HEADER VIRAL PROTEIN/IMMUNE SYSTEM 28-MAR-24 8YVK TITLE NEURAMINIDASE OF A/RED KNOT/DELAWARE BAY/310/2016 H10N4 IN COMPLEX TITLE 2 WITH CAV-F6 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAMINIDASE; COMPND 3 CHAIN: A, B, C, D; COMPND 4 EC: 3.2.1.18; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CAV-F6 HEAVY CHAIN; COMPND 8 CHAIN: E, G, I, K; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: CAV-F6 KAPPA CHAIN; COMPND 12 CHAIN: F, H, J, L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/RED KNOT/DELAWARE SOURCE 3 BAY/310/2016(H10N4)); SOURCE 4 ORGANISM_COMMON: A/RED KNOT/DELAWARE BAY/310/2016(H10N4); SOURCE 5 ORGANISM_TAXID: 1985803; SOURCE 6 GENE: NA; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS INFLUENZA VIRUS, NEURAMINIDASE, ANTIBODY, VIRAL PROTEIN/IMMUNE KEYWDS 2 SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR X.WANG,J.GE,X.LI REVDAT 1 02-JUL-25 8YVK 0 JRNL AUTH X.WANG,J.GE,X.LI JRNL TITL NEURAMINIDASE OF A/RED KNOT/DELAWARE BAY/310/2016 H10N4 IN JRNL TITL 2 COMPLEX WITH CAV-F6 FAB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.09 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : 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) : 3.090 REMARK 3 NUMBER OF PARTICLES : 17312 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8YVK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 02-APR-24. REMARK 100 THE DEPOSITION ID IS D_1300046014. 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 : NEURAMINIDASE OF A/RED REMARK 245 KNOT/DELAWARE BAY/310/2016 REMARK 245 H10N4 IN COMPLEX WITH CAV-F6 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 : 7.20 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1300.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 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) : 200 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, G, H, I, J, REMARK 350 AND CHAINS: K, L 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 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 OG1 THR B 214 OG SER C 451 2.14 REMARK 500 OG1 THR C 214 OG SER D 451 2.16 REMARK 500 OG SER A 451 OG1 THR D 214 2.17 REMARK 500 OG1 THR A 214 OG SER B 451 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS A 183 CA - CB - SG ANGL. DEV. = 8.5 DEGREES REMARK 500 CYS B 183 CA - CB - SG ANGL. DEV. = 8.6 DEGREES REMARK 500 CYS C 183 CA - CB - SG ANGL. DEV. = 8.6 DEGREES REMARK 500 CYS D 183 CA - CB - SG ANGL. DEV. = 8.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 124 -169.62 -125.85 REMARK 500 GLU A 235 -4.51 73.17 REMARK 500 ARG A 296 27.21 -160.15 REMARK 500 ASN A 339 -64.39 -90.30 REMARK 500 TYR A 345 169.94 88.47 REMARK 500 ARG A 369 76.29 -100.55 REMARK 500 SER A 388 -163.98 -129.57 REMARK 500 ASN A 389 13.39 -143.10 REMARK 500 SER A 401 -167.75 -127.12 REMARK 500 ASN A 450 59.65 -97.74 REMARK 500 SER A 451 -168.03 -160.27 REMARK 500 SER B 85 -165.45 -72.44 REMARK 500 ASP B 89 152.70 89.23 REMARK 500 SER B 124 -169.65 -125.89 REMARK 500 GLU B 235 -4.49 73.10 REMARK 500 ARG B 296 22.71 -146.02 REMARK 500 ASN B 339 -63.39 -90.28 REMARK 500 TYR B 345 174.47 84.93 REMARK 500 ARG B 369 76.32 -100.53 REMARK 500 SER B 401 -167.73 -127.09 REMARK 500 ASN B 450 59.68 -97.76 REMARK 500 SER B 451 -168.10 -160.30 REMARK 500 SER C 85 -168.13 -72.56 REMARK 500 SER C 124 -169.61 -125.90 REMARK 500 GLU C 235 -4.60 73.17 REMARK 500 ARG C 296 22.65 -145.91 REMARK 500 ASN C 339 -62.70 -90.31 REMARK 500 TYR C 345 174.61 84.15 REMARK 500 ARG C 369 76.31 -100.48 REMARK 500 SER C 401 -167.77 -127.07 REMARK 500 ASN C 450 59.66 -97.65 REMARK 500 SER C 451 -168.05 -160.32 REMARK 500 SER D 85 -168.30 -72.56 REMARK 500 SER D 124 -169.61 -125.90 REMARK 500 GLU D 235 -4.57 73.26 REMARK 500 CYS D 291 -168.68 -118.56 REMARK 500 ARG D 296 26.11 -163.87 REMARK 500 ASN D 339 -62.73 -90.38 REMARK 500 TYR D 345 176.34 83.08 REMARK 500 ARG D 369 76.30 -100.49 REMARK 500 SER D 401 -167.78 -127.10 REMARK 500 ASN D 450 59.58 -97.64 REMARK 500 SER D 451 -168.00 -160.29 REMARK 500 TYR E 107 70.23 58.83 REMARK 500 ALA F 52 -20.92 79.59 REMARK 500 PRO F 60 171.01 -59.89 REMARK 500 SER F 66 -169.42 -161.84 REMARK 500 PRO F 81 -5.70 -57.37 REMARK 500 TYR G 107 70.23 58.88 REMARK 500 ALA H 52 -1.99 71.02 REMARK 500 REMARK 500 THIS ENTRY HAS 65 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL 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 502 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 293 O REMARK 620 2 GLY A 297 O 91.5 REMARK 620 3 ASP A 323 OD2 83.9 101.7 REMARK 620 4 GLY A 343 O 103.2 82.7 171.7 REMARK 620 5 TYR A 345 O 87.3 158.5 99.5 76.7 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 502 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 293 O REMARK 620 2 GLY B 297 O 87.5 REMARK 620 3 ASP B 323 OD2 81.3 87.8 REMARK 620 4 GLY B 343 O 111.8 81.7 162.6 REMARK 620 5 TYR B 345 O 94.3 163.4 108.9 82.3 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 502 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 293 O REMARK 620 2 GLY C 297 O 88.1 REMARK 620 3 ASP C 323 OD2 76.1 93.0 REMARK 620 4 GLY C 343 O 109.8 91.7 172.6 REMARK 620 5 TYR C 345 O 83.4 164.4 97.5 79.1 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 502 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 293 O REMARK 620 2 GLY D 297 O 92.7 REMARK 620 3 ASP D 323 OD2 87.0 89.9 REMARK 620 4 GLY D 343 O 107.4 86.8 165.3 REMARK 620 5 TYR D 345 O 85.7 167.6 102.3 81.9 REMARK 620 N 1 2 3 4 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-39605 RELATED DB: EMDB REMARK 900 NEURAMINIDASE OF A/RED KNOT/DELAWARE BAY/310/2016 H10N4 IN COMPLEX REMARK 900 WITH F6 FAB DBREF1 8YVK A 82 470 UNP A0A248T7C3_9INFA DBREF2 8YVK A A0A248T7C3 82 470 DBREF1 8YVK B 82 470 UNP A0A248T7C3_9INFA DBREF2 8YVK B A0A248T7C3 82 470 DBREF1 8YVK C 82 470 UNP A0A248T7C3_9INFA DBREF2 8YVK C A0A248T7C3 82 470 DBREF1 8YVK D 82 470 UNP A0A248T7C3_9INFA DBREF2 8YVK D A0A248T7C3 82 470 DBREF 8YVK E 1 123 PDB 8YVK 8YVK 1 123 DBREF 8YVK F 1 107 PDB 8YVK 8YVK 1 107 DBREF 8YVK G 1 123 PDB 8YVK 8YVK 1 123 DBREF 8YVK H 1 107 PDB 8YVK 8YVK 1 107 DBREF 8YVK I 1 123 PDB 8YVK 8YVK 1 123 DBREF 8YVK J 1 107 PDB 8YVK 8YVK 1 107 DBREF 8YVK K 1 123 PDB 8YVK 8YVK 1 123 DBREF 8YVK L 1 107 PDB 8YVK 8YVK 1 107 SEQRES 1 A 389 VAL HIS TYR SER SER GLY ARG ASP LEU CYS PRO ILE ARG SEQRES 2 A 389 GLY TRP ALA PRO LEU SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 A 389 GLY SER ARG GLY GLU VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 A 389 ILE SER CYS SER ILE SER GLU CYS ARG THR PHE PHE LEU SEQRES 5 A 389 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN GLY SEQRES 6 A 389 THR VAL LYS ASP ARG SER PRO PHE ARG THR LEU MET SER SEQRES 7 A 389 CYS PRO ILE GLY VAL ALA PRO SER PRO SER ASN SER ARG SEQRES 8 A 389 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS SER ASP SEQRES 9 A 389 GLY PRO GLY TRP LEU THR LEU GLY ILE THR GLY PRO ASP SEQRES 10 A 389 SER THR ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE ILE SEQRES 11 A 389 THR ASP THR LEU LYS SER TRP LYS GLY ASN ILE MET ARG SEQRES 12 A 389 THR GLN GLU SER GLU CYS VAL CYS GLN ASP GLU PHE CYS SEQRES 13 A 389 TYR THR LEU VAL THR ASP GLY PRO SER ASP ALA GLN ALA SEQRES 14 A 389 PHE TYR LYS ILE LEU LYS ILE ARG LYS GLY LYS ILE VAL SEQRES 15 A 389 SER MET LYS ASP VAL ASP ALA THR GLY PHE HIS PHE GLU SEQRES 16 A 389 GLU CYS SER CYS TYR PRO SER GLY THR GLU ILE GLU CYS SEQRES 17 A 389 VAL CYS ARG ASP ASN TRP ARG GLY SER ASN ARG PRO TRP SEQRES 18 A 389 ILE ARG PHE ASN SER ASP LEU ASP TYR GLN ILE GLY TYR SEQRES 19 A 389 VAL CYS SER GLY ILE PHE GLY ASP ASN PRO ARG PRO VAL SEQRES 20 A 389 ASP GLY THR GLY SER CYS ASN GLY PRO VAL ASN ASN GLY SEQRES 21 A 389 LYS GLY ARG TYR GLY VAL LYS GLY PHE SER PHE ARG TYR SEQRES 22 A 389 GLY ASP GLY VAL TRP ILE GLY ARG THR LYS SER LEU GLU SEQRES 23 A 389 SER ARG SER GLY PHE GLU MET VAL TRP ASP ALA ASN GLY SEQRES 24 A 389 TRP VAL SER THR ASP LYS ASP SER ASN GLY VAL GLN ASP SEQRES 25 A 389 ILE ILE ASP ASN ASP ASN TRP SER GLY TYR SER GLY SER SEQRES 26 A 389 PHE SER ILE ARG GLY GLU THR THR GLY LYS ASN CYS THR SEQRES 27 A 389 VAL PRO CYS PHE TRP VAL GLU MET ILE ARG GLY GLN PRO SEQRES 28 A 389 LYS GLU LYS THR ILE TRP THR SER GLY SER SER ILE ALA SEQRES 29 A 389 PHE CYS GLY VAL ASN SER ASP THR THR GLY TRP SER TRP SEQRES 30 A 389 PRO ASP GLY ALA LEU LEU PRO PHE ASP ILE ASP LYS SEQRES 1 B 389 VAL HIS TYR SER SER GLY ARG ASP LEU CYS PRO ILE ARG SEQRES 2 B 389 GLY TRP ALA PRO LEU SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 B 389 GLY SER ARG GLY GLU VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 B 389 ILE SER CYS SER ILE SER GLU CYS ARG THR PHE PHE LEU SEQRES 5 B 389 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN GLY SEQRES 6 B 389 THR VAL LYS ASP ARG SER PRO PHE ARG THR LEU MET SER SEQRES 7 B 389 CYS PRO ILE GLY VAL ALA PRO SER PRO SER ASN SER ARG SEQRES 8 B 389 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS SER ASP SEQRES 9 B 389 GLY PRO GLY TRP LEU THR LEU GLY ILE THR GLY PRO ASP SEQRES 10 B 389 SER THR ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE ILE SEQRES 11 B 389 THR ASP THR LEU LYS SER TRP LYS GLY ASN ILE MET ARG SEQRES 12 B 389 THR GLN GLU SER GLU CYS VAL CYS GLN ASP GLU PHE CYS SEQRES 13 B 389 TYR THR LEU VAL THR ASP GLY PRO SER ASP ALA GLN ALA SEQRES 14 B 389 PHE TYR LYS ILE LEU LYS ILE ARG LYS GLY LYS ILE VAL SEQRES 15 B 389 SER MET LYS ASP VAL ASP ALA THR GLY PHE HIS PHE GLU SEQRES 16 B 389 GLU CYS SER CYS TYR PRO SER GLY THR GLU ILE GLU CYS SEQRES 17 B 389 VAL CYS ARG ASP ASN TRP ARG GLY SER ASN ARG PRO TRP SEQRES 18 B 389 ILE ARG PHE ASN SER ASP LEU ASP TYR GLN ILE GLY TYR SEQRES 19 B 389 VAL CYS SER GLY ILE PHE GLY ASP ASN PRO ARG PRO VAL SEQRES 20 B 389 ASP GLY THR GLY SER CYS ASN GLY PRO VAL ASN ASN GLY SEQRES 21 B 389 LYS GLY ARG TYR GLY VAL LYS GLY PHE SER PHE ARG TYR SEQRES 22 B 389 GLY ASP GLY VAL TRP ILE GLY ARG THR LYS SER LEU GLU SEQRES 23 B 389 SER ARG SER GLY PHE GLU MET VAL TRP ASP ALA ASN GLY SEQRES 24 B 389 TRP VAL SER THR ASP LYS ASP SER ASN GLY VAL GLN ASP SEQRES 25 B 389 ILE ILE ASP ASN ASP ASN TRP SER GLY TYR SER GLY SER SEQRES 26 B 389 PHE SER ILE ARG GLY GLU THR THR GLY LYS ASN CYS THR SEQRES 27 B 389 VAL PRO CYS PHE TRP VAL GLU MET ILE ARG GLY GLN PRO SEQRES 28 B 389 LYS GLU LYS THR ILE TRP THR SER GLY SER SER ILE ALA SEQRES 29 B 389 PHE CYS GLY VAL ASN SER ASP THR THR GLY TRP SER TRP SEQRES 30 B 389 PRO ASP GLY ALA LEU LEU PRO PHE ASP ILE ASP LYS SEQRES 1 C 389 VAL HIS TYR SER SER GLY ARG ASP LEU CYS PRO ILE ARG SEQRES 2 C 389 GLY TRP ALA PRO LEU SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 C 389 GLY SER ARG GLY GLU VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 C 389 ILE SER CYS SER ILE SER GLU CYS ARG THR PHE PHE LEU SEQRES 5 C 389 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN GLY SEQRES 6 C 389 THR VAL LYS ASP ARG SER PRO PHE ARG THR LEU MET SER SEQRES 7 C 389 CYS PRO ILE GLY VAL ALA PRO SER PRO SER ASN SER ARG SEQRES 8 C 389 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS SER ASP SEQRES 9 C 389 GLY PRO GLY TRP LEU THR LEU GLY ILE THR GLY PRO ASP SEQRES 10 C 389 SER THR ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE ILE SEQRES 11 C 389 THR ASP THR LEU LYS SER TRP LYS GLY ASN ILE MET ARG SEQRES 12 C 389 THR GLN GLU SER GLU CYS VAL CYS GLN ASP GLU PHE CYS SEQRES 13 C 389 TYR THR LEU VAL THR ASP GLY PRO SER ASP ALA GLN ALA SEQRES 14 C 389 PHE TYR LYS ILE LEU LYS ILE ARG LYS GLY LYS ILE VAL SEQRES 15 C 389 SER MET LYS ASP VAL ASP ALA THR GLY PHE HIS PHE GLU SEQRES 16 C 389 GLU CYS SER CYS TYR PRO SER GLY THR GLU ILE GLU CYS SEQRES 17 C 389 VAL CYS ARG ASP ASN TRP ARG GLY SER ASN ARG PRO TRP SEQRES 18 C 389 ILE ARG PHE ASN SER ASP LEU ASP TYR GLN ILE GLY TYR SEQRES 19 C 389 VAL CYS SER GLY ILE PHE GLY ASP ASN PRO ARG PRO VAL SEQRES 20 C 389 ASP GLY THR GLY SER CYS ASN GLY PRO VAL ASN ASN GLY SEQRES 21 C 389 LYS GLY ARG TYR GLY VAL LYS GLY PHE SER PHE ARG TYR SEQRES 22 C 389 GLY ASP GLY VAL TRP ILE GLY ARG THR LYS SER LEU GLU SEQRES 23 C 389 SER ARG SER GLY PHE GLU MET VAL TRP ASP ALA ASN GLY SEQRES 24 C 389 TRP VAL SER THR ASP LYS ASP SER ASN GLY VAL GLN ASP SEQRES 25 C 389 ILE ILE ASP ASN ASP ASN TRP SER GLY TYR SER GLY SER SEQRES 26 C 389 PHE SER ILE ARG GLY GLU THR THR GLY LYS ASN CYS THR SEQRES 27 C 389 VAL PRO CYS PHE TRP VAL GLU MET ILE ARG GLY GLN PRO SEQRES 28 C 389 LYS GLU LYS THR ILE TRP THR SER GLY SER SER ILE ALA SEQRES 29 C 389 PHE CYS GLY VAL ASN SER ASP THR THR GLY TRP SER TRP SEQRES 30 C 389 PRO ASP GLY ALA LEU LEU PRO PHE ASP ILE ASP LYS SEQRES 1 D 389 VAL HIS TYR SER SER GLY ARG ASP LEU CYS PRO ILE ARG SEQRES 2 D 389 GLY TRP ALA PRO LEU SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 D 389 GLY SER ARG GLY GLU VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 D 389 ILE SER CYS SER ILE SER GLU CYS ARG THR PHE PHE LEU SEQRES 5 D 389 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN GLY SEQRES 6 D 389 THR VAL LYS ASP ARG SER PRO PHE ARG THR LEU MET SER SEQRES 7 D 389 CYS PRO ILE GLY VAL ALA PRO SER PRO SER ASN SER ARG SEQRES 8 D 389 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS SER ASP SEQRES 9 D 389 GLY PRO GLY TRP LEU THR LEU GLY ILE THR GLY PRO ASP SEQRES 10 D 389 SER THR ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE ILE SEQRES 11 D 389 THR ASP THR LEU LYS SER TRP LYS GLY ASN ILE MET ARG SEQRES 12 D 389 THR GLN GLU SER GLU CYS VAL CYS GLN ASP GLU PHE CYS SEQRES 13 D 389 TYR THR LEU VAL THR ASP GLY PRO SER ASP ALA GLN ALA SEQRES 14 D 389 PHE TYR LYS ILE LEU LYS ILE ARG LYS GLY LYS ILE VAL SEQRES 15 D 389 SER MET LYS ASP VAL ASP ALA THR GLY PHE HIS PHE GLU SEQRES 16 D 389 GLU CYS SER CYS TYR PRO SER GLY THR GLU ILE GLU CYS SEQRES 17 D 389 VAL CYS ARG ASP ASN TRP ARG GLY SER ASN ARG PRO TRP SEQRES 18 D 389 ILE ARG PHE ASN SER ASP LEU ASP TYR GLN ILE GLY TYR SEQRES 19 D 389 VAL CYS SER GLY ILE PHE GLY ASP ASN PRO ARG PRO VAL SEQRES 20 D 389 ASP GLY THR GLY SER CYS ASN GLY PRO VAL ASN ASN GLY SEQRES 21 D 389 LYS GLY ARG TYR GLY VAL LYS GLY PHE SER PHE ARG TYR SEQRES 22 D 389 GLY ASP GLY VAL TRP ILE GLY ARG THR LYS SER LEU GLU SEQRES 23 D 389 SER ARG SER GLY PHE GLU MET VAL TRP ASP ALA ASN GLY SEQRES 24 D 389 TRP VAL SER THR ASP LYS ASP SER ASN GLY VAL GLN ASP SEQRES 25 D 389 ILE ILE ASP ASN ASP ASN TRP SER GLY TYR SER GLY SER SEQRES 26 D 389 PHE SER ILE ARG GLY GLU THR THR GLY LYS ASN CYS THR SEQRES 27 D 389 VAL PRO CYS PHE TRP VAL GLU MET ILE ARG GLY GLN PRO SEQRES 28 D 389 LYS GLU LYS THR ILE TRP THR SER GLY SER SER ILE ALA SEQRES 29 D 389 PHE CYS GLY VAL ASN SER ASP THR THR GLY TRP SER TRP SEQRES 30 D 389 PRO ASP GLY ALA LEU LEU PRO PHE ASP ILE ASP LYS SEQRES 1 E 123 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 123 PHE SER PHE THR THR TYR GLU MET ASN TRP VAL ARG GLN SEQRES 4 E 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER HIS ILE SER SEQRES 5 E 123 SER ARG GLY LEU VAL ILE TYR TYR ALA ASP SER VAL LYS SEQRES 6 E 123 GLY ARG PHE THR MET SER ARG ASP THR ALA LYS ASN SER SEQRES 7 E 123 LEU TYR LEU GLN MET ASP SER LEU THR VAL ALA ASP THR SEQRES 8 E 123 ALA VAL TYR TYR CYS ALA ARG HIS TYR PHE ASP ARG ASP SEQRES 9 E 123 TRP GLY TYR SER GLY MET ASP LEU TRP GLY GLN GLY THR SEQRES 10 E 123 THR VAL THR VAL SER SER SEQRES 1 F 107 GLU VAL VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 F 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 F 107 GLN SER LEU GLY THR ASN TYR LEU ALA TRP TYR GLN HIS SEQRES 4 F 107 LYS PRO GLY GLN SER PRO ARG LEU LEU ILE ASP GLY ALA SEQRES 5 F 107 SER THR ARG ALA ILE GLY ILE PRO ASP ARG PHE SER ALA SEQRES 6 F 107 SER GLY SER GLY THR ASP PHE THR LEU THR VAL SER ARG SEQRES 7 F 107 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN HIS SEQRES 8 F 107 TYR GLY ASN PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 F 107 GLU ILE LYS SEQRES 1 G 123 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 123 PHE SER PHE THR THR TYR GLU MET ASN TRP VAL ARG GLN SEQRES 4 G 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER HIS ILE SER SEQRES 5 G 123 SER ARG GLY LEU VAL ILE TYR TYR ALA ASP SER VAL LYS SEQRES 6 G 123 GLY ARG PHE THR MET SER ARG ASP THR ALA LYS ASN SER SEQRES 7 G 123 LEU TYR LEU GLN MET ASP SER LEU THR VAL ALA ASP THR SEQRES 8 G 123 ALA VAL TYR TYR CYS ALA ARG HIS TYR PHE ASP ARG ASP SEQRES 9 G 123 TRP GLY TYR SER GLY MET ASP LEU TRP GLY GLN GLY THR SEQRES 10 G 123 THR VAL THR VAL SER SER SEQRES 1 H 107 GLU VAL VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 H 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 H 107 GLN SER LEU GLY THR ASN TYR LEU ALA TRP TYR GLN HIS SEQRES 4 H 107 LYS PRO GLY GLN SER PRO ARG LEU LEU ILE ASP GLY ALA SEQRES 5 H 107 SER THR ARG ALA ILE GLY ILE PRO ASP ARG PHE SER ALA SEQRES 6 H 107 SER GLY SER GLY THR ASP PHE THR LEU THR VAL SER ARG SEQRES 7 H 107 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN HIS SEQRES 8 H 107 TYR GLY ASN PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 H 107 GLU ILE LYS SEQRES 1 I 123 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 I 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 I 123 PHE SER PHE THR THR TYR GLU MET ASN TRP VAL ARG GLN SEQRES 4 I 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER HIS ILE SER SEQRES 5 I 123 SER ARG GLY LEU VAL ILE TYR TYR ALA ASP SER VAL LYS SEQRES 6 I 123 GLY ARG PHE THR MET SER ARG ASP THR ALA LYS ASN SER SEQRES 7 I 123 LEU TYR LEU GLN MET ASP SER LEU THR VAL ALA ASP THR SEQRES 8 I 123 ALA VAL TYR TYR CYS ALA ARG HIS TYR PHE ASP ARG ASP SEQRES 9 I 123 TRP GLY TYR SER GLY MET ASP LEU TRP GLY GLN GLY THR SEQRES 10 I 123 THR VAL THR VAL SER SER SEQRES 1 J 107 GLU VAL VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 J 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 J 107 GLN SER LEU GLY THR ASN TYR LEU ALA TRP TYR GLN HIS SEQRES 4 J 107 LYS PRO GLY GLN SER PRO ARG LEU LEU ILE ASP GLY ALA SEQRES 5 J 107 SER THR ARG ALA ILE GLY ILE PRO ASP ARG PHE SER ALA SEQRES 6 J 107 SER GLY SER GLY THR ASP PHE THR LEU THR VAL SER ARG SEQRES 7 J 107 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN HIS SEQRES 8 J 107 TYR GLY ASN PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 J 107 GLU ILE LYS SEQRES 1 K 123 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 K 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 K 123 PHE SER PHE THR THR TYR GLU MET ASN TRP VAL ARG GLN SEQRES 4 K 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER HIS ILE SER SEQRES 5 K 123 SER ARG GLY LEU VAL ILE TYR TYR ALA ASP SER VAL LYS SEQRES 6 K 123 GLY ARG PHE THR MET SER ARG ASP THR ALA LYS ASN SER SEQRES 7 K 123 LEU TYR LEU GLN MET ASP SER LEU THR VAL ALA ASP THR SEQRES 8 K 123 ALA VAL TYR TYR CYS ALA ARG HIS TYR PHE ASP ARG ASP SEQRES 9 K 123 TRP GLY TYR SER GLY MET ASP LEU TRP GLY GLN GLY THR SEQRES 10 K 123 THR VAL THR VAL SER SER SEQRES 1 L 107 GLU VAL VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 107 GLN SER LEU GLY THR ASN TYR LEU ALA TRP TYR GLN HIS SEQRES 4 L 107 LYS PRO GLY GLN SER PRO ARG LEU LEU ILE ASP GLY ALA SEQRES 5 L 107 SER THR ARG ALA ILE GLY ILE PRO ASP ARG PHE SER ALA SEQRES 6 L 107 SER GLY SER GLY THR ASP PHE THR LEU THR VAL SER ARG SEQRES 7 L 107 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN HIS SEQRES 8 L 107 TYR GLY ASN PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 L 107 GLU ILE LYS HET NAG A 501 14 HET CA A 502 1 HET NAG B 501 14 HET CA B 502 1 HET NAG C 501 14 HET CA C 502 1 HET NAG D 501 14 HET CA D 502 1 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 13 NAG 4(C8 H15 N O6) FORMUL 14 CA 4(CA 2+) HELIX 1 AA1 ASN A 103 GLY A 108 1 6 HELIX 2 AA2 ASP A 141 ASN A 145 5 5 HELIX 3 AA3 ARG A 410 GLY A 415 1 6 HELIX 4 AA4 ASN B 103 GLY B 108 1 6 HELIX 5 AA5 ASP B 141 ASN B 145 5 5 HELIX 6 AA6 ARG B 410 GLY B 415 1 6 HELIX 7 AA7 ASN C 103 GLY C 108 1 6 HELIX 8 AA8 ASP C 141 ASN C 145 5 5 HELIX 9 AA9 ARG C 410 GLY C 415 1 6 HELIX 10 AB1 ASN D 103 GLY D 108 1 6 HELIX 11 AB2 ASP D 141 ASN D 145 5 5 HELIX 12 AB3 ARG D 410 GLY D 415 1 6 HELIX 13 AB4 ASP E 62 LYS E 65 5 4 HELIX 14 AB5 THR E 87 THR E 91 5 5 HELIX 15 AB6 ASP G 62 LYS G 65 5 4 HELIX 16 AB7 THR G 87 THR G 91 5 5 HELIX 17 AB8 ASP I 62 LYS I 65 5 4 HELIX 18 AB9 THR I 87 THR I 91 5 5 HELIX 19 AC1 ASP K 62 LYS K 65 5 4 HELIX 20 AC2 THR K 87 THR K 91 5 5 SHEET 1 AA1 4 GLY A 95 LYS A 101 0 SHEET 2 AA1 4 THR A 439 VAL A 449 -1 O CYS A 447 N ALA A 97 SHEET 3 AA1 4 VAL A 420 GLY A 430 -1 N PHE A 423 O PHE A 446 SHEET 4 AA1 4 SER A 404 ILE A 409 -1 N ILE A 409 O VAL A 420 SHEET 1 AA2 4 PHE A 114 CYS A 123 0 SHEET 2 AA2 4 CYS A 128 LEU A 138 -1 O ARG A 129 N SER A 122 SHEET 3 AA2 4 THR A 156 PRO A 161 -1 O CYS A 160 N THR A 130 SHEET 4 AA2 4 ARG A 172 SER A 175 -1 O ARG A 172 N SER A 159 SHEET 1 AA3 4 SER A 179 SER A 184 0 SHEET 2 AA3 4 TRP A 189 THR A 195 -1 O ILE A 194 N SER A 179 SHEET 3 AA3 4 VAL A 202 TYR A 207 -1 O VAL A 204 N GLY A 193 SHEET 4 AA3 4 ILE A 210 LYS A 216 -1 O ASP A 213 N LEU A 205 SHEET 1 AA4 3 MET A 223 ARG A 224 0 SHEET 2 AA4 3 PHE A 236 ASP A 243 -1 O THR A 242 N ARG A 224 SHEET 3 AA4 3 VAL A 231 GLN A 233 -1 N VAL A 231 O TYR A 238 SHEET 1 AA5 4 MET A 223 ARG A 224 0 SHEET 2 AA5 4 PHE A 236 ASP A 243 -1 O THR A 242 N ARG A 224 SHEET 3 AA5 4 PHE A 251 ARG A 258 -1 O ILE A 257 N CYS A 237 SHEET 4 AA5 4 LYS A 261 VAL A 268 -1 O SER A 264 N LYS A 256 SHEET 1 AA6 4 GLU A 276 SER A 283 0 SHEET 2 AA6 4 GLU A 286 ARG A 292 -1 O GLU A 288 N TYR A 281 SHEET 3 AA6 4 PRO A 301 PHE A 305 -1 O PRO A 301 N CYS A 291 SHEET 4 AA6 4 TYR A 311 TYR A 315 -1 O GLY A 314 N TRP A 302 SHEET 1 AA7 4 PHE A 350 TYR A 354 0 SHEET 2 AA7 4 GLY A 357 ARG A 362 -1 O GLY A 357 N TYR A 354 SHEET 3 AA7 4 SER A 370 ASP A 377 -1 O VAL A 375 N ILE A 360 SHEET 4 AA7 4 VAL A 391 TRP A 400 -1 O GLN A 392 N MET A 374 SHEET 1 AA8 4 GLY B 95 LYS B 101 0 SHEET 2 AA8 4 THR B 439 VAL B 449 -1 O CYS B 447 N ALA B 97 SHEET 3 AA8 4 VAL B 420 GLY B 430 -1 N PHE B 423 O PHE B 446 SHEET 4 AA8 4 SER B 404 ILE B 409 -1 N ILE B 409 O VAL B 420 SHEET 1 AA9 4 PHE B 114 CYS B 123 0 SHEET 2 AA9 4 CYS B 128 LEU B 138 -1 O ARG B 129 N SER B 122 SHEET 3 AA9 4 THR B 156 PRO B 161 -1 O CYS B 160 N THR B 130 SHEET 4 AA9 4 ARG B 172 SER B 175 -1 O ARG B 172 N SER B 159 SHEET 1 AB1 4 SER B 179 SER B 184 0 SHEET 2 AB1 4 TRP B 189 THR B 195 -1 O ILE B 194 N SER B 179 SHEET 3 AB1 4 VAL B 202 TYR B 207 -1 O VAL B 204 N GLY B 193 SHEET 4 AB1 4 ILE B 210 LYS B 216 -1 O ASP B 213 N LEU B 205 SHEET 1 AB2 3 MET B 223 ARG B 224 0 SHEET 2 AB2 3 PHE B 236 ASP B 243 -1 O THR B 242 N ARG B 224 SHEET 3 AB2 3 VAL B 231 GLN B 233 -1 N VAL B 231 O TYR B 238 SHEET 1 AB3 4 MET B 223 ARG B 224 0 SHEET 2 AB3 4 PHE B 236 ASP B 243 -1 O THR B 242 N ARG B 224 SHEET 3 AB3 4 PHE B 251 ARG B 258 -1 O ILE B 257 N CYS B 237 SHEET 4 AB3 4 LYS B 261 VAL B 268 -1 O SER B 264 N LYS B 256 SHEET 1 AB4 4 GLU B 276 SER B 283 0 SHEET 2 AB4 4 GLU B 286 ARG B 292 -1 O GLU B 288 N TYR B 281 SHEET 3 AB4 4 PRO B 301 PHE B 305 -1 O PRO B 301 N CYS B 291 SHEET 4 AB4 4 TYR B 311 TYR B 315 -1 O GLY B 314 N TRP B 302 SHEET 1 AB5 4 PHE B 350 TYR B 354 0 SHEET 2 AB5 4 GLY B 357 ARG B 362 -1 O GLY B 357 N TYR B 354 SHEET 3 AB5 4 SER B 370 ASP B 377 -1 O VAL B 375 N ILE B 360 SHEET 4 AB5 4 VAL B 391 TRP B 400 -1 O GLN B 392 N MET B 374 SHEET 1 AB6 4 GLY C 95 LYS C 101 0 SHEET 2 AB6 4 THR C 439 VAL C 449 -1 O CYS C 447 N ALA C 97 SHEET 3 AB6 4 VAL C 420 GLY C 430 -1 N PHE C 423 O PHE C 446 SHEET 4 AB6 4 SER C 404 ILE C 409 -1 N ILE C 409 O VAL C 420 SHEET 1 AB7 4 PHE C 114 CYS C 123 0 SHEET 2 AB7 4 CYS C 128 LEU C 138 -1 O ARG C 129 N SER C 122 SHEET 3 AB7 4 THR C 156 PRO C 161 -1 O CYS C 160 N THR C 130 SHEET 4 AB7 4 ARG C 172 SER C 175 -1 O ARG C 172 N SER C 159 SHEET 1 AB8 4 SER C 179 SER C 184 0 SHEET 2 AB8 4 TRP C 189 THR C 195 -1 O ILE C 194 N SER C 179 SHEET 3 AB8 4 VAL C 202 TYR C 207 -1 O VAL C 204 N GLY C 193 SHEET 4 AB8 4 ILE C 210 LYS C 216 -1 O ASP C 213 N LEU C 205 SHEET 1 AB9 3 MET C 223 ARG C 224 0 SHEET 2 AB9 3 PHE C 236 ASP C 243 -1 O THR C 242 N ARG C 224 SHEET 3 AB9 3 VAL C 231 GLN C 233 -1 N VAL C 231 O TYR C 238 SHEET 1 AC1 4 MET C 223 ARG C 224 0 SHEET 2 AC1 4 PHE C 236 ASP C 243 -1 O THR C 242 N ARG C 224 SHEET 3 AC1 4 PHE C 251 ARG C 258 -1 O ILE C 257 N CYS C 237 SHEET 4 AC1 4 LYS C 261 VAL C 268 -1 O SER C 264 N LYS C 256 SHEET 1 AC2 4 GLU C 276 SER C 283 0 SHEET 2 AC2 4 GLU C 286 ARG C 292 -1 O GLU C 288 N TYR C 281 SHEET 3 AC2 4 PRO C 301 PHE C 305 -1 O PRO C 301 N CYS C 291 SHEET 4 AC2 4 TYR C 311 TYR C 315 -1 O GLY C 314 N TRP C 302 SHEET 1 AC3 4 PHE C 350 TYR C 354 0 SHEET 2 AC3 4 GLY C 357 ARG C 362 -1 O GLY C 357 N TYR C 354 SHEET 3 AC3 4 SER C 370 ASP C 377 -1 O VAL C 375 N ILE C 360 SHEET 4 AC3 4 VAL C 391 TRP C 400 -1 O GLN C 392 N MET C 374 SHEET 1 AC4 4 GLY D 95 LYS D 101 0 SHEET 2 AC4 4 THR D 439 VAL D 449 -1 O CYS D 447 N ALA D 97 SHEET 3 AC4 4 VAL D 420 GLY D 430 -1 N PHE D 423 O PHE D 446 SHEET 4 AC4 4 SER D 404 ILE D 409 -1 N ILE D 409 O VAL D 420 SHEET 1 AC5 4 PHE D 114 CYS D 123 0 SHEET 2 AC5 4 CYS D 128 LEU D 138 -1 O ARG D 129 N SER D 122 SHEET 3 AC5 4 THR D 156 PRO D 161 -1 O CYS D 160 N THR D 130 SHEET 4 AC5 4 ARG D 172 SER D 175 -1 O ARG D 172 N SER D 159 SHEET 1 AC6 4 SER D 179 SER D 184 0 SHEET 2 AC6 4 TRP D 189 THR D 195 -1 O ILE D 194 N SER D 179 SHEET 3 AC6 4 VAL D 202 TYR D 207 -1 O VAL D 204 N GLY D 193 SHEET 4 AC6 4 ILE D 210 LYS D 216 -1 O ASP D 213 N LEU D 205 SHEET 1 AC7 3 MET D 223 ARG D 224 0 SHEET 2 AC7 3 PHE D 236 ASP D 243 -1 O THR D 242 N ARG D 224 SHEET 3 AC7 3 VAL D 231 GLN D 233 -1 N VAL D 231 O TYR D 238 SHEET 1 AC8 4 MET D 223 ARG D 224 0 SHEET 2 AC8 4 PHE D 236 ASP D 243 -1 O THR D 242 N ARG D 224 SHEET 3 AC8 4 PHE D 251 ARG D 258 -1 O ILE D 257 N CYS D 237 SHEET 4 AC8 4 LYS D 261 VAL D 268 -1 O SER D 264 N LYS D 256 SHEET 1 AC9 4 GLU D 276 SER D 283 0 SHEET 2 AC9 4 GLU D 286 ARG D 292 -1 O GLU D 288 N TYR D 281 SHEET 3 AC9 4 PRO D 301 PHE D 305 -1 O PRO D 301 N CYS D 291 SHEET 4 AC9 4 TYR D 311 TYR D 315 -1 O GLY D 314 N TRP D 302 SHEET 1 AD1 4 PHE D 350 TYR D 354 0 SHEET 2 AD1 4 GLY D 357 ARG D 362 -1 O GLY D 357 N TYR D 354 SHEET 3 AD1 4 SER D 370 ASP D 377 -1 O VAL D 375 N ILE D 360 SHEET 4 AD1 4 VAL D 391 TRP D 400 -1 O GLN D 392 N MET D 374 SHEET 1 AD2 4 GLN E 3 SER E 7 0 SHEET 2 AD2 4 SER E 17 SER E 25 -1 O ALA E 23 N VAL E 5 SHEET 3 AD2 4 SER E 78 ASP E 84 -1 O MET E 83 N LEU E 18 SHEET 4 AD2 4 PHE E 68 ASP E 73 -1 N SER E 71 O TYR E 80 SHEET 1 AD3 6 GLY E 10 VAL E 12 0 SHEET 2 AD3 6 THR E 117 VAL E 121 1 O THR E 120 N GLY E 10 SHEET 3 AD3 6 ALA E 92 HIS E 99 -1 N TYR E 94 O THR E 117 SHEET 4 AD3 6 GLU E 33 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AD3 6 LEU E 45 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AD3 6 TYR E 59 TYR E 60 -1 O TYR E 59 N HIS E 50 SHEET 1 AD4 4 GLY E 10 VAL E 12 0 SHEET 2 AD4 4 THR E 117 VAL E 121 1 O THR E 120 N GLY E 10 SHEET 3 AD4 4 ALA E 92 HIS E 99 -1 N TYR E 94 O THR E 117 SHEET 4 AD4 4 LEU E 112 TRP E 113 -1 O LEU E 112 N ARG E 98 SHEET 1 AD5 4 THR F 5 SER F 7 0 SHEET 2 AD5 4 ALA F 19 ARG F 24 -1 O ARG F 24 N THR F 5 SHEET 3 AD5 4 ASP F 71 VAL F 76 -1 O LEU F 74 N LEU F 21 SHEET 4 AD5 4 PHE F 63 SER F 68 -1 N SER F 64 O THR F 75 SHEET 1 AD6 5 THR F 10 LEU F 13 0 SHEET 2 AD6 5 THR F 102 ILE F 106 1 O GLU F 105 N LEU F 11 SHEET 3 AD6 5 VAL F 86 HIS F 91 -1 N TYR F 87 O THR F 102 SHEET 4 AD6 5 LEU F 34 HIS F 39 -1 N ALA F 35 O GLN F 90 SHEET 5 AD6 5 ARG F 46 ILE F 49 -1 O ARG F 46 N GLN F 38 SHEET 1 AD7 4 THR F 10 LEU F 13 0 SHEET 2 AD7 4 THR F 102 ILE F 106 1 O GLU F 105 N LEU F 11 SHEET 3 AD7 4 VAL F 86 HIS F 91 -1 N TYR F 87 O THR F 102 SHEET 4 AD7 4 THR F 97 PHE F 98 -1 O THR F 97 N HIS F 91 SHEET 1 AD8 4 GLN G 3 SER G 7 0 SHEET 2 AD8 4 SER G 17 SER G 25 -1 O ALA G 23 N VAL G 5 SHEET 3 AD8 4 SER G 78 ASP G 84 -1 O MET G 83 N LEU G 18 SHEET 4 AD8 4 PHE G 68 ASP G 73 -1 N SER G 71 O TYR G 80 SHEET 1 AD9 6 GLY G 10 VAL G 12 0 SHEET 2 AD9 6 THR G 117 VAL G 121 1 O THR G 120 N GLY G 10 SHEET 3 AD9 6 ALA G 92 HIS G 99 -1 N TYR G 94 O THR G 117 SHEET 4 AD9 6 GLU G 33 GLN G 39 -1 N VAL G 37 O TYR G 95 SHEET 5 AD9 6 LEU G 45 ILE G 51 -1 O ILE G 51 N MET G 34 SHEET 6 AD9 6 TYR G 59 TYR G 60 -1 O TYR G 59 N HIS G 50 SHEET 1 AE1 4 GLY G 10 VAL G 12 0 SHEET 2 AE1 4 THR G 117 VAL G 121 1 O THR G 120 N GLY G 10 SHEET 3 AE1 4 ALA G 92 HIS G 99 -1 N TYR G 94 O THR G 117 SHEET 4 AE1 4 LEU G 112 TRP G 113 -1 O LEU G 112 N ARG G 98 SHEET 1 AE2 4 THR H 5 SER H 7 0 SHEET 2 AE2 4 ALA H 19 ARG H 24 -1 O ARG H 24 N THR H 5 SHEET 3 AE2 4 ASP H 71 VAL H 76 -1 O LEU H 74 N LEU H 21 SHEET 4 AE2 4 PHE H 63 SER H 68 -1 N SER H 64 O THR H 75 SHEET 1 AE3 6 THR H 10 LEU H 13 0 SHEET 2 AE3 6 THR H 102 ILE H 106 1 O GLU H 105 N LEU H 11 SHEET 3 AE3 6 VAL H 86 HIS H 91 -1 N TYR H 87 O THR H 102 SHEET 4 AE3 6 LEU H 34 HIS H 39 -1 N ALA H 35 O GLN H 90 SHEET 5 AE3 6 ARG H 46 ASP H 50 -1 O ARG H 46 N GLN H 38 SHEET 6 AE3 6 THR H 54 ARG H 55 -1 O THR H 54 N ASP H 50 SHEET 1 AE4 4 THR H 10 LEU H 13 0 SHEET 2 AE4 4 THR H 102 ILE H 106 1 O GLU H 105 N LEU H 11 SHEET 3 AE4 4 VAL H 86 HIS H 91 -1 N TYR H 87 O THR H 102 SHEET 4 AE4 4 THR H 97 PHE H 98 -1 O THR H 97 N HIS H 91 SHEET 1 AE5 4 GLN I 3 SER I 7 0 SHEET 2 AE5 4 SER I 17 SER I 25 -1 O SER I 21 N SER I 7 SHEET 3 AE5 4 SER I 78 ASP I 84 -1 O MET I 83 N LEU I 18 SHEET 4 AE5 4 PHE I 68 ASP I 73 -1 N SER I 71 O TYR I 80 SHEET 1 AE6 6 GLY I 10 VAL I 12 0 SHEET 2 AE6 6 THR I 117 VAL I 121 1 O THR I 120 N GLY I 10 SHEET 3 AE6 6 ALA I 92 HIS I 99 -1 N TYR I 94 O THR I 117 SHEET 4 AE6 6 GLU I 33 GLN I 39 -1 N VAL I 37 O TYR I 95 SHEET 5 AE6 6 LEU I 45 ILE I 51 -1 O GLU I 46 N ARG I 38 SHEET 6 AE6 6 TYR I 59 TYR I 60 -1 O TYR I 59 N HIS I 50 SHEET 1 AE7 4 GLY I 10 VAL I 12 0 SHEET 2 AE7 4 THR I 117 VAL I 121 1 O THR I 120 N GLY I 10 SHEET 3 AE7 4 ALA I 92 HIS I 99 -1 N TYR I 94 O THR I 117 SHEET 4 AE7 4 LEU I 112 TRP I 113 -1 O LEU I 112 N ARG I 98 SHEET 1 AE8 4 THR J 5 SER J 7 0 SHEET 2 AE8 4 ALA J 19 ARG J 24 -1 O ARG J 24 N THR J 5 SHEET 3 AE8 4 ASP J 71 VAL J 76 -1 O LEU J 74 N LEU J 21 SHEET 4 AE8 4 PHE J 63 SER J 68 -1 N SER J 64 O THR J 75 SHEET 1 AE9 6 THR J 10 LEU J 13 0 SHEET 2 AE9 6 THR J 102 ILE J 106 1 O GLU J 105 N LEU J 11 SHEET 3 AE9 6 VAL J 86 HIS J 91 -1 N TYR J 87 O THR J 102 SHEET 4 AE9 6 LEU J 34 HIS J 39 -1 N ALA J 35 O GLN J 90 SHEET 5 AE9 6 ARG J 46 ASP J 50 -1 O ARG J 46 N GLN J 38 SHEET 6 AE9 6 THR J 54 ARG J 55 -1 O THR J 54 N ASP J 50 SHEET 1 AF1 4 THR J 10 LEU J 13 0 SHEET 2 AF1 4 THR J 102 ILE J 106 1 O GLU J 105 N LEU J 11 SHEET 3 AF1 4 VAL J 86 HIS J 91 -1 N TYR J 87 O THR J 102 SHEET 4 AF1 4 THR J 97 PHE J 98 -1 O THR J 97 N HIS J 91 SHEET 1 AF2 4 GLN K 3 SER K 7 0 SHEET 2 AF2 4 SER K 17 SER K 25 -1 O ALA K 23 N VAL K 5 SHEET 3 AF2 4 SER K 78 ASP K 84 -1 O MET K 83 N LEU K 18 SHEET 4 AF2 4 PHE K 68 ASP K 73 -1 N SER K 71 O TYR K 80 SHEET 1 AF3 6 GLY K 10 VAL K 12 0 SHEET 2 AF3 6 THR K 117 VAL K 121 1 O THR K 120 N GLY K 10 SHEET 3 AF3 6 ALA K 92 HIS K 99 -1 N TYR K 94 O THR K 117 SHEET 4 AF3 6 GLU K 33 GLN K 39 -1 N VAL K 37 O TYR K 95 SHEET 5 AF3 6 LEU K 45 ILE K 51 -1 O ILE K 51 N MET K 34 SHEET 6 AF3 6 TYR K 59 TYR K 60 -1 O TYR K 59 N HIS K 50 SHEET 1 AF4 4 GLY K 10 VAL K 12 0 SHEET 2 AF4 4 THR K 117 VAL K 121 1 O THR K 120 N GLY K 10 SHEET 3 AF4 4 ALA K 92 HIS K 99 -1 N TYR K 94 O THR K 117 SHEET 4 AF4 4 LEU K 112 TRP K 113 -1 O LEU K 112 N ARG K 98 SHEET 1 AF5 4 THR L 5 SER L 7 0 SHEET 2 AF5 4 ALA L 19 ARG L 24 -1 O ARG L 24 N THR L 5 SHEET 3 AF5 4 ASP L 71 VAL L 76 -1 O LEU L 74 N LEU L 21 SHEET 4 AF5 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AF6 6 THR L 10 LEU L 13 0 SHEET 2 AF6 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AF6 6 VAL L 86 HIS L 91 -1 N TYR L 87 O THR L 102 SHEET 4 AF6 6 LEU L 34 HIS L 39 -1 N ALA L 35 O GLN L 90 SHEET 5 AF6 6 ARG L 46 ASP L 50 -1 O ARG L 46 N GLN L 38 SHEET 6 AF6 6 THR L 54 ARG L 55 -1 O THR L 54 N ASP L 50 SHEET 1 AF7 4 THR L 10 LEU L 13 0 SHEET 2 AF7 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AF7 4 VAL L 86 HIS L 91 -1 N TYR L 87 O THR L 102 SHEET 4 AF7 4 THR L 97 PHE L 98 -1 O THR L 97 N HIS L 91 SSBOND 1 CYS A 91 CYS A 418 1555 1555 2.03 SSBOND 2 CYS A 123 CYS A 128 1555 1555 2.03 SSBOND 3 CYS A 183 CYS A 230 1555 1555 2.03 SSBOND 4 CYS A 183 CYS A 232 1555 1555 2.53 SSBOND 5 CYS A 232 CYS A 237 1555 1555 2.03 SSBOND 6 CYS A 278 CYS A 291 1555 1555 2.03 SSBOND 7 CYS A 280 CYS A 289 1555 1555 2.03 SSBOND 8 CYS A 317 CYS A 334 1555 1555 2.04 SSBOND 9 CYS A 422 CYS A 447 1555 1555 2.03 SSBOND 10 CYS B 91 CYS B 418 1555 1555 2.04 SSBOND 11 CYS B 123 CYS B 128 1555 1555 2.03 SSBOND 12 CYS B 183 CYS B 230 1555 1555 2.03 SSBOND 13 CYS B 183 CYS B 232 1555 1555 2.53 SSBOND 14 CYS B 232 CYS B 237 1555 1555 2.03 SSBOND 15 CYS B 278 CYS B 291 1555 1555 2.03 SSBOND 16 CYS B 280 CYS B 289 1555 1555 2.03 SSBOND 17 CYS B 317 CYS B 334 1555 1555 2.04 SSBOND 18 CYS B 422 CYS B 447 1555 1555 2.03 SSBOND 19 CYS C 91 CYS C 418 1555 1555 2.04 SSBOND 20 CYS C 123 CYS C 128 1555 1555 2.03 SSBOND 21 CYS C 183 CYS C 230 1555 1555 2.03 SSBOND 22 CYS C 183 CYS C 232 1555 1555 2.53 SSBOND 23 CYS C 232 CYS C 237 1555 1555 2.03 SSBOND 24 CYS C 278 CYS C 291 1555 1555 2.03 SSBOND 25 CYS C 280 CYS C 289 1555 1555 2.03 SSBOND 26 CYS C 317 CYS C 334 1555 1555 2.04 SSBOND 27 CYS C 422 CYS C 447 1555 1555 2.03 SSBOND 28 CYS D 91 CYS D 418 1555 1555 2.04 SSBOND 29 CYS D 123 CYS D 128 1555 1555 2.03 SSBOND 30 CYS D 183 CYS D 230 1555 1555 2.03 SSBOND 31 CYS D 183 CYS D 232 1555 1555 2.53 SSBOND 32 CYS D 232 CYS D 237 1555 1555 2.03 SSBOND 33 CYS D 278 CYS D 291 1555 1555 2.03 SSBOND 34 CYS D 280 CYS D 289 1555 1555 2.03 SSBOND 35 CYS D 317 CYS D 334 1555 1555 2.04 SSBOND 36 CYS D 422 CYS D 447 1555 1555 2.03 SSBOND 37 CYS E 22 CYS E 96 1555 1555 2.04 SSBOND 38 CYS F 23 CYS F 89 1555 1555 2.04 SSBOND 39 CYS G 22 CYS G 96 1555 1555 2.04 SSBOND 40 CYS H 23 CYS H 89 1555 1555 2.04 SSBOND 41 CYS I 22 CYS I 96 1555 1555 2.04 SSBOND 42 CYS J 23 CYS J 89 1555 1555 2.04 SSBOND 43 CYS K 22 CYS K 96 1555 1555 2.04 SSBOND 44 CYS L 23 CYS L 89 1555 1555 2.04 LINK ND2 ASN A 145 C1 NAG A 501 1555 1555 1.45 LINK ND2 ASN B 145 C1 NAG B 501 1555 1555 1.45 LINK ND2 ASN C 145 C1 NAG C 501 1555 1555 1.45 LINK ND2 ASN D 145 C1 NAG D 501 1555 1555 1.45 LINK O ASP A 293 CA CA A 502 1555 1555 2.72 LINK O GLY A 297 CA CA A 502 1555 1555 2.20 LINK OD2 ASP A 323 CA CA A 502 1555 1555 2.54 LINK O GLY A 343 CA CA A 502 1555 1555 2.48 LINK O TYR A 345 CA CA A 502 1555 1555 2.42 LINK O ASP B 293 CA CA B 502 1555 1555 2.69 LINK O GLY B 297 CA CA B 502 1555 1555 2.33 LINK OD2 ASP B 323 CA CA B 502 1555 1555 2.43 LINK O GLY B 343 CA CA B 502 1555 1555 2.38 LINK O TYR B 345 CA CA B 502 1555 1555 2.24 LINK O ASP C 293 CA CA C 502 1555 1555 2.90 LINK O GLY C 297 CA CA C 502 1555 1555 2.03 LINK OD2 ASP C 323 CA CA C 502 1555 1555 2.50 LINK O GLY C 343 CA CA C 502 1555 1555 2.27 LINK O TYR C 345 CA CA C 502 1555 1555 2.55 LINK O ASP D 293 CA CA D 502 1555 1555 2.70 LINK O GLY D 297 CA CA D 502 1555 1555 2.18 LINK OD2 ASP D 323 CA CA D 502 1555 1555 2.49 LINK O GLY D 343 CA CA D 502 1555 1555 2.31 LINK O TYR D 345 CA CA D 502 1555 1555 2.38 CISPEP 1 ASN A 324 PRO A 325 0 10.82 CISPEP 2 GLN A 431 PRO A 432 0 25.99 CISPEP 3 LEU A 464 PRO A 465 0 -3.36 CISPEP 4 ASN B 324 PRO B 325 0 6.57 CISPEP 5 GLN B 431 PRO B 432 0 26.15 CISPEP 6 LEU B 464 PRO B 465 0 -3.42 CISPEP 7 ASN C 324 PRO C 325 0 6.57 CISPEP 8 GLN C 431 PRO C 432 0 26.17 CISPEP 9 LEU C 464 PRO C 465 0 -3.41 CISPEP 10 ASN D 324 PRO D 325 0 6.63 CISPEP 11 GLN D 431 PRO D 432 0 26.05 CISPEP 12 LEU D 464 PRO D 465 0 -3.38 CISPEP 13 SER F 7 PRO F 8 0 -0.72 CISPEP 14 ASN F 94 PRO F 95 0 -4.32 CISPEP 15 SER H 7 PRO H 8 0 -4.73 CISPEP 16 ASN H 94 PRO H 95 0 -13.14 CISPEP 17 SER J 7 PRO J 8 0 -4.76 CISPEP 18 ASN J 94 PRO J 95 0 -4.36 CISPEP 19 SER L 7 PRO L 8 0 -4.69 CISPEP 20 ASN L 94 PRO L 95 0 -4.39 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