HEADER VIRAL PROTEIN/IMMUNE SYSTEM 20-NOV-24 9KOD TITLE NEURAMINIDASE OF A/DAIRY COW/MINNESOTA/24_016288-003/2024 (DCMN24 N1) TITLE 2 IN COMPLEX 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; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 GENE: NA; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 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 9KOD 0 JRNL AUTH X.WANG,J.GE,X.LI JRNL TITL NEURAMINIDASE OF A/DAIRY COW/MINNESOTA/24_016288-003/2024 JRNL TITL 2 (DCMN24 N1) IN COMPLEX WITH CAV-F6 FAB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.95 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) : 2.950 REMARK 3 NUMBER OF PARTICLES : 545144 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 9KOD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 22-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1300053966. 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/DAIRY REMARK 245 COW/MINNESOTA/24_016288-003/2024 (DCMN24 N1) IN COMPLEX WITH CAV- REMARK 245 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K 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) : 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, 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 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 LEU A 85 CG CD1 CD2 REMARK 470 LEU B 85 CG CD1 CD2 REMARK 470 LEU C 85 CG CD1 CD2 REMARK 470 LEU D 85 CG CD1 CD2 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 OD2 ASP A 384 CA CA A 504 1.65 REMARK 500 O TYR D 344 CA CA D 503 1.69 REMARK 500 NH2 ARG A 118 OD2 ASP I 104 1.98 REMARK 500 OG SER C 450 OG1 THR D 215 2.11 REMARK 500 OD2 ASP D 294 OH TYR D 316 2.14 REMARK 500 OD2 ASP A 294 OH TYR A 316 2.14 REMARK 500 OD2 ASP C 294 OH TYR C 316 2.14 REMARK 500 OD2 ASP B 294 OH TYR B 316 2.14 REMARK 500 OG SER L 14 OE1 GLU L 17 2.19 REMARK 500 OG SER J 14 OE1 GLU J 17 2.19 REMARK 500 OG SER F 14 OE1 GLU F 17 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 SER D 95 CA SER D 95 CB -0.096 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 GLU A 382 CB - CA - C ANGL. DEV. = 12.7 DEGREES REMARK 500 PRO A 431 CA - N - CD ANGL. DEV. = -12.4 DEGREES REMARK 500 PRO B 431 CA - N - CD ANGL. DEV. = -13.3 DEGREES REMARK 500 PRO C 431 CA - N - CD ANGL. DEV. = -12.9 DEGREES REMARK 500 PRO D 431 C - N - CD ANGL. DEV. = 14.3 DEGREES REMARK 500 PRO D 431 CA - N - CD ANGL. DEV. = -12.5 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 ILE A 188 -51.09 -122.45 REMARK 500 ALA A 251 -169.22 -124.21 REMARK 500 HIS A 297 39.12 -154.36 REMARK 500 SER A 319 126.47 -32.48 REMARK 500 ALA A 343 44.18 -85.24 REMARK 500 TYR A 344 -164.95 -162.24 REMARK 500 SER A 350 148.57 -170.64 REMARK 500 SER A 385 1.90 87.24 REMARK 500 LEU A 415 -168.42 -74.17 REMARK 500 ILE B 188 -51.11 -122.49 REMARK 500 ASN B 235 34.79 74.55 REMARK 500 ALA B 251 -169.25 -124.27 REMARK 500 HIS B 297 36.84 -145.85 REMARK 500 ALA B 343 44.20 -85.25 REMARK 500 TYR B 344 -165.04 -162.24 REMARK 500 SER B 350 148.55 -170.62 REMARK 500 ILE C 188 -51.04 -122.55 REMARK 500 ALA C 251 -169.25 -124.26 REMARK 500 HIS C 297 36.81 -145.90 REMARK 500 ALA C 343 44.20 -85.24 REMARK 500 TYR C 344 -165.03 -162.20 REMARK 500 SER C 350 148.60 -170.62 REMARK 500 ASP C 384 154.70 -35.64 REMARK 500 ALA D 86 -147.38 58.32 REMARK 500 ASN D 88 -30.68 -151.84 REMARK 500 ILE D 188 -51.09 -122.47 REMARK 500 ALA D 251 -169.24 -124.25 REMARK 500 HIS D 297 36.80 -145.90 REMARK 500 ALA D 343 44.26 -85.25 REMARK 500 TYR D 344 -165.03 -162.28 REMARK 500 SER D 350 148.61 -170.68 REMARK 500 ASP D 384 170.62 -59.43 REMARK 500 SER F 26 0.11 -68.26 REMARK 500 ALA F 52 -16.36 86.52 REMARK 500 ILE F 59 126.60 -38.93 REMARK 500 ALA G 92 -175.26 -172.89 REMARK 500 ALA H 52 -2.12 68.71 REMARK 500 SER H 53 -3.55 -141.69 REMARK 500 ALA I 92 -175.31 -172.92 REMARK 500 ALA J 52 -1.96 68.65 REMARK 500 SER J 53 -3.56 -141.73 REMARK 500 SER J 66 -164.44 -164.17 REMARK 500 ALA K 92 -175.33 -172.95 REMARK 500 ALA L 52 -2.00 68.63 REMARK 500 SER L 53 -3.48 -141.77 REMARK 500 PRO L 60 -174.00 -62.85 REMARK 500 ALA L 85 -167.01 -162.39 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ARG A 430 PRO A 431 35.37 REMARK 500 ARG C 430 PRO C 431 30.95 REMARK 500 ARG D 430 PRO D 431 36.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 PRO L 60 -10.99 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 503 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 294 O REMARK 620 2 GLY A 298 O 80.0 REMARK 620 3 ASP A 324 OD2 78.1 71.2 REMARK 620 4 GLY A 342 O 107.5 82.8 152.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 504 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 376 OD1 REMARK 620 2 ASP A 376 OD2 51.4 REMARK 620 3 ASN A 378 OD1 87.1 118.2 REMARK 620 4 ASP A 384 OD1 134.9 83.5 119.9 REMARK 620 5 SER A 386 O 72.4 86.1 127.1 108.4 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 503 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 294 O REMARK 620 2 GLY B 298 O 84.7 REMARK 620 3 ASP B 324 OD2 74.8 80.0 REMARK 620 4 GLY B 342 O 105.4 78.9 158.7 REMARK 620 5 TYR B 344 O 87.6 169.9 104.4 96.8 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 504 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 376 OD1 REMARK 620 2 ASP B 376 OD2 51.5 REMARK 620 3 ASN B 378 OD1 77.1 110.3 REMARK 620 4 SER B 386 O 73.1 90.4 118.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 503 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 294 O REMARK 620 2 GLY C 298 O 85.2 REMARK 620 3 GLY C 342 O 108.9 85.6 REMARK 620 4 TYR C 344 O 83.3 168.4 99.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 504 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 376 OD1 REMARK 620 2 ASP C 376 OD2 44.7 REMARK 620 3 ASN C 378 OD1 88.7 110.6 REMARK 620 4 SER C 386 O 73.2 81.7 139.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 503 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 294 O REMARK 620 2 GLY D 298 O 84.9 REMARK 620 3 ASP D 324 OD2 75.4 76.4 REMARK 620 4 GLY D 342 O 110.2 75.5 150.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 504 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 376 OD1 REMARK 620 2 ASP D 376 OD2 51.9 REMARK 620 3 ASN D 378 OD1 92.7 123.8 REMARK 620 4 SER D 386 O 71.9 85.6 127.8 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-62473 RELATED DB: EMDB REMARK 900 NEURAMINIDASE OF A/DAIRY COW/MINNESOTA/24_016288-003/2024 (DCMN24 REMARK 900 N1) IN COMPLEX WITH F6 FAB DBREF1 9KOD A 83 469 UNP A0A8K1VZ50_9INFA DBREF2 9KOD A A0A8K1VZ50 83 469 DBREF1 9KOD B 83 469 UNP A0A8K1VZ50_9INFA DBREF2 9KOD B A0A8K1VZ50 83 469 DBREF1 9KOD C 83 469 UNP A0A8K1VZ50_9INFA DBREF2 9KOD C A0A8K1VZ50 83 469 DBREF1 9KOD D 83 469 UNP A0A8K1VZ50_9INFA DBREF2 9KOD D A0A8K1VZ50 83 469 DBREF 9KOD E 1 123 PDB 9KOD 9KOD 1 123 DBREF 9KOD F 1 107 PDB 9KOD 9KOD 1 107 DBREF 9KOD G 1 123 PDB 9KOD 9KOD 1 123 DBREF 9KOD H 1 107 PDB 9KOD 9KOD 1 107 DBREF 9KOD I 1 123 PDB 9KOD 9KOD 1 123 DBREF 9KOD J 1 107 PDB 9KOD 9KOD 1 107 DBREF 9KOD K 1 123 PDB 9KOD 9KOD 1 123 DBREF 9KOD L 1 107 PDB 9KOD 9KOD 1 107 SEQADV 9KOD MET A 269 UNP A0A8K1VZ5 LEU 269 CONFLICT SEQADV 9KOD ILE A 321 UNP A0A8K1VZ5 VAL 321 CONFLICT SEQADV 9KOD PRO A 339 UNP A0A8K1VZ5 SER 339 CONFLICT SEQADV 9KOD MET B 269 UNP A0A8K1VZ5 LEU 269 CONFLICT SEQADV 9KOD ILE B 321 UNP A0A8K1VZ5 VAL 321 CONFLICT SEQADV 9KOD PRO B 339 UNP A0A8K1VZ5 SER 339 CONFLICT SEQADV 9KOD MET C 269 UNP A0A8K1VZ5 LEU 269 CONFLICT SEQADV 9KOD ILE C 321 UNP A0A8K1VZ5 VAL 321 CONFLICT SEQADV 9KOD PRO C 339 UNP A0A8K1VZ5 SER 339 CONFLICT SEQADV 9KOD MET D 269 UNP A0A8K1VZ5 LEU 269 CONFLICT SEQADV 9KOD ILE D 321 UNP A0A8K1VZ5 VAL 321 CONFLICT SEQADV 9KOD PRO D 339 UNP A0A8K1VZ5 SER 339 CONFLICT SEQRES 1 A 387 VAL THR LEU ALA GLY ASN SER SER LEU CYS PRO ILE SER SEQRES 2 A 387 GLY TRP ALA ILE TYR SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 A 387 GLY SER LYS GLY ASP VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 A 387 ILE SER CYS SER HIS LEU GLU CYS ARG THR PHE PHE LEU SEQRES 5 A 387 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN GLY SEQRES 6 A 387 THR VAL LYS ASP ARG SER PRO TYR ARG THR LEU MET SER SEQRES 7 A 387 CYS PRO VAL GLY GLU ALA PRO SER PRO TYR ASN SER ARG SEQRES 8 A 387 PHE GLU SER VAL ALA TRP SER ALA SER ALA CYS HIS ASP SEQRES 9 A 387 GLY ILE SER TRP LEU THR ILE GLY ILE SER GLY PRO ASP SEQRES 10 A 387 ASN GLY ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE ILE SEQRES 11 A 387 THR ASP THR ILE LYS SER TRP ARG ASN ASN ILE LEU ARG SEQRES 12 A 387 THR GLN GLU SER GLU CYS ALA CYS VAL ASN GLY SER CYS SEQRES 13 A 387 PHE THR VAL MET THR ASP GLY PRO SER ASN GLY GLN ALA SEQRES 14 A 387 SER TYR LYS ILE PHE LYS ILE GLU LYS GLY LYS VAL VAL SEQRES 15 A 387 LYS SER VAL GLU MET ASN ALA PRO ASN TYR HIS TYR GLU SEQRES 16 A 387 GLU CYS SER CYS TYR PRO ASP ALA GLY ASP ILE MET CYS SEQRES 17 A 387 VAL CYS ARG ASP ASN TRP HIS GLY SER ASN ARG PRO TRP SEQRES 18 A 387 VAL SER PHE ASN GLN ASN LEU GLU TYR GLN ILE GLY TYR SEQRES 19 A 387 ILE CYS SER GLY ILE PHE GLY ASP ASN PRO ARG PRO ASN SEQRES 20 A 387 ASP GLY THR GLY SER CYS SER PRO MET PRO SER ASN GLY SEQRES 21 A 387 ALA TYR GLY VAL LYS GLY PHE SER PHE LYS TYR GLY ASN SEQRES 22 A 387 GLY VAL TRP ILE GLY ARG THR LYS SER THR SER SER ARG SEQRES 23 A 387 SER GLY PHE GLU MET ILE TRP ASP PRO ASN GLY TRP THR SEQRES 24 A 387 GLU THR ASP SER SER PHE SER VAL LYS GLN ASP ILE VAL SEQRES 25 A 387 GLU ILE THR ASP TRP SER GLY TYR SER GLY SER PHE VAL SEQRES 26 A 387 GLN HIS PRO GLU LEU THR GLY LEU ASP CYS MET ARG PRO SEQRES 27 A 387 CYS PHE TRP VAL GLU LEU ILE ARG GLY ARG PRO LYS GLU SEQRES 28 A 387 ASN THR ILE TRP THR SER GLY SER SER ILE SER PHE CYS SEQRES 29 A 387 GLY VAL ASN SER ASP THR VAL GLY TRP SER TRP PRO ASP SEQRES 30 A 387 GLY ALA GLU LEU PRO PHE THR ILE ASP LYS SEQRES 1 B 387 VAL THR LEU ALA GLY ASN SER SER LEU CYS PRO ILE SER SEQRES 2 B 387 GLY TRP ALA ILE TYR SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 B 387 GLY SER LYS GLY ASP VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 B 387 ILE SER CYS SER HIS LEU GLU CYS ARG THR PHE PHE LEU SEQRES 5 B 387 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN GLY SEQRES 6 B 387 THR VAL LYS ASP ARG SER PRO TYR ARG THR LEU MET SER SEQRES 7 B 387 CYS PRO VAL GLY GLU ALA PRO SER PRO TYR ASN SER ARG SEQRES 8 B 387 PHE GLU SER VAL ALA TRP SER ALA SER ALA CYS HIS ASP SEQRES 9 B 387 GLY ILE SER TRP LEU THR ILE GLY ILE SER GLY PRO ASP SEQRES 10 B 387 ASN GLY ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE ILE SEQRES 11 B 387 THR ASP THR ILE LYS SER TRP ARG ASN ASN ILE LEU ARG SEQRES 12 B 387 THR GLN GLU SER GLU CYS ALA CYS VAL ASN GLY SER CYS SEQRES 13 B 387 PHE THR VAL MET THR ASP GLY PRO SER ASN GLY GLN ALA SEQRES 14 B 387 SER TYR LYS ILE PHE LYS ILE GLU LYS GLY LYS VAL VAL SEQRES 15 B 387 LYS SER VAL GLU MET ASN ALA PRO ASN TYR HIS TYR GLU SEQRES 16 B 387 GLU CYS SER CYS TYR PRO ASP ALA GLY ASP ILE MET CYS SEQRES 17 B 387 VAL CYS ARG ASP ASN TRP HIS GLY SER ASN ARG PRO TRP SEQRES 18 B 387 VAL SER PHE ASN GLN ASN LEU GLU TYR GLN ILE GLY TYR SEQRES 19 B 387 ILE CYS SER GLY ILE PHE GLY ASP ASN PRO ARG PRO ASN SEQRES 20 B 387 ASP GLY THR GLY SER CYS SER PRO MET PRO SER ASN GLY SEQRES 21 B 387 ALA TYR GLY VAL LYS GLY PHE SER PHE LYS TYR GLY ASN SEQRES 22 B 387 GLY VAL TRP ILE GLY ARG THR LYS SER THR SER SER ARG SEQRES 23 B 387 SER GLY PHE GLU MET ILE TRP ASP PRO ASN GLY TRP THR SEQRES 24 B 387 GLU THR ASP SER SER PHE SER VAL LYS GLN ASP ILE VAL SEQRES 25 B 387 GLU ILE THR ASP TRP SER GLY TYR SER GLY SER PHE VAL SEQRES 26 B 387 GLN HIS PRO GLU LEU THR GLY LEU ASP CYS MET ARG PRO SEQRES 27 B 387 CYS PHE TRP VAL GLU LEU ILE ARG GLY ARG PRO LYS GLU SEQRES 28 B 387 ASN THR ILE TRP THR SER GLY SER SER ILE SER PHE CYS SEQRES 29 B 387 GLY VAL ASN SER ASP THR VAL GLY TRP SER TRP PRO ASP SEQRES 30 B 387 GLY ALA GLU LEU PRO PHE THR ILE ASP LYS SEQRES 1 C 387 VAL THR LEU ALA GLY ASN SER SER LEU CYS PRO ILE SER SEQRES 2 C 387 GLY TRP ALA ILE TYR SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 C 387 GLY SER LYS GLY ASP VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 C 387 ILE SER CYS SER HIS LEU GLU CYS ARG THR PHE PHE LEU SEQRES 5 C 387 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN GLY SEQRES 6 C 387 THR VAL LYS ASP ARG SER PRO TYR ARG THR LEU MET SER SEQRES 7 C 387 CYS PRO VAL GLY GLU ALA PRO SER PRO TYR ASN SER ARG SEQRES 8 C 387 PHE GLU SER VAL ALA TRP SER ALA SER ALA CYS HIS ASP SEQRES 9 C 387 GLY ILE SER TRP LEU THR ILE GLY ILE SER GLY PRO ASP SEQRES 10 C 387 ASN GLY ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE ILE SEQRES 11 C 387 THR ASP THR ILE LYS SER TRP ARG ASN ASN ILE LEU ARG SEQRES 12 C 387 THR GLN GLU SER GLU CYS ALA CYS VAL ASN GLY SER CYS SEQRES 13 C 387 PHE THR VAL MET THR ASP GLY PRO SER ASN GLY GLN ALA SEQRES 14 C 387 SER TYR LYS ILE PHE LYS ILE GLU LYS GLY LYS VAL VAL SEQRES 15 C 387 LYS SER VAL GLU MET ASN ALA PRO ASN TYR HIS TYR GLU SEQRES 16 C 387 GLU CYS SER CYS TYR PRO ASP ALA GLY ASP ILE MET CYS SEQRES 17 C 387 VAL CYS ARG ASP ASN TRP HIS GLY SER ASN ARG PRO TRP SEQRES 18 C 387 VAL SER PHE ASN GLN ASN LEU GLU TYR GLN ILE GLY TYR SEQRES 19 C 387 ILE CYS SER GLY ILE PHE GLY ASP ASN PRO ARG PRO ASN SEQRES 20 C 387 ASP GLY THR GLY SER CYS SER PRO MET PRO SER ASN GLY SEQRES 21 C 387 ALA TYR GLY VAL LYS GLY PHE SER PHE LYS TYR GLY ASN SEQRES 22 C 387 GLY VAL TRP ILE GLY ARG THR LYS SER THR SER SER ARG SEQRES 23 C 387 SER GLY PHE GLU MET ILE TRP ASP PRO ASN GLY TRP THR SEQRES 24 C 387 GLU THR ASP SER SER PHE SER VAL LYS GLN ASP ILE VAL SEQRES 25 C 387 GLU ILE THR ASP TRP SER GLY TYR SER GLY SER PHE VAL SEQRES 26 C 387 GLN HIS PRO GLU LEU THR GLY LEU ASP CYS MET ARG PRO SEQRES 27 C 387 CYS PHE TRP VAL GLU LEU ILE ARG GLY ARG PRO LYS GLU SEQRES 28 C 387 ASN THR ILE TRP THR SER GLY SER SER ILE SER PHE CYS SEQRES 29 C 387 GLY VAL ASN SER ASP THR VAL GLY TRP SER TRP PRO ASP SEQRES 30 C 387 GLY ALA GLU LEU PRO PHE THR ILE ASP LYS SEQRES 1 D 387 VAL THR LEU ALA GLY ASN SER SER LEU CYS PRO ILE SER SEQRES 2 D 387 GLY TRP ALA ILE TYR SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 D 387 GLY SER LYS GLY ASP VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 D 387 ILE SER CYS SER HIS LEU GLU CYS ARG THR PHE PHE LEU SEQRES 5 D 387 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN GLY SEQRES 6 D 387 THR VAL LYS ASP ARG SER PRO TYR ARG THR LEU MET SER SEQRES 7 D 387 CYS PRO VAL GLY GLU ALA PRO SER PRO TYR ASN SER ARG SEQRES 8 D 387 PHE GLU SER VAL ALA TRP SER ALA SER ALA CYS HIS ASP SEQRES 9 D 387 GLY ILE SER TRP LEU THR ILE GLY ILE SER GLY PRO ASP SEQRES 10 D 387 ASN GLY ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE ILE SEQRES 11 D 387 THR ASP THR ILE LYS SER TRP ARG ASN ASN ILE LEU ARG SEQRES 12 D 387 THR GLN GLU SER GLU CYS ALA CYS VAL ASN GLY SER CYS SEQRES 13 D 387 PHE THR VAL MET THR ASP GLY PRO SER ASN GLY GLN ALA SEQRES 14 D 387 SER TYR LYS ILE PHE LYS ILE GLU LYS GLY LYS VAL VAL SEQRES 15 D 387 LYS SER VAL GLU MET ASN ALA PRO ASN TYR HIS TYR GLU SEQRES 16 D 387 GLU CYS SER CYS TYR PRO ASP ALA GLY ASP ILE MET CYS SEQRES 17 D 387 VAL CYS ARG ASP ASN TRP HIS GLY SER ASN ARG PRO TRP SEQRES 18 D 387 VAL SER PHE ASN GLN ASN LEU GLU TYR GLN ILE GLY TYR SEQRES 19 D 387 ILE CYS SER GLY ILE PHE GLY ASP ASN PRO ARG PRO ASN SEQRES 20 D 387 ASP GLY THR GLY SER CYS SER PRO MET PRO SER ASN GLY SEQRES 21 D 387 ALA TYR GLY VAL LYS GLY PHE SER PHE LYS TYR GLY ASN SEQRES 22 D 387 GLY VAL TRP ILE GLY ARG THR LYS SER THR SER SER ARG SEQRES 23 D 387 SER GLY PHE GLU MET ILE TRP ASP PRO ASN GLY TRP THR SEQRES 24 D 387 GLU THR ASP SER SER PHE SER VAL LYS GLN ASP ILE VAL SEQRES 25 D 387 GLU ILE THR ASP TRP SER GLY TYR SER GLY SER PHE VAL SEQRES 26 D 387 GLN HIS PRO GLU LEU THR GLY LEU ASP CYS MET ARG PRO SEQRES 27 D 387 CYS PHE TRP VAL GLU LEU ILE ARG GLY ARG PRO LYS GLU SEQRES 28 D 387 ASN THR ILE TRP THR SER GLY SER SER ILE SER PHE CYS SEQRES 29 D 387 GLY VAL ASN SER ASP THR VAL GLY TRP SER TRP PRO ASP SEQRES 30 D 387 GLY ALA GLU LEU PRO PHE THR 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 NAG A 502 14 HET CA A 503 1 HET CA A 504 1 HET NAG B 501 14 HET NAG B 502 14 HET CA B 503 1 HET CA B 504 1 HET NAG C 501 14 HET NAG C 502 14 HET CA C 503 1 HET CA C 504 1 HET NAG D 501 14 HET NAG D 502 14 HET CA D 503 1 HET CA D 504 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 8(C8 H15 N O6) FORMUL 15 CA 8(CA 2+) HELIX 1 AA1 ASN A 104 GLY A 109 1 6 HELIX 2 AA2 ASP A 142 ASN A 146 5 5 HELIX 3 AA3 HIS A 409 GLY A 414 1 6 HELIX 4 AA4 ASN B 104 GLY B 109 1 6 HELIX 5 AA5 ASP B 142 ASN B 146 5 5 HELIX 6 AA6 HIS B 409 GLY B 414 1 6 HELIX 7 AA7 ASN C 104 GLY C 109 1 6 HELIX 8 AA8 ASP C 142 ASN C 146 5 5 HELIX 9 AA9 HIS C 409 GLY C 414 1 6 HELIX 10 AB1 ASN D 104 GLY D 109 1 6 HELIX 11 AB2 ASP D 142 ASN D 146 5 5 HELIX 12 AB3 HIS D 409 GLY D 414 1 6 HELIX 13 AB4 THR E 87 THR E 91 5 5 HELIX 14 AB5 GLU F 80 PHE F 84 5 5 HELIX 15 AB6 THR G 87 THR G 91 5 5 HELIX 16 AB7 GLU H 80 PHE H 84 5 5 HELIX 17 AB8 THR I 87 THR I 91 5 5 HELIX 18 AB9 GLU J 80 PHE J 84 5 5 HELIX 19 AC1 THR K 87 THR K 91 5 5 HELIX 20 AC2 GLU L 80 PHE L 84 5 5 SHEET 1 AA1 4 GLY A 96 LYS A 102 0 SHEET 2 AA1 4 THR A 438 VAL A 448 -1 O SER A 444 N TYR A 100 SHEET 3 AA1 4 ARG A 419 GLY A 429 -1 N VAL A 424 O ILE A 443 SHEET 4 AA1 4 SER A 403 GLN A 408 -1 N PHE A 406 O CYS A 421 SHEET 1 AA2 4 PHE A 115 CYS A 124 0 SHEET 2 AA2 4 CYS A 129 LEU A 139 -1 O PHE A 132 N PHE A 121 SHEET 3 AA2 4 THR A 157 PRO A 162 -1 O CYS A 161 N THR A 131 SHEET 4 AA2 4 ARG A 173 VAL A 177 -1 O SER A 176 N LEU A 158 SHEET 1 AA3 4 SER A 180 HIS A 185 0 SHEET 2 AA3 4 TRP A 190 SER A 196 -1 O ILE A 195 N SER A 180 SHEET 3 AA3 4 VAL A 203 TYR A 208 -1 O LYS A 207 N THR A 192 SHEET 4 AA3 4 ILE A 211 LYS A 217 -1 O ILE A 216 N ALA A 204 SHEET 1 AA4 3 LEU A 224 ARG A 225 0 SHEET 2 AA4 3 SER A 237 ASP A 244 -1 O THR A 243 N ARG A 225 SHEET 3 AA4 3 ALA A 232 VAL A 234 -1 N ALA A 232 O PHE A 239 SHEET 1 AA5 4 LEU A 224 ARG A 225 0 SHEET 2 AA5 4 SER A 237 ASP A 244 -1 O THR A 243 N ARG A 225 SHEET 3 AA5 4 SER A 252 GLU A 259 -1 O PHE A 256 N THR A 240 SHEET 4 AA5 4 LYS A 262 GLU A 268 -1 O LYS A 265 N LYS A 257 SHEET 1 AA6 4 GLU A 277 ASP A 284 0 SHEET 2 AA6 4 ASP A 287 ARG A 293 -1 O ASP A 287 N ASP A 284 SHEET 3 AA6 4 PRO A 302 PHE A 306 -1 O PHE A 306 N ILE A 288 SHEET 4 AA6 4 TYR A 312 TYR A 316 -1 O GLY A 315 N TRP A 303 SHEET 1 AA7 4 PHE A 349 TYR A 353 0 SHEET 2 AA7 4 GLY A 356 ARG A 361 -1 O GLY A 356 N TYR A 353 SHEET 3 AA7 4 SER A 369 ASP A 376 -1 O ILE A 374 N ILE A 359 SHEET 4 AA7 4 VAL A 389 TRP A 399 -1 O GLN A 391 N MET A 373 SHEET 1 AA8 4 GLY B 96 LYS B 102 0 SHEET 2 AA8 4 THR B 438 VAL B 448 -1 O SER B 444 N TYR B 100 SHEET 3 AA8 4 ARG B 419 GLY B 429 -1 N VAL B 424 O ILE B 443 SHEET 4 AA8 4 SER B 403 GLN B 408 -1 N PHE B 406 O CYS B 421 SHEET 1 AA9 4 PHE B 115 CYS B 124 0 SHEET 2 AA9 4 CYS B 129 LEU B 139 -1 O PHE B 132 N PHE B 121 SHEET 3 AA9 4 THR B 157 PRO B 162 -1 O CYS B 161 N THR B 131 SHEET 4 AA9 4 ARG B 173 VAL B 177 -1 O SER B 176 N LEU B 158 SHEET 1 AB1 4 SER B 180 HIS B 185 0 SHEET 2 AB1 4 TRP B 190 SER B 196 -1 O ILE B 195 N SER B 180 SHEET 3 AB1 4 VAL B 203 TYR B 208 -1 O LYS B 207 N THR B 192 SHEET 4 AB1 4 ILE B 211 LYS B 217 -1 O ILE B 216 N ALA B 204 SHEET 1 AB2 3 LEU B 224 ARG B 225 0 SHEET 2 AB2 3 SER B 237 ASP B 244 -1 O THR B 243 N ARG B 225 SHEET 3 AB2 3 ALA B 232 VAL B 234 -1 N ALA B 232 O PHE B 239 SHEET 1 AB3 4 LEU B 224 ARG B 225 0 SHEET 2 AB3 4 SER B 237 ASP B 244 -1 O THR B 243 N ARG B 225 SHEET 3 AB3 4 SER B 252 GLU B 259 -1 O PHE B 256 N THR B 240 SHEET 4 AB3 4 LYS B 262 GLU B 268 -1 O LYS B 265 N LYS B 257 SHEET 1 AB4 4 GLU B 277 ASP B 284 0 SHEET 2 AB4 4 ASP B 287 ARG B 293 -1 O ASP B 287 N ASP B 284 SHEET 3 AB4 4 PRO B 302 PHE B 306 -1 O PHE B 306 N ILE B 288 SHEET 4 AB4 4 TYR B 312 TYR B 316 -1 O GLY B 315 N TRP B 303 SHEET 1 AB5 4 PHE B 349 TYR B 353 0 SHEET 2 AB5 4 GLY B 356 ARG B 361 -1 O GLY B 356 N TYR B 353 SHEET 3 AB5 4 SER B 369 ASP B 376 -1 O ILE B 374 N ILE B 359 SHEET 4 AB5 4 VAL B 389 TRP B 399 -1 O GLN B 391 N MET B 373 SHEET 1 AB6 4 GLY C 96 LYS C 102 0 SHEET 2 AB6 4 THR C 438 VAL C 448 -1 O SER C 444 N TYR C 100 SHEET 3 AB6 4 ARG C 419 GLY C 429 -1 N VAL C 424 O ILE C 443 SHEET 4 AB6 4 SER C 403 GLN C 408 -1 N PHE C 406 O CYS C 421 SHEET 1 AB7 4 PHE C 115 CYS C 124 0 SHEET 2 AB7 4 CYS C 129 LEU C 139 -1 O PHE C 132 N PHE C 121 SHEET 3 AB7 4 THR C 157 PRO C 162 -1 O CYS C 161 N THR C 131 SHEET 4 AB7 4 ARG C 173 VAL C 177 -1 O SER C 176 N LEU C 158 SHEET 1 AB8 4 SER C 180 HIS C 185 0 SHEET 2 AB8 4 TRP C 190 SER C 196 -1 O ILE C 195 N SER C 180 SHEET 3 AB8 4 VAL C 203 TYR C 208 -1 O LYS C 207 N THR C 192 SHEET 4 AB8 4 ILE C 211 LYS C 217 -1 O ILE C 216 N ALA C 204 SHEET 1 AB9 3 LEU C 224 ARG C 225 0 SHEET 2 AB9 3 SER C 237 ASP C 244 -1 O THR C 243 N ARG C 225 SHEET 3 AB9 3 ALA C 232 VAL C 234 -1 N ALA C 232 O PHE C 239 SHEET 1 AC1 4 LEU C 224 ARG C 225 0 SHEET 2 AC1 4 SER C 237 ASP C 244 -1 O THR C 243 N ARG C 225 SHEET 3 AC1 4 SER C 252 GLU C 259 -1 O PHE C 256 N THR C 240 SHEET 4 AC1 4 LYS C 262 GLU C 268 -1 O LYS C 265 N LYS C 257 SHEET 1 AC2 4 GLU C 277 ASP C 284 0 SHEET 2 AC2 4 ASP C 287 ARG C 293 -1 O ASP C 287 N ASP C 284 SHEET 3 AC2 4 PRO C 302 PHE C 306 -1 O PHE C 306 N ILE C 288 SHEET 4 AC2 4 TYR C 312 TYR C 316 -1 O GLY C 315 N TRP C 303 SHEET 1 AC3 4 PHE C 349 TYR C 353 0 SHEET 2 AC3 4 GLY C 356 ARG C 361 -1 O GLY C 356 N TYR C 353 SHEET 3 AC3 4 SER C 369 ASP C 376 -1 O ILE C 374 N ILE C 359 SHEET 4 AC3 4 VAL C 389 TRP C 399 -1 O GLN C 391 N MET C 373 SHEET 1 AC4 4 GLY D 96 LYS D 102 0 SHEET 2 AC4 4 THR D 438 VAL D 448 -1 O SER D 444 N TYR D 100 SHEET 3 AC4 4 ARG D 419 GLY D 429 -1 N VAL D 424 O ILE D 443 SHEET 4 AC4 4 SER D 403 GLN D 408 -1 N PHE D 406 O CYS D 421 SHEET 1 AC5 4 PHE D 115 CYS D 124 0 SHEET 2 AC5 4 CYS D 129 LEU D 139 -1 O PHE D 132 N PHE D 121 SHEET 3 AC5 4 THR D 157 PRO D 162 -1 O CYS D 161 N THR D 131 SHEET 4 AC5 4 ARG D 173 VAL D 177 -1 O SER D 176 N LEU D 158 SHEET 1 AC6 4 SER D 180 HIS D 185 0 SHEET 2 AC6 4 TRP D 190 SER D 196 -1 O ILE D 195 N SER D 180 SHEET 3 AC6 4 VAL D 203 TYR D 208 -1 O LYS D 207 N THR D 192 SHEET 4 AC6 4 ILE D 211 LYS D 217 -1 O ILE D 216 N ALA D 204 SHEET 1 AC7 3 LEU D 224 ARG D 225 0 SHEET 2 AC7 3 SER D 237 ASP D 244 -1 O THR D 243 N ARG D 225 SHEET 3 AC7 3 ALA D 232 VAL D 234 -1 N ALA D 232 O PHE D 239 SHEET 1 AC8 4 LEU D 224 ARG D 225 0 SHEET 2 AC8 4 SER D 237 ASP D 244 -1 O THR D 243 N ARG D 225 SHEET 3 AC8 4 SER D 252 GLU D 259 -1 O PHE D 256 N THR D 240 SHEET 4 AC8 4 LYS D 262 GLU D 268 -1 O LYS D 265 N LYS D 257 SHEET 1 AC9 4 GLU D 277 ASP D 284 0 SHEET 2 AC9 4 ASP D 287 ARG D 293 -1 O ASP D 287 N ASP D 284 SHEET 3 AC9 4 PRO D 302 PHE D 306 -1 O PHE D 306 N ILE D 288 SHEET 4 AC9 4 TYR D 312 TYR D 316 -1 O GLY D 315 N TRP D 303 SHEET 1 AD1 4 PHE D 349 TYR D 353 0 SHEET 2 AD1 4 GLY D 356 ARG D 361 -1 O GLY D 356 N TYR D 353 SHEET 3 AD1 4 SER D 369 ASP D 376 -1 O ILE D 374 N ILE D 359 SHEET 4 AD1 4 VAL D 389 TRP D 399 -1 O GLN D 391 N MET D 373 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 LEU E 79 N CYS E 22 SHEET 4 AD2 4 PHE E 68 ASP E 73 -1 N SER E 71 O TYR E 80 SHEET 1 AD3 6 LEU E 11 VAL E 12 0 SHEET 2 AD3 6 THR E 117 VAL E 121 1 O THR E 120 N VAL E 12 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 VAL E 57 TYR E 60 -1 O TYR E 59 N HIS E 50 SHEET 1 AD4 2 PHE E 101 ASP E 102 0 SHEET 2 AD4 2 GLY E 106 TYR E 107 -1 O GLY E 106 N ASP E 102 SHEET 1 AD5 4 LEU F 4 THR F 5 0 SHEET 2 AD5 4 ALA F 19 ALA F 25 -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 66 O THR F 73 SHEET 1 AD6 2 THR F 10 LEU F 13 0 SHEET 2 AD6 2 LYS F 103 ILE F 106 1 O LYS F 103 N LEU F 11 SHEET 1 AD7 5 THR F 54 ARG F 55 0 SHEET 2 AD7 5 ARG F 46 ASP F 50 -1 N ASP F 50 O THR F 54 SHEET 3 AD7 5 ALA F 35 HIS F 39 -1 N GLN F 38 O ARG F 46 SHEET 4 AD7 5 VAL F 86 HIS F 91 -1 O VAL F 86 N HIS F 39 SHEET 5 AD7 5 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 LEU G 79 N CYS G 22 SHEET 4 AD8 4 PHE G 68 ASP G 73 -1 N SER G 71 O TYR G 80 SHEET 1 AD9 6 LEU G 11 VAL G 12 0 SHEET 2 AD9 6 THR G 117 VAL G 121 1 O THR G 120 N VAL G 12 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 GLU G 46 N ARG G 38 SHEET 6 AD9 6 VAL G 57 TYR G 60 -1 O TYR G 59 N HIS G 50 SHEET 1 AE1 2 PHE G 101 ASP G 102 0 SHEET 2 AE1 2 GLY G 106 TYR G 107 -1 O GLY G 106 N ASP G 102 SHEET 1 AE2 4 LEU H 4 GLN H 6 0 SHEET 2 AE2 4 ALA H 19 ALA H 25 -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 66 O THR H 73 SHEET 1 AE3 2 THR H 10 LEU H 13 0 SHEET 2 AE3 2 LYS H 103 ILE H 106 1 O LYS H 103 N LEU H 11 SHEET 1 AE4 5 THR H 54 ARG H 55 0 SHEET 2 AE4 5 ARG H 46 ASP H 50 -1 N ASP H 50 O THR H 54 SHEET 3 AE4 5 LEU H 34 HIS H 39 -1 N GLN H 38 O ARG H 46 SHEET 4 AE4 5 VAL H 86 HIS H 91 -1 O VAL H 86 N HIS H 39 SHEET 5 AE4 5 THR H 97 PHE H 98 -1 O THR H 97 N HIS H 91 SHEET 1 AE5 4 GLN I 3 VAL I 5 0 SHEET 2 AE5 4 SER I 17 SER I 25 -1 O ALA I 23 N VAL I 5 SHEET 3 AE5 4 SER I 78 ASP I 84 -1 O LEU I 79 N CYS I 22 SHEET 4 AE5 4 PHE I 68 ASP I 73 -1 N SER I 71 O TYR I 80 SHEET 1 AE6 6 LEU I 11 VAL I 12 0 SHEET 2 AE6 6 THR I 117 VAL I 121 1 O THR I 120 N VAL I 12 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 VAL I 57 TYR I 60 -1 O TYR I 59 N HIS I 50 SHEET 1 AE7 2 PHE I 101 ASP I 102 0 SHEET 2 AE7 2 GLY I 106 TYR I 107 -1 O GLY I 106 N ASP I 102 SHEET 1 AE8 4 LEU J 4 GLN J 6 0 SHEET 2 AE8 4 ALA J 19 ALA J 25 -1 O ARG J 24 N THR J 5 SHEET 3 AE8 4 ASP J 71 VAL J 76 -1 O VAL J 76 N ALA J 19 SHEET 4 AE8 4 PHE J 63 SER J 68 -1 N SER J 64 O THR J 75 SHEET 1 AE9 2 THR J 10 LEU J 13 0 SHEET 2 AE9 2 LYS J 103 ILE J 106 1 O LYS J 103 N LEU J 11 SHEET 1 AF1 5 THR J 54 ARG J 55 0 SHEET 2 AF1 5 ARG J 46 ASP J 50 -1 N ASP J 50 O THR J 54 SHEET 3 AF1 5 LEU J 34 HIS J 39 -1 N GLN J 38 O ARG J 46 SHEET 4 AF1 5 VAL J 86 HIS J 91 -1 O GLN J 90 N ALA J 35 SHEET 5 AF1 5 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 SER K 25 N GLN K 3 SHEET 3 AF2 4 SER K 78 ASP K 84 -1 O LEU K 79 N CYS K 22 SHEET 4 AF2 4 PHE K 68 ASP K 73 -1 N SER K 71 O TYR K 80 SHEET 1 AF3 6 LEU K 11 VAL K 12 0 SHEET 2 AF3 6 THR K 117 VAL K 121 1 O THR K 120 N VAL K 12 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 GLU K 46 N ARG K 38 SHEET 6 AF3 6 VAL K 57 TYR K 60 -1 O TYR K 59 N HIS K 50 SHEET 1 AF4 2 PHE K 101 ASP K 102 0 SHEET 2 AF4 2 GLY K 106 TYR K 107 -1 O GLY K 106 N ASP K 102 SHEET 1 AF5 4 LEU L 4 GLN L 6 0 SHEET 2 AF5 4 ALA L 19 ALA L 25 -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 ALA L 65 SER L 68 -1 N SER L 66 O THR L 73 SHEET 1 AF6 2 THR L 10 LEU L 13 0 SHEET 2 AF6 2 LYS L 103 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 1 AF7 5 THR L 54 ARG L 55 0 SHEET 2 AF7 5 ARG L 46 ASP L 50 -1 N ASP L 50 O THR L 54 SHEET 3 AF7 5 LEU L 34 HIS L 39 -1 N GLN L 38 O ARG L 46 SHEET 4 AF7 5 VAL L 86 HIS L 91 -1 O VAL L 86 N HIS L 39 SHEET 5 AF7 5 THR L 97 PHE L 98 -1 O THR L 97 N HIS L 91 SSBOND 1 CYS A 92 CYS A 417 1555 1555 2.08 SSBOND 2 CYS A 124 CYS A 129 1555 1555 2.03 SSBOND 3 CYS A 184 CYS A 231 1555 1555 2.03 SSBOND 4 CYS A 233 CYS A 238 1555 1555 2.02 SSBOND 5 CYS A 279 CYS A 292 1555 1555 2.03 SSBOND 6 CYS A 281 CYS A 290 1555 1555 2.03 SSBOND 7 CYS A 318 CYS A 335 1555 1555 2.08 SSBOND 8 CYS A 421 CYS A 446 1555 1555 2.04 SSBOND 9 CYS B 92 CYS B 417 1555 1555 2.05 SSBOND 10 CYS B 124 CYS B 129 1555 1555 2.03 SSBOND 11 CYS B 184 CYS B 231 1555 1555 2.03 SSBOND 12 CYS B 233 CYS B 238 1555 1555 2.02 SSBOND 13 CYS B 279 CYS B 292 1555 1555 2.03 SSBOND 14 CYS B 281 CYS B 290 1555 1555 2.03 SSBOND 15 CYS B 318 CYS B 335 1555 1555 2.06 SSBOND 16 CYS B 421 CYS B 446 1555 1555 2.04 SSBOND 17 CYS C 92 CYS C 417 1555 1555 2.02 SSBOND 18 CYS C 124 CYS C 129 1555 1555 2.03 SSBOND 19 CYS C 184 CYS C 231 1555 1555 2.03 SSBOND 20 CYS C 233 CYS C 238 1555 1555 2.02 SSBOND 21 CYS C 279 CYS C 292 1555 1555 2.03 SSBOND 22 CYS C 281 CYS C 290 1555 1555 2.03 SSBOND 23 CYS C 318 CYS C 335 1555 1555 2.05 SSBOND 24 CYS C 421 CYS C 446 1555 1555 2.04 SSBOND 25 CYS D 92 CYS D 417 1555 1555 2.02 SSBOND 26 CYS D 124 CYS D 129 1555 1555 2.03 SSBOND 27 CYS D 184 CYS D 231 1555 1555 2.03 SSBOND 28 CYS D 233 CYS D 238 1555 1555 2.02 SSBOND 29 CYS D 279 CYS D 292 1555 1555 2.03 SSBOND 30 CYS D 281 CYS D 290 1555 1555 2.03 SSBOND 31 CYS D 318 CYS D 335 1555 1555 2.02 SSBOND 32 CYS D 421 CYS D 446 1555 1555 2.04 SSBOND 33 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 34 CYS F 23 CYS F 89 1555 1555 2.08 SSBOND 35 CYS G 22 CYS G 96 1555 1555 2.03 SSBOND 36 CYS H 23 CYS H 89 1555 1555 2.02 SSBOND 37 CYS I 22 CYS I 96 1555 1555 2.03 SSBOND 38 CYS J 23 CYS J 89 1555 1555 2.01 SSBOND 39 CYS K 22 CYS K 96 1555 1555 2.03 SSBOND 40 CYS L 23 CYS L 89 1555 1555 2.05 LINK ND2 ASN A 146 C1 NAG A 501 1555 1555 1.43 LINK ND2 ASN A 235 C1 NAG A 502 1555 1555 1.44 LINK ND2 ASN B 146 C1 NAG B 501 1555 1555 1.42 LINK ND2 ASN B 235 C1 NAG B 502 1555 1555 1.43 LINK ND2 ASN C 146 C1 NAG C 501 1555 1555 1.41 LINK ND2 ASN C 235 C1 NAG C 502 1555 1555 1.43 LINK ND2 ASN D 146 C1 NAG D 501 1555 1555 1.43 LINK ND2 ASN D 235 C1 NAG D 502 1555 1555 1.44 LINK O ASP A 294 CA CA A 503 1555 1555 2.32 LINK O GLY A 298 CA CA A 503 1555 1555 2.71 LINK OD2 ASP A 324 CA CA A 503 1555 1555 3.04 LINK O GLY A 342 CA CA A 503 1555 1555 2.42 LINK OD1 ASP A 376 CA CA A 504 1555 1555 2.05 LINK OD2 ASP A 376 CA CA A 504 1555 1555 2.77 LINK OD1 ASN A 378 CA CA A 504 1555 1555 2.23 LINK OD1 ASP A 384 CA CA A 504 1555 1555 2.22 LINK O SER A 386 CA CA A 504 1555 1555 2.66 LINK O ASP B 294 CA CA B 503 1555 1555 2.50 LINK O GLY B 298 CA CA B 503 1555 1555 2.28 LINK OD2 ASP B 324 CA CA B 503 1555 1555 3.08 LINK O GLY B 342 CA CA B 503 1555 1555 2.31 LINK O TYR B 344 CA CA B 503 1555 1555 1.86 LINK OD1 ASP B 376 CA CA B 504 1555 1555 2.21 LINK OD2 ASP B 376 CA CA B 504 1555 1555 2.71 LINK OD1 ASN B 378 CA CA B 504 1555 1555 2.52 LINK O SER B 386 CA CA B 504 1555 1555 2.58 LINK O ASP C 294 CA CA C 503 1555 1555 2.57 LINK O GLY C 298 CA CA C 503 1555 1555 2.17 LINK O GLY C 342 CA CA C 503 1555 1555 2.12 LINK O TYR C 344 CA CA C 503 1555 1555 1.97 LINK OD1 ASP C 376 CA CA C 504 1555 1555 2.16 LINK OD2 ASP C 376 CA CA C 504 1555 1555 3.11 LINK OD1 ASN C 378 CA CA C 504 1555 1555 2.07 LINK O SER C 386 CA CA C 504 1555 1555 2.60 LINK O ASP D 294 CA CA D 503 1555 1555 2.34 LINK O GLY D 298 CA CA D 503 1555 1555 2.43 LINK OD2 ASP D 324 CA CA D 503 1555 1555 3.15 LINK O GLY D 342 CA CA D 503 1555 1555 2.32 LINK OD1 ASP D 376 CA CA D 504 1555 1555 1.98 LINK OD2 ASP D 376 CA CA D 504 1555 1555 2.76 LINK OD1 ASN D 378 CA CA D 504 1555 1555 2.10 LINK O SER D 386 CA CA D 504 1555 1555 2.77 CISPEP 1 ASN A 325 PRO A 326 0 7.51 CISPEP 2 LEU A 463 PRO A 464 0 1.36 CISPEP 3 ASN B 325 PRO B 326 0 7.54 CISPEP 4 ARG B 430 PRO B 431 0 3.08 CISPEP 5 LEU B 463 PRO B 464 0 1.28 CISPEP 6 ASN C 325 PRO C 326 0 7.44 CISPEP 7 LEU C 463 PRO C 464 0 1.27 CISPEP 8 ASN D 325 PRO D 326 0 7.45 CISPEP 9 LEU D 463 PRO D 464 0 1.30 CISPEP 10 ASN F 94 PRO F 95 0 -2.05 CISPEP 11 ASN H 94 PRO H 95 0 -2.04 CISPEP 12 ASN J 94 PRO J 95 0 -2.03 CISPEP 13 ASN L 94 PRO L 95 0 -2.02 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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