 171 30.21 -140.78 REMARK 500 SER E 265 -131.81 -97.93 REMARK 500 PRO E 284 -2.58 -58.49 REMARK 500 ARG E 310 36.00 -99.07 REMARK 500 SER L 28 64.55 -100.17 REMARK 500 ALA L 51 -9.94 71.79 REMARK 500 ASN L 92 -65.85 -101.13 REMARK 500 SER L 93 -64.20 -120.14 REMARK 500 TYR L 94 40.44 -142.51 REMARK 500 SER X 28 64.42 -100.21 REMARK 500 ALA X 51 -9.62 71.76 REMARK 500 ASN X 92 -64.60 -101.55 REMARK 500 TYR X 94 40.40 -142.62 REMARK 500 ALA Z 51 -9.45 71.80 REMARK 500 ASN Z 92 -64.44 -101.85 REMARK 500 TYR Z 94 40.62 -142.72 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-46727 RELATED DB: EMDB REMARK 900 STRUCTURE OF AG11-2F01 FAB IN COMPLEX WITH A/SOLOMON ISLANDS/3/2006 REMARK 900 (H1N1) INFLUENZA VIRUS HEMAGGLUTININ DBREF 9DBX A 11 325 UNP A7Y8I1 A7Y8I1_9INFA 18 339 DBREF 9DBX B 6 173 UNP A7Y8I1 A7Y8I1_9INFA 349 516 DBREF 9DBX C 11 325 UNP A7Y8I1 A7Y8I1_9INFA 18 339 DBREF 9DBX D 6 173 UNP A7Y8I1 A7Y8I1_9INFA 349 516 DBREF 9DBX E 11 325 UNP A7Y8I1 A7Y8I1_9INFA 18 339 DBREF 9DBX F 6 173 UNP A7Y8I1 A7Y8I1_9INFA 349 516 DBREF 9DBX H 1 113 PDB 9DBX 9DBX 1 113 DBREF 9DBX L 2 106 PDB 9DBX 9DBX 2 106 DBREF 9DBX W 1 113 PDB 9DBX 9DBX 1 113 DBREF 9DBX X 2 106 PDB 9DBX 9DBX 2 106 DBREF 9DBX Y 1 113 PDB 9DBX 9DBX 1 113 DBREF 9DBX Z 2 106 PDB 9DBX 9DBX 2 106 SEQADV 9DBX ARG A 53 UNP A7Y8I1 LEU 60 CONFLICT SEQADV 9DBX ARG C 53 UNP A7Y8I1 LEU 60 CONFLICT SEQADV 9DBX ARG E 53 UNP A7Y8I1 LEU 60 CONFLICT SEQRES 1 A 321 ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 A 321 ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR VAL SEQRES 3 A 321 THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN GLY SEQRES 4 A 321 LYS LEU CYS ARG LEU GLY ILE ALA PRO LEU GLN LEU GLY SEQRES 5 A 321 ASN CYS SER VAL ALA GLY TRP ILE LEU GLY ASN PRO GLU SEQRES 6 A 321 CYS GLU LEU LEU ILE SER ARG GLU SER TRP SER TYR ILE SEQRES 7 A 321 VAL GLU LYS PRO ASN PRO GLU ASN GLY THR CYS TYR PRO SEQRES 8 A 321 GLY HIS PHE ALA ASP TYR GLU GLU LEU ARG GLU GLN LEU SEQRES 9 A 321 SER SER VAL SER SER PHE GLU ARG PHE GLU ILE PHE PRO SEQRES 10 A 321 LYS GLU SER SER TRP PRO ASN HIS THR THR THR GLY VAL SEQRES 11 A 321 SER ALA SER CYS SER HIS ASN GLY GLU SER SER PHE TYR SEQRES 12 A 321 LYS ASN LEU LEU TRP LEU THR GLY LYS ASN GLY LEU TYR SEQRES 13 A 321 PRO ASN LEU SER LYS SER TYR ALA ASN ASN LYS GLU LYS SEQRES 14 A 321 GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO PRO ASN SEQRES 15 A 321 ILE GLY ASP GLN ARG ALA LEU TYR HIS LYS GLU ASN ALA SEQRES 16 A 321 TYR VAL SER VAL VAL SER SER HIS TYR SER ARG LYS PHE SEQRES 17 A 321 THR PRO GLU ILE ALA LYS ARG PRO LYS VAL ARG ASP GLN SEQRES 18 A 321 GLU GLY ARG ILE ASN TYR TYR TRP THR LEU LEU GLU PRO SEQRES 19 A 321 GLY ASP THR ILE ILE PHE GLU ALA ASN GLY ASN LEU ILE SEQRES 20 A 321 ALA PRO ARG TYR ALA PHE ALA LEU SER ARG GLY PHE GLY SEQRES 21 A 321 SER GLY ILE ILE ASN SER ASN ALA PRO MET ASP GLU CYS SEQRES 22 A 321 ASP ALA LYS CYS GLN THR PRO GLN GLY ALA ILE ASN SER SEQRES 23 A 321 SER LEU PRO PHE GLN ASN VAL HIS PRO VAL THR ILE GLY SEQRES 24 A 321 GLU CYS PRO LYS TYR VAL ARG SER ALA LYS LEU ARG MET SEQRES 25 A 321 VAL THR GLY LEU ARG ASN ILE PRO SER SEQRES 1 B 168 ILE ALA GLY PHE ILE GLU GLY GLY TRP THR GLY MET VAL SEQRES 2 B 168 ASP GLY TRP TYR GLY TYR HIS HIS GLN ASN GLU GLN GLY SEQRES 3 B 168 SER GLY TYR ALA ALA ASP GLN LYS SER THR GLN ASN ALA SEQRES 4 B 168 ILE ASN GLY ILE THR ASN LYS VAL ASN SER VAL ILE GLU SEQRES 5 B 168 LYS MET ASN THR GLN PHE THR ALA VAL GLY LYS GLU PHE SEQRES 6 B 168 ASN LYS LEU GLU ARG ARG MET GLU ASN LEU ASN LYS LYS SEQRES 7 B 168 VAL ASP ASP GLY PHE ILE ASP ILE TRP THR TYR ASN ALA SEQRES 8 B 168 GLU LEU LEU VAL LEU LEU GLU ASN GLU ARG THR LEU ASP SEQRES 9 B 168 PHE HIS ASP SER ASN VAL LYS ASN LEU TYR GLU LYS VAL SEQRES 10 B 168 LYS SER GLN LEU LYS ASN ASN ALA LYS GLU ILE GLY ASN SEQRES 11 B 168 GLY CYS PHE GLU PHE TYR HIS LYS CYS ASN ASP GLU CYS SEQRES 12 B 168 MET GLU SER VAL LYS ASN GLY THR TYR ASP TYR PRO LYS SEQRES 13 B 168 TYR SER GLU GLU SER LYS LEU ASN ARG GLU LYS ILE SEQRES 1 C 321 ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 C 321 ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR VAL SEQRES 3 C 321 THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN GLY SEQRES 4 C 321 LYS LEU CYS ARG LEU GLY ILE ALA PRO LEU GLN LEU GLY SEQRES 5 C 321 ASN CYS SER VAL ALA GLY TRP ILE LEU GLY ASN PRO GLU SEQRES 6 C 321 CYS GLU LEU LEU ILE SER ARG GLU SER TRP SER TYR ILE SEQRES 7 C 321 VAL GLU LYS PRO ASN PRO GLU ASN GLY THR CYS TYR PRO SEQRES 8 C 321 GLY HIS PHE ALA ASP TYR GLU GLU LEU ARG GLU GLN LEU SEQRES 9 C 321 SER SER VAL SER SER PHE GLU ARG PHE GLU ILE PHE PRO SEQRES 10 C 321 LYS GLU SER SER TRP PRO ASN HIS THR THR THR GLY VAL SEQRES 11 C 321 SER ALA SER CYS SER HIS ASN GLY GLU SER SER PHE TYR SEQRES 12 C 321 LYS ASN LEU LEU TRP LEU THR GLY LYS ASN GLY LEU TYR SEQRES 13 C 321 PRO ASN LEU SER LYS SER TYR ALA ASN ASN LYS GLU LYS SEQRES 14 C 321 GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO PRO ASN SEQRES 15 C 321 ILE GLY ASP GLN ARG ALA LEU TYR HIS LYS GLU ASN ALA SEQRES 16 C 321 TYR VAL SER VAL VAL SER SER HIS TYR SER ARG LYS PHE SEQRES 17 C 321 THR PRO GLU ILE ALA LYS ARG PRO LYS VAL ARG ASP GLN SEQRES 18 C 321 GLU GLY ARG ILE ASN TYR TYR TRP THR LEU LEU GLU PRO SEQRES 19 C 321 GLY ASP THR ILE ILE PHE GLU ALA ASN GLY ASN LEU ILE SEQRES 20 C 321 ALA PRO ARG TYR ALA PHE ALA LEU SER ARG GLY PHE GLY SEQRES 21 C 321 SER GLY ILE ILE ASN SER ASN ALA PRO MET ASP GLU CYS SEQRES 22 C 321 ASP ALA LYS CYS GLN THR PRO GLN GLY ALA ILE ASN SER SEQRES 23 C 321 SER LEU PRO PHE GLN ASN VAL HIS PRO VAL THR ILE GLY SEQRES 24 C 321 GLU CYS PRO LYS TYR VAL ARG SER ALA LYS LEU ARG MET SEQRES 25 C 321 VAL THR GLY LEU ARG ASN ILE PRO SER SEQRES 1 D 168 ILE ALA GLY PHE ILE GLU GLY GLY TRP THR GLY MET VAL SEQRES 2 D 168 ASP GLY TRP TYR GLY TYR HIS HIS GLN ASN GLU GLN GLY SEQRES 3 D 168 SER GLY TYR ALA ALA ASP GLN LYS SER THR GLN ASN ALA SEQRES 4 D 168 ILE ASN GLY ILE THR ASN LYS VAL ASN SER VAL ILE GLU SEQRES 5 D 168 LYS MET ASN THR GLN PHE THR ALA VAL GLY LYS GLU PHE SEQRES 6 D 168 ASN LYS LEU GLU ARG ARG MET GLU ASN LEU ASN LYS LYS SEQRES 7 D 168 VAL ASP ASP GLY PHE ILE ASP ILE TRP THR TYR ASN ALA SEQRES 8 D 168 GLU LEU LEU VAL LEU LEU GLU ASN GLU ARG THR LEU ASP SEQRES 9 D 168 PHE HIS ASP SER ASN VAL LYS ASN LEU TYR GLU LYS VAL SEQRES 10 D 168 LYS SER GLN LEU LYS ASN ASN ALA LYS GLU ILE GLY ASN SEQRES 11 D 168 GLY CYS PHE GLU PHE TYR HIS LYS CYS ASN ASP GLU CYS SEQRES 12 D 168 MET GLU SER VAL LYS ASN GLY THR TYR ASP TYR PRO LYS SEQRES 13 D 168 TYR SER GLU GLU SER LYS LEU ASN ARG GLU LYS ILE SEQRES 1 E 321 ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 E 321 ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR VAL SEQRES 3 E 321 THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN GLY SEQRES 4 E 321 LYS LEU CYS ARG LEU GLY ILE ALA PRO LEU GLN LEU GLY SEQRES 5 E 321 ASN CYS SER VAL ALA GLY TRP ILE LEU GLY ASN PRO GLU SEQRES 6 E 321 CYS GLU LEU LEU ILE SER ARG GLU SER TRP SER TYR ILE SEQRES 7 E 321 VAL GLU LYS PRO ASN PRO GLU ASN GLY THR CYS TYR PRO SEQRES 8 E 321 GLY HIS PHE ALA ASP TYR GLU GLU LEU ARG GLU GLN LEU SEQRES 9 E 321 SER SER VAL SER SER PHE GLU ARG PHE GLU ILE PHE PRO SEQRES 10 E 321 LYS GLU SER SER TRP PRO ASN HIS THR THR THR GLY VAL SEQRES 11 E 321 SER ALA SER CYS SER HIS ASN GLY GLU SER SER PHE TYR SEQRES 12 E 321 LYS ASN LEU LEU TRP LEU THR GLY LYS ASN GLY LEU TYR SEQRES 13 E 321 PRO ASN LEU SER LYS SER TYR ALA ASN ASN LYS GLU LYS SEQRES 14 E 321 GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO PRO ASN SEQRES 15 E 321 ILE GLY ASP GLN ARG ALA LEU TYR HIS LYS GLU ASN ALA SEQRES 16 E 321 TYR VAL SER VAL VAL SER SER HIS TYR SER ARG LYS PHE SEQRES 17 E 321 THR PRO GLU ILE ALA LYS ARG PRO LYS VAL ARG ASP GLN SEQRES 18 E 321 GLU GLY ARG ILE ASN TYR TYR TRP THR LEU LEU GLU PRO SEQRES 19 E 321 GLY ASP THR ILE ILE PHE GLU ALA ASN GLY ASN LEU ILE SEQRES 20 E 321 ALA PRO ARG TYR ALA PHE ALA LEU SER ARG GLY PHE GLY SEQRES 21 E 321 SER GLY ILE ILE ASN SER ASN ALA PRO MET ASP GLU CYS SEQRES 22 E 321 ASP ALA LYS CYS GLN THR PRO GLN GLY ALA ILE ASN SER SEQRES 23 E 321 SER LEU PRO PHE GLN ASN VAL HIS PRO VAL THR ILE GLY SEQRES 24 E 321 GLU CYS PRO LYS TYR VAL ARG SER ALA LYS LEU ARG MET SEQRES 25 E 321 VAL THR GLY LEU ARG ASN ILE PRO SER SEQRES 1 F 168 ILE ALA GLY PHE ILE GLU GLY GLY TRP THR GLY MET VAL SEQRES 2 F 168 ASP GLY TRP TYR GLY TYR HIS HIS GLN ASN GLU GLN GLY SEQRES 3 F 168 SER GLY TYR ALA ALA ASP GLN LYS SER THR GLN ASN ALA SEQRES 4 F 168 ILE ASN GLY ILE THR ASN LYS VAL ASN SER VAL ILE GLU SEQRES 5 F 168 LYS MET ASN THR GLN PHE THR ALA VAL GLY LYS GLU PHE SEQRES 6 F 168 ASN LYS LEU GLU ARG ARG MET GLU ASN LEU ASN LYS LYS SEQRES 7 F 168 VAL ASP ASP GLY PHE ILE ASP ILE TRP THR TYR ASN ALA SEQRES 8 F 168 GLU LEU LEU VAL LEU LEU GLU ASN GLU ARG THR LEU ASP SEQRES 9 F 168 PHE HIS ASP SER ASN VAL LYS ASN LEU TYR GLU LYS VAL SEQRES 10 F 168 LYS SER GLN LEU LYS ASN ASN ALA LYS GLU ILE GLY ASN SEQRES 11 F 168 GLY CYS PHE GLU PHE TYR HIS LYS CYS ASN ASP GLU CYS SEQRES 12 F 168 MET GLU SER VAL LYS ASN GLY THR TYR ASP TYR PRO LYS SEQRES 13 F 168 TYR SER GLU GLU SER LYS LEU ASN ARG GLU LYS ILE SEQRES 1 H 125 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 125 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 125 ASN SER ILE SER SER GLU TYR TYR TRP ALA TRP ILE ARG SEQRES 4 H 125 GLN PRO PRO GLY MET PRO PRO GLU TRP VAL GLY THR ILE SEQRES 5 H 125 TYR HIS THR GLY ASN THR TYR TYR ASN PRO SER LEU LYS SEQRES 6 H 125 SER ARG THR THR ILE SER MET ASP THR SER LYS ASN GLN SEQRES 7 H 125 PHE SER LEU ARG LEU ARG SER VAL THR ALA ALA ASP SER SEQRES 8 H 125 ALA VAL TYR TYR CYS ALA ARG ALA GLY VAL THR ILE PHE SEQRES 9 H 125 GLY LEU THR LEU PRO ASN TYR PHE HIS HIS TRP GLY GLN SEQRES 10 H 125 GLY THR LEU VAL THR VAL SER SER SEQRES 1 L 105 ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SER SEQRES 2 L 105 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 L 105 SER ILE SER ASN TRP MET ALA TRP TYR GLN GLN LYS PRO SEQRES 4 L 105 GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER THR SEQRES 5 L 105 LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY GLY GLY SEQRES 6 L 105 SER GLY PRO GLU PHE THR LEU THR ILE SER SER LEU GLN SEQRES 7 L 105 PRO ASP ASP SER ALA THR TYR TYR CYS GLN GLN TYR ASN SEQRES 8 L 105 SER TYR MET TYR THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 9 L 105 ILE SEQRES 1 W 125 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 W 125 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 W 125 ASN SER ILE SER SER GLU TYR TYR TRP ALA TRP ILE ARG SEQRES 4 W 125 GLN PRO PRO GLY MET PRO PRO GLU TRP VAL GLY THR ILE SEQRES 5 W 125 TYR HIS THR GLY ASN THR TYR TYR ASN PRO SER LEU LYS SEQRES 6 W 125 SER ARG THR THR ILE SER MET ASP THR SER LYS ASN GLN SEQRES 7 W 125 PHE SER LEU ARG LEU ARG SER VAL THR ALA ALA ASP SER SEQRES 8 W 125 ALA VAL TYR TYR CYS ALA ARG ALA GLY VAL THR ILE PHE SEQRES 9 W 125 GLY LEU THR LEU PRO ASN TYR PHE HIS HIS TRP GLY GLN SEQRES 10 W 125 GLY THR LEU VAL THR VAL SER SER SEQRES 1 X 105 ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SER SEQRES 2 X 105 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 X 105 SER ILE SER ASN TRP MET ALA TRP TYR GLN GLN LYS PRO SEQRES 4 X 105 GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER THR SEQRES 5 X 105 LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY GLY GLY SEQRES 6 X 105 SER GLY PRO GLU PHE THR LEU THR ILE SER SER LEU GLN SEQRES 7 X 105 PRO ASP ASP SER ALA THR TYR TYR CYS GLN GLN TYR ASN SEQRES 8 X 105 SER TYR MET TYR THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 9 X 105 ILE SEQRES 1 Y 125 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 Y 125 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 Y 125 ASN SER ILE SER SER GLU TYR TYR TRP ALA TRP ILE ARG SEQRES 4 Y 125 GLN PRO PRO GLY MET PRO PRO GLU TRP VAL GLY THR ILE SEQRES 5 Y 125 TYR HIS THR GLY ASN THR TYR TYR ASN PRO SER LEU LYS SEQRES 6 Y 125 SER ARG THR THR ILE SER MET ASP THR SER LYS ASN GLN SEQRES 7 Y 125 PHE SER LEU ARG LEU ARG SER VAL THR ALA ALA ASP SER SEQRES 8 Y 125 ALA VAL TYR TYR CYS ALA ARG ALA GLY VAL THR ILE PHE SEQRES 9 Y 125 GLY LEU THR LEU PRO ASN TYR PHE HIS HIS TRP GLY GLN SEQRES 10 Y 125 GLY THR LEU VAL THR VAL SER SER SEQRES 1 Z 105 ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SER SEQRES 2 Z 105 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 Z 105 SER ILE SER ASN TRP MET ALA TRP TYR GLN GLN LYS PRO SEQRES 4 Z 105 GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER THR SEQRES 5 Z 105 LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY GLY GLY SEQRES 6 Z 105 SER GLY PRO GLU PHE THR LEU THR ILE SER SER LEU GLN SEQRES 7 Z 105 PRO ASP ASP SER ALA THR TYR TYR CYS GLN GLN TYR ASN SEQRES 8 Z 105 SER TYR MET TYR THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 9 Z 105 ILE HET NAG A 401 14 HET NAG B 501 14 HET NAG C 401 14 HET NAG D 501 14 HET NAG E 401 14 HET NAG F 501 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 13 NAG 6(C8 H15 N O6) HELIX 1 AA1 SER A 65 GLY A 72 1 8 HELIX 2 AA2 ASN A 73 ILE A 80 5 8 HELIX 3 AA3 ASP A 104 LEU A 112 1 9 HELIX 4 AA4 PRO A 125 TRP A 127 1 6 HELIX 5 AA5 ASN A 187 HIS A 196 1 10 HELIX 6 AA6 ASP B 37 LYS B 58 1 22 HELIX 7 AA7 GLU B 74 LEU B 126 1 53 HELIX 8 AA8 ASN B 145 GLY B 155 1 11 HELIX 9 AA9 ASP B 158 ILE B 173 1 16 HELIX 10 AB1 SER C 65 GLY C 72 1 8 HELIX 11 AB2 ASN C 73 ILE C 80 5 8 HELIX 12 AB3 ASP C 104 LEU C 112 1 9 HELIX 13 AB4 ASN C 187 HIS C 196 1 10 HELIX 14 AB5 ASP D 37 LYS D 58 1 22 HELIX 15 AB6 GLU D 74 LEU D 126 1 53 HELIX 16 AB7 ASN D 145 GLY D 155 1 11 HELIX 17 AB8 ASP D 158 ILE D 173 1 16 HELIX 18 AB9 SER E 65 GLY E 72 1 8 HELIX 19 AC1 ASN E 73 ILE E 80 5 8 HELIX 20 AC2 ASP E 104 LEU E 112 1 9 HELIX 21 AC3 ASN E 187 HIS E 196 1 10 HELIX 22 AC4 ASP F 37 LYS F 58 1 22 HELIX 23 AC5 GLU F 74 LEU F 126 1 53 HELIX 24 AC6 ASN F 145 GLY F 155 1 11 HELIX 25 AC7 ASP F 158 ILE F 173 1 16 HELIX 26 AC8 THR H 83 SER H 87 5 5 HELIX 27 AC9 GLN L 79 SER L 83 5 5 HELIX 28 AD1 THR W 83 SER W 87 5 5 HELIX 29 AD2 GLN X 79 SER X 83 5 5 HELIX 30 AD3 THR Y 83 SER Y 87 5 5 HELIX 31 AD4 GLN Z 79 SER Z 83 5 5 SHEET 1 AA1 4 TYR B 22 GLN B 27 0 SHEET 2 AA1 4 THR A 12 TYR A 17 -1 N CYS A 14 O HIS B 25 SHEET 3 AA1 4 CYS B 137 PHE B 140 -1 O PHE B 138 N ILE A 13 SHEET 4 AA1 4 ALA B 130 GLU B 132 -1 N LYS B 131 O GLU B 139 SHEET 1 AA2 2 ASP A 24 VAL A 26 0 SHEET 2 AA2 2 VAL A 34 VAL A 36 -1 O VAL A 34 N VAL A 26 SHEET 1 AA3 2 SER A 39 ASN A 41 0 SHEET 2 AA3 2 ARG A 315 VAL A 317 -1 O MET A 316 N VAL A 40 SHEET 1 AA4 3 LEU A 43 GLU A 44 0 SHEET 2 AA4 3 PHE A 294 GLN A 295 1 O PHE A 294 N GLU A 44 SHEET 3 AA4 3 LYS A 307 TYR A 308 1 O LYS A 307 N GLN A 295 SHEET 1 AA5 2 LEU A 51 ARG A 53 0 SHEET 2 AA5 2 MET A 274 ASP A 278 1 O ASP A 275 N LEU A 51 SHEET 1 AA6 3 LEU A 59 GLN A 60 0 SHEET 2 AA6 3 ILE A 87 GLU A 89 1 O VAL A 88 N LEU A 59 SHEET 3 AA6 3 ILE A 267 ASN A 269 1 O ILE A 268 N GLU A 89 SHEET 1 AA7 5 VAL A 115 GLU A 122 0 SHEET 2 AA7 5 TYR A 256 ARG A 262 -1 O SER A 261 N SER A 116 SHEET 3 AA7 5 GLU A 175 HIS A 183 -1 N LEU A 177 O PHE A 258 SHEET 4 AA7 5 LEU A 251 PRO A 254 -1 O ILE A 252 N GLY A 181 SHEET 5 AA7 5 LEU A 151 TRP A 153 -1 N LEU A 152 O ALA A 253 SHEET 1 AA8 4 VAL A 115 GLU A 122 0 SHEET 2 AA8 4 TYR A 256 ARG A 262 -1 O SER A 261 N SER A 116 SHEET 3 AA8 4 GLU A 175 HIS A 183 -1 N LEU A 177 O PHE A 258 SHEET 4 AA8 4 ILE A 230 LEU A 237 -1 O LEU A 237 N VAL A 176 SHEET 1 AA9 2 SER A 136 HIS A 141 0 SHEET 2 AA9 2 GLU A 144 SER A 146 -1 O GLU A 144 N HIS A 141 SHEET 1 AB1 4 LEU A 164 ALA A 169 0 SHEET 2 AB1 4 THR A 242 ALA A 247 -1 O PHE A 245 N LYS A 166 SHEET 3 AB1 4 VAL A 202 VAL A 205 -1 N VAL A 205 O ILE A 244 SHEET 4 AB1 4 SER A 210 PHE A 213 -1 O ARG A 211 N VAL A 204 SHEET 1 AB2 2 CYS A 281 GLN A 282 0 SHEET 2 AB2 2 ILE A 302 GLY A 303 -1 O ILE A 302 N GLN A 282 SHEET 1 AB3 4 TYR D 22 GLN D 27 0 SHEET 2 AB3 4 THR C 12 TYR C 17 -1 N CYS C 14 O HIS D 25 SHEET 3 AB3 4 CYS D 137 PHE D 140 -1 O PHE D 138 N ILE C 13 SHEET 4 AB3 4 ALA D 130 GLU D 132 -1 N LYS D 131 O GLU D 139 SHEET 1 AB4 2 ASP C 24 VAL C 26 0 SHEET 2 AB4 2 VAL C 34 VAL C 36 -1 O VAL C 34 N VAL C 26 SHEET 1 AB5 2 SER C 39 ASN C 41 0 SHEET 2 AB5 2 ARG C 315 VAL C 317 -1 O MET C 316 N VAL C 40 SHEET 1 AB6 3 LEU C 43 GLU C 44 0 SHEET 2 AB6 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLU C 44 SHEET 3 AB6 3 LYS C 307 TYR C 308 1 O LYS C 307 N GLN C 295 SHEET 1 AB7 2 LEU C 51 ARG C 53 0 SHEET 2 AB7 2 MET C 274 ASP C 278 1 O CYS C 277 N ARG C 53 SHEET 1 AB8 3 LEU C 59 GLN C 60 0 SHEET 2 AB8 3 ILE C 87 GLU C 89 1 O VAL C 88 N LEU C 59 SHEET 3 AB8 3 ILE C 267 ASN C 269 1 O ILE C 268 N ILE C 87 SHEET 1 AB9 5 VAL C 115 GLU C 122 0 SHEET 2 AB9 5 TYR C 256 ARG C 262 -1 O SER C 261 N SER C 116 SHEET 3 AB9 5 GLU C 175 HIS C 183 -1 N LEU C 177 O PHE C 258 SHEET 4 AB9 5 LEU C 251 PRO C 254 -1 O ILE C 252 N GLY C 181 SHEET 5 AB9 5 LEU C 151 TRP C 153 -1 N LEU C 152 O ALA C 253 SHEET 1 AC1 4 VAL C 115 GLU C 122 0 SHEET 2 AC1 4 TYR C 256 ARG C 262 -1 O SER C 261 N SER C 116 SHEET 3 AC1 4 GLU C 175 HIS C 183 -1 N LEU C 177 O PHE C 258 SHEET 4 AC1 4 ILE C 230 LEU C 237 -1 O THR C 235 N VAL C 178 SHEET 1 AC2 2 SER C 136 HIS C 141 0 SHEET 2 AC2 2 GLU C 144 SER C 146 -1 O GLU C 144 N HIS C 141 SHEET 1 AC3 4 LEU C 164 ALA C 169 0 SHEET 2 AC3 4 THR C 242 ALA C 247 -1 O PHE C 245 N LYS C 166 SHEET 3 AC3 4 VAL C 202 VAL C 205 -1 N VAL C 205 O ILE C 244 SHEET 4 AC3 4 SER C 210 PHE C 213 -1 O ARG C 211 N VAL C 204 SHEET 1 AC4 2 CYS C 281 GLN C 282 0 SHEET 2 AC4 2 ILE C 302 GLY C 303 -1 O ILE C 302 N GLN C 282 SHEET 1 AC5 4 TYR F 22 GLN F 27 0 SHEET 2 AC5 4 THR E 12 TYR E 17 -1 N CYS E 14 O HIS F 25 SHEET 3 AC5 4 CYS F 137 PHE F 140 -1 O PHE F 138 N ILE E 13 SHEET 4 AC5 4 ALA F 130 GLU F 132 -1 N LYS F 131 O GLU F 139 SHEET 1 AC6 2 ASP E 24 VAL E 26 0 SHEET 2 AC6 2 VAL E 34 VAL E 36 -1 O VAL E 34 N VAL E 26 SHEET 1 AC7 2 SER E 39 ASN E 41 0 SHEET 2 AC7 2 ARG E 315 VAL E 317 -1 O MET E 316 N VAL E 40 SHEET 1 AC8 3 LEU E 43 GLU E 44 0 SHEET 2 AC8 3 PHE E 294 GLN E 295 1 O PHE E 294 N GLU E 44 SHEET 3 AC8 3 LYS E 307 TYR E 308 1 O LYS E 307 N GLN E 295 SHEET 1 AC9 2 LEU E 51 ARG E 53 0 SHEET 2 AC9 2 MET E 274 ASP E 278 1 O CYS E 277 N ARG E 53 SHEET 1 AD1 3 LEU E 59 GLN E 60 0 SHEET 2 AD1 3 ILE E 87 GLU E 89 1 O VAL E 88 N LEU E 59 SHEET 3 AD1 3 ILE E 267 ASN E 269 1 O ILE E 268 N GLU E 89 SHEET 1 AD2 5 VAL E 115 GLU E 122 0 SHEET 2 AD2 5 TYR E 256 ARG E 262 -1 O SER E 261 N SER E 116 SHEET 3 AD2 5 GLU E 175 HIS E 183 -1 N LEU E 177 O PHE E 258 SHEET 4 AD2 5 LEU E 251 PRO E 254 -1 O ILE E 252 N GLY E 181 SHEET 5 AD2 5 LEU E 151 TRP E 153 -1 N LEU E 152 O ALA E 253 SHEET 1 AD3 4 VAL E 115 GLU E 122 0 SHEET 2 AD3 4 TYR E 256 ARG E 262 -1 O SER E 261 N SER E 116 SHEET 3 AD3 4 GLU E 175 HIS E 183 -1 N LEU E 177 O PHE E 258 SHEET 4 AD3 4 ILE E 230 LEU E 237 -1 O LEU E 237 N VAL E 176 SHEET 1 AD4 2 SER E 136 HIS E 141 0 SHEET 2 AD4 2 GLU E 144 SER E 146 -1 O GLU E 144 N HIS E 141 SHEET 1 AD5 4 LEU E 164 ALA E 169 0 SHEET 2 AD5 4 THR E 242 ALA E 247 -1 O PHE E 245 N LYS E 166 SHEET 3 AD5 4 VAL E 202 VAL E 205 -1 N VAL E 205 O ILE E 244 SHEET 4 AD5 4 SER E 210 PHE E 213 -1 O ARG E 211 N VAL E 204 SHEET 1 AD6 2 CYS E 281 GLN E 282 0 SHEET 2 AD6 2 ILE E 302 GLY E 303 -1 O ILE E 302 N GLN E 282 SHEET 1 AD7 4 GLN H 3 SER H 7 0 SHEET 2 AD7 4 LEU H 18 SER H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 AD7 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AD7 4 ILE H 69 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AD8 6 LEU H 11 VAL H 12 0 SHEET 2 AD8 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AD8 6 ALA H 88 ILE H 99 -1 N ALA H 88 O VAL H 109 SHEET 4 AD8 6 TYR H 34 GLN H 39 -1 N GLN H 39 O VAL H 89 SHEET 5 AD8 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AD8 6 THR H 57 TYR H 59 -1 O TYR H 58 N THR H 50 SHEET 1 AD9 4 LEU H 11 VAL H 12 0 SHEET 2 AD9 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AD9 4 ALA H 88 ILE H 99 -1 N ALA H 88 O VAL H 109 SHEET 4 AD9 4 LEU H 100B TRP H 103 -1 O LEU H 100B N ILE H 99 SHEET 1 AE1 4 MET L 4 SER L 7 0 SHEET 2 AE1 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AE1 4 GLU L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AE1 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AE2 6 THR L 10 SER L 12 0 SHEET 2 AE2 6 THR L 102 GLU L 105 1 O GLU L 105 N LEU L 11 SHEET 3 AE2 6 THR L 85 TYR L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AE2 6 ALA L 34 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AE2 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AE2 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AE3 4 THR L 10 SER L 12 0 SHEET 2 AE3 4 THR L 102 GLU L 105 1 O GLU L 105 N LEU L 11 SHEET 3 AE3 4 THR L 85 TYR L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AE3 4 TYR L 96 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AE4 4 GLN W 3 SER W 7 0 SHEET 2 AE4 4 LEU W 18 SER W 25 -1 O ALA W 23 N GLN W 5 SHEET 3 AE4 4 GLN W 77 LEU W 82 -1 O PHE W 78 N CYS W 22 SHEET 4 AE4 4 ILE W 69 ASP W 72 -1 N ASP W 72 O GLN W 77 SHEET 1 AE5 5 THR W 57 TYR W 59 0 SHEET 2 AE5 5 GLU W 46 ILE W 51 -1 N THR W 50 O TYR W 58 SHEET 3 AE5 5 TYR W 34 GLN W 39 -1 N ARG W 38 O GLU W 46 SHEET 4 AE5 5 ALA W 88 ILE W 99 -1 O VAL W 89 N GLN W 39 SHEET 5 AE5 5 LEU W 100B TRP W 103 -1 O LEU W 100B N ILE W 99 SHEET 1 AE6 5 THR W 57 TYR W 59 0 SHEET 2 AE6 5 GLU W 46 ILE W 51 -1 N THR W 50 O TYR W 58 SHEET 3 AE6 5 TYR W 34 GLN W 39 -1 N ARG W 38 O GLU W 46 SHEET 4 AE6 5 ALA W 88 ILE W 99 -1 O VAL W 89 N GLN W 39 SHEET 5 AE6 5 THR W 107 VAL W 109 -1 O VAL W 109 N ALA W 88 SHEET 1 AE7 4 MET X 4 SER X 7 0 SHEET 2 AE7 4 VAL X 19 ALA X 25 -1 O THR X 22 N SER X 7 SHEET 3 AE7 4 GLU X 70 ILE X 75 -1 O PHE X 71 N CYS X 23 SHEET 4 AE7 4 PHE X 62 SER X 67 -1 N SER X 63 O THR X 74 SHEET 1 AE8 6 THR X 10 SER X 12 0 SHEET 2 AE8 6 THR X 102 GLU X 105 1 O GLU X 105 N LEU X 11 SHEET 3 AE8 6 THR X 85 TYR X 91 -1 N TYR X 86 O THR X 102 SHEET 4 AE8 6 ALA X 34 GLN X 38 -1 N GLN X 38 O THR X 85 SHEET 5 AE8 6 LYS X 45 TYR X 49 -1 O LEU X 47 N TRP X 35 SHEET 6 AE8 6 THR X 53 LEU X 54 -1 O THR X 53 N TYR X 49 SHEET 1 AE9 4 THR X 10 SER X 12 0 SHEET 2 AE9 4 THR X 102 GLU X 105 1 O GLU X 105 N LEU X 11 SHEET 3 AE9 4 THR X 85 TYR X 91 -1 N TYR X 86 O THR X 102 SHEET 4 AE9 4 TYR X 96 PHE X 98 -1 O THR X 97 N GLN X 90 SHEET 1 AF1 4 GLN Y 3 SER Y 7 0 SHEET 2 AF1 4 LEU Y 18 SER Y 25 -1 O ALA Y 23 N GLN Y 5 SHEET 3 AF1 4 GLN Y 77 LEU Y 82 -1 O PHE Y 78 N CYS Y 22 SHEET 4 AF1 4 ILE Y 69 ASP Y 72 -1 N ASP Y 72 O GLN Y 77 SHEET 1 AF2 5 THR Y 57 TYR Y 59 0 SHEET 2 AF2 5 GLU Y 46 ILE Y 51 -1 N THR Y 50 O TYR Y 58 SHEET 3 AF2 5 TYR Y 34 GLN Y 39 -1 N ARG Y 38 O GLU Y 46 SHEET 4 AF2 5 ALA Y 88 ILE Y 99 -1 O VAL Y 89 N GLN Y 39 SHEET 5 AF2 5 LEU Y 100B TRP Y 103 -1 O LEU Y 100B N ILE Y 99 SHEET 1 AF3 5 THR Y 57 TYR Y 59 0 SHEET 2 AF3 5 GLU Y 46 ILE Y 51 -1 N THR Y 50 O TYR Y 58 SHEET 3 AF3 5 TYR Y 34 GLN Y 39 -1 N ARG Y 38 O GLU Y 46 SHEET 4 AF3 5 ALA Y 88 ILE Y 99 -1 O VAL Y 89 N GLN Y 39 SHEET 5 AF3 5 THR Y 107 VAL Y 109 -1 O VAL Y 109 N ALA Y 88 SHEET 1 AF4 4 MET Z 4 SER Z 7 0 SHEET 2 AF4 4 VAL Z 19 ALA Z 25 -1 O THR Z 22 N SER Z 7 SHEET 3 AF4 4 GLU Z 70 ILE Z 75 -1 O PHE Z 71 N CYS Z 23 SHEET 4 AF4 4 PHE Z 62 SER Z 67 -1 N SER Z 63 O THR Z 74 SHEET 1 AF5 6 THR Z 10 SER Z 12 0 SHEET 2 AF5 6 THR Z 102 GLU Z 105 1 O LYS Z 103 N LEU Z 11 SHEET 3 AF5 6 THR Z 85 TYR Z 91 -1 N TYR Z 86 O THR Z 102 SHEET 4 AF5 6 ALA Z 34 GLN Z 38 -1 N GLN Z 38 O THR Z 85 SHEET 5 AF5 6 LYS Z 45 TYR Z 49 -1 O LEU Z 47 N TRP Z 35 SHEET 6 AF5 6 THR Z 53 LEU Z 54 -1 O THR Z 53 N TYR Z 49 SHEET 1 AF6 4 THR Z 10 SER Z 12 0 SHEET 2 AF6 4 THR Z 102 GLU Z 105 1 O LYS Z 103 N LEU Z 11 SHEET 3 AF6 4 THR Z 85 TYR Z 91 -1 N TYR Z 86 O THR Z 102 SHEET 4 AF6 4 TYR Z 96 PHE Z 98 -1 O THR Z 97 N GLN Z 90 SSBOND 1 CYS A 14 CYS B 137 1555 1555 2.03 SSBOND 2 CYS A 52 CYS A 277 1555 1555 2.04 SSBOND 3 CYS A 64 CYS A 76 1555 1555 2.03 SSBOND 4 CYS A 97 CYS A 139 1555 1555 2.03 SSBOND 5 CYS A 281 CYS A 305 1555 1555 2.03 SSBOND 6 CYS B 144 CYS B 148 1555 1555 2.03 SSBOND 7 CYS C 14 CYS D 137 1555 1555 2.03 SSBOND 8 CYS C 52 CYS C 277 1555 1555 2.03 SSBOND 9 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 10 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 11 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 12 CYS D 144 CYS D 148 1555 1555 2.03 SSBOND 13 CYS E 14 CYS F 137 1555 1555 2.03 SSBOND 14 CYS E 52 CYS E 277 1555 1555 2.03 SSBOND 15 CYS E 64 CYS E 76 1555 1555 2.03 SSBOND 16 CYS E 97 CYS E 139 1555 1555 2.03 SSBOND 17 CYS E 281 CYS E 305 1555 1555 2.03 SSBOND 18 CYS F 144 CYS F 148 1555 1555 2.03 SSBOND 19 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 20 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 21 CYS W 22 CYS W 92 1555 1555 2.03 SSBOND 22 CYS X 23 CYS X 88 1555 1555 2.04 SSBOND 23 CYS Y 22 CYS Y 92 1555 1555 2.03 SSBOND 24 CYS Z 23 CYS Z 88 1555 1555 2.04 LINK ND2 ASN A 129 C1 NAG A 401 1555 1555 1.44 LINK ND2 ASN B 154 C1 NAG B 501 1555 1555 1.44 LINK ND2 ASN C 129 C1 NAG C 401 1555 1555 1.44 LINK ND2 ASN D 154 C1 NAG D 501 1555 1555 1.44 LINK ND2 ASN E 129 C1 NAG E 401 1555 1555 1.44 LINK ND2 ASN F 154 C1 NAG F 501 1555 1555 1.44 CISPEP 1 SER L 7 PRO L 8 0 -4.99 CISPEP 2 SER X 7 PRO X 8 0 -4.98 CISPEP 3 SER Z 7 PRO Z 8 0 -7.28 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