HEADER VIRAL PROTEIN/IMMUNE SYSTEM 03-JUN-24 8ZR4 TITLE CRYO-EM STRUCTURE OF THE N2-4N2C402 COMPLEX AT A RESOLUTION OF 1.9 TITLE 2 ANGSTROM COMPND MOL_ID: 1; COMPND 2 MOLECULE: 4N2C402_FAB_H; COMPND 3 CHAIN: A, F, I, L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 4N2C402_FAB_L; COMPND 7 CHAIN: B, G, J, M; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: NEURAMINIDASE; COMPND 11 CHAIN: D, H, K, N; COMPND 12 EC: 3.2.1.18; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 17 ORGANISM_TAXID: 11320; SOURCE 18 GENE: NA; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS VIRAL ENZYME, ANTIBODY, COMPLEX, INHIBITOR, VIRAL PROTEIN/IMMUNE KEYWDS 2 SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR B.X.CHU,X.WANG,Q.YANG,X.D.WU,Z.L.ZHANG REVDAT 1 01-JAN-25 8ZR4 0 JRNL AUTH X.WANG,Q.YANG,B.X.CHU,X.D.WU,Z.L.ZHANG JRNL TITL PROFILING INFLUENZA NEURAMINIDASE PRE-EXISTING HUMORAL JRNL TITL 2 IMMUNITY IN HUMANS JRNL REF CELL HOST MICROBE 2024 JRNL REFN ESSN 1934-6069 REMARK 2 REMARK 2 RESOLUTION. 1.90 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) : 1.900 REMARK 3 NUMBER OF PARTICLES : 663111 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 8ZR4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 07-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1300048391. 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 : A COMPLEX OF N2 WITH 4N2C402 REMARK 245 -FAB 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 : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : OTHER REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : OTHER 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, F, G, H, I, J, K, L, REMARK 350 AND CHAINS: M, N, O, P, Q, R 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 A 1 REMARK 465 ARG A 15 REMARK 465 PRO A 41 REMARK 465 GLY A 42 REMARK 465 LYS A 43 REMARK 465 ALA A 88 REMARK 465 GLU A 89 REMARK 465 SER A 134 REMARK 465 SER A 135 REMARK 465 ASP B 1 REMARK 465 LYS B 113 REMARK 465 ILE D 1 REMARK 465 CYS D 2 REMARK 465 PRO D 3 REMARK 465 LYS D 4 REMARK 465 PRO D 5 REMARK 465 HIS D 392 REMARK 465 ILE D 393 REMARK 465 GLN F 1 REMARK 465 ARG F 15 REMARK 465 PRO F 41 REMARK 465 GLY F 42 REMARK 465 LYS F 43 REMARK 465 ALA F 88 REMARK 465 GLU F 89 REMARK 465 VAL F 133 REMARK 465 SER F 134 REMARK 465 SER F 135 REMARK 465 ASP G 1 REMARK 465 ILE G 112 REMARK 465 LYS G 113 REMARK 465 ILE H 1 REMARK 465 CYS H 2 REMARK 465 PRO H 3 REMARK 465 LYS H 4 REMARK 465 PRO H 5 REMARK 465 HIS H 392 REMARK 465 ILE H 393 REMARK 465 GLN I 1 REMARK 465 ARG I 15 REMARK 465 PRO I 41 REMARK 465 GLY I 42 REMARK 465 LYS I 43 REMARK 465 ALA I 88 REMARK 465 GLU I 89 REMARK 465 SER I 134 REMARK 465 SER I 135 REMARK 465 ASP J 1 REMARK 465 ILE J 112 REMARK 465 LYS J 113 REMARK 465 ILE K 1 REMARK 465 CYS K 2 REMARK 465 PRO K 3 REMARK 465 LYS K 4 REMARK 465 PRO K 5 REMARK 465 HIS K 392 REMARK 465 ILE K 393 REMARK 465 GLN L 1 REMARK 465 ARG L 15 REMARK 465 PRO L 41 REMARK 465 GLY L 42 REMARK 465 LYS L 43 REMARK 465 ALA L 88 REMARK 465 GLU L 89 REMARK 465 SER L 134 REMARK 465 SER L 135 REMARK 465 ASP M 1 REMARK 465 ILE M 112 REMARK 465 LYS M 113 REMARK 465 ILE N 1 REMARK 465 CYS N 2 REMARK 465 PRO N 3 REMARK 465 LYS N 4 REMARK 465 PRO N 5 REMARK 465 HIS N 392 REMARK 465 ILE N 393 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 OE1 GLN K 15 HE ARG K 344 1.50 REMARK 500 O VAL N 304 HG SER N 312 1.52 REMARK 500 OE1 GLN D 15 HE ARG D 344 1.54 REMARK 500 OE1 GLN H 15 HE ARG H 344 1.57 REMARK 500 O VAL I 37 H TYR I 95 1.58 REMARK 500 O VAL L 37 H TYR L 95 1.58 REMARK 500 OE1 GLN N 15 HE ARG N 344 1.58 REMARK 500 H ILE D 226 O SER D 239 1.58 REMARK 500 H ILE K 226 O SER K 239 1.59 REMARK 500 H ILE H 226 O SER H 239 1.59 REMARK 500 H ILE N 226 O SER N 239 1.59 REMARK 500 OD1 ASP A 115 HH22 ARG D 295 1.59 REMARK 500 O VAL F 37 H TYR F 95 1.59 REMARK 500 OD1 ASP I 115 HH22 ARG K 295 1.59 REMARK 500 OE1 GLN K 315 HO2 BMA O 3 1.60 REMARK 500 OE1 GLN H 315 HO2 BMA R 3 1.60 REMARK 500 OH TYR B 54 O HOH B 201 2.07 REMARK 500 OG SER D 141 OD2 ASP D 167 2.11 REMARK 500 OG SER N 141 OD2 ASP N 167 2.11 REMARK 500 OG SER H 141 OD2 ASP H 167 2.11 REMARK 500 OG SER K 141 OD2 ASP K 167 2.11 REMARK 500 O SER D 328 O HOH D 501 2.12 REMARK 500 OD1 ASN A 113 O HOH A 201 2.13 REMARK 500 OD1 ASN I 113 O HOH I 201 2.14 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 VAL A 48 -60.94 -107.45 REMARK 500 ARG A 116 70.27 -112.98 REMARK 500 ASP B 65 2.39 -68.98 REMARK 500 ASN D 124 41.46 -141.31 REMARK 500 ILE D 146 72.26 52.63 REMARK 500 ILE D 146 73.37 51.46 REMARK 500 THR D 149 -166.46 -128.98 REMARK 500 CYS D 215 -169.18 -124.92 REMARK 500 SER D 239 -165.44 -161.81 REMARK 500 SER D 243 127.28 -38.26 REMARK 500 HIS D 271 -178.42 60.32 REMARK 500 SER D 328 -169.25 -125.74 REMARK 500 VAL F 48 -61.37 -107.49 REMARK 500 ARG F 116 70.40 -113.16 REMARK 500 ASP G 65 2.96 -69.30 REMARK 500 ASN H 124 44.26 -141.54 REMARK 500 ILE H 146 71.80 51.25 REMARK 500 ILE H 146 72.91 50.11 REMARK 500 THR H 149 -166.35 -128.85 REMARK 500 CYS H 215 -168.91 -125.13 REMARK 500 SER H 239 -165.21 -161.91 REMARK 500 SER H 243 125.02 -38.13 REMARK 500 HIS H 271 -178.35 60.04 REMARK 500 VAL I 48 -61.15 -107.37 REMARK 500 ARG I 116 69.39 -113.89 REMARK 500 ASP J 65 3.03 -69.37 REMARK 500 ASN K 124 46.26 -141.97 REMARK 500 ILE K 146 71.91 51.26 REMARK 500 ILE K 146 72.96 50.18 REMARK 500 THR K 149 -166.28 -128.88 REMARK 500 CYS K 215 -168.90 -125.13 REMARK 500 SER K 239 -165.23 -161.95 REMARK 500 SER K 243 125.02 -37.79 REMARK 500 HIS K 271 -178.35 59.94 REMARK 500 GLU K 292 -9.25 73.94 REMARK 500 VAL L 48 -61.12 -107.51 REMARK 500 ARG L 116 69.35 -113.98 REMARK 500 ASP M 65 2.94 -69.45 REMARK 500 ASN N 124 45.99 -141.48 REMARK 500 ILE N 146 71.87 51.28 REMARK 500 ILE N 146 72.97 50.13 REMARK 500 THR N 149 -166.36 -128.97 REMARK 500 CYS N 215 -168.92 -125.13 REMARK 500 SER N 239 -165.30 -161.98 REMARK 500 SER N 243 125.06 -38.66 REMARK 500 HIS N 271 -178.43 60.10 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG O 1 REMARK 610 NAG P 1 REMARK 610 NAG Q 1 REMARK 610 NAG R 1 REMARK 610 NAG D 401 REMARK 610 NAG D 402 REMARK 610 NAG H 401 REMARK 610 NAG H 402 REMARK 610 NAG K 401 REMARK 610 NAG K 402 REMARK 610 NAG N 401 REMARK 610 NAG N 402 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 D 403 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 217 O REMARK 620 2 GLY D 221 O 80.6 REMARK 620 3 ASP D 248 OD2 94.1 92.3 REMARK 620 4 GLY D 269 O 91.9 91.8 173.2 REMARK 620 5 HIS D 271 O 91.2 160.8 105.7 71.0 REMARK 620 6 HOH D 511 O 167.8 95.7 97.7 76.5 88.7 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA H 403 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP H 217 O REMARK 620 2 GLY H 221 O 80.1 REMARK 620 3 ASP H 248 OD2 92.7 91.1 REMARK 620 4 GLY H 269 O 91.3 91.5 175.5 REMARK 620 5 HIS H 271 O 91.2 159.7 107.7 70.2 REMARK 620 6 HOH H 508 O 166.8 95.6 99.9 76.2 88.8 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA K 403 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP K 217 O REMARK 620 2 GLY K 221 O 80.0 REMARK 620 3 ASP K 248 OD2 92.7 90.7 REMARK 620 4 GLY K 269 O 91.2 91.6 175.8 REMARK 620 5 HIS K 271 O 91.2 160.0 107.8 70.5 REMARK 620 6 HOH K 510 O 166.9 95.6 99.8 76.5 88.9 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA N 403 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP N 217 O REMARK 620 2 GLY N 221 O 80.0 REMARK 620 3 ASP N 248 OD2 92.6 90.8 REMARK 620 4 GLY N 269 O 91.1 91.5 175.9 REMARK 620 5 HIS N 271 O 91.3 159.9 107.8 70.4 REMARK 620 6 HOH N 511 O 166.8 95.6 99.9 76.5 88.9 REMARK 620 N 1 2 3 4 5 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60391 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE N2-4N2C402 COMPLEX AT A RESOLUTION OF 1.9 REMARK 900 ANGSTROM DBREF 8ZR4 A 1 135 PDB 8ZR4 8ZR4 1 135 DBREF 8ZR4 B 1 113 PDB 8ZR4 8ZR4 1 113 DBREF1 8ZR4 D 1 393 UNP A0A346HBH4_9INFA DBREF2 8ZR4 D A0A346HBH4 77 469 DBREF 8ZR4 F 1 135 PDB 8ZR4 8ZR4 1 135 DBREF 8ZR4 G 1 113 PDB 8ZR4 8ZR4 1 113 DBREF1 8ZR4 H 1 393 UNP A0A346HBH4_9INFA DBREF2 8ZR4 H A0A346HBH4 77 469 DBREF 8ZR4 I 1 135 PDB 8ZR4 8ZR4 1 135 DBREF 8ZR4 J 1 113 PDB 8ZR4 8ZR4 1 113 DBREF1 8ZR4 K 1 393 UNP A0A346HBH4_9INFA DBREF2 8ZR4 K A0A346HBH4 77 469 DBREF 8ZR4 L 1 135 PDB 8ZR4 8ZR4 1 135 DBREF 8ZR4 M 1 113 PDB 8ZR4 8ZR4 1 113 DBREF1 8ZR4 N 1 393 UNP A0A346HBH4_9INFA DBREF2 8ZR4 N A0A346HBH4 77 469 SEQRES 1 A 135 GLN GLY ARG LEU GLN GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 A 135 PRO ARG ARG SER LEU THR LEU SER CYS ALA ALA SER GLY SEQRES 3 A 135 PHE THR LEU GLU THR TYR THR MET HIS TRP VAL ARG GLN SEQRES 4 A 135 THR PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL SER SER SEQRES 5 A 135 LYS ASP GLY ASN ASN VAL TYR TYR ARG ASP SER VAL LYS SEQRES 6 A 135 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 135 LEU PHE LEU GLN MET ASN HIS LEU ARG ALA GLU ASP THR SEQRES 8 A 135 ALA LEU TYR TYR CYS ALA ARG GLY SER ASP PRO ASP TYR SEQRES 9 A 135 ASP LYS GLY TRP GLY ALA TYR ARG ASN THR ASP ARG PRO SEQRES 10 A 135 SER TYR ASP GLY LEU ASP VAL TRP GLY GLN GLY THR THR SEQRES 11 A 135 VAL THR VAL SER SER SEQRES 1 B 113 ASP ILE VAL MET THR GLN SER PRO LEU PHE LEU SER VAL SEQRES 2 B 113 THR PRO GLY GLU SER ALA SER ILE SER CYS ARG SER SER SEQRES 3 B 113 GLN SER LEU LEU HIS SER ASN GLY TYR ASN TYR LEU ASP SEQRES 4 B 113 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 B 113 ILE TYR TRP GLY SER ASN ARG ALA SER GLY VAL SER ASP SEQRES 6 B 113 ARG PHE SER GLY ARG GLY SER GLY THR ASP PHE THR LEU SEQRES 7 B 113 THR ILE TYR ASN VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 B 113 TYR CYS MET GLN ALA LEU GLN THR PRO PRO TRP THR PHE SEQRES 9 B 113 GLY GLN GLY THR LYS VAL ASP ILE LYS SEQRES 1 D 393 ILE CYS PRO LYS PRO ALA GLU TYR ARG ASN TRP SER LYS SEQRES 2 D 393 PRO GLN CYS GLY ILE THR GLY PHE ALA PRO PHE SER LYS SEQRES 3 D 393 ASP ASN SER ILE ARG LEU SER ALA GLY GLY ASP ILE TRP SEQRES 4 D 393 VAL THR ARG GLU PRO TYR VAL SER CYS ASP PRO ASP LYS SEQRES 5 D 393 CYS TYR GLN PHE ALA LEU GLY GLN GLY THR THR ILE ASN SEQRES 6 D 393 ASN VAL HIS SER ASN ASN THR ALA ARG ASP ARG THR PRO SEQRES 7 D 393 HIS ARG THR LEU LEU MET ASN GLU LEU GLY VAL PRO PHE SEQRES 8 D 393 HIS LEU GLY THR LYS GLN VAL CYS ILE ALA TRP SER SER SEQRES 9 D 393 SER SER CYS HIS ASP GLY LYS ALA TRP LEU HIS VAL CYS SEQRES 10 D 393 ILE THR GLY ASP ASP LYS ASN ALA THR ALA SER PHE ILE SEQRES 11 D 393 TYR ASN GLY ARG LEU VAL ASP SER VAL VAL SER TRP SER SEQRES 12 D 393 LYS ASP ILE LEU ARG THR GLN GLU SER GLU CYS VAL CYS SEQRES 13 D 393 ILE ASN GLY THR CYS THR VAL VAL MET THR ASP GLY ASN SEQRES 14 D 393 ALA THR GLY LYS ALA ASP THR LYS ILE LEU PHE ILE GLU SEQRES 15 D 393 GLU GLY LYS ILE VAL HIS THR SER LYS LEU SER GLY SER SEQRES 16 D 393 ALA GLN HIS VAL GLU GLU CYS SER CYS TYR PRO ARG TYR SEQRES 17 D 393 PRO GLY VAL ARG CYS VAL CYS ARG ASP ASN TRP LYS GLY SEQRES 18 D 393 SER ASN ARG PRO ILE VAL ASP ILE ASN ILE LYS ASP HIS SEQRES 19 D 393 SER ILE VAL SER SER TYR VAL CYS SER GLY LEU VAL GLY SEQRES 20 D 393 ASP THR PRO ARG LYS THR ASP SER SER SER SER SER HIS SEQRES 21 D 393 CYS LEU ASN PRO ASN ASN GLU LYS GLY GLY HIS GLY VAL SEQRES 22 D 393 LYS GLY TRP ALA PHE ASP ASP GLY ASN ASP VAL TRP MET SEQRES 23 D 393 GLY ARG THR ILE ASN GLU THR SER ARG LEU GLY TYR GLU SEQRES 24 D 393 THR PHE LYS VAL VAL GLU GLY TRP SER ASN PRO LYS SER SEQRES 25 D 393 LYS LEU GLN ILE ASN ARG GLN VAL ILE VAL ASP ARG GLY SEQRES 26 D 393 ASP ARG SER GLY TYR SER GLY ILE PHE SER VAL GLU GLY SEQRES 27 D 393 LYS SER CYS ILE ASN ARG CYS PHE TYR VAL GLU LEU ILE SEQRES 28 D 393 ARG GLY ARG LYS GLU GLU THR GLU VAL LEU TRP THR SER SEQRES 29 D 393 ASN SER ILE VAL VAL PHE CYS GLY THR SER GLY THR TYR SEQRES 30 D 393 GLY THR GLY SER TRP PRO ASP GLY ALA ASP LEU ASN LEU SEQRES 31 D 393 MET HIS ILE SEQRES 1 F 135 GLN GLY ARG LEU GLN GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 F 135 PRO ARG ARG SER LEU THR LEU SER CYS ALA ALA SER GLY SEQRES 3 F 135 PHE THR LEU GLU THR TYR THR MET HIS TRP VAL ARG GLN SEQRES 4 F 135 THR PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL SER SER SEQRES 5 F 135 LYS ASP GLY ASN ASN VAL TYR TYR ARG ASP SER VAL LYS SEQRES 6 F 135 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASN THR SEQRES 7 F 135 LEU PHE LEU GLN MET ASN HIS LEU ARG ALA GLU ASP THR SEQRES 8 F 135 ALA LEU TYR TYR CYS ALA ARG GLY SER ASP PRO ASP TYR SEQRES 9 F 135 ASP LYS GLY TRP GLY ALA TYR ARG ASN THR ASP ARG PRO SEQRES 10 F 135 SER TYR ASP GLY LEU ASP VAL TRP GLY GLN GLY THR THR SEQRES 11 F 135 VAL THR VAL SER SER SEQRES 1 G 113 ASP ILE VAL MET THR GLN SER PRO LEU PHE LEU SER VAL SEQRES 2 G 113 THR PRO GLY GLU SER ALA SER ILE SER CYS ARG SER SER SEQRES 3 G 113 GLN SER LEU LEU HIS SER ASN GLY TYR ASN TYR LEU ASP SEQRES 4 G 113 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 G 113 ILE TYR TRP GLY SER ASN ARG ALA SER GLY VAL SER ASP SEQRES 6 G 113 ARG PHE SER GLY ARG GLY SER GLY THR ASP PHE THR LEU SEQRES 7 G 113 THR ILE TYR ASN VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 G 113 TYR CYS MET GLN ALA LEU GLN THR PRO PRO TRP THR PHE SEQRES 9 G 113 GLY GLN GLY THR LYS VAL ASP ILE LYS SEQRES 1 H 393 ILE CYS PRO LYS PRO ALA GLU TYR ARG ASN TRP SER LYS SEQRES 2 H 393 PRO GLN CYS GLY ILE THR GLY PHE ALA PRO PHE SER LYS SEQRES 3 H 393 ASP ASN SER ILE ARG LEU SER ALA GLY GLY ASP ILE TRP SEQRES 4 H 393 VAL THR ARG GLU PRO TYR VAL SER CYS ASP PRO ASP LYS SEQRES 5 H 393 CYS TYR GLN PHE ALA LEU GLY GLN GLY THR THR ILE ASN SEQRES 6 H 393 ASN VAL HIS SER ASN ASN THR ALA ARG ASP ARG THR PRO SEQRES 7 H 393 HIS ARG THR LEU LEU MET ASN GLU LEU GLY VAL PRO PHE SEQRES 8 H 393 HIS LEU GLY THR LYS GLN VAL CYS ILE ALA TRP SER SER SEQRES 9 H 393 SER SER CYS HIS ASP GLY LYS ALA TRP LEU HIS VAL CYS SEQRES 10 H 393 ILE THR GLY ASP ASP LYS ASN ALA THR ALA SER PHE ILE SEQRES 11 H 393 TYR ASN GLY ARG LEU VAL ASP SER VAL VAL SER TRP SER SEQRES 12 H 393 LYS ASP ILE LEU ARG THR GLN GLU SER GLU CYS VAL CYS SEQRES 13 H 393 ILE ASN GLY THR CYS THR VAL VAL MET THR ASP GLY ASN SEQRES 14 H 393 ALA THR GLY LYS ALA ASP THR LYS ILE LEU PHE ILE GLU SEQRES 15 H 393 GLU GLY LYS ILE VAL HIS THR SER LYS LEU SER GLY SER SEQRES 16 H 393 ALA GLN HIS VAL GLU GLU CYS SER CYS TYR PRO ARG TYR SEQRES 17 H 393 PRO GLY VAL ARG CYS VAL CYS ARG ASP ASN TRP LYS GLY SEQRES 18 H 393 SER ASN ARG PRO ILE VAL ASP ILE ASN ILE LYS ASP HIS SEQRES 19 H 393 SER ILE VAL SER SER TYR VAL CYS SER GLY LEU VAL GLY SEQRES 20 H 393 ASP THR PRO ARG LYS THR ASP SER SER SER SER SER HIS SEQRES 21 H 393 CYS LEU ASN PRO ASN ASN GLU LYS GLY GLY HIS GLY VAL SEQRES 22 H 393 LYS GLY TRP ALA PHE ASP ASP GLY ASN ASP VAL TRP MET SEQRES 23 H 393 GLY ARG THR ILE ASN GLU THR SER ARG LEU GLY TYR GLU SEQRES 24 H 393 THR PHE LYS VAL VAL GLU GLY TRP SER ASN PRO LYS SER SEQRES 25 H 393 LYS LEU GLN ILE ASN ARG GLN VAL ILE VAL ASP ARG GLY SEQRES 26 H 393 ASP ARG SER GLY TYR SER GLY ILE PHE SER VAL GLU GLY SEQRES 27 H 393 LYS SER CYS ILE ASN ARG CYS PHE TYR VAL GLU LEU ILE SEQRES 28 H 393 ARG GLY ARG LYS GLU GLU THR GLU VAL LEU TRP THR SER SEQRES 29 H 393 ASN SER ILE VAL VAL PHE CYS GLY THR SER GLY THR TYR SEQRES 30 H 393 GLY THR GLY SER TRP PRO ASP GLY ALA ASP LEU ASN LEU SEQRES 31 H 393 MET HIS ILE SEQRES 1 I 135 GLN GLY ARG LEU GLN GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 I 135 PRO ARG ARG SER LEU THR LEU SER CYS ALA ALA SER GLY SEQRES 3 I 135 PHE THR LEU GLU THR TYR THR MET HIS TRP VAL ARG GLN SEQRES 4 I 135 THR PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL SER SER SEQRES 5 I 135 LYS ASP GLY ASN ASN VAL TYR TYR ARG ASP SER VAL LYS SEQRES 6 I 135 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASN THR SEQRES 7 I 135 LEU PHE LEU GLN MET ASN HIS LEU ARG ALA GLU ASP THR SEQRES 8 I 135 ALA LEU TYR TYR CYS ALA ARG GLY SER ASP PRO ASP TYR SEQRES 9 I 135 ASP LYS GLY TRP GLY ALA TYR ARG ASN THR ASP ARG PRO SEQRES 10 I 135 SER TYR ASP GLY LEU ASP VAL TRP GLY GLN GLY THR THR SEQRES 11 I 135 VAL THR VAL SER SER SEQRES 1 J 113 ASP ILE VAL MET THR GLN SER PRO LEU PHE LEU SER VAL SEQRES 2 J 113 THR PRO GLY GLU SER ALA SER ILE SER CYS ARG SER SER SEQRES 3 J 113 GLN SER LEU LEU HIS SER ASN GLY TYR ASN TYR LEU ASP SEQRES 4 J 113 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 J 113 ILE TYR TRP GLY SER ASN ARG ALA SER GLY VAL SER ASP SEQRES 6 J 113 ARG PHE SER GLY ARG GLY SER GLY THR ASP PHE THR LEU SEQRES 7 J 113 THR ILE TYR ASN VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 J 113 TYR CYS MET GLN ALA LEU GLN THR PRO PRO TRP THR PHE SEQRES 9 J 113 GLY GLN GLY THR LYS VAL ASP ILE LYS SEQRES 1 K 393 ILE CYS PRO LYS PRO ALA GLU TYR ARG ASN TRP SER LYS SEQRES 2 K 393 PRO GLN CYS GLY ILE THR GLY PHE ALA PRO PHE SER LYS SEQRES 3 K 393 ASP ASN SER ILE ARG LEU SER ALA GLY GLY ASP ILE TRP SEQRES 4 K 393 VAL THR ARG GLU PRO TYR VAL SER CYS ASP PRO ASP LYS SEQRES 5 K 393 CYS TYR GLN PHE ALA LEU GLY GLN GLY THR THR ILE ASN SEQRES 6 K 393 ASN VAL HIS SER ASN ASN THR ALA ARG ASP ARG THR PRO SEQRES 7 K 393 HIS ARG THR LEU LEU MET ASN GLU LEU GLY VAL PRO PHE SEQRES 8 K 393 HIS LEU GLY THR LYS GLN VAL CYS ILE ALA TRP SER SER SEQRES 9 K 393 SER SER CYS HIS ASP GLY LYS ALA TRP LEU HIS VAL CYS SEQRES 10 K 393 ILE THR GLY ASP ASP LYS ASN ALA THR ALA SER PHE ILE SEQRES 11 K 393 TYR ASN GLY ARG LEU VAL ASP SER VAL VAL SER TRP SER SEQRES 12 K 393 LYS ASP ILE LEU ARG THR GLN GLU SER GLU CYS VAL CYS SEQRES 13 K 393 ILE ASN GLY THR CYS THR VAL VAL MET THR ASP GLY ASN SEQRES 14 K 393 ALA THR GLY LYS ALA ASP THR LYS ILE LEU PHE ILE GLU SEQRES 15 K 393 GLU GLY LYS ILE VAL HIS THR SER LYS LEU SER GLY SER SEQRES 16 K 393 ALA GLN HIS VAL GLU GLU CYS SER CYS TYR PRO ARG TYR SEQRES 17 K 393 PRO GLY VAL ARG CYS VAL CYS ARG ASP ASN TRP LYS GLY SEQRES 18 K 393 SER ASN ARG PRO ILE VAL ASP ILE ASN ILE LYS ASP HIS SEQRES 19 K 393 SER ILE VAL SER SER TYR VAL CYS SER GLY LEU VAL GLY SEQRES 20 K 393 ASP THR PRO ARG LYS THR ASP SER SER SER SER SER HIS SEQRES 21 K 393 CYS LEU ASN PRO ASN ASN GLU LYS GLY GLY HIS GLY VAL SEQRES 22 K 393 LYS GLY TRP ALA PHE ASP ASP GLY ASN ASP VAL TRP MET SEQRES 23 K 393 GLY ARG THR ILE ASN GLU THR SER ARG LEU GLY TYR GLU SEQRES 24 K 393 THR PHE LYS VAL VAL GLU GLY TRP SER ASN PRO LYS SER SEQRES 25 K 393 LYS LEU GLN ILE ASN ARG GLN VAL ILE VAL ASP ARG GLY SEQRES 26 K 393 ASP ARG SER GLY TYR SER GLY ILE PHE SER VAL GLU GLY SEQRES 27 K 393 LYS SER CYS ILE ASN ARG CYS PHE TYR VAL GLU LEU ILE SEQRES 28 K 393 ARG GLY ARG LYS GLU GLU THR GLU VAL LEU TRP THR SER SEQRES 29 K 393 ASN SER ILE VAL VAL PHE CYS GLY THR SER GLY THR TYR SEQRES 30 K 393 GLY THR GLY SER TRP PRO ASP GLY ALA ASP LEU ASN LEU SEQRES 31 K 393 MET HIS ILE SEQRES 1 L 135 GLN GLY ARG LEU GLN GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 L 135 PRO ARG ARG SER LEU THR LEU SER CYS ALA ALA SER GLY SEQRES 3 L 135 PHE THR LEU GLU THR TYR THR MET HIS TRP VAL ARG GLN SEQRES 4 L 135 THR PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL SER SER SEQRES 5 L 135 LYS ASP GLY ASN ASN VAL TYR TYR ARG ASP SER VAL LYS SEQRES 6 L 135 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASN THR SEQRES 7 L 135 LEU PHE LEU GLN MET ASN HIS LEU ARG ALA GLU ASP THR SEQRES 8 L 135 ALA LEU TYR TYR CYS ALA ARG GLY SER ASP PRO ASP TYR SEQRES 9 L 135 ASP LYS GLY TRP GLY ALA TYR ARG ASN THR ASP ARG PRO SEQRES 10 L 135 SER TYR ASP GLY LEU ASP VAL TRP GLY GLN GLY THR THR SEQRES 11 L 135 VAL THR VAL SER SER SEQRES 1 M 113 ASP ILE VAL MET THR GLN SER PRO LEU PHE LEU SER VAL SEQRES 2 M 113 THR PRO GLY GLU SER ALA SER ILE SER CYS ARG SER SER SEQRES 3 M 113 GLN SER LEU LEU HIS SER ASN GLY TYR ASN TYR LEU ASP SEQRES 4 M 113 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 M 113 ILE TYR TRP GLY SER ASN ARG ALA SER GLY VAL SER ASP SEQRES 6 M 113 ARG PHE SER GLY ARG GLY SER GLY THR ASP PHE THR LEU SEQRES 7 M 113 THR ILE TYR ASN VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 M 113 TYR CYS MET GLN ALA LEU GLN THR PRO PRO TRP THR PHE SEQRES 9 M 113 GLY GLN GLY THR LYS VAL ASP ILE LYS SEQRES 1 N 393 ILE CYS PRO LYS PRO ALA GLU TYR ARG ASN TRP SER LYS SEQRES 2 N 393 PRO GLN CYS GLY ILE THR GLY PHE ALA PRO PHE SER LYS SEQRES 3 N 393 ASP ASN SER ILE ARG LEU SER ALA GLY GLY ASP ILE TRP SEQRES 4 N 393 VAL THR ARG GLU PRO TYR VAL SER CYS ASP PRO ASP LYS SEQRES 5 N 393 CYS TYR GLN PHE ALA LEU GLY GLN GLY THR THR ILE ASN SEQRES 6 N 393 ASN VAL HIS SER ASN ASN THR ALA ARG ASP ARG THR PRO SEQRES 7 N 393 HIS ARG THR LEU LEU MET ASN GLU LEU GLY VAL PRO PHE SEQRES 8 N 393 HIS LEU GLY THR LYS GLN VAL CYS ILE ALA TRP SER SER SEQRES 9 N 393 SER SER CYS HIS ASP GLY LYS ALA TRP LEU HIS VAL CYS SEQRES 10 N 393 ILE THR GLY ASP ASP LYS ASN ALA THR ALA SER PHE ILE SEQRES 11 N 393 TYR ASN GLY ARG LEU VAL ASP SER VAL VAL SER TRP SER SEQRES 12 N 393 LYS ASP ILE LEU ARG THR GLN GLU SER GLU CYS VAL CYS SEQRES 13 N 393 ILE ASN GLY THR CYS THR VAL VAL MET THR ASP GLY ASN SEQRES 14 N 393 ALA THR GLY LYS ALA ASP THR LYS ILE LEU PHE ILE GLU SEQRES 15 N 393 GLU GLY LYS ILE VAL HIS THR SER LYS LEU SER GLY SER SEQRES 16 N 393 ALA GLN HIS VAL GLU GLU CYS SER CYS TYR PRO ARG TYR SEQRES 17 N 393 PRO GLY VAL ARG CYS VAL CYS ARG ASP ASN TRP LYS GLY SEQRES 18 N 393 SER ASN ARG PRO ILE VAL ASP ILE ASN ILE LYS ASP HIS SEQRES 19 N 393 SER ILE VAL SER SER TYR VAL CYS SER GLY LEU VAL GLY SEQRES 20 N 393 ASP THR PRO ARG LYS THR ASP SER SER SER SER SER HIS SEQRES 21 N 393 CYS LEU ASN PRO ASN ASN GLU LYS GLY GLY HIS GLY VAL SEQRES 22 N 393 LYS GLY TRP ALA PHE ASP ASP GLY ASN ASP VAL TRP MET SEQRES 23 N 393 GLY ARG THR ILE ASN GLU THR SER ARG LEU GLY TYR GLU SEQRES 24 N 393 THR PHE LYS VAL VAL GLU GLY TRP SER ASN PRO LYS SER SEQRES 25 N 393 LYS LEU GLN ILE ASN ARG GLN VAL ILE VAL ASP ARG GLY SEQRES 26 N 393 ASP ARG SER GLY TYR SER GLY ILE PHE SER VAL GLU GLY SEQRES 27 N 393 LYS SER CYS ILE ASN ARG CYS PHE TYR VAL GLU LEU ILE SEQRES 28 N 393 ARG GLY ARG LYS GLU GLU THR GLU VAL LEU TRP THR SER SEQRES 29 N 393 ASN SER ILE VAL VAL PHE CYS GLY THR SER GLY THR TYR SEQRES 30 N 393 GLY THR GLY SER TRP PRO ASP GLY ALA ASP LEU ASN LEU SEQRES 31 N 393 MET HIS ILE HET NAG O 1 26 HET NAG O 2 26 HET BMA O 3 19 HET MAN O 4 21 HET MAN O 5 21 HET NAG P 1 26 HET NAG P 2 26 HET BMA P 3 19 HET MAN P 4 21 HET MAN P 5 21 HET NAG Q 1 26 HET NAG Q 2 26 HET BMA Q 3 19 HET MAN Q 4 21 HET MAN Q 5 21 HET NAG R 1 26 HET NAG R 2 26 HET BMA R 3 19 HET MAN R 4 21 HET MAN R 5 21 HET NAG D 401 27 HET NAG D 402 27 HET CA D 403 1 HET NAG H 401 27 HET NAG H 402 27 HET CA H 403 1 HET NAG K 401 27 HET NAG K 402 27 HET CA K 403 1 HET NAG N 401 27 HET NAG N 402 27 HET CA N 403 1 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM CA CALCIUM ION HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 13 NAG 16(C8 H15 N O6) FORMUL 13 BMA 4(C6 H12 O6) FORMUL 13 MAN 8(C6 H12 O6) FORMUL 19 CA 4(CA 2+) FORMUL 29 HOH *789(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ASP A 62 LYS A 65 5 4 HELIX 3 AA3 ASP A 103 GLY A 107 5 5 HELIX 4 AA4 GLU B 84 VAL B 88 5 5 HELIX 5 AA5 ASN D 28 ALA D 34 1 7 HELIX 6 AA6 ASN D 66 ASN D 70 5 5 HELIX 7 AA7 ASP D 387 MET D 391 5 5 HELIX 8 AA8 THR F 28 TYR F 32 5 5 HELIX 9 AA9 ASP F 62 LYS F 65 5 4 HELIX 10 AB1 ASP F 103 GLY F 107 5 5 HELIX 11 AB2 GLU G 84 VAL G 88 5 5 HELIX 12 AB3 ASN H 28 ALA H 34 1 7 HELIX 13 AB4 ASN H 66 ASN H 70 5 5 HELIX 14 AB5 ASP H 387 MET H 391 5 5 HELIX 15 AB6 THR I 28 TYR I 32 5 5 HELIX 16 AB7 ASP I 62 LYS I 65 5 4 HELIX 17 AB8 ASP I 103 GLY I 107 5 5 HELIX 18 AB9 GLU J 84 VAL J 88 5 5 HELIX 19 AC1 ASN K 28 ALA K 34 1 7 HELIX 20 AC2 ASN K 66 ASN K 70 5 5 HELIX 21 AC3 ASP K 387 MET K 391 5 5 HELIX 22 AC4 THR L 28 TYR L 32 5 5 HELIX 23 AC5 ASP L 62 LYS L 65 5 4 HELIX 24 AC6 ASP L 103 GLY L 107 5 5 HELIX 25 AC7 GLU M 84 VAL M 88 5 5 HELIX 26 AC8 ASN N 28 ALA N 34 1 7 HELIX 27 AC9 ASN N 66 ASN N 70 5 5 HELIX 28 AD1 ASP N 387 MET N 391 5 5 SHEET 1 AA1 4 ARG A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 25 N ARG A 3 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O LEU A 79 N CYS A 22 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82 SHEET 1 AA2 5 VAL A 58 TYR A 60 0 SHEET 2 AA2 5 GLU A 46 SER A 51 -1 N VAL A 50 O TYR A 59 SHEET 3 AA2 5 MET A 34 GLN A 39 -1 N MET A 34 O SER A 51 SHEET 4 AA2 5 ALA A 92 ARG A 98 -1 O TYR A 95 N VAL A 37 SHEET 5 AA2 5 VAL A 124 TRP A 125 -1 O VAL A 124 N ARG A 98 SHEET 1 AA3 5 VAL A 58 TYR A 60 0 SHEET 2 AA3 5 GLU A 46 SER A 51 -1 N VAL A 50 O TYR A 59 SHEET 3 AA3 5 MET A 34 GLN A 39 -1 N MET A 34 O SER A 51 SHEET 4 AA3 5 ALA A 92 ARG A 98 -1 O TYR A 95 N VAL A 37 SHEET 5 AA3 5 THR A 129 VAL A 131 -1 O THR A 129 N TYR A 94 SHEET 1 AA4 4 MET B 4 SER B 7 0 SHEET 2 AA4 4 ALA B 19 SER B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AA4 4 ASP B 75 ILE B 80 -1 O ILE B 80 N ALA B 19 SHEET 4 AA4 4 PHE B 67 SER B 72 -1 N SER B 68 O THR B 79 SHEET 1 AA5 6 PHE B 10 SER B 12 0 SHEET 2 AA5 6 THR B 108 ASP B 111 1 O LYS B 109 N LEU B 11 SHEET 3 AA5 6 GLY B 89 GLN B 95 -1 N GLY B 89 O VAL B 110 SHEET 4 AA5 6 LEU B 38 GLN B 43 -1 N ASP B 39 O MET B 94 SHEET 5 AA5 6 GLN B 50 TYR B 54 -1 O LEU B 52 N TRP B 40 SHEET 6 AA5 6 ASN B 58 ARG B 59 -1 O ASN B 58 N TYR B 54 SHEET 1 AA6 4 PHE B 10 SER B 12 0 SHEET 2 AA6 4 THR B 108 ASP B 111 1 O LYS B 109 N LEU B 11 SHEET 3 AA6 4 GLY B 89 GLN B 95 -1 N GLY B 89 O VAL B 110 SHEET 4 AA6 4 THR B 103 PHE B 104 -1 O THR B 103 N GLN B 95 SHEET 1 AA7 4 GLY D 20 LYS D 26 0 SHEET 2 AA7 4 THR D 363 THR D 373 -1 O VAL D 369 N SER D 25 SHEET 3 AA7 4 ILE D 342 GLY D 353 -1 N LEU D 350 O SER D 366 SHEET 4 AA7 4 SER D 331 GLU D 337 -1 N VAL D 336 O ASN D 343 SHEET 1 AA8 4 TRP D 39 CYS D 48 0 SHEET 2 AA8 4 CYS D 53 THR D 63 -1 O PHE D 56 N TYR D 45 SHEET 3 AA8 4 THR D 81 GLU D 86 -1 O LEU D 83 N ALA D 57 SHEET 4 AA8 4 LYS D 96 ILE D 100 -1 O VAL D 98 N LEU D 82 SHEET 1 AA9 4 SER D 103 HIS D 108 0 SHEET 2 AA9 4 TRP D 113 ASP D 121 -1 O LEU D 114 N CYS D 107 SHEET 3 AA9 4 ASN D 124 TYR D 131 -1 O SER D 128 N CYS D 117 SHEET 4 AA9 4 ARG D 134 VAL D 140 -1 O ASP D 137 N PHE D 129 SHEET 1 AB1 3 ARG D 148 THR D 149 0 SHEET 2 AB1 3 THR D 160 GLY D 168 -1 O THR D 166 N ARG D 148 SHEET 3 AB1 3 VAL D 155 ILE D 157 -1 N ILE D 157 O THR D 160 SHEET 1 AB2 4 ARG D 148 THR D 149 0 SHEET 2 AB2 4 THR D 160 GLY D 168 -1 O THR D 166 N ARG D 148 SHEET 3 AB2 4 ALA D 174 GLU D 182 -1 O ILE D 181 N CYS D 161 SHEET 4 AB2 4 LYS D 185 LYS D 191 -1 O SER D 190 N ILE D 178 SHEET 1 AB3 4 GLU D 200 ARG D 207 0 SHEET 2 AB3 4 GLY D 210 ARG D 216 -1 O VAL D 214 N SER D 203 SHEET 3 AB3 4 PRO D 225 ILE D 229 -1 O ILE D 229 N VAL D 211 SHEET 4 AB3 4 ILE D 236 TYR D 240 -1 O SER D 239 N ILE D 226 SHEET 1 AB4 4 ALA D 277 ASP D 280 0 SHEET 2 AB4 4 ASP D 283 ARG D 288 -1 O TRP D 285 N PHE D 278 SHEET 3 AB4 4 LEU D 296 VAL D 303 -1 O GLU D 299 N ARG D 288 SHEET 4 AB4 4 GLN D 315 ARG D 327 -1 O ASP D 326 N GLY D 297 SHEET 1 AB5 4 ARG F 3 SER F 7 0 SHEET 2 AB5 4 LEU F 18 SER F 25 -1 O SER F 21 N SER F 7 SHEET 3 AB5 4 THR F 78 MET F 83 -1 O LEU F 79 N CYS F 22 SHEET 4 AB5 4 PHE F 68 ASP F 73 -1 N THR F 69 O GLN F 82 SHEET 1 AB6 5 VAL F 58 TYR F 60 0 SHEET 2 AB6 5 GLU F 46 SER F 51 -1 N VAL F 50 O TYR F 59 SHEET 3 AB6 5 MET F 34 GLN F 39 -1 N MET F 34 O SER F 51 SHEET 4 AB6 5 ALA F 92 ARG F 98 -1 O TYR F 95 N VAL F 37 SHEET 5 AB6 5 VAL F 124 TRP F 125 -1 O VAL F 124 N ARG F 98 SHEET 1 AB7 5 VAL F 58 TYR F 60 0 SHEET 2 AB7 5 GLU F 46 SER F 51 -1 N VAL F 50 O TYR F 59 SHEET 3 AB7 5 MET F 34 GLN F 39 -1 N MET F 34 O SER F 51 SHEET 4 AB7 5 ALA F 92 ARG F 98 -1 O TYR F 95 N VAL F 37 SHEET 5 AB7 5 THR F 129 VAL F 131 -1 O THR F 129 N TYR F 94 SHEET 1 AB8 4 MET G 4 SER G 7 0 SHEET 2 AB8 4 ALA G 19 SER G 25 -1 O ARG G 24 N THR G 5 SHEET 3 AB8 4 ASP G 75 ILE G 80 -1 O ILE G 80 N ALA G 19 SHEET 4 AB8 4 PHE G 67 SER G 72 -1 N SER G 68 O THR G 79 SHEET 1 AB9 6 PHE G 10 SER G 12 0 SHEET 2 AB9 6 THR G 108 ASP G 111 1 O LYS G 109 N LEU G 11 SHEET 3 AB9 6 GLY G 89 GLN G 95 -1 N GLY G 89 O VAL G 110 SHEET 4 AB9 6 LEU G 38 GLN G 43 -1 N ASP G 39 O MET G 94 SHEET 5 AB9 6 GLN G 50 TYR G 54 -1 O LEU G 52 N TRP G 40 SHEET 6 AB9 6 ASN G 58 ARG G 59 -1 O ASN G 58 N TYR G 54 SHEET 1 AC1 4 PHE G 10 SER G 12 0 SHEET 2 AC1 4 THR G 108 ASP G 111 1 O LYS G 109 N LEU G 11 SHEET 3 AC1 4 GLY G 89 GLN G 95 -1 N GLY G 89 O VAL G 110 SHEET 4 AC1 4 THR G 103 PHE G 104 -1 O THR G 103 N GLN G 95 SHEET 1 AC2 4 GLY H 20 LYS H 26 0 SHEET 2 AC2 4 THR H 363 THR H 373 -1 O VAL H 369 N SER H 25 SHEET 3 AC2 4 ILE H 342 GLY H 353 -1 N LEU H 350 O SER H 366 SHEET 4 AC2 4 SER H 331 GLU H 337 -1 N VAL H 336 O ASN H 343 SHEET 1 AC3 4 TRP H 39 CYS H 48 0 SHEET 2 AC3 4 CYS H 53 THR H 63 -1 O PHE H 56 N TYR H 45 SHEET 3 AC3 4 THR H 81 GLU H 86 -1 O LEU H 83 N ALA H 57 SHEET 4 AC3 4 LYS H 96 ILE H 100 -1 O VAL H 98 N LEU H 82 SHEET 1 AC4 4 SER H 103 HIS H 108 0 SHEET 2 AC4 4 TRP H 113 ASP H 121 -1 O LEU H 114 N CYS H 107 SHEET 3 AC4 4 ASN H 124 TYR H 131 -1 O SER H 128 N CYS H 117 SHEET 4 AC4 4 ARG H 134 VAL H 140 -1 O ASP H 137 N PHE H 129 SHEET 1 AC5 3 ARG H 148 THR H 149 0 SHEET 2 AC5 3 THR H 160 GLY H 168 -1 O THR H 166 N ARG H 148 SHEET 3 AC5 3 VAL H 155 ILE H 157 -1 N ILE H 157 O THR H 160 SHEET 1 AC6 4 ARG H 148 THR H 149 0 SHEET 2 AC6 4 THR H 160 GLY H 168 -1 O THR H 166 N ARG H 148 SHEET 3 AC6 4 ALA H 174 GLU H 182 -1 O ILE H 181 N CYS H 161 SHEET 4 AC6 4 LYS H 185 LYS H 191 -1 O SER H 190 N ILE H 178 SHEET 1 AC7 4 GLU H 200 ARG H 207 0 SHEET 2 AC7 4 GLY H 210 ARG H 216 -1 O VAL H 214 N SER H 203 SHEET 3 AC7 4 PRO H 225 ILE H 229 -1 O ILE H 229 N VAL H 211 SHEET 4 AC7 4 ILE H 236 TYR H 240 -1 O SER H 239 N ILE H 226 SHEET 1 AC8 4 ALA H 277 ASP H 280 0 SHEET 2 AC8 4 ASP H 283 ARG H 288 -1 O TRP H 285 N PHE H 278 SHEET 3 AC8 4 LEU H 296 VAL H 303 -1 O GLU H 299 N ARG H 288 SHEET 4 AC8 4 GLN H 315 ARG H 327 -1 O ASP H 326 N GLY H 297 SHEET 1 AC9 4 ARG I 3 SER I 7 0 SHEET 2 AC9 4 LEU I 18 SER I 25 -1 O SER I 25 N ARG I 3 SHEET 3 AC9 4 THR I 78 MET I 83 -1 O LEU I 79 N CYS I 22 SHEET 4 AC9 4 PHE I 68 ASP I 73 -1 N THR I 69 O GLN I 82 SHEET 1 AD1 5 VAL I 58 TYR I 60 0 SHEET 2 AD1 5 GLU I 46 SER I 51 -1 N VAL I 50 O TYR I 59 SHEET 3 AD1 5 MET I 34 GLN I 39 -1 N MET I 34 O SER I 51 SHEET 4 AD1 5 ALA I 92 ARG I 98 -1 O TYR I 95 N VAL I 37 SHEET 5 AD1 5 VAL I 124 TRP I 125 -1 O VAL I 124 N ARG I 98 SHEET 1 AD2 5 VAL I 58 TYR I 60 0 SHEET 2 AD2 5 GLU I 46 SER I 51 -1 N VAL I 50 O TYR I 59 SHEET 3 AD2 5 MET I 34 GLN I 39 -1 N MET I 34 O SER I 51 SHEET 4 AD2 5 ALA I 92 ARG I 98 -1 O TYR I 95 N VAL I 37 SHEET 5 AD2 5 THR I 129 VAL I 131 -1 O THR I 129 N TYR I 94 SHEET 1 AD3 4 MET J 4 SER J 7 0 SHEET 2 AD3 4 ALA J 19 SER J 25 -1 O ARG J 24 N THR J 5 SHEET 3 AD3 4 ASP J 75 ILE J 80 -1 O ILE J 80 N ALA J 19 SHEET 4 AD3 4 PHE J 67 SER J 72 -1 N SER J 68 O THR J 79 SHEET 1 AD4 6 PHE J 10 SER J 12 0 SHEET 2 AD4 6 THR J 108 ASP J 111 1 O LYS J 109 N LEU J 11 SHEET 3 AD4 6 GLY J 89 GLN J 95 -1 N GLY J 89 O VAL J 110 SHEET 4 AD4 6 LEU J 38 GLN J 43 -1 N ASP J 39 O MET J 94 SHEET 5 AD4 6 GLN J 50 TYR J 54 -1 O LEU J 52 N TRP J 40 SHEET 6 AD4 6 ASN J 58 ARG J 59 -1 O ASN J 58 N TYR J 54 SHEET 1 AD5 4 PHE J 10 SER J 12 0 SHEET 2 AD5 4 THR J 108 ASP J 111 1 O LYS J 109 N LEU J 11 SHEET 3 AD5 4 GLY J 89 GLN J 95 -1 N GLY J 89 O VAL J 110 SHEET 4 AD5 4 THR J 103 PHE J 104 -1 O THR J 103 N GLN J 95 SHEET 1 AD6 4 GLY K 20 LYS K 26 0 SHEET 2 AD6 4 THR K 363 THR K 373 -1 O VAL K 369 N SER K 25 SHEET 3 AD6 4 ILE K 342 GLY K 353 -1 N LEU K 350 O SER K 366 SHEET 4 AD6 4 SER K 331 GLU K 337 -1 N VAL K 336 O ASN K 343 SHEET 1 AD7 4 TRP K 39 CYS K 48 0 SHEET 2 AD7 4 CYS K 53 THR K 63 -1 O PHE K 56 N TYR K 45 SHEET 3 AD7 4 THR K 81 GLU K 86 -1 O LEU K 83 N ALA K 57 SHEET 4 AD7 4 LYS K 96 ILE K 100 -1 O VAL K 98 N LEU K 82 SHEET 1 AD8 4 SER K 103 HIS K 108 0 SHEET 2 AD8 4 TRP K 113 ASP K 121 -1 O LEU K 114 N CYS K 107 SHEET 3 AD8 4 ASN K 124 TYR K 131 -1 O SER K 128 N CYS K 117 SHEET 4 AD8 4 ARG K 134 VAL K 140 -1 O ASP K 137 N PHE K 129 SHEET 1 AD9 3 ARG K 148 THR K 149 0 SHEET 2 AD9 3 THR K 160 GLY K 168 -1 O THR K 166 N ARG K 148 SHEET 3 AD9 3 VAL K 155 ILE K 157 -1 N ILE K 157 O THR K 160 SHEET 1 AE1 4 ARG K 148 THR K 149 0 SHEET 2 AE1 4 THR K 160 GLY K 168 -1 O THR K 166 N ARG K 148 SHEET 3 AE1 4 ALA K 174 GLU K 182 -1 O ILE K 181 N CYS K 161 SHEET 4 AE1 4 LYS K 185 LYS K 191 -1 O SER K 190 N ILE K 178 SHEET 1 AE2 4 GLU K 200 ARG K 207 0 SHEET 2 AE2 4 GLY K 210 ARG K 216 -1 O VAL K 214 N SER K 203 SHEET 3 AE2 4 PRO K 225 ILE K 229 -1 O ILE K 229 N VAL K 211 SHEET 4 AE2 4 ILE K 236 TYR K 240 -1 O SER K 239 N ILE K 226 SHEET 1 AE3 4 ALA K 277 ASP K 280 0 SHEET 2 AE3 4 ASP K 283 ARG K 288 -1 O TRP K 285 N PHE K 278 SHEET 3 AE3 4 LEU K 296 VAL K 303 -1 O GLU K 299 N ARG K 288 SHEET 4 AE3 4 GLN K 315 ARG K 327 -1 O ASP K 326 N GLY K 297 SHEET 1 AE4 4 ARG L 3 SER L 7 0 SHEET 2 AE4 4 LEU L 18 SER L 25 -1 O SER L 25 N ARG L 3 SHEET 3 AE4 4 THR L 78 MET L 83 -1 O LEU L 79 N CYS L 22 SHEET 4 AE4 4 PHE L 68 ASP L 73 -1 N THR L 69 O GLN L 82 SHEET 1 AE5 5 VAL L 58 TYR L 60 0 SHEET 2 AE5 5 GLU L 46 SER L 51 -1 N VAL L 50 O TYR L 59 SHEET 3 AE5 5 MET L 34 GLN L 39 -1 N MET L 34 O SER L 51 SHEET 4 AE5 5 ALA L 92 ARG L 98 -1 O TYR L 95 N VAL L 37 SHEET 5 AE5 5 VAL L 124 TRP L 125 -1 O VAL L 124 N ARG L 98 SHEET 1 AE6 5 VAL L 58 TYR L 60 0 SHEET 2 AE6 5 GLU L 46 SER L 51 -1 N VAL L 50 O TYR L 59 SHEET 3 AE6 5 MET L 34 GLN L 39 -1 N MET L 34 O SER L 51 SHEET 4 AE6 5 ALA L 92 ARG L 98 -1 O TYR L 95 N VAL L 37 SHEET 5 AE6 5 THR L 129 VAL L 131 -1 O THR L 129 N TYR L 94 SHEET 1 AE7 4 MET M 4 SER M 7 0 SHEET 2 AE7 4 ALA M 19 SER M 25 -1 O ARG M 24 N THR M 5 SHEET 3 AE7 4 ASP M 75 ILE M 80 -1 O ILE M 80 N ALA M 19 SHEET 4 AE7 4 PHE M 67 SER M 72 -1 N SER M 68 O THR M 79 SHEET 1 AE8 6 PHE M 10 SER M 12 0 SHEET 2 AE8 6 THR M 108 ASP M 111 1 O LYS M 109 N LEU M 11 SHEET 3 AE8 6 GLY M 89 GLN M 95 -1 N GLY M 89 O VAL M 110 SHEET 4 AE8 6 LEU M 38 GLN M 43 -1 N ASP M 39 O MET M 94 SHEET 5 AE8 6 GLN M 50 TYR M 54 -1 O LEU M 52 N TRP M 40 SHEET 6 AE8 6 ASN M 58 ARG M 59 -1 O ASN M 58 N TYR M 54 SHEET 1 AE9 4 PHE M 10 SER M 12 0 SHEET 2 AE9 4 THR M 108 ASP M 111 1 O LYS M 109 N LEU M 11 SHEET 3 AE9 4 GLY M 89 GLN M 95 -1 N GLY M 89 O VAL M 110 SHEET 4 AE9 4 THR M 103 PHE M 104 -1 O THR M 103 N GLN M 95 SHEET 1 AF1 4 GLY N 20 LYS N 26 0 SHEET 2 AF1 4 THR N 363 THR N 373 -1 O VAL N 369 N SER N 25 SHEET 3 AF1 4 ILE N 342 GLY N 353 -1 N LEU N 350 O SER N 366 SHEET 4 AF1 4 SER N 331 GLU N 337 -1 N VAL N 336 O ASN N 343 SHEET 1 AF2 4 TRP N 39 CYS N 48 0 SHEET 2 AF2 4 CYS N 53 THR N 63 -1 O PHE N 56 N TYR N 45 SHEET 3 AF2 4 THR N 81 GLU N 86 -1 O LEU N 83 N ALA N 57 SHEET 4 AF2 4 LYS N 96 ILE N 100 -1 O VAL N 98 N LEU N 82 SHEET 1 AF3 4 SER N 103 HIS N 108 0 SHEET 2 AF3 4 TRP N 113 ASP N 121 -1 O LEU N 114 N CYS N 107 SHEET 3 AF3 4 ASN N 124 TYR N 131 -1 O SER N 128 N CYS N 117 SHEET 4 AF3 4 ARG N 134 VAL N 140 -1 O ASP N 137 N PHE N 129 SHEET 1 AF4 3 ARG N 148 THR N 149 0 SHEET 2 AF4 3 THR N 160 GLY N 168 -1 O THR N 166 N ARG N 148 SHEET 3 AF4 3 VAL N 155 ILE N 157 -1 N ILE N 157 O THR N 160 SHEET 1 AF5 4 ARG N 148 THR N 149 0 SHEET 2 AF5 4 THR N 160 GLY N 168 -1 O THR N 166 N ARG N 148 SHEET 3 AF5 4 ALA N 174 GLU N 182 -1 O ILE N 181 N CYS N 161 SHEET 4 AF5 4 LYS N 185 LYS N 191 -1 O SER N 190 N ILE N 178 SHEET 1 AF6 4 GLU N 200 ARG N 207 0 SHEET 2 AF6 4 GLY N 210 ARG N 216 -1 O VAL N 214 N SER N 203 SHEET 3 AF6 4 PRO N 225 ILE N 229 -1 O ILE N 229 N VAL N 211 SHEET 4 AF6 4 ILE N 236 TYR N 240 -1 O SER N 239 N ILE N 226 SHEET 1 AF7 4 ALA N 277 ASP N 280 0 SHEET 2 AF7 4 ASP N 283 ARG N 288 -1 O TRP N 285 N PHE N 278 SHEET 3 AF7 4 LEU N 296 VAL N 303 -1 O GLU N 299 N ARG N 288 SHEET 4 AF7 4 GLN N 315 ARG N 327 -1 O ASP N 326 N GLY N 297 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS B 23 CYS B 93 1555 1555 2.04 SSBOND 3 CYS D 16 CYS D 341 1555 1555 2.03 SSBOND 4 CYS D 48 CYS D 53 1555 1555 2.03 SSBOND 5 CYS D 99 CYS D 117 1555 1555 2.03 SSBOND 6 CYS D 107 CYS D 154 1555 1555 2.04 SSBOND 7 CYS D 107 CYS D 156 1555 1555 2.07 SSBOND 8 CYS D 156 CYS D 161 1555 1555 2.03 SSBOND 9 CYS D 202 CYS D 215 1555 1555 2.03 SSBOND 10 CYS D 204 CYS D 213 1555 1555 2.03 SSBOND 11 CYS D 242 CYS D 261 1555 1555 2.04 SSBOND 12 CYS D 345 CYS D 371 1555 1555 2.03 SSBOND 13 CYS F 22 CYS F 96 1555 1555 2.03 SSBOND 14 CYS G 23 CYS G 93 1555 1555 2.03 SSBOND 15 CYS H 16 CYS H 341 1555 1555 2.03 SSBOND 16 CYS H 48 CYS H 53 1555 1555 2.03 SSBOND 17 CYS H 99 CYS H 117 1555 1555 2.03 SSBOND 18 CYS H 107 CYS H 154 1555 1555 2.04 SSBOND 19 CYS H 107 CYS H 156 1555 1555 2.07 SSBOND 20 CYS H 156 CYS H 161 1555 1555 2.03 SSBOND 21 CYS H 202 CYS H 215 1555 1555 2.03 SSBOND 22 CYS H 204 CYS H 213 1555 1555 2.03 SSBOND 23 CYS H 242 CYS H 261 1555 1555 2.04 SSBOND 24 CYS H 345 CYS H 371 1555 1555 2.03 SSBOND 25 CYS I 22 CYS I 96 1555 1555 2.03 SSBOND 26 CYS J 23 CYS J 93 1555 1555 2.03 SSBOND 27 CYS K 16 CYS K 341 1555 1555 2.03 SSBOND 28 CYS K 48 CYS K 53 1555 1555 2.04 SSBOND 29 CYS K 99 CYS K 117 1555 1555 2.03 SSBOND 30 CYS K 107 CYS K 154 1555 1555 2.04 SSBOND 31 CYS K 107 CYS K 156 1555 1555 2.07 SSBOND 32 CYS K 156 CYS K 161 1555 1555 2.03 SSBOND 33 CYS K 202 CYS K 215 1555 1555 2.03 SSBOND 34 CYS K 204 CYS K 213 1555 1555 2.03 SSBOND 35 CYS K 242 CYS K 261 1555 1555 2.04 SSBOND 36 CYS K 345 CYS K 371 1555 1555 2.03 SSBOND 37 CYS L 22 CYS L 96 1555 1555 2.03 SSBOND 38 CYS M 23 CYS M 93 1555 1555 2.03 SSBOND 39 CYS N 16 CYS N 341 1555 1555 2.03 SSBOND 40 CYS N 48 CYS N 53 1555 1555 2.03 SSBOND 41 CYS N 99 CYS N 117 1555 1555 2.03 SSBOND 42 CYS N 107 CYS N 154 1555 1555 2.04 SSBOND 43 CYS N 107 CYS N 156 1555 1555 2.07 SSBOND 44 CYS N 156 CYS N 161 1555 1555 2.03 SSBOND 45 CYS N 202 CYS N 215 1555 1555 2.03 SSBOND 46 CYS N 204 CYS N 213 1555 1555 2.03 SSBOND 47 CYS N 242 CYS N 261 1555 1555 2.04 SSBOND 48 CYS N 345 CYS N 371 1555 1555 2.03 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.43 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O3 BMA O 3 C1 MAN O 4 1555 1555 1.44 LINK O6 BMA O 3 C1 MAN O 5 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.43 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44 LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.44 LINK O6 BMA P 3 C1 MAN P 5 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.42 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.44 LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.44 LINK O6 BMA Q 3 C1 MAN Q 5 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.42 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.44 LINK O3 BMA R 3 C1 MAN R 4 1555 1555 1.44 LINK O6 BMA R 3 C1 MAN R 5 1555 1555 1.44 LINK O ASP D 217 CA CA D 403 1555 1555 2.26 LINK O GLY D 221 CA CA D 403 1555 1555 2.43 LINK OD2 ASP D 248 CA CA D 403 1555 1555 2.20 LINK O GLY D 269 CA CA D 403 1555 1555 2.59 LINK O HIS D 271 CA CA D 403 1555 1555 2.52 LINK CA CA D 403 O HOH D 511 1555 1555 2.62 LINK O ASP H 217 CA CA H 403 1555 1555 2.25 LINK O GLY H 221 CA CA H 403 1555 1555 2.44 LINK OD2 ASP H 248 CA CA H 403 1555 1555 2.23 LINK O GLY H 269 CA CA H 403 1555 1555 2.58 LINK O HIS H 271 CA CA H 403 1555 1555 2.52 LINK CA CA H 403 O HOH H 508 1555 1555 2.61 LINK O ASP K 217 CA CA K 403 1555 1555 2.25 LINK O GLY K 221 CA CA K 403 1555 1555 2.44 LINK OD2 ASP K 248 CA CA K 403 1555 1555 2.23 LINK O GLY K 269 CA CA K 403 1555 1555 2.59 LINK O HIS K 271 CA CA K 403 1555 1555 2.52 LINK CA CA K 403 O HOH K 510 1555 1555 2.61 LINK O ASP N 217 CA CA N 403 1555 1555 2.26 LINK O GLY N 221 CA CA N 403 1555 1555 2.44 LINK OD2 ASP N 248 CA CA N 403 1555 1555 2.23 LINK O GLY N 269 CA CA N 403 1555 1555 2.59 LINK O HIS N 271 CA CA N 403 1555 1555 2.52 LINK CA CA N 403 O HOH N 511 1555 1555 2.61 CISPEP 1 SER B 7 PRO B 8 0 -3.11 CISPEP 2 THR B 99 PRO B 100 0 -2.38 CISPEP 3 PRO B 100 PRO B 101 0 -4.94 CISPEP 4 TYR D 208 PRO D 209 0 9.64 CISPEP 5 THR D 249 PRO D 250 0 7.60 CISPEP 6 ARG D 354 LYS D 355 0 1.85 CISPEP 7 SER G 7 PRO G 8 0 -3.02 CISPEP 8 THR G 99 PRO G 100 0 -2.42 CISPEP 9 PRO G 100 PRO G 101 0 -4.97 CISPEP 10 TYR H 208 PRO H 209 0 9.18 CISPEP 11 THR H 249 PRO H 250 0 7.60 CISPEP 12 ARG H 354 LYS H 355 0 1.81 CISPEP 13 SER J 7 PRO J 8 0 -3.10 CISPEP 14 THR J 99 PRO J 100 0 -2.47 CISPEP 15 PRO J 100 PRO J 101 0 -5.02 CISPEP 16 TYR K 208 PRO K 209 0 9.26 CISPEP 17 THR K 249 PRO K 250 0 7.45 CISPEP 18 ARG K 354 LYS K 355 0 1.70 CISPEP 19 SER M 7 PRO M 8 0 -3.16 CISPEP 20 THR M 99 PRO M 100 0 -2.46 CISPEP 21 PRO M 100 PRO M 101 0 -4.94 CISPEP 22 TYR N 208 PRO N 209 0 9.10 CISPEP 23 THR N 249 PRO N 250 0 7.56 CISPEP 24 ARG N 354 LYS N 355 0 1.87 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