HEADER VIRAL PROTEIN/IMMUNE SYSTEM 28-SEP-24 9JQV TITLE THE CRYSTAL STRUCTURE OF SFTSV GN AND SD12 ANTIBODY COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPMENT POLYPROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: M POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: SEQUENCE REFERENCE FOR SOURCE ORGANISM SFTS VIRUS JS4 COMPND 7 IS NOT AVAILABLE IN UNIPROT AT THE TIME OF BIOCURATION. CURRENT COMPND 8 SEQUENCE REFERENCE IS FROM UNIPROT ID A0A1S6K8S9.; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: SD12 HEAVY CHAIN; COMPND 11 CHAIN: H, C; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: SD12 LIGHT CHAIN; COMPND 15 CHAIN: L, D; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SFTS VIRUS HB29; SOURCE 3 ORGANISM_TAXID: 992212; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SFTSV, GN, SD12, ANTIBODY, SEVERE FEVER WITH THROMBOCYTOPENIA KEYWDS 2 SYNDROME VIRUS, VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE KEYWDS 3 SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR W.F.SHI,C.S.QUAN,J.X.QI REVDAT 1 18-JUN-25 9JQV 0 JRNL AUTH C.S.QUAN,J.X.QI,W.F.SHI JRNL TITL HIGH AFFINITY HUMAN-DERIVED ANTIBODIES EFFECTIVELY RESCUE JRNL TITL 2 MORIBUND MICE WITH LETHAL SEVERE FEVER WITH THROMBOCYTOPENIA JRNL TITL 3 VIRUS INFECTION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.92 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 89.6 REMARK 3 NUMBER OF REFLECTIONS : 66789 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.227 REMARK 3 R VALUE (WORKING SET) : 0.225 REMARK 3 FREE R VALUE : 0.255 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050 REMARK 3 FREE R VALUE TEST SET COUNT : 3373 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 45.9200 - 6.9100 0.99 3005 166 0.2114 0.1932 REMARK 3 2 6.9100 - 5.4900 1.00 2970 174 0.2043 0.1928 REMARK 3 3 5.4900 - 4.7900 1.00 2989 162 0.1732 0.1935 REMARK 3 4 4.7900 - 4.3600 1.00 2953 150 0.1612 0.2140 REMARK 3 5 4.3600 - 4.0400 1.00 2957 158 0.1783 0.2026 REMARK 3 6 4.0400 - 3.8100 1.00 2957 158 0.2028 0.2556 REMARK 3 7 3.8100 - 3.6200 1.00 2941 160 0.2166 0.2392 REMARK 3 8 3.6200 - 3.4600 1.00 2972 141 0.2307 0.2643 REMARK 3 9 3.4600 - 3.3300 1.00 2949 139 0.2354 0.2935 REMARK 3 10 3.3300 - 3.2100 1.00 2931 163 0.2408 0.2888 REMARK 3 11 3.2100 - 3.1100 1.00 2941 160 0.2588 0.3062 REMARK 3 12 3.1100 - 3.0200 1.00 2949 153 0.2701 0.2913 REMARK 3 13 3.0200 - 2.9400 1.00 2873 173 0.2800 0.2972 REMARK 3 14 2.9400 - 2.8700 0.99 2941 132 0.2707 0.3404 REMARK 3 15 2.8700 - 2.8000 0.98 2893 160 0.2737 0.2950 REMARK 3 16 2.8000 - 2.7500 0.93 2705 152 0.2722 0.3404 REMARK 3 17 2.7500 - 2.6900 0.88 2563 151 0.2724 0.3385 REMARK 3 18 2.6900 - 2.6400 0.83 2476 118 0.2818 0.2726 REMARK 3 19 2.6400 - 2.5900 0.78 2260 123 0.2786 0.2988 REMARK 3 20 2.5900 - 2.5500 0.74 2190 104 0.2828 0.3788 REMARK 3 21 2.5500 - 2.5100 0.68 1993 94 0.2900 0.4162 REMARK 3 22 2.5100 - 2.4700 0.63 1859 87 0.3156 0.4005 REMARK 3 23 2.4700 - 2.4300 0.57 1647 105 0.3232 0.3482 REMARK 3 24 2.4300 - 2.4000 0.51 1502 90 0.3294 0.4059 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.330 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.674 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 37.92 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.00 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 : 0.004 11740 REMARK 3 ANGLE : 0.712 15901 REMARK 3 CHIRALITY : 0.045 1752 REMARK 3 PLANARITY : 0.006 2038 REMARK 3 DIHEDRAL : 16.270 4268 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): -27.0787 20.7076 -15.5159 REMARK 3 T TENSOR REMARK 3 T11: 0.3285 T22: 0.2022 REMARK 3 T33: 0.1782 T12: 0.0620 REMARK 3 T13: 0.0228 T23: -0.0084 REMARK 3 L TENSOR REMARK 3 L11: 0.2858 L22: 0.5583 REMARK 3 L33: 0.7734 L12: -0.0481 REMARK 3 L13: 0.1274 L23: -0.2009 REMARK 3 S TENSOR REMARK 3 S11: -0.0518 S12: 0.0254 S13: 0.0655 REMARK 3 S21: 0.2395 S22: 0.0527 S23: -0.0331 REMARK 3 S31: 0.0141 S32: -0.0864 S33: 0.0074 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): 19.2421 25.2362 -7.0085 REMARK 3 T TENSOR REMARK 3 T11: 0.4371 T22: 0.2439 REMARK 3 T33: 0.2255 T12: -0.0731 REMARK 3 T13: -0.0465 T23: 0.0358 REMARK 3 L TENSOR REMARK 3 L11: 0.2678 L22: 0.2133 REMARK 3 L33: 0.6786 L12: 0.0344 REMARK 3 L13: 0.1853 L23: 0.0529 REMARK 3 S TENSOR REMARK 3 S11: 0.1893 S12: -0.0575 S13: -0.0664 REMARK 3 S21: 0.2429 S22: -0.1020 S23: 0.0073 REMARK 3 S31: 0.2264 S32: -0.0306 S33: 0.0559 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN C REMARK 3 ORIGIN FOR THE GROUP (A): 18.1162 17.6832 -59.6237 REMARK 3 T TENSOR REMARK 3 T11: 0.1641 T22: 0.2898 REMARK 3 T33: 0.2879 T12: -0.0378 REMARK 3 T13: 0.0369 T23: -0.0396 REMARK 3 L TENSOR REMARK 3 L11: 0.1538 L22: 0.5892 REMARK 3 L33: 0.1767 L12: 0.1962 REMARK 3 L13: 0.0483 L23: 0.1850 REMARK 3 S TENSOR REMARK 3 S11: -0.0948 S12: 0.0678 S13: -0.0771 REMARK 3 S21: 0.0358 S22: 0.1349 S23: -0.1643 REMARK 3 S31: 0.2585 S32: -0.0836 S33: -0.0024 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN D REMARK 3 ORIGIN FOR THE GROUP (A): 24.8608 34.3138 -65.2808 REMARK 3 T TENSOR REMARK 3 T11: 0.1292 T22: 0.2654 REMARK 3 T33: 0.2215 T12: -0.1716 REMARK 3 T13: -0.0038 T23: -0.0048 REMARK 3 L TENSOR REMARK 3 L11: 0.6535 L22: 1.0461 REMARK 3 L33: 0.1598 L12: 0.2849 REMARK 3 L13: -0.2266 L23: -0.1665 REMARK 3 S TENSOR REMARK 3 S11: -0.3284 S12: 0.0968 S13: 0.0267 REMARK 3 S21: -0.1588 S22: 0.3134 S23: 0.0589 REMARK 3 S31: -0.0235 S32: -0.0364 S33: -0.0026 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN H REMARK 3 ORIGIN FOR THE GROUP (A): -21.2847 28.3412 -67.4830 REMARK 3 T TENSOR REMARK 3 T11: 0.1298 T22: 0.1219 REMARK 3 T33: 0.2082 T12: -0.0932 REMARK 3 T13: -0.0528 T23: 0.0967 REMARK 3 L TENSOR REMARK 3 L11: 0.2282 L22: 0.6314 REMARK 3 L33: 0.2510 L12: 0.0726 REMARK 3 L13: -0.0470 L23: 0.3713 REMARK 3 S TENSOR REMARK 3 S11: -0.1970 S12: -0.0137 S13: 0.2387 REMARK 3 S21: -0.2036 S22: 0.1551 S23: 0.1879 REMARK 3 S31: -0.3359 S32: 0.0121 S33: -0.0201 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN L REMARK 3 ORIGIN FOR THE GROUP (A): -18.5105 10.1517 -72.2865 REMARK 3 T TENSOR REMARK 3 T11: 0.1724 T22: 0.2151 REMARK 3 T33: 0.2368 T12: -0.0958 REMARK 3 T13: 0.0220 T23: 0.0038 REMARK 3 L TENSOR REMARK 3 L11: 0.5812 L22: 0.8870 REMARK 3 L33: 0.3354 L12: 0.3220 REMARK 3 L13: 0.4104 L23: 0.4299 REMARK 3 S TENSOR REMARK 3 S11: -0.2329 S12: 0.1331 S13: -0.0055 REMARK 3 S21: -0.2463 S22: 0.1517 S23: -0.0780 REMARK 3 S31: -0.2088 S32: 0.1056 S33: -0.0829 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 9JQV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 03-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1300052007. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-SEP-24 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 : SSRF REMARK 200 BEAMLINE : BL02U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97853 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74450 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.1050 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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 (%): 57.44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MAGNESIUM CHLORIDE HEXAHYDRATE, REMARK 280 0.1 M SODIUM HEPES, 7.0, 15 % W/V PEG 4000, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 41.17100 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, E, F 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, G 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 GLY A 20 REMARK 465 HIS A 342 REMARK 465 HIS A 343 REMARK 465 HIS A 344 REMARK 465 PRO H 134 REMARK 465 SER H 135 REMARK 465 SER H 136 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 GLY H 142 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 GLY B 20 REMARK 465 GLU B 294 REMARK 465 HIS B 295 REMARK 465 GLY B 296 REMARK 465 GLU B 297 REMARK 465 GLU B 298 REMARK 465 THR B 299 REMARK 465 SER B 300 REMARK 465 GLU B 301 REMARK 465 ALA B 302 REMARK 465 HIS B 342 REMARK 465 HIS B 343 REMARK 465 HIS B 344 REMARK 465 PRO C 134 REMARK 465 SER C 135 REMARK 465 SER C 136 REMARK 465 LYS C 137 REMARK 465 SER C 138 REMARK 465 THR C 139 REMARK 465 SER C 140 REMARK 465 GLY C 141 REMARK 465 GLY C 142 REMARK 465 GLY D 212 REMARK 465 GLU D 213 REMARK 465 CYS D 214 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 GLU A 115 CG CD OE1 OE2 REMARK 470 LYS A 255 CG CD CE NZ REMARK 470 THR A 299 OG1 CG2 REMARK 470 GLU B 115 CG CD OE1 OE2 REMARK 470 LYS D 103 CD CE NZ 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 B 89 OD2 ASP B 178 2.09 REMARK 500 OG SER B 199 O ILE B 240 2.15 REMARK 500 OG SER H 211 OG1 THR H 213 2.17 REMARK 500 NZ LYS B 238 O HOH B 501 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 22 -81.64 52.49 REMARK 500 ARG A 75 -11.84 72.46 REMARK 500 CYS A 217 -58.96 -123.93 REMARK 500 GLU A 218 -26.56 69.18 REMARK 500 HIS A 235 -167.76 -122.04 REMARK 500 GLU A 301 -166.78 18.20 REMARK 500 ALA A 302 109.36 -165.62 REMARK 500 ASP H 152 66.52 60.21 REMARK 500 PRO H 193 37.13 -80.74 REMARK 500 SER H 194 -14.64 62.16 REMARK 500 SER H 195 48.51 -98.68 REMARK 500 LYS H 222 -160.35 83.59 REMARK 500 SER L 30 -119.65 38.91 REMARK 500 ALA L 51 -15.19 70.97 REMARK 500 SER L 52 -12.93 -141.98 REMARK 500 ALA L 144 142.70 -170.46 REMARK 500 SER B 22 -73.90 37.30 REMARK 500 ARG B 75 -12.20 72.23 REMARK 500 ASP B 171 0.66 -68.77 REMARK 500 CYS B 217 -57.77 -121.00 REMARK 500 GLU B 218 -13.95 72.49 REMARK 500 LYS C 222 178.21 82.84 REMARK 500 SER D 30 -117.88 45.38 REMARK 500 ALA D 51 -13.90 71.85 REMARK 500 SER D 52 -13.77 -141.88 REMARK 500 LEU D 125 43.78 -80.85 REMARK 500 SER D 127 -17.37 -147.92 REMARK 500 LEU D 154 114.69 66.09 REMARK 500 REMARK 500 REMARK: NULL DBREF1 9JQV A 20 338 UNP A0A1S6K8S9_SFTS DBREF2 9JQV A A0A1S6K8S9 19 337 DBREF 9JQV H 1 223 PDB 9JQV 9JQV 1 223 DBREF 9JQV L 1 214 PDB 9JQV 9JQV 1 214 DBREF1 9JQV B 20 338 UNP A0A1S6K8S9_SFTS DBREF2 9JQV B A0A1S6K8S9 19 337 DBREF 9JQV C 1 223 PDB 9JQV 9JQV 1 223 DBREF 9JQV D 1 214 PDB 9JQV 9JQV 1 214 SEQADV 9JQV HIS A 339 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQV HIS A 340 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQV HIS A 341 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQV HIS A 342 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQV HIS A 343 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQV HIS A 344 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQV HIS B 339 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQV HIS B 340 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQV HIS B 341 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQV HIS B 342 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQV HIS B 343 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQV HIS B 344 UNP A0A1S6K8S EXPRESSION TAG SEQRES 1 A 325 GLY ASP SER GLY PRO ILE ILE CYS ALA GLY PRO ILE HIS SEQRES 2 A 325 SER ASN LYS SER ALA GLY ILE PRO HIS LEU LEU GLY TYR SEQRES 3 A 325 SER GLU LYS ILE CYS GLN ILE ASP ARG LEU ILE HIS VAL SEQRES 4 A 325 SER SER TRP LEU ARG ASN HIS SER GLN PHE GLN GLY TYR SEQRES 5 A 325 VAL GLY GLN ARG GLY GLY ARG SER GLN VAL SER TYR TYR SEQRES 6 A 325 PRO ALA GLU ASN SER TYR SER ARG TRP SER GLY LEU LEU SEQRES 7 A 325 SER PRO CYS ASP ALA ASP TRP LEU GLY MET LEU VAL VAL SEQRES 8 A 325 LYS LYS ALA ARG GLU SER ASP MET ILE VAL PRO GLY PRO SEQRES 9 A 325 SER TYR LYS GLY LYS VAL PHE PHE GLU ARG PRO THR PHE SEQRES 10 A 325 ASP GLY TYR VAL GLY TRP GLY CYS GLY SER GLY LYS SER SEQRES 11 A 325 ARG THR GLU SER GLY GLU LEU CYS SER SER ASP SER GLY SEQRES 12 A 325 THR SER SER GLY LEU LEU PRO SER ASP ARG VAL LEU TRP SEQRES 13 A 325 ILE GLY ASP VAL ALA CYS GLN LEU MET THR PRO ILE PRO SEQRES 14 A 325 GLU GLU THR PHE LEU GLU LEU LYS SER PHE SER GLN SER SEQRES 15 A 325 GLU PHE PRO ASP ILE CYS LYS ILE ASP GLY ILE VAL PHE SEQRES 16 A 325 ASN GLN CYS GLU GLY GLU SER LEU PRO GLN PRO PHE ASP SEQRES 17 A 325 VAL ALA TRP MET ASP VAL GLY HIS SER HIS LYS ILE ILE SEQRES 18 A 325 MET ARG GLU HIS LYS THR LYS TRP VAL GLN GLU SER SER SEQRES 19 A 325 SER LYS ASP PHE VAL CYS TYR LYS GLU GLY THR GLY PRO SEQRES 20 A 325 CYS SER GLU SER GLU GLU LYS ALA CYS LYS THR SER GLY SEQRES 21 A 325 SER CYS ARG GLY ASP MET GLN PHE CYS LYS VAL ALA GLY SEQRES 22 A 325 CYS GLU HIS GLY GLU GLU THR SER GLU ALA LYS CYS ARG SEQRES 23 A 325 CYS SER LEU VAL HIS LYS PRO GLY GLU VAL VAL VAL SER SEQRES 24 A 325 TYR GLY GLY MET ARG VAL ARG PRO LYS CYS TYR GLY PHE SEQRES 25 A 325 SER ARG MET MET ALA THR LEU HIS HIS HIS HIS HIS HIS SEQRES 1 H 223 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 223 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 223 PHE ILE PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 H 223 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE SER SEQRES 5 H 223 GLY SER GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 223 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 223 LEU TYR LEU GLN MET ASN SER LEU ARG ASP GLU ASP THR SEQRES 8 H 223 ALA VAL TYR TYR CYS ALA LYS ASP ARG SER TYR VAL SER SEQRES 9 H 223 SER GLY PHE PHE ASP ASP TRP GLY GLN GLY THR LEU VAL SEQRES 10 H 223 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 223 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 223 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 223 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 223 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 223 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 223 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 223 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 H 223 LYS SER SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 L 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN ARG SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE PHE GLU ALA SER SEQRES 5 L 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 214 GLU ASN LEU LEU TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 B 325 GLY ASP SER GLY PRO ILE ILE CYS ALA GLY PRO ILE HIS SEQRES 2 B 325 SER ASN LYS SER ALA GLY ILE PRO HIS LEU LEU GLY TYR SEQRES 3 B 325 SER GLU LYS ILE CYS GLN ILE ASP ARG LEU ILE HIS VAL SEQRES 4 B 325 SER SER TRP LEU ARG ASN HIS SER GLN PHE GLN GLY TYR SEQRES 5 B 325 VAL GLY GLN ARG GLY GLY ARG SER GLN VAL SER TYR TYR SEQRES 6 B 325 PRO ALA GLU ASN SER TYR SER ARG TRP SER GLY LEU LEU SEQRES 7 B 325 SER PRO CYS ASP ALA ASP TRP LEU GLY MET LEU VAL VAL SEQRES 8 B 325 LYS LYS ALA ARG GLU SER ASP MET ILE VAL PRO GLY PRO SEQRES 9 B 325 SER TYR LYS GLY LYS VAL PHE PHE GLU ARG PRO THR PHE SEQRES 10 B 325 ASP GLY TYR VAL GLY TRP GLY CYS GLY SER GLY LYS SER SEQRES 11 B 325 ARG THR GLU SER GLY GLU LEU CYS SER SER ASP SER GLY SEQRES 12 B 325 THR SER SER GLY LEU LEU PRO SER ASP ARG VAL LEU TRP SEQRES 13 B 325 ILE GLY ASP VAL ALA CYS GLN LEU MET THR PRO ILE PRO SEQRES 14 B 325 GLU GLU THR PHE LEU GLU LEU LYS SER PHE SER GLN SER SEQRES 15 B 325 GLU PHE PRO ASP ILE CYS LYS ILE ASP GLY ILE VAL PHE SEQRES 16 B 325 ASN GLN CYS GLU GLY GLU SER LEU PRO GLN PRO PHE ASP SEQRES 17 B 325 VAL ALA TRP MET ASP VAL GLY HIS SER HIS LYS ILE ILE SEQRES 18 B 325 MET ARG GLU HIS LYS THR LYS TRP VAL GLN GLU SER SER SEQRES 19 B 325 SER LYS ASP PHE VAL CYS TYR LYS GLU GLY THR GLY PRO SEQRES 20 B 325 CYS SER GLU SER GLU GLU LYS ALA CYS LYS THR SER GLY SEQRES 21 B 325 SER CYS ARG GLY ASP MET GLN PHE CYS LYS VAL ALA GLY SEQRES 22 B 325 CYS GLU HIS GLY GLU GLU THR SER GLU ALA LYS CYS ARG SEQRES 23 B 325 CYS SER LEU VAL HIS LYS PRO GLY GLU VAL VAL VAL SER SEQRES 24 B 325 TYR GLY GLY MET ARG VAL ARG PRO LYS CYS TYR GLY PHE SEQRES 25 B 325 SER ARG MET MET ALA THR LEU HIS HIS HIS HIS HIS HIS SEQRES 1 C 223 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 223 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 223 PHE ILE PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 C 223 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE SER SEQRES 5 C 223 GLY SER GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 C 223 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 C 223 LEU TYR LEU GLN MET ASN SER LEU ARG ASP GLU ASP THR SEQRES 8 C 223 ALA VAL TYR TYR CYS ALA LYS ASP ARG SER TYR VAL SER SEQRES 9 C 223 SER GLY PHE PHE ASP ASP TRP GLY GLN GLY THR LEU VAL SEQRES 10 C 223 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 C 223 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 C 223 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 C 223 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 C 223 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 C 223 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 C 223 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 C 223 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 C 223 LYS SER SEQRES 1 D 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 D 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN ARG SEQRES 4 D 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE PHE GLU ALA SER SEQRES 5 D 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU SEQRES 7 D 214 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 D 214 GLU ASN LEU LEU TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 D 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 D 214 PHE ASN ARG GLY GLU CYS HET NAG E 1 14 HET NAG E 2 14 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET NAG B 401 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 7 NAG 7(C8 H15 N O6) FORMUL 8 BMA 2(C6 H12 O6) FORMUL 11 HOH *337(H2 O) HELIX 1 AA1 GLY A 44 ARG A 54 1 11 HELIX 2 AA2 LEU A 55 GLN A 67 1 13 HELIX 3 AA3 GLY A 77 VAL A 81 5 5 HELIX 4 AA4 SER A 89 TRP A 93 5 5 HELIX 5 AA5 SER A 98 LEU A 105 1 8 HELIX 6 AA6 PRO A 169 ASP A 171 5 3 HELIX 7 AA7 PRO A 188 PHE A 203 1 16 HELIX 8 AA8 SER A 253 LYS A 255 5 3 HELIX 9 AA9 SER A 268 GLY A 279 1 12 HELIX 10 AB1 ASP A 284 ALA A 291 1 8 HELIX 11 AB2 ILE H 28 TYR H 32 5 5 HELIX 12 AB3 ARG H 87 THR H 91 5 5 HELIX 13 AB4 SER H 164 ALA H 166 5 3 HELIX 14 AB5 LYS H 209 ASN H 212 5 4 HELIX 15 AB6 GLN L 79 ILE L 83 5 5 HELIX 16 AB7 SER L 121 LYS L 126 1 6 HELIX 17 AB8 LYS L 183 GLU L 187 1 5 HELIX 18 AB9 GLY B 44 ARG B 54 1 11 HELIX 19 AC1 LEU B 55 SER B 66 1 12 HELIX 20 AC2 GLY B 77 VAL B 81 5 5 HELIX 21 AC3 SER B 89 TRP B 93 5 5 HELIX 22 AC4 SER B 98 LEU B 105 1 8 HELIX 23 AC5 PRO B 169 ASP B 171 5 3 HELIX 24 AC6 PRO B 188 PHE B 203 1 16 HELIX 25 AC7 SER B 253 LYS B 255 5 3 HELIX 26 AC8 SER B 268 GLY B 279 1 12 HELIX 27 AC9 ASP B 284 ALA B 291 1 8 HELIX 28 AD1 ILE C 28 TYR C 32 5 5 HELIX 29 AD2 ARG C 87 THR C 91 5 5 HELIX 30 AD3 SER C 164 ALA C 166 5 3 HELIX 31 AD4 LYS C 209 ASN C 212 5 4 HELIX 32 AD5 GLN D 79 ILE D 83 5 5 HELIX 33 AD6 LYS D 183 LYS D 188 1 6 SHEET 1 AA1 2 TYR A 71 VAL A 72 0 SHEET 2 AA1 2 LEU A 167 LEU A 168 1 O LEU A 168 N TYR A 71 SHEET 1 AA2 5 SER A 82 TYR A 84 0 SHEET 2 AA2 5 VAL A 173 ILE A 176 1 O TRP A 175 N SER A 82 SHEET 3 AA2 5 PHE A 130 THR A 135 1 N GLU A 132 O ILE A 176 SHEET 4 AA2 5 GLY A 138 GLY A 143 -1 O GLY A 138 N THR A 135 SHEET 5 AA2 5 VAL A 110 LYS A 112 1 N LYS A 111 O TYR A 139 SHEET 1 AA3 2 LYS A 148 ARG A 150 0 SHEET 2 AA3 2 CYS A 157 SER A 159 -1 O SER A 158 N SER A 149 SHEET 1 AA4 4 ASP A 178 CYS A 181 0 SHEET 2 AA4 4 CYS A 328 LEU A 338 -1 O TYR A 329 N ALA A 180 SHEET 3 AA4 4 ILE A 206 ILE A 209 -1 N CYS A 207 O THR A 337 SHEET 4 AA4 4 ILE A 212 VAL A 213 -1 O ILE A 212 N ILE A 209 SHEET 1 AA5 4 ASP A 178 CYS A 181 0 SHEET 2 AA5 4 CYS A 328 LEU A 338 -1 O TYR A 329 N ALA A 180 SHEET 3 AA5 4 GLN A 224 ASP A 232 -1 N PHE A 226 O MET A 334 SHEET 4 AA5 4 ILE A 239 MET A 241 -1 O MET A 241 N ALA A 229 SHEET 1 AA6 3 LYS A 245 VAL A 249 0 SHEET 2 AA6 3 GLU A 314 TYR A 319 -1 O GLU A 314 N VAL A 249 SHEET 3 AA6 3 MET A 322 VAL A 324 -1 O VAL A 324 N VAL A 317 SHEET 1 AA7 4 GLY A 265 PRO A 266 0 SHEET 2 AA7 4 PHE A 257 LYS A 261 -1 N LYS A 261 O GLY A 265 SHEET 3 AA7 4 CYS A 304 LEU A 308 -1 O ARG A 305 N TYR A 260 SHEET 4 AA7 4 ARG A 282 GLY A 283 1 N ARG A 282 O CYS A 306 SHEET 1 AA8 4 GLN H 3 SER H 7 0 SHEET 2 AA8 4 LEU H 18 SER H 25 -1 O ALA H 23 N LEU H 5 SHEET 3 AA8 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA8 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AA9 6 LEU H 11 VAL H 12 0 SHEET 2 AA9 6 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AA9 6 ALA H 92 LYS H 98 -1 N TYR H 94 O THR H 115 SHEET 4 AA9 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA9 6 GLU H 46 ILE H 51 -1 O SER H 49 N TRP H 36 SHEET 6 AA9 6 THR H 58 TYR H 60 -1 O TYR H 59 N ALA H 50 SHEET 1 AB1 4 LEU H 11 VAL H 12 0 SHEET 2 AB1 4 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AB1 4 ALA H 92 LYS H 98 -1 N TYR H 94 O THR H 115 SHEET 4 AB1 4 ASP H 110 TRP H 111 -1 O ASP H 110 N LYS H 98 SHEET 1 AB2 4 SER H 128 LEU H 132 0 SHEET 2 AB2 4 ALA H 144 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AB2 4 TYR H 184 VAL H 192 -1 O TYR H 184 N TYR H 153 SHEET 4 AB2 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 189 SHEET 1 AB3 4 SER H 128 LEU H 132 0 SHEET 2 AB3 4 ALA H 144 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AB3 4 TYR H 184 VAL H 192 -1 O TYR H 184 N TYR H 153 SHEET 4 AB3 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 185 SHEET 1 AB4 3 THR H 159 TRP H 162 0 SHEET 2 AB4 3 ILE H 203 HIS H 208 -1 O ASN H 205 N SER H 161 SHEET 3 AB4 3 THR H 213 ARG H 218 -1 O THR H 213 N HIS H 208 SHEET 1 AB5 4 MET L 4 SER L 7 0 SHEET 2 AB5 4 VAL L 19 ALA L 25 -1 O GLN L 24 N THR L 5 SHEET 3 AB5 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21 SHEET 4 AB5 4 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AB6 6 SER L 10 SER L 14 0 SHEET 2 AB6 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AB6 6 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AB6 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AB6 6 LYS L 45 PHE L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB6 6 ASN L 53 LEU L 54 -1 O ASN L 53 N PHE L 49 SHEET 1 AB7 4 SER L 10 SER L 14 0 SHEET 2 AB7 4 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AB7 4 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AB7 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB8 4 SER L 114 PHE L 118 0 SHEET 2 AB8 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB8 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB8 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB9 4 ALA L 153 LEU L 154 0 SHEET 2 AB9 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB9 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AB9 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AC1 2 TYR B 71 VAL B 72 0 SHEET 2 AC1 2 LEU B 167 LEU B 168 1 O LEU B 168 N TYR B 71 SHEET 1 AC2 5 SER B 82 TYR B 84 0 SHEET 2 AC2 5 VAL B 173 ILE B 176 1 O TRP B 175 N SER B 82 SHEET 3 AC2 5 PHE B 130 PRO B 134 1 N PHE B 130 O LEU B 174 SHEET 4 AC2 5 TYR B 139 GLY B 143 -1 O TRP B 142 N PHE B 131 SHEET 5 AC2 5 LYS B 111 LYS B 112 1 N LYS B 111 O GLY B 141 SHEET 1 AC3 2 LYS B 148 ARG B 150 0 SHEET 2 AC3 2 CYS B 157 SER B 159 -1 O SER B 158 N SER B 149 SHEET 1 AC4 4 ASP B 178 CYS B 181 0 SHEET 2 AC4 4 CYS B 328 LEU B 338 -1 O TYR B 329 N ALA B 180 SHEET 3 AC4 4 ILE B 206 ILE B 209 -1 N CYS B 207 O THR B 337 SHEET 4 AC4 4 ILE B 212 VAL B 213 -1 O ILE B 212 N ILE B 209 SHEET 1 AC5 3 ASP B 178 CYS B 181 0 SHEET 2 AC5 3 CYS B 328 LEU B 338 -1 O TYR B 329 N ALA B 180 SHEET 3 AC5 3 GLN B 224 ASP B 232 -1 N PHE B 226 O MET B 334 SHEET 1 AC6 3 LYS B 245 VAL B 249 0 SHEET 2 AC6 3 GLU B 314 TYR B 319 -1 O GLU B 314 N VAL B 249 SHEET 3 AC6 3 MET B 322 VAL B 324 -1 O VAL B 324 N VAL B 317 SHEET 1 AC7 4 GLY B 265 PRO B 266 0 SHEET 2 AC7 4 PHE B 257 LYS B 261 -1 N LYS B 261 O GLY B 265 SHEET 3 AC7 4 ARG B 305 LEU B 308 -1 O ARG B 305 N TYR B 260 SHEET 4 AC7 4 ARG B 282 GLY B 283 1 N ARG B 282 O CYS B 306 SHEET 1 AC8 4 GLN C 3 SER C 7 0 SHEET 2 AC8 4 LEU C 18 SER C 25 -1 O ALA C 23 N LEU C 5 SHEET 3 AC8 4 THR C 78 MET C 83 -1 O LEU C 79 N CYS C 22 SHEET 4 AC8 4 PHE C 68 ASP C 73 -1 N SER C 71 O TYR C 80 SHEET 1 AC9 6 LEU C 11 VAL C 12 0 SHEET 2 AC9 6 THR C 115 VAL C 119 1 O THR C 118 N VAL C 12 SHEET 3 AC9 6 ALA C 92 LYS C 98 -1 N TYR C 94 O THR C 115 SHEET 4 AC9 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AC9 6 LEU C 45 ILE C 51 -1 O SER C 49 N TRP C 36 SHEET 6 AC9 6 THR C 58 TYR C 60 -1 O TYR C 59 N ALA C 50 SHEET 1 AD1 4 LEU C 11 VAL C 12 0 SHEET 2 AD1 4 THR C 115 VAL C 119 1 O THR C 118 N VAL C 12 SHEET 3 AD1 4 ALA C 92 LYS C 98 -1 N TYR C 94 O THR C 115 SHEET 4 AD1 4 ASP C 110 TRP C 111 -1 O ASP C 110 N LYS C 98 SHEET 1 AD2 4 SER C 128 LEU C 132 0 SHEET 2 AD2 4 ALA C 144 TYR C 153 -1 O LEU C 149 N PHE C 130 SHEET 3 AD2 4 TYR C 184 VAL C 192 -1 O TYR C 184 N TYR C 153 SHEET 4 AD2 4 HIS C 172 THR C 173 -1 N HIS C 172 O VAL C 189 SHEET 1 AD3 4 SER C 128 LEU C 132 0 SHEET 2 AD3 4 ALA C 144 TYR C 153 -1 O LEU C 149 N PHE C 130 SHEET 3 AD3 4 TYR C 184 VAL C 192 -1 O TYR C 184 N TYR C 153 SHEET 4 AD3 4 VAL C 177 LEU C 178 -1 N VAL C 177 O SER C 185 SHEET 1 AD4 3 THR C 159 TRP C 162 0 SHEET 2 AD4 3 TYR C 202 HIS C 208 -1 O ASN C 205 N SER C 161 SHEET 3 AD4 3 THR C 213 VAL C 219 -1 O THR C 213 N HIS C 208 SHEET 1 AD5 4 MET D 4 SER D 7 0 SHEET 2 AD5 4 VAL D 19 ALA D 25 -1 O GLN D 24 N THR D 5 SHEET 3 AD5 4 ASP D 70 ILE D 75 -1 O PHE D 73 N ILE D 21 SHEET 4 AD5 4 PHE D 62 GLY D 66 -1 N SER D 65 O THR D 72 SHEET 1 AD6 6 SER D 10 SER D 14 0 SHEET 2 AD6 6 THR D 102 LYS D 107 1 O GLU D 105 N LEU D 11 SHEET 3 AD6 6 ALA D 84 GLN D 90 -1 N ALA D 84 O LEU D 104 SHEET 4 AD6 6 LEU D 33 GLN D 38 -1 N ASN D 34 O GLN D 89 SHEET 5 AD6 6 LYS D 45 PHE D 49 -1 O ILE D 48 N TRP D 35 SHEET 6 AD6 6 ASN D 53 LEU D 54 -1 O ASN D 53 N PHE D 49 SHEET 1 AD7 4 SER D 10 SER D 14 0 SHEET 2 AD7 4 THR D 102 LYS D 107 1 O GLU D 105 N LEU D 11 SHEET 3 AD7 4 ALA D 84 GLN D 90 -1 N ALA D 84 O LEU D 104 SHEET 4 AD7 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AD8 4 SER D 114 PHE D 118 0 SHEET 2 AD8 4 THR D 129 PHE D 139 -1 O VAL D 133 N PHE D 118 SHEET 3 AD8 4 TYR D 173 SER D 182 -1 O LEU D 181 N ALA D 130 SHEET 4 AD8 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178 SHEET 1 AD9 3 LYS D 145 VAL D 150 0 SHEET 2 AD9 3 VAL D 191 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 3 AD9 3 VAL D 205 ASN D 210 -1 O VAL D 205 N VAL D 196 SSBOND 1 CYS A 27 CYS A 50 1555 1555 2.03 SSBOND 2 CYS A 144 CYS A 157 1555 1555 2.04 SSBOND 3 CYS A 181 CYS A 328 1555 1555 2.04 SSBOND 4 CYS A 207 CYS A 217 1555 1555 2.02 SSBOND 5 CYS A 259 CYS A 306 1555 1555 2.03 SSBOND 6 CYS A 267 CYS A 304 1555 1555 2.03 SSBOND 7 CYS A 275 CYS A 281 1555 1555 2.03 SSBOND 8 CYS A 288 CYS A 293 1555 1555 2.03 SSBOND 9 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 10 CYS H 148 CYS H 204 1555 1555 2.03 SSBOND 11 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 12 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 13 CYS B 27 CYS B 50 1555 1555 2.03 SSBOND 14 CYS B 144 CYS B 157 1555 1555 2.04 SSBOND 15 CYS B 181 CYS B 328 1555 1555 2.04 SSBOND 16 CYS B 207 CYS B 217 1555 1555 2.02 SSBOND 17 CYS B 259 CYS B 306 1555 1555 2.04 SSBOND 18 CYS B 267 CYS B 304 1555 1555 2.03 SSBOND 19 CYS B 275 CYS B 281 1555 1555 2.03 SSBOND 20 CYS B 288 CYS B 293 1555 1555 2.03 SSBOND 21 CYS C 22 CYS C 96 1555 1555 2.04 SSBOND 22 CYS C 148 CYS C 204 1555 1555 2.03 SSBOND 23 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 24 CYS D 134 CYS D 194 1555 1555 2.03 LINK ND2 ASN A 34 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN A 64 C1 NAG F 1 1555 1555 1.43 LINK ND2 ASN B 34 C1 NAG B 401 1555 1555 1.44 LINK ND2 ASN B 64 C1 NAG G 1 1555 1555 1.43 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.43 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.43 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.44 CISPEP 1 TYR A 84 PRO A 85 0 -2.21 CISPEP 2 PHE H 154 PRO H 155 0 -1.28 CISPEP 3 GLU H 156 PRO H 157 0 0.37 CISPEP 4 SER L 7 PRO L 8 0 -4.40 CISPEP 5 TYR L 140 PRO L 141 0 1.91 CISPEP 6 TYR B 84 PRO B 85 0 1.70 CISPEP 7 PHE C 154 PRO C 155 0 -2.26 CISPEP 8 GLU C 156 PRO C 157 0 0.09 CISPEP 9 SER D 7 PRO D 8 0 -4.67 CISPEP 10 TYR D 140 PRO D 141 0 -0.09 CRYST1 96.064 82.342 125.293 90.00 104.31 90.00 P 1 21 1 4 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 0.010410 0.000000 0.002655 0.00000 SCALE2 0.000000 0.012144 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008237 0.00000