HEADER VIRAL PROTEIN/IMMUNE SYSTEM 26-SEP-24 9DS2 TITLE CRYSTAL STRUCTURE OF 346-54 FAB IN COMPLEX WITH H1 HA FROM TITLE 2 A/CALIFORNIA/04/2009(H1N1) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ HA1 CHAI; COMPND 3 CHAIN: C, A, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMAGGLUTININ HA2 CHAIN; COMPND 7 CHAIN: D, B, F; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 346-54, HEAVY CHAIN; COMPND 11 CHAIN: G, H, K; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: 346-54, LIGHT CHAIN; COMPND 15 CHAIN: I, J, L; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 GENE: HA; SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 9 ORGANISM_TAXID: 11320; SOURCE 10 GENE: HA; SOURCE 11 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS H1N1, ANTIBODY, HEMAGGLUTININ, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.H.LIN,I.A.WILSON REVDAT 1 19-MAR-25 9DS2 0 JRNL AUTH T.H.LIN,C.D.LEE,M.L.FERNANDEZ-QUINTERO,J.A.FERGUSON,J.HAN, JRNL AUTH 2 X.ZHU,W.YU,J.J.GUTHMILLER,F.KRAMMER,P.C.WILSON,A.B.WARD, JRNL AUTH 3 I.A.WILSON JRNL TITL STRUCTURALLY CONVERGENT ANTIBODIES DERIVED FROM DIFFERENT JRNL TITL 2 VACCINE STRATEGIES TARGET THE INFLUENZA VIRUS HA ANCHOR JRNL TITL 3 EPITOPE WITH A SUBSET OF V H 3 AND V K 3 GENES. JRNL REF NAT COMMUN V. 16 1268 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 39894881 JRNL DOI 10.1038/S41467-025-56496-4 REMARK 2 REMARK 2 RESOLUTION. 3.29 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21RC1_5127: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.29 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.82 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 3 NUMBER OF REFLECTIONS : 117639 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.246 REMARK 3 R VALUE (WORKING SET) : 0.244 REMARK 3 FREE R VALUE : 0.279 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960 REMARK 3 FREE R VALUE TEST SET COUNT : 5832 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 47.8200 - 10.1800 0.98 4150 219 0.2139 0.2481 REMARK 3 2 10.1800 - 8.0900 0.97 3917 224 0.2002 0.2206 REMARK 3 3 8.0900 - 7.0700 0.99 3991 215 0.2243 0.2710 REMARK 3 4 7.0700 - 6.4300 0.99 3980 227 0.2476 0.3055 REMARK 3 5 6.4300 - 5.9700 0.99 3922 225 0.2434 0.3124 REMARK 3 6 5.9700 - 5.6200 0.99 3987 179 0.2344 0.2851 REMARK 3 7 5.6200 - 5.3400 0.99 3932 202 0.2191 0.2714 REMARK 3 8 5.3400 - 5.1000 0.99 3939 194 0.2171 0.2517 REMARK 3 9 5.1000 - 4.9100 0.94 3748 201 0.2245 0.2391 REMARK 3 10 4.9100 - 4.7400 0.99 3931 201 0.2128 0.2601 REMARK 3 11 4.7400 - 4.5900 0.98 3904 205 0.2087 0.2275 REMARK 3 12 4.5900 - 4.4600 0.99 3905 198 0.2077 0.2363 REMARK 3 13 4.4600 - 4.3400 0.99 3952 188 0.2092 0.2412 REMARK 3 14 4.3400 - 4.2400 0.98 3890 198 0.2274 0.2593 REMARK 3 15 4.2400 - 4.1400 0.98 3856 180 0.2495 0.2872 REMARK 3 16 4.1400 - 4.0500 0.98 3904 205 0.2523 0.2782 REMARK 3 17 4.0500 - 3.9700 0.98 3899 193 0.2516 0.2879 REMARK 3 18 3.9700 - 3.9000 0.97 3832 213 0.2566 0.2813 REMARK 3 19 3.9000 - 3.8300 0.97 3850 174 0.2697 0.3101 REMARK 3 20 3.8300 - 3.7600 0.97 3818 179 0.2803 0.3392 REMARK 3 21 3.7600 - 3.7000 0.97 3833 182 0.3033 0.3677 REMARK 3 22 3.7000 - 3.6400 0.95 3740 215 0.3100 0.3113 REMARK 3 23 3.6400 - 3.5900 0.95 3716 195 0.3198 0.3318 REMARK 3 24 3.5900 - 3.5400 0.93 3715 181 0.3393 0.3379 REMARK 3 25 3.5400 - 3.4900 0.90 3526 199 0.3393 0.3702 REMARK 3 26 3.4900 - 3.4500 0.86 3349 192 0.3472 0.3555 REMARK 3 27 3.4500 - 3.4000 0.81 3194 185 0.3495 0.3724 REMARK 3 28 3.4000 - 3.3600 0.77 2987 178 0.3471 0.4156 REMARK 3 29 3.3600 - 3.3200 0.74 2918 148 0.3604 0.3566 REMARK 3 30 3.3200 - 3.2900 0.65 2522 137 0.3954 0.4063 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.500 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.320 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 22507 REMARK 3 ANGLE : 0.486 30561 REMARK 3 CHIRALITY : 0.042 3381 REMARK 3 PLANARITY : 0.004 3941 REMARK 3 DIHEDRAL : 13.132 8066 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9DS2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000288700. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-SEP-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0337 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118176 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.290 REMARK 200 RESOLUTION RANGE LOW (A) : 47.820 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0 REMARK 200 DATA REDUNDANCY : 9.000 REMARK 200 R MERGE (I) : 0.25000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.36 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.78000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 81.36 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, PH 6.2, 20% REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X,-Y+1/2,Z REMARK 290 7555 -X+1/2,Y,-Z REMARK 290 8555 X,-Y,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 80.90800 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 162.76100 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 156.55050 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 162.76100 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 80.90800 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 156.55050 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 80.90800 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 156.55050 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 162.76100 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 156.55050 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 80.90800 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 162.76100 REMARK 290 REMARK 290 REMARK: NULL 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 33850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 61460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -139.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, A, B, E, F, M, N 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 ILE E 326 REMARK 465 GLN E 327 REMARK 465 SER G 228 REMARK 465 GLY G 229 REMARK 465 CYS I 215 REMARK 465 SER H 228 REMARK 465 GLY H 229 REMARK 465 CYS J 215 REMARK 465 SER K 228 REMARK 465 GLY K 229 REMARK 465 CYS L 215 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 SER G 199 OG REMARK 470 LEU G 200 CG CD1 CD2 REMARK 470 THR G 202 OG1 CG2 REMARK 470 GLN G 203 CG CD OE1 NE2 REMARK 470 ARG G 221 CD NE CZ NH1 NH2 REMARK 470 GLU G 223 CG CD OE1 OE2 REMARK 470 PRO G 224 CG CD REMARK 470 LYS G 225 CG CD CE NZ REMARK 470 SER G 226 OG REMARK 470 ASP I 123 CG OD1 OD2 REMARK 470 SER H 199 OG REMARK 470 LEU H 200 CG CD1 CD2 REMARK 470 THR H 202 OG1 CG2 REMARK 470 GLN H 203 CG CD OE1 NE2 REMARK 470 ARG H 221 CD NE CZ NH1 NH2 REMARK 470 GLU H 223 CG CD OE1 OE2 REMARK 470 PRO H 224 CG CD REMARK 470 LYS H 225 CG CD CE NZ REMARK 470 SER H 226 OG REMARK 470 ASP J 123 CG OD1 OD2 REMARK 470 SER K 199 OG REMARK 470 LEU K 200 CG CD1 CD2 REMARK 470 THR K 202 OG1 CG2 REMARK 470 GLN K 203 CG CD OE1 NE2 REMARK 470 ARG K 221 CD NE CZ NH1 NH2 REMARK 470 GLU K 223 CG CD OE1 OE2 REMARK 470 PRO K 224 CG CD REMARK 470 LYS K 225 CG CD CE NZ REMARK 470 SER K 226 OG REMARK 470 ASP L 123 CG OD1 OD2 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 OG SER K 141 O ILE L 118 2.12 REMARK 500 OG SER C 116 OD1 ASN C 263 2.15 REMARK 500 OG SER H 52 O ASP H 54 2.15 REMARK 500 OG1 THR C 283 O GLY C 286 2.19 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 GLU C 77 -155.36 -77.13 REMARK 500 THR C 81 -107.34 54.00 REMARK 500 ALA C 82 144.51 74.35 REMARK 500 GLN C 196 -69.09 62.91 REMARK 500 THR C 279 160.35 55.76 REMARK 500 LYS C 313 116.50 -161.02 REMARK 500 ALA D 7 18.55 58.77 REMARK 500 SER D 124 44.80 -89.60 REMARK 500 LYS D 127 -123.66 60.99 REMARK 500 GLU A 77 -1.60 66.30 REMARK 500 THR A 81 -118.86 40.67 REMARK 500 SER A 132 49.69 -93.52 REMARK 500 ASN A 133 -36.53 -132.19 REMARK 500 GLN A 196 -4.74 69.09 REMARK 500 THR A 279 154.78 54.01 REMARK 500 ALA B 7 14.55 58.90 REMARK 500 LYS B 127 -128.14 59.54 REMARK 500 ASN E 33 -81.87 68.15 REMARK 500 VAL E 34 82.96 45.73 REMARK 500 GLU E 77 -108.88 33.46 REMARK 500 SER E 80 -131.73 57.64 REMARK 500 GLN E 196 -69.95 63.09 REMARK 500 LYS F 127 -131.42 61.50 REMARK 500 ASP F 145 -169.09 -78.81 REMARK 500 THR F 156 30.79 -143.55 REMARK 500 PHE G 29 -7.88 70.94 REMARK 500 GLN G 39 -86.88 -86.91 REMARK 500 ALA G 40 172.73 167.51 REMARK 500 VAL G 48 -61.46 -121.75 REMARK 500 ASP G 155 63.91 60.17 REMARK 500 SER I 30 -123.29 57.47 REMARK 500 ALA I 51 -12.21 63.43 REMARK 500 LYS I 127 49.32 -86.41 REMARK 500 PHE H 29 -9.50 72.28 REMARK 500 VAL H 48 -61.44 -105.61 REMARK 500 ARG H 72 -50.17 -126.86 REMARK 500 ASP H 73 120.80 -35.71 REMARK 500 ALA H 125 -166.82 -166.04 REMARK 500 SER H 126 -167.63 -167.97 REMARK 500 GLU H 159 149.26 66.53 REMARK 500 SER H 199 51.83 -91.43 REMARK 500 PRO J 15 84.16 -70.00 REMARK 500 SER J 30 -133.08 57.83 REMARK 500 ALA J 51 -7.82 72.62 REMARK 500 SER J 52 -24.28 -140.67 REMARK 500 SER J 77 58.88 -94.02 REMARK 500 ARG J 91 14.95 -140.84 REMARK 500 LYS J 170 -61.65 -93.77 REMARK 500 LYS K 16 -169.80 -126.34 REMARK 500 PHE K 29 -8.95 72.30 REMARK 500 REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF1 9DS2 C 11 327 UNP A0A5B9ZSV0_9INFA DBREF2 9DS2 C A0A5B9ZSV0 18 342 DBREF1 9DS2 D 1 174 UNP A0A6J3XB93_9INFA DBREF2 9DS2 D A0A6J3XB93 345 518 DBREF1 9DS2 A 11 327 UNP A0A5B9ZSV0_9INFA DBREF2 9DS2 A A0A5B9ZSV0 18 342 DBREF1 9DS2 B 1 174 UNP A0A6J3XB93_9INFA DBREF2 9DS2 B A0A6J3XB93 345 518 DBREF1 9DS2 E 11 327 UNP A0A5B9ZSV0_9INFA DBREF2 9DS2 E A0A5B9ZSV0 18 342 DBREF1 9DS2 F 1 174 UNP A0A6J3XB93_9INFA DBREF2 9DS2 F A0A6J3XB93 345 518 DBREF 9DS2 G 1 229 PDB 9DS2 9DS2 1 229 DBREF 9DS2 I 1 215 PDB 9DS2 9DS2 1 215 DBREF 9DS2 H 1 229 PDB 9DS2 9DS2 1 229 DBREF 9DS2 J 1 215 PDB 9DS2 9DS2 1 215 DBREF 9DS2 K 1 229 PDB 9DS2 9DS2 1 229 DBREF 9DS2 L 1 215 PDB 9DS2 9DS2 1 215 SEQADV 9DS2 ASP C 8 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS2 PRO C 9 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS2 GLY C 10 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS2 SER C 186 UNP A0A5B9ZSV UNK 200 CONFLICT SEQADV 9DS2 GLY C 206 UNP A0A5B9ZSV SER 220 CONFLICT SEQADV 9DS2 SER D 175 UNP A0A6J3XB9 EXPRESSION TAG SEQADV 9DS2 ASP A 8 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS2 PRO A 9 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS2 GLY A 10 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS2 SER A 186 UNP A0A5B9ZSV UNK 200 CONFLICT SEQADV 9DS2 GLY A 206 UNP A0A5B9ZSV SER 220 CONFLICT SEQADV 9DS2 SER B 175 UNP A0A6J3XB9 EXPRESSION TAG SEQADV 9DS2 ASP E 8 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS2 PRO E 9 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS2 GLY E 10 UNP A0A5B9ZSV EXPRESSION TAG SEQADV 9DS2 SER E 186 UNP A0A5B9ZSV UNK 200 CONFLICT SEQADV 9DS2 GLY E 206 UNP A0A5B9ZSV SER 220 CONFLICT SEQADV 9DS2 SER F 175 UNP A0A6J3XB9 EXPRESSION TAG SEQRES 1 C 328 ASP PRO GLY ASP THR LEU CYS ILE GLY TYR HIS ALA ASN SEQRES 2 C 328 ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN SEQRES 3 C 328 VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP LYS SEQRES 4 C 328 HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA PRO SEQRES 5 C 328 LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE LEU SEQRES 6 C 328 GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SER SEQRES 7 C 328 TRP SER TYR ILE VAL GLU THR PRO SER SER ASP ASN GLY SEQRES 8 C 328 THR CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU LEU SEQRES 9 C 328 ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG PHE SEQRES 10 C 328 GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS ASP SEQRES 11 C 328 SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA GLY SEQRES 12 C 328 ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL LYS SEQRES 13 C 328 LYS GLY ASN SER TYR PRO LYS LEU SER LYS SER TYR ILE SEQRES 14 C 328 ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE SEQRES 15 C 328 HIS HIS PRO SER THR SER ALA ASP GLN GLN SER LEU TYR SEQRES 16 C 328 GLN ASN ALA ASP THR TYR VAL PHE VAL GLY GLY SER ARG SEQRES 17 C 328 TYR SER LYS LYS PHE LYS PRO GLU ILE ALA ILE ARG PRO SEQRES 18 C 328 LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR TRP SEQRES 19 C 328 THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU ALA SEQRES 20 C 328 THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE ALA MET SEQRES 21 C 328 GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP THR SEQRES 22 C 328 PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO LYS SEQRES 23 C 328 GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE HIS SEQRES 24 C 328 PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SER SEQRES 25 C 328 THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN ILE PRO SEQRES 26 C 328 SER ILE GLN SEQRES 1 D 175 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 D 175 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 D 175 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 D 175 SER THR GLN ASN ALA ILE ASP GLY ILE THR ASN LYS VAL SEQRES 5 D 175 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 D 175 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 D 175 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 D 175 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 D 175 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 D 175 LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN ASN ALA SEQRES 11 D 175 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 D 175 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 D 175 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 D 175 ARG GLU GLU ILE ASP SER SEQRES 1 A 328 ASP PRO GLY ASP THR LEU CYS ILE GLY TYR HIS ALA ASN SEQRES 2 A 328 ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN SEQRES 3 A 328 VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP LYS SEQRES 4 A 328 HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA PRO SEQRES 5 A 328 LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE LEU SEQRES 6 A 328 GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SER SEQRES 7 A 328 TRP SER TYR ILE VAL GLU THR PRO SER SER ASP ASN GLY SEQRES 8 A 328 THR CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU LEU SEQRES 9 A 328 ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG PHE SEQRES 10 A 328 GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS ASP SEQRES 11 A 328 SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA GLY SEQRES 12 A 328 ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL LYS SEQRES 13 A 328 LYS GLY ASN SER TYR PRO LYS LEU SER LYS SER TYR ILE SEQRES 14 A 328 ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE SEQRES 15 A 328 HIS HIS PRO SER THR SER ALA ASP GLN GLN SER LEU TYR SEQRES 16 A 328 GLN ASN ALA ASP THR TYR VAL PHE VAL GLY GLY SER ARG SEQRES 17 A 328 TYR SER LYS LYS PHE LYS PRO GLU ILE ALA ILE ARG PRO SEQRES 18 A 328 LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR TRP SEQRES 19 A 328 THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU ALA SEQRES 20 A 328 THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE ALA MET SEQRES 21 A 328 GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP THR SEQRES 22 A 328 PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO LYS SEQRES 23 A 328 GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE HIS SEQRES 24 A 328 PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SER SEQRES 25 A 328 THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN ILE PRO SEQRES 26 A 328 SER ILE GLN SEQRES 1 B 175 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 B 175 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 B 175 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 B 175 SER THR GLN ASN ALA ILE ASP GLY ILE THR ASN LYS VAL SEQRES 5 B 175 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 B 175 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 B 175 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 B 175 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 B 175 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 B 175 LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN ASN ALA SEQRES 11 B 175 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 B 175 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 B 175 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 B 175 ARG GLU GLU ILE ASP SER SEQRES 1 E 328 ASP PRO GLY ASP THR LEU CYS ILE GLY TYR HIS ALA ASN SEQRES 2 E 328 ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN SEQRES 3 E 328 VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP LYS SEQRES 4 E 328 HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA PRO SEQRES 5 E 328 LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE LEU SEQRES 6 E 328 GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SER SEQRES 7 E 328 TRP SER TYR ILE VAL GLU THR PRO SER SER ASP ASN GLY SEQRES 8 E 328 THR CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU LEU SEQRES 9 E 328 ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG PHE SEQRES 10 E 328 GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS ASP SEQRES 11 E 328 SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA GLY SEQRES 12 E 328 ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL LYS SEQRES 13 E 328 LYS GLY ASN SER TYR PRO LYS LEU SER LYS SER TYR ILE SEQRES 14 E 328 ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE SEQRES 15 E 328 HIS HIS PRO SER THR SER ALA ASP GLN GLN SER LEU TYR SEQRES 16 E 328 GLN ASN ALA ASP THR TYR VAL PHE VAL GLY GLY SER ARG SEQRES 17 E 328 TYR SER LYS LYS PHE LYS PRO GLU ILE ALA ILE ARG PRO SEQRES 18 E 328 LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR TRP SEQRES 19 E 328 THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU ALA SEQRES 20 E 328 THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE ALA MET SEQRES 21 E 328 GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP THR SEQRES 22 E 328 PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO LYS SEQRES 23 E 328 GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE HIS SEQRES 24 E 328 PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SER SEQRES 25 E 328 THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN ILE PRO SEQRES 26 E 328 SER ILE GLN SEQRES 1 F 175 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 F 175 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 F 175 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 F 175 SER THR GLN ASN ALA ILE ASP GLY ILE THR ASN LYS VAL SEQRES 5 F 175 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 F 175 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 F 175 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 F 175 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 F 175 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 F 175 LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN ASN ALA SEQRES 11 F 175 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 F 175 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 F 175 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 F 175 ARG GLU GLU ILE ASP SER SEQRES 1 G 229 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 G 229 PRO GLY LYS SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 229 PHE THR PHE SER ALA TYR GLY ILE HIS TRP VAL ARG GLN SEQRES 4 G 229 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA PHE ILE SER SEQRES 5 G 229 PHE ASP GLY GLY SER LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 G 229 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 G 229 LEU TYR VAL HIS MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8 G 229 ALA VAL TYR TYR CYS ALA ARG ASP ARG GLY GLY LYS TYR SEQRES 9 G 229 PRO PRO SER MET GLY PHE PHE ASP PRO TRP GLY GLN GLY SEQRES 10 G 229 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 G 229 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 G 229 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 G 229 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 G 229 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 G 229 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 G 229 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 G 229 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18 G 229 VAL GLU PRO LYS SER CYS SER GLY SEQRES 1 I 215 GLU ILE VAL LEU THR GLN SER PRO PRO THR LEU SER LEU SEQRES 2 I 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 I 215 GLN SER ILE SER ASN SER LEU ALA TRP TYR GLN GLN LYS SEQRES 4 I 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 I 215 ASN ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 I 215 GLY PHE GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 I 215 GLU PRO GLU ASP CYS ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 I 215 ASN ASN TRP PRO PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 I 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 I 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 I 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 I 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 I 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 I 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 I 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 I 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 I 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 H 229 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 229 PRO GLY LYS SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 229 PHE THR PHE SER ALA TYR GLY ILE HIS TRP VAL ARG GLN SEQRES 4 H 229 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA PHE ILE SER SEQRES 5 H 229 PHE ASP GLY GLY SER LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 229 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 229 LEU TYR VAL HIS MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8 H 229 ALA VAL TYR TYR CYS ALA ARG ASP ARG GLY GLY LYS TYR SEQRES 9 H 229 PRO PRO SER MET GLY PHE PHE ASP PRO TRP GLY GLN GLY SEQRES 10 H 229 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 229 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 229 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 229 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 229 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 229 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 229 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 229 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18 H 229 VAL GLU PRO LYS SER CYS SER GLY SEQRES 1 J 215 GLU ILE VAL LEU THR GLN SER PRO PRO THR LEU SER LEU SEQRES 2 J 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 J 215 GLN SER ILE SER ASN SER LEU ALA TRP TYR GLN GLN LYS SEQRES 4 J 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 J 215 ASN ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 J 215 GLY PHE GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 J 215 GLU PRO GLU ASP CYS ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 J 215 ASN ASN TRP PRO PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 J 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 J 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 J 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 J 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 J 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 J 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 J 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 J 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 J 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 K 229 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 K 229 PRO GLY LYS SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 K 229 PHE THR PHE SER ALA TYR GLY ILE HIS TRP VAL ARG GLN SEQRES 4 K 229 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA PHE ILE SER SEQRES 5 K 229 PHE ASP GLY GLY SER LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 K 229 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 K 229 LEU TYR VAL HIS MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8 K 229 ALA VAL TYR TYR CYS ALA ARG ASP ARG GLY GLY LYS TYR SEQRES 9 K 229 PRO PRO SER MET GLY PHE PHE ASP PRO TRP GLY GLN GLY SEQRES 10 K 229 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 K 229 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 K 229 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 K 229 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 K 229 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 K 229 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 K 229 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 K 229 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18 K 229 VAL GLU PRO LYS SER CYS SER GLY SEQRES 1 L 215 GLU ILE VAL LEU THR GLN SER PRO PRO THR LEU SER LEU SEQRES 2 L 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER ILE SER ASN SER LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 215 ASN ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 215 GLY PHE GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 215 GLU PRO GLU ASP CYS ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 L 215 ASN ASN TRP PRO PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET NAG C 401 14 HET NAG C 402 14 HET NAG D 201 14 HET NAG A 401 14 HET NAG B 201 14 HET NAG E 401 14 HET NAG F 201 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE 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 FORMUL 13 NAG 11(C8 H15 N O6) FORMUL 14 BMA C6 H12 O6 HELIX 1 AA1 LYS C 53 VAL C 56 5 5 HELIX 2 AA2 ASN C 65 GLY C 72 1 8 HELIX 3 AA3 ASP C 104 LEU C 112 1 9 HELIX 4 AA4 THR C 187 GLN C 196 1 10 HELIX 5 AA5 ASP D 37 LYS D 58 1 22 HELIX 6 AA6 GLU D 74 LYS D 127 1 54 HELIX 7 AA7 ASP D 145 ASN D 154 1 10 HELIX 8 AA8 ASP D 158 ASP D 174 1 17 HELIX 9 AA9 LYS A 53 VAL A 56 5 5 HELIX 10 AB1 ASN A 65 GLY A 72 1 8 HELIX 11 AB2 ASP A 104 SER A 113 1 10 HELIX 12 AB3 THR A 187 GLN A 196 1 10 HELIX 13 AB4 LYS B 39 LYS B 58 1 20 HELIX 14 AB5 GLU B 74 LYS B 127 1 54 HELIX 15 AB6 ASP B 145 ASN B 154 1 10 HELIX 16 AB7 ASP B 158 SER B 175 1 18 HELIX 17 AB8 ASN E 65 GLY E 72 1 8 HELIX 18 AB9 ASP E 104 LEU E 112 1 9 HELIX 19 AC1 PRO E 122 SER E 126 5 5 HELIX 20 AC2 THR E 187 GLN E 196 1 10 HELIX 21 AC3 ASP F 37 GLU F 57 1 21 HELIX 22 AC4 GLU F 74 LYS F 127 1 54 HELIX 23 AC5 ASP F 145 ASN F 154 1 10 HELIX 24 AC6 ASP F 158 ASP F 174 1 17 HELIX 25 AC7 ARG G 87 THR G 91 5 5 HELIX 26 AC8 TYR G 104 MET G 108 5 5 HELIX 27 AC9 SER G 138 THR G 142 5 5 HELIX 28 AD1 HIS G 211 ASN G 215 5 5 HELIX 29 AD2 GLU I 79 CYS I 83 5 5 HELIX 30 AD3 SER I 122 LYS I 127 1 6 HELIX 31 AD4 LYS I 184 GLU I 188 1 5 HELIX 32 AD5 ARG H 87 THR H 91 5 5 HELIX 33 AD6 TYR H 104 MET H 108 5 5 HELIX 34 AD7 SER H 198 GLY H 201 5 4 HELIX 35 AD8 GLU J 79 CYS J 83 5 5 HELIX 36 AD9 GLU J 124 GLY J 129 1 6 HELIX 37 AE1 LYS J 184 GLU J 188 1 5 HELIX 38 AE2 ARG K 87 THR K 91 5 5 HELIX 39 AE3 TYR K 104 MET K 108 5 5 HELIX 40 AE4 SER K 198 GLY K 201 5 4 HELIX 41 AE5 GLU L 79 CYS L 83 5 5 HELIX 42 AE6 SER L 122 LYS L 127 1 6 HELIX 43 AE7 LYS L 184 GLU L 188 1 5 SHEET 1 AA1 5 GLY D 31 ALA D 36 0 SHEET 2 AA1 5 TYR D 22 ASN D 28 -1 N TYR D 24 O ALA D 35 SHEET 3 AA1 5 THR C 12 TYR C 17 -1 N CYS C 14 O HIS D 25 SHEET 4 AA1 5 CYS D 137 PHE D 140 -1 O PHE D 138 N LEU C 13 SHEET 5 AA1 5 ALA D 130 GLY D 134 -1 N LYS D 131 O GLU D 139 SHEET 1 AA2 2 THR C 25 VAL C 26 0 SHEET 2 AA2 2 VAL C 34 THR C 35 -1 O VAL C 34 N VAL C 26 SHEET 1 AA3 2 SER C 39 ASN C 41 0 SHEET 2 AA3 2 ARG C 315 ALA C 317 -1 O LEU C 316 N VAL C 40 SHEET 1 AA4 3 LEU C 43 GLU C 44 0 SHEET 2 AA4 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLU C 44 SHEET 3 AA4 3 LYS C 307 TYR C 308 1 O LYS C 307 N GLN C 295 SHEET 1 AA5 3 LEU C 59 GLY C 62 0 SHEET 2 AA5 3 ILE C 87 GLU C 89 1 O VAL C 88 N LEU C 59 SHEET 3 AA5 3 ILE C 267 ILE C 269 1 O ILE C 268 N GLU C 89 SHEET 1 AA6 5 VAL C 115 PHE C 118 0 SHEET 2 AA6 5 ALA C 257 ARG C 262 -1 O GLU C 261 N SER C 116 SHEET 3 AA6 5 GLU C 175 HIS C 184 -1 N LEU C 177 O PHE C 258 SHEET 4 AA6 5 LEU C 251 PRO C 254 -1 O VAL C 252 N GLY C 181 SHEET 5 AA6 5 LEU C 151 TRP C 153 -1 N ILE C 152 O VAL C 253 SHEET 1 AA7 4 VAL C 115 PHE C 118 0 SHEET 2 AA7 4 ALA C 257 ARG C 262 -1 O GLU C 261 N SER C 116 SHEET 3 AA7 4 GLU C 175 HIS C 184 -1 N LEU C 177 O PHE C 258 SHEET 4 AA7 4 ARG C 229 VAL C 237 -1 O ARG C 229 N HIS C 184 SHEET 1 AA8 2 THR C 136 HIS C 141 0 SHEET 2 AA8 2 ALA C 144 SER C 146 -1 O ALA C 144 N HIS C 141 SHEET 1 AA9 4 LEU C 164 ILE C 169 0 SHEET 2 AA9 4 LYS C 242 ALA C 247 -1 O ALA C 247 N LEU C 164 SHEET 3 AA9 4 VAL C 202 GLY C 205 -1 N PHE C 203 O GLU C 246 SHEET 4 AA9 4 SER C 210 PHE C 213 -1 O PHE C 213 N VAL C 202 SHEET 1 AB1 3 ALA C 287 ILE C 288 0 SHEET 2 AB1 3 CYS C 281 GLN C 282 -1 N CYS C 281 O ILE C 288 SHEET 3 AB1 3 ILE C 302 GLY C 303 -1 O ILE C 302 N GLN C 282 SHEET 1 AB2 5 SER B 32 ALA B 36 0 SHEET 2 AB2 5 TYR B 22 GLN B 27 -1 N TYR B 24 O ALA B 35 SHEET 3 AB2 5 THR A 12 TYR A 17 -1 N THR A 12 O GLN B 27 SHEET 4 AB2 5 CYS B 137 PHE B 140 -1 O PHE B 138 N LEU A 13 SHEET 5 AB2 5 ALA B 130 GLY B 134 -1 N LYS B 131 O GLU B 139 SHEET 1 AB3 2 THR A 25 VAL A 26 0 SHEET 2 AB3 2 VAL A 34 THR A 35 -1 O VAL A 34 N VAL A 26 SHEET 1 AB4 2 SER A 39 ASN A 41 0 SHEET 2 AB4 2 ARG A 315 ALA A 317 -1 O LEU A 316 N VAL A 40 SHEET 1 AB5 3 LEU A 43 GLU A 44 0 SHEET 2 AB5 3 PHE A 294 GLN A 295 1 O PHE A 294 N GLU A 44 SHEET 3 AB5 3 LYS A 307 TYR A 308 1 O LYS A 307 N GLN A 295 SHEET 1 AB6 3 LEU A 59 HIS A 60 0 SHEET 2 AB6 3 ILE A 87 GLU A 89 1 O VAL A 88 N LEU A 59 SHEET 3 AB6 3 ILE A 267 ILE A 269 1 O ILE A 268 N GLU A 89 SHEET 1 AB7 5 VAL A 115 GLU A 119 0 SHEET 2 AB7 5 TYR A 256 ARG A 262 -1 O GLU A 261 N SER A 116 SHEET 3 AB7 5 GLU A 175 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 4 AB7 5 LEU A 251 PRO A 254 -1 O VAL A 252 N GLY A 181 SHEET 5 AB7 5 LEU A 151 TRP A 153 -1 N ILE A 152 O VAL A 253 SHEET 1 AB8 4 VAL A 115 GLU A 119 0 SHEET 2 AB8 4 TYR A 256 ARG A 262 -1 O GLU A 261 N SER A 116 SHEET 3 AB8 4 GLU A 175 HIS A 184 -1 N LEU A 177 O PHE A 258 SHEET 4 AB8 4 ARG A 229 VAL A 237 -1 O ARG A 229 N HIS A 184 SHEET 1 AB9 2 HIS A 130 ASP A 131 0 SHEET 2 AB9 2 VAL A 155 LYS A 156 -1 O VAL A 155 N ASP A 131 SHEET 1 AC1 2 THR A 136 HIS A 141 0 SHEET 2 AC1 2 ALA A 144 SER A 146 -1 O ALA A 144 N HIS A 141 SHEET 1 AC2 4 LEU A 164 ILE A 169 0 SHEET 2 AC2 4 LYS A 242 ALA A 247 -1 O ILE A 243 N TYR A 168 SHEET 3 AC2 4 VAL A 202 GLY A 205 -1 N GLY A 205 O THR A 244 SHEET 4 AC2 4 SER A 210 PHE A 213 -1 O PHE A 213 N VAL A 202 SHEET 1 AC3 2 CYS A 281 GLN A 282 0 SHEET 2 AC3 2 ALA A 287 ILE A 288 -1 O ILE A 288 N CYS A 281 SHEET 1 AC4 5 SER F 32 ALA F 36 0 SHEET 2 AC4 5 TYR F 22 GLN F 27 -1 N TYR F 24 O ALA F 35 SHEET 3 AC4 5 THR E 12 TYR E 17 -1 N CYS E 14 O HIS F 25 SHEET 4 AC4 5 CYS F 137 PHE F 140 -1 O PHE F 138 N LEU E 13 SHEET 5 AC4 5 ALA F 130 GLY F 134 -1 N LYS F 131 O GLU F 139 SHEET 1 AC5 2 SER E 39 ASN E 41 0 SHEET 2 AC5 2 ARG E 315 ALA E 317 -1 O LEU E 316 N VAL E 40 SHEET 1 AC6 3 LEU E 43 GLU E 44 0 SHEET 2 AC6 3 PHE E 294 GLN E 295 1 O PHE E 294 N GLU E 44 SHEET 3 AC6 3 LYS E 307 TYR E 308 1 O LYS E 307 N GLN E 295 SHEET 1 AC7 2 LEU E 51 LEU E 54 0 SHEET 2 AC7 2 VAL E 274 THR E 279 1 O CYS E 277 N LYS E 53 SHEET 1 AC8 3 LEU E 59 HIS E 60 0 SHEET 2 AC8 3 ILE E 87 GLU E 89 1 O VAL E 88 N LEU E 59 SHEET 3 AC8 3 ILE E 267 ILE E 269 1 O ILE E 268 N GLU E 89 SHEET 1 AC9 5 VAL E 115 PHE E 118 0 SHEET 2 AC9 5 ALA E 257 ARG E 262 -1 O ALA E 257 N PHE E 118 SHEET 3 AC9 5 GLU E 175 HIS E 184 -1 N LEU E 177 O PHE E 258 SHEET 4 AC9 5 LEU E 251 PRO E 254 -1 O VAL E 252 N GLY E 181 SHEET 5 AC9 5 LEU E 151 TRP E 153 -1 N ILE E 152 O VAL E 253 SHEET 1 AD1 4 VAL E 115 PHE E 118 0 SHEET 2 AD1 4 ALA E 257 ARG E 262 -1 O ALA E 257 N PHE E 118 SHEET 3 AD1 4 GLU E 175 HIS E 184 -1 N LEU E 177 O PHE E 258 SHEET 4 AD1 4 ARG E 229 VAL E 237 -1 O ARG E 229 N HIS E 184 SHEET 1 AD2 2 HIS E 130 ASP E 131 0 SHEET 2 AD2 2 VAL E 155 LYS E 156 -1 O VAL E 155 N ASP E 131 SHEET 1 AD3 2 THR E 136 HIS E 141 0 SHEET 2 AD3 2 ALA E 144 SER E 146 -1 O ALA E 144 N HIS E 141 SHEET 1 AD4 4 LEU E 164 ILE E 169 0 SHEET 2 AD4 4 LYS E 242 ALA E 247 -1 O ILE E 243 N TYR E 168 SHEET 3 AD4 4 VAL E 202 GLY E 205 -1 N PHE E 203 O GLU E 246 SHEET 4 AD4 4 SER E 210 PHE E 213 -1 O PHE E 213 N VAL E 202 SHEET 1 AD5 2 CYS E 281 GLN E 282 0 SHEET 2 AD5 2 ILE E 302 GLY E 303 -1 O ILE E 302 N GLN E 282 SHEET 1 AD6 4 GLN G 3 SER G 7 0 SHEET 2 AD6 4 LEU G 18 SER G 25 -1 O ALA G 23 N VAL G 5 SHEET 3 AD6 4 THR G 78 MET G 83 -1 O LEU G 79 N CYS G 22 SHEET 4 AD6 4 PHE G 68 ASP G 73 -1 N SER G 71 O TYR G 80 SHEET 1 AD7 6 GLY G 10 VAL G 12 0 SHEET 2 AD7 6 THR G 118 VAL G 122 1 O THR G 121 N GLY G 10 SHEET 3 AD7 6 ALA G 92 ARG G 98 -1 N ALA G 92 O VAL G 120 SHEET 4 AD7 6 ILE G 34 ARG G 38 -1 N VAL G 37 O TYR G 95 SHEET 5 AD7 6 GLU G 46 ILE G 51 -1 O ILE G 51 N ILE G 34 SHEET 6 AD7 6 LYS G 58 TYR G 60 -1 O TYR G 59 N PHE G 50 SHEET 1 AD8 4 SER G 131 LEU G 135 0 SHEET 2 AD8 4 THR G 146 TYR G 156 -1 O LEU G 152 N PHE G 133 SHEET 3 AD8 4 TYR G 187 PRO G 196 -1 O TYR G 187 N TYR G 156 SHEET 4 AD8 4 VAL G 180 LEU G 181 -1 N VAL G 180 O SER G 188 SHEET 1 AD9 3 THR G 162 TRP G 165 0 SHEET 2 AD9 3 ILE G 206 ASN G 210 -1 O ASN G 208 N SER G 164 SHEET 3 AD9 3 ASP G 219 ARG G 221 -1 O LYS G 220 N CYS G 207 SHEET 1 AE1 4 LEU I 4 SER I 7 0 SHEET 2 AE1 4 ALA I 19 ALA I 25 -1 O ARG I 24 N THR I 5 SHEET 3 AE1 4 ASP I 70 ILE I 75 -1 O LEU I 73 N LEU I 21 SHEET 4 AE1 4 PHE I 62 PHE I 67 -1 N SER I 63 O THR I 74 SHEET 1 AE2 6 THR I 10 LEU I 13 0 SHEET 2 AE2 6 THR I 103 ILE I 107 1 O LYS I 104 N LEU I 11 SHEET 3 AE2 6 VAL I 85 GLN I 90 -1 N TYR I 86 O THR I 103 SHEET 4 AE2 6 LEU I 33 GLN I 38 -1 N GLN I 38 O VAL I 85 SHEET 5 AE2 6 PRO I 44 TYR I 49 -1 O LEU I 47 N TRP I 35 SHEET 6 AE2 6 ASN I 53 ARG I 54 -1 O ASN I 53 N TYR I 49 SHEET 1 AE3 4 SER I 115 PHE I 119 0 SHEET 2 AE3 4 THR I 130 PHE I 140 -1 O LEU I 136 N PHE I 117 SHEET 3 AE3 4 TYR I 174 SER I 183 -1 O LEU I 182 N ALA I 131 SHEET 4 AE3 4 SER I 160 VAL I 164 -1 N GLN I 161 O THR I 179 SHEET 1 AE4 3 ALA I 145 VAL I 151 0 SHEET 2 AE4 3 VAL I 192 HIS I 199 -1 O ALA I 194 N LYS I 150 SHEET 3 AE4 3 VAL I 206 THR I 207 -1 O VAL I 206 N VAL I 197 SHEET 1 AE5 3 ALA I 145 VAL I 151 0 SHEET 2 AE5 3 VAL I 192 HIS I 199 -1 O ALA I 194 N LYS I 150 SHEET 3 AE5 3 PHE I 210 ASN I 211 -1 O PHE I 210 N TYR I 193 SHEET 1 AE6 4 GLN H 3 SER H 7 0 SHEET 2 AE6 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AE6 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AE6 4 PHE H 68 ILE H 70 -1 N THR H 69 O HIS H 82 SHEET 1 AE7 5 LYS H 58 TYR H 60 0 SHEET 2 AE7 5 GLY H 44 ILE H 51 -1 N PHE H 50 O TYR H 59 SHEET 3 AE7 5 ILE H 34 ALA H 40 -1 N TRP H 36 O VAL H 48 SHEET 4 AE7 5 ALA H 92 ARG H 98 -1 O TYR H 95 N VAL H 37 SHEET 5 AE7 5 THR H 118 VAL H 120 -1 O THR H 118 N TYR H 94 SHEET 1 AE8 4 SER H 131 LEU H 135 0 SHEET 2 AE8 4 THR H 146 TYR H 156 -1 O LEU H 152 N PHE H 133 SHEET 3 AE8 4 TYR H 187 PRO H 196 -1 O LEU H 189 N VAL H 153 SHEET 4 AE8 4 VAL H 180 LEU H 181 -1 N VAL H 180 O SER H 188 SHEET 1 AE9 3 VAL H 161 TRP H 165 0 SHEET 2 AE9 3 ILE H 206 HIS H 211 -1 O ASN H 208 N SER H 164 SHEET 3 AE9 3 THR H 216 ARG H 221 -1 O LYS H 220 N CYS H 207 SHEET 1 AF1 4 LEU J 4 SER J 7 0 SHEET 2 AF1 4 ALA J 19 ALA J 25 -1 O SER J 22 N SER J 7 SHEET 3 AF1 4 ASP J 70 ILE J 75 -1 O ILE J 75 N ALA J 19 SHEET 4 AF1 4 PHE J 62 PHE J 67 -1 N SER J 63 O THR J 74 SHEET 1 AF2 6 THR J 10 LEU J 13 0 SHEET 2 AF2 6 THR J 103 ILE J 107 1 O LYS J 104 N LEU J 11 SHEET 3 AF2 6 VAL J 85 GLN J 90 -1 N TYR J 86 O THR J 103 SHEET 4 AF2 6 LEU J 33 GLN J 38 -1 N ALA J 34 O GLN J 89 SHEET 5 AF2 6 ARG J 45 TYR J 49 -1 O ILE J 48 N TRP J 35 SHEET 6 AF2 6 ASN J 53 ARG J 54 -1 O ASN J 53 N TYR J 49 SHEET 1 AF3 4 PHE J 117 PHE J 119 0 SHEET 2 AF3 4 THR J 130 PHE J 140 -1 O LEU J 136 N PHE J 117 SHEET 3 AF3 4 TYR J 174 SER J 183 -1 O LEU J 182 N ALA J 131 SHEET 4 AF3 4 SER J 160 VAL J 164 -1 N SER J 163 O SER J 177 SHEET 1 AF4 4 ALA J 154 GLN J 156 0 SHEET 2 AF4 4 LYS J 146 VAL J 151 -1 N TRP J 149 O GLN J 156 SHEET 3 AF4 4 VAL J 192 THR J 198 -1 O GLU J 196 N GLN J 148 SHEET 4 AF4 4 VAL J 206 ASN J 211 -1 O PHE J 210 N TYR J 193 SHEET 1 AF5 4 GLN K 3 SER K 7 0 SHEET 2 AF5 4 LEU K 18 SER K 25 -1 O SER K 21 N SER K 7 SHEET 3 AF5 4 THR K 78 MET K 83 -1 O LEU K 79 N CYS K 22 SHEET 4 AF5 4 PHE K 68 ILE K 70 -1 N THR K 69 O HIS K 82 SHEET 1 AF6 6 GLY K 10 VAL K 12 0 SHEET 2 AF6 6 THR K 118 VAL K 122 1 O THR K 121 N GLY K 10 SHEET 3 AF6 6 ALA K 92 ARG K 98 -1 N TYR K 94 O THR K 118 SHEET 4 AF6 6 ILE K 34 GLN K 39 -1 N VAL K 37 O TYR K 95 SHEET 5 AF6 6 GLU K 46 ILE K 51 -1 O VAL K 48 N TRP K 36 SHEET 6 AF6 6 LYS K 58 TYR K 60 -1 O TYR K 59 N PHE K 50 SHEET 1 AF7 4 SER K 131 LEU K 135 0 SHEET 2 AF7 4 THR K 146 TYR K 156 -1 O LEU K 152 N PHE K 133 SHEET 3 AF7 4 TYR K 187 PRO K 196 -1 O LEU K 189 N VAL K 153 SHEET 4 AF7 4 VAL K 174 THR K 176 -1 N HIS K 175 O VAL K 192 SHEET 1 AF8 4 SER K 131 LEU K 135 0 SHEET 2 AF8 4 THR K 146 TYR K 156 -1 O LEU K 152 N PHE K 133 SHEET 3 AF8 4 TYR K 187 PRO K 196 -1 O LEU K 189 N VAL K 153 SHEET 4 AF8 4 VAL K 180 LEU K 181 -1 N VAL K 180 O SER K 188 SHEET 1 AF9 3 THR K 162 TRP K 165 0 SHEET 2 AF9 3 ILE K 206 ASN K 210 -1 O ASN K 208 N SER K 164 SHEET 3 AF9 3 ASP K 219 ARG K 221 -1 O LYS K 220 N CYS K 207 SHEET 1 AG1 4 LEU L 4 SER L 7 0 SHEET 2 AG1 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AG1 4 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AG1 4 PHE L 62 PHE L 67 -1 N SER L 65 O THR L 72 SHEET 1 AG2 6 THR L 10 LEU L 13 0 SHEET 2 AG2 6 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 11 SHEET 3 AG2 6 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 103 SHEET 4 AG2 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AG2 6 ARG L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AG2 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AG3 4 SER L 115 PHE L 119 0 SHEET 2 AG3 4 THR L 130 PHE L 140 -1 O VAL L 134 N PHE L 119 SHEET 3 AG3 4 TYR L 174 SER L 183 -1 O LEU L 176 N LEU L 137 SHEET 4 AG3 4 SER L 160 THR L 165 -1 N THR L 165 O SER L 175 SHEET 1 AG4 4 ALA L 154 LEU L 155 0 SHEET 2 AG4 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AG4 4 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 4 AG4 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SSBOND 1 CYS C 14 CYS D 137 1555 1555 2.03 SSBOND 2 CYS C 52 CYS C 277 1555 1555 2.03 SSBOND 3 CYS C 64 CYS C 76 1555 1555 2.03 SSBOND 4 CYS C 97 CYS C 139 1555 1555 2.03 SSBOND 5 CYS C 281 CYS C 305 1555 1555 2.03 SSBOND 6 CYS D 144 CYS D 148 1555 1555 2.03 SSBOND 7 CYS A 14 CYS B 137 1555 1555 2.03 SSBOND 8 CYS A 64 CYS A 76 1555 1555 2.03 SSBOND 9 CYS A 97 CYS A 139 1555 1555 2.03 SSBOND 10 CYS A 281 CYS A 305 1555 1555 2.03 SSBOND 11 CYS B 144 CYS B 148 1555 1555 2.03 SSBOND 12 CYS E 14 CYS F 137 1555 1555 2.03 SSBOND 13 CYS E 52 CYS E 277 1555 1555 2.03 SSBOND 14 CYS E 64 CYS E 76 1555 1555 2.03 SSBOND 15 CYS E 97 CYS E 139 1555 1555 2.03 SSBOND 16 CYS E 281 CYS E 305 1555 1555 2.03 SSBOND 17 CYS F 144 CYS F 148 1555 1555 2.03 SSBOND 18 CYS G 22 CYS G 96 1555 1555 2.03 SSBOND 19 CYS G 151 CYS G 207 1555 1555 2.03 SSBOND 20 CYS I 23 CYS I 88 1555 1555 2.04 SSBOND 21 CYS I 135 CYS I 195 1555 1555 2.04 SSBOND 22 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 23 CYS J 23 CYS J 88 1555 1555 2.03 SSBOND 24 CYS J 135 CYS J 195 1555 1555 2.03 SSBOND 25 CYS K 22 CYS K 96 1555 1555 2.03 SSBOND 26 CYS K 151 CYS K 207 1555 1555 2.03 SSBOND 27 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 28 CYS L 135 CYS L 195 1555 1555 2.03 LINK ND2 ASN C 21 C1 NAG C 401 1555 1555 1.44 LINK ND2 ASN C 94 C1 NAG M 1 1555 1555 1.43 LINK ND2 ASN C 278 C1 NAG C 402 1555 1555 1.45 LINK ND2 ASN D 154 C1 NAG D 201 1555 1555 1.44 LINK ND2 ASN A 94 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN A 278 C1 NAG A 401 1555 1555 1.45 LINK ND2 ASN B 154 C1 NAG B 201 1555 1555 1.44 LINK ND2 ASN E 21 C1 NAG E 401 1555 1555 1.44 LINK ND2 ASN F 154 C1 NAG F 201 1555 1555 1.45 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.46 CISPEP 1 PHE G 157 PRO G 158 0 -3.35 CISPEP 2 GLU G 159 PRO G 160 0 8.16 CISPEP 3 SER I 7 PRO I 8 0 -2.32 CISPEP 4 TRP I 94 PRO I 95 0 1.62 CISPEP 5 PRO I 95 PRO I 96 0 -0.46 CISPEP 6 TYR I 141 PRO I 142 0 0.74 CISPEP 7 ASP H 112 PRO H 113 0 -1.31 CISPEP 8 PHE H 157 PRO H 158 0 7.74 CISPEP 9 GLU H 159 PRO H 160 0 -3.39 CISPEP 10 SER J 7 PRO J 8 0 -3.56 CISPEP 11 TRP J 94 PRO J 95 0 4.17 CISPEP 12 PRO J 95 PRO J 96 0 -0.30 CISPEP 13 TYR J 141 PRO J 142 0 3.08 CISPEP 14 PHE K 157 PRO K 158 0 -1.27 CISPEP 15 GLU K 159 PRO K 160 0 -4.00 CISPEP 16 SER L 7 PRO L 8 0 -5.82 CISPEP 17 TRP L 94 PRO L 95 0 2.35 CISPEP 18 PRO L 95 PRO L 96 0 -1.86 CISPEP 19 TYR L 141 PRO L 142 0 2.95 CRYST1 161.816 313.101 325.522 90.00 90.00 90.00 I 21 21 21 24 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 0.006180 0.000000 0.000000 0.00000 SCALE2 0.000000 0.003194 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003072 0.00000