HEADER VIRAL PROTEIN 28-JUL-22 8DV6 TITLE ZIKA VIRUS ENVELOPE PROTEIN STRUCTURE IN COMPLEX WITH A POTENT HUMAN TITLE 2 MAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE PROTEIN E; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MAB FAB HEAVY CHAIN; COMPND 7 CHAIN: C, H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MAB FAB LIGHT CHAIN; COMPND 11 CHAIN: D, L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ZIKA VIRUS ZIKV/HUMAN/CAMBODIA/FSS13025/2010; SOURCE 3 ORGANISM_COMMON: ZIKV; SOURCE 4 ORGANISM_TAXID: 2316109; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ZIKA VIRUS, ENVELOPE PROTEIN, NEUTRALIZING ANTIBODY, NEUTRALIZATION KEYWDS 2 MECHANISM, FLAVIVIRUS, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM KEYWDS 3 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR A.CAMERON,A.C.PUHL,A.M.DESILVA,L.PREMKUMAR JRNL AUTH A.CAMERON,A.C.PUHL,A.M.DESILVA,L.PREMKUMAR JRNL TITL ZIKA VIRUS ENVELOPE PROTEIN STRUCTRE IN COMPLEX WITH A JRNL TITL 2 POTENT HUMAN MAB TARGETING JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.38 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.17.1_3660 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) : 3.38 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.57 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 35167 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.234 REMARK 3 R VALUE (WORKING SET) : 0.232 REMARK 3 FREE R VALUE : 0.259 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800 REMARK 3 FREE R VALUE TEST SET COUNT : 1689 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 45.5700 - 7.7300 1.00 2866 147 0.1773 0.2064 REMARK 3 2 7.7300 - 6.1400 1.00 2844 129 0.2253 0.2525 REMARK 3 3 6.1400 - 5.3600 1.00 2807 147 0.2178 0.2421 REMARK 3 4 5.3600 - 4.8700 1.00 2792 137 0.2031 0.2307 REMARK 3 5 4.8700 - 4.5200 1.00 2779 151 0.2006 0.2129 REMARK 3 6 4.5200 - 4.2600 1.00 2823 146 0.2262 0.2517 REMARK 3 7 4.2600 - 4.0400 1.00 2782 133 0.2553 0.2935 REMARK 3 8 4.0400 - 3.8700 1.00 2804 129 0.2744 0.2850 REMARK 3 9 3.8700 - 3.7200 1.00 2774 153 0.3052 0.3611 REMARK 3 10 3.7200 - 3.5900 1.00 2827 125 0.3308 0.3986 REMARK 3 11 3.5900 - 3.4800 1.00 2770 153 0.3217 0.3146 REMARK 3 12 3.4800 - 3.3800 0.94 2610 139 0.3468 0.3558 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) : 0.433 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.763 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 95.67 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 120.6 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 13136 REMARK 3 ANGLE : 0.619 17856 REMARK 3 CHIRALITY : 0.044 1993 REMARK 3 PLANARITY : 0.004 2299 REMARK 3 DIHEDRAL : 5.162 1815 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN A AND RESID 1:405 ) REMARK 3 ORIGIN FOR THE GROUP (A): -75.404 -20.031 35.704 REMARK 3 T TENSOR REMARK 3 T11: 0.5800 T22: 0.8114 REMARK 3 T33: 0.6871 T12: -0.0763 REMARK 3 T13: -0.1508 T23: -0.2053 REMARK 3 L TENSOR REMARK 3 L11: 2.7332 L22: 3.2926 REMARK 3 L33: 3.9444 L12: 2.3049 REMARK 3 L13: -3.0238 L23: -3.1490 REMARK 3 S TENSOR REMARK 3 S11: -0.0106 S12: 0.4104 S13: 0.1193 REMARK 3 S21: -0.2605 S22: 0.3358 S23: -0.0653 REMARK 3 S31: 0.0669 S32: -0.1700 S33: -0.2881 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN B AND RESID 1:405 ) REMARK 3 ORIGIN FOR THE GROUP (A): -96.023 -32.395 85.408 REMARK 3 T TENSOR REMARK 3 T11: 1.2324 T22: 1.1448 REMARK 3 T33: 0.7421 T12: 0.1596 REMARK 3 T13: -0.0653 T23: -0.1829 REMARK 3 L TENSOR REMARK 3 L11: 1.0786 L22: 2.8621 REMARK 3 L33: 3.7607 L12: 0.5175 REMARK 3 L13: -0.7181 L23: -2.1466 REMARK 3 S TENSOR REMARK 3 S11: 0.0396 S12: -0.7243 S13: 0.1702 REMARK 3 S21: 1.2066 S22: 0.0980 S23: -0.0101 REMARK 3 S31: -0.1425 S32: -0.0980 S33: -0.1004 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN C AND RESID 1:231 ) REMARK 3 ORIGIN FOR THE GROUP (A): -109.243 -21.405 20.276 REMARK 3 T TENSOR REMARK 3 T11: 0.8858 T22: 1.1956 REMARK 3 T33: 1.4306 T12: 0.0107 REMARK 3 T13: 0.2330 T23: -0.5722 REMARK 3 L TENSOR REMARK 3 L11: 4.5948 L22: 0.9016 REMARK 3 L33: 2.2506 L12: 1.4158 REMARK 3 L13: 1.6239 L23: 0.8254 REMARK 3 S TENSOR REMARK 3 S11: -0.0747 S12: 1.6176 S13: -1.1606 REMARK 3 S21: -0.2748 S22: 0.1669 S23: -0.1958 REMARK 3 S31: 0.4715 S32: 0.2453 S33: -0.1137 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN D AND RESID 2:213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -137.174 -35.730 57.128 REMARK 3 T TENSOR REMARK 3 T11: 0.5089 T22: 0.6212 REMARK 3 T33: 1.2211 T12: 0.0124 REMARK 3 T13: -0.0591 T23: -0.0160 REMARK 3 L TENSOR REMARK 3 L11: 5.5440 L22: 1.6498 REMARK 3 L33: 1.1796 L12: 0.4344 REMARK 3 L13: -0.4883 L23: -0.2984 REMARK 3 S TENSOR REMARK 3 S11: 0.0655 S12: 0.3571 S13: 1.5913 REMARK 3 S21: 0.1222 S22: -0.0107 S23: 0.8579 REMARK 3 S31: -0.1131 S32: -0.4918 S33: -0.0644 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN H AND RESID 1:229 ) REMARK 3 ORIGIN FOR THE GROUP (A): -129.588 -31.030 73.015 REMARK 3 T TENSOR REMARK 3 T11: 0.7225 T22: 0.8566 REMARK 3 T33: 1.0867 T12: 0.0555 REMARK 3 T13: -0.0697 T23: -0.3432 REMARK 3 L TENSOR REMARK 3 L11: 7.4203 L22: 0.3192 REMARK 3 L33: 0.8782 L12: -0.6169 REMARK 3 L13: 0.4968 L23: -0.6666 REMARK 3 S TENSOR REMARK 3 S11: -0.2785 S12: -1.2604 S13: 1.3214 REMARK 3 S21: 0.3918 S22: 0.1712 S23: 0.3455 REMARK 3 S31: -0.3920 S32: -0.3071 S33: 0.1028 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: ( CHAIN L AND RESID 2:213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -125.392 -16.332 26.506 REMARK 3 T TENSOR REMARK 3 T11: 0.8002 T22: 0.7792 REMARK 3 T33: 1.0515 T12: -0.0939 REMARK 3 T13: 0.1332 T23: -0.4304 REMARK 3 L TENSOR REMARK 3 L11: 3.5987 L22: 1.3345 REMARK 3 L33: 1.9723 L12: -0.2040 REMARK 3 L13: 0.2988 L23: 0.7638 REMARK 3 S TENSOR REMARK 3 S11: -0.1492 S12: 0.8523 S13: -0.9173 REMARK 3 S21: -0.3744 S22: -0.2488 S23: 0.1195 REMARK 3 S31: 0.2828 S32: -0.4814 S33: 0.2608 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 3 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: (CHAIN 'A' AND (RESID 1 THROUGH 184 OR REMARK 3 RESID 186 THROUGH 405)) REMARK 3 SELECTION : (CHAIN 'B' AND (RESID 1 THROUGH 184 OR REMARK 3 RESID 186 THROUGH 405)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: (CHAIN 'C' AND RESID 1 THROUGH 230) REMARK 3 SELECTION : CHAIN 'H' REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : 3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN 'D' REMARK 3 SELECTION : CHAIN 'L' REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8DV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000267425. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-NOV-17 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 : 22-BM REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35195 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.380 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 (%) : 99.4 REMARK 200 DATA REDUNDANCY : 7.500 REMARK 200 R MERGE (I) : 0.17700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.38 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.46 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 7.00 REMARK 200 R MERGE FOR SHELL (I) : 1.43400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 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: 5JHM REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.78 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, HEPES, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K 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 66.80450 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, H, 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 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 SER A 406 REMARK 465 GLY A 407 REMARK 465 GLY A 408 REMARK 465 SER A 409 REMARK 465 HIS A 410 REMARK 465 HIS A 411 REMARK 465 HIS A 412 REMARK 465 HIS A 413 REMARK 465 HIS A 414 REMARK 465 HIS A 415 REMARK 465 SER B 406 REMARK 465 GLY B 407 REMARK 465 GLY B 408 REMARK 465 SER B 409 REMARK 465 HIS B 410 REMARK 465 HIS B 411 REMARK 465 HIS B 412 REMARK 465 HIS B 413 REMARK 465 HIS B 414 REMARK 465 HIS B 415 REMARK 465 ASP C 232 REMARK 465 LYS C 233 REMARK 465 THR C 234 REMARK 465 HIS C 235 REMARK 465 HIS C 236 REMARK 465 HIS C 237 REMARK 465 HIS C 238 REMARK 465 HIS C 239 REMARK 465 HIS C 240 REMARK 465 GLN D 1 REMARK 465 GLU D 214 REMARK 465 CYS D 215 REMARK 465 SER D 216 REMARK 465 CYS H 231 REMARK 465 ASP H 232 REMARK 465 LYS H 233 REMARK 465 THR H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 HIS H 237 REMARK 465 HIS H 238 REMARK 465 HIS H 239 REMARK 465 HIS H 240 REMARK 465 GLN L 1 REMARK 465 GLU L 214 REMARK 465 CYS L 215 REMARK 465 SER L 216 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 ARG A 2 178.88 -58.92 REMARK 500 CYS A 3 -38.83 79.03 REMARK 500 MET A 15 -128.80 -116.83 REMARK 500 THR A 19 -49.98 65.75 REMARK 500 VAL A 56 -57.59 -130.36 REMARK 500 GLN A 77 42.19 -103.99 REMARK 500 ASN A 134 35.04 -88.26 REMARK 500 SER A 146 -176.39 -172.61 REMARK 500 GLN A 147 179.61 64.85 REMARK 500 HIS A 148 -40.98 -145.30 REMARK 500 MET A 151 -123.35 -89.62 REMARK 500 ASP A 161 -131.62 55.99 REMARK 500 GLU A 162 -71.13 65.76 REMARK 500 SER A 173 68.65 -153.06 REMARK 500 ASP A 230 -66.13 68.12 REMARK 500 ASP A 247 168.91 71.78 REMARK 500 ALA A 248 59.58 -153.47 REMARK 500 GLN A 253 -166.12 -104.62 REMARK 500 ALA A 268 45.16 -78.53 REMARK 500 MET A 277 83.18 -151.27 REMARK 500 HIS A 288 148.42 -179.09 REMARK 500 PRO A 354 97.59 -66.50 REMARK 500 ASN A 362 87.63 37.66 REMARK 500 LYS A 394 38.26 -77.98 REMARK 500 ARG B 2 178.54 -59.32 REMARK 500 CYS B 3 -39.14 79.19 REMARK 500 MET B 15 -127.66 -117.13 REMARK 500 THR B 19 -49.86 61.19 REMARK 500 VAL B 56 -57.40 -130.27 REMARK 500 GLN B 77 41.35 -103.09 REMARK 500 ASN B 134 37.19 -85.09 REMARK 500 SER B 146 108.30 -172.74 REMARK 500 GLN B 147 -164.45 62.21 REMARK 500 HIS B 148 -39.70 -137.24 REMARK 500 MET B 151 -126.17 -88.36 REMARK 500 THR B 156 35.02 -98.29 REMARK 500 ASP B 161 -129.14 53.55 REMARK 500 GLU B 162 -71.48 64.32 REMARK 500 SER B 173 69.28 -152.02 REMARK 500 ASP B 247 169.55 72.75 REMARK 500 ALA B 248 61.49 -153.02 REMARK 500 GLN B 253 -165.80 -104.10 REMARK 500 ALA B 268 46.68 -77.57 REMARK 500 LEU B 269 -27.52 -141.43 REMARK 500 MET B 277 80.58 -154.24 REMARK 500 HIS B 288 146.60 -178.78 REMARK 500 PRO B 354 97.37 -66.60 REMARK 500 ASN B 362 86.53 43.93 REMARK 500 LYS B 394 37.70 -76.56 REMARK 500 ARG C 16 -141.81 -127.40 REMARK 500 REMARK 500 THIS ENTRY HAS 93 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF1 8DV6 A 1 405 UNP A0A384KMW4_ZIKV DBREF2 8DV6 A A0A384KMW4 291 695 DBREF1 8DV6 B 1 405 UNP A0A384KMW4_ZIKV DBREF2 8DV6 B A0A384KMW4 291 695 DBREF 8DV6 C 1 240 PDB 8DV6 8DV6 1 240 DBREF 8DV6 D 1 216 PDB 8DV6 8DV6 1 216 DBREF 8DV6 H 1 240 PDB 8DV6 8DV6 1 240 DBREF 8DV6 L 1 216 PDB 8DV6 8DV6 1 216 SEQADV 8DV6 SER A 406 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 GLY A 407 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 GLY A 408 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 SER A 409 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS A 410 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS A 411 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS A 412 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS A 413 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS A 414 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS A 415 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 SER B 406 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 GLY B 407 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 GLY B 408 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 SER B 409 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS B 410 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS B 411 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS B 412 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS B 413 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS B 414 UNP A0A384KMW EXPRESSION TAG SEQADV 8DV6 HIS B 415 UNP A0A384KMW EXPRESSION TAG SEQRES 1 A 415 ILE ARG CYS ILE GLY VAL SER ASN ARG ASP PHE VAL GLU SEQRES 2 A 415 GLY MET SER GLY GLY THR TRP VAL ASP VAL VAL LEU GLU SEQRES 3 A 415 HIS GLY GLY CYS VAL THR VAL MET ALA GLN ASP LYS PRO SEQRES 4 A 415 THR VAL ASP ILE GLU LEU VAL THR THR THR VAL SER ASN SEQRES 5 A 415 MET ALA GLU VAL ARG SER TYR CYS TYR GLU ALA SER ILE SEQRES 6 A 415 SER ASP MET ALA SER ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 A 415 GLU ALA TYR LEU ASP LYS GLN SER ASP THR GLN TYR VAL SEQRES 8 A 415 CYS LYS ARG THR LEU VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 A 415 CYS GLY LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA SEQRES 10 A 415 LYS PHE ALA CYS SER LYS LYS MET THR GLY LYS SER ILE SEQRES 11 A 415 GLN PRO GLU ASN LEU GLU TYR ARG ILE MET LEU SER VAL SEQRES 12 A 415 HIS GLY SER GLN HIS SER GLY MET ILE VAL ASN ASP THR SEQRES 13 A 415 GLY HIS GLU THR ASP GLU ASN ARG ALA LYS VAL GLU ILE SEQRES 14 A 415 THR PRO ASN SER PRO ARG ALA GLU ALA THR LEU GLY GLY SEQRES 15 A 415 PHE GLY SER LEU GLY LEU ASP CYS GLU PRO ARG THR GLY SEQRES 16 A 415 LEU ASP PHE SER ASP LEU TYR TYR LEU THR MET ASN ASN SEQRES 17 A 415 LYS HIS TRP LEU VAL HIS LYS GLU TRP PHE HIS ASP ILE SEQRES 18 A 415 PRO LEU PRO TRP HIS ALA GLY ALA ASP THR GLY THR PRO SEQRES 19 A 415 HIS TRP ASN ASN LYS GLU ALA LEU VAL GLU PHE LYS ASP SEQRES 20 A 415 ALA HIS ALA LYS ARG GLN THR VAL VAL VAL LEU GLY SER SEQRES 21 A 415 GLN GLU GLY ALA VAL HIS THR ALA LEU ALA GLY ALA LEU SEQRES 22 A 415 GLU ALA GLU MET ASP GLY ALA LYS GLY ARG LEU SER SER SEQRES 23 A 415 GLY HIS LEU LYS CYS ARG LEU LYS MET ASP LYS LEU ARG SEQRES 24 A 415 LEU LYS GLY VAL SER TYR SER LEU CYS THR ALA ALA PHE SEQRES 25 A 415 THR PHE THR LYS ILE PRO ALA GLU THR LEU HIS GLY THR SEQRES 26 A 415 VAL THR VAL GLU VAL GLN TYR ALA GLY THR ASP GLY PRO SEQRES 27 A 415 CYS LYS VAL PRO ALA GLN MET ALA VAL ASP MET GLN THR SEQRES 28 A 415 LEU THR PRO VAL GLY ARG LEU ILE THR ALA ASN PRO VAL SEQRES 29 A 415 ILE THR GLU SER THR GLU ASN SER LYS MET MET LEU GLU SEQRES 30 A 415 LEU ASP PRO PRO PHE GLY ASP SER TYR ILE VAL ILE GLY SEQRES 31 A 415 VAL GLY GLU LYS LYS ILE THR HIS HIS TRP HIS ARG SER SEQRES 32 A 415 GLY SER SER GLY GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 415 ILE ARG CYS ILE GLY VAL SER ASN ARG ASP PHE VAL GLU SEQRES 2 B 415 GLY MET SER GLY GLY THR TRP VAL ASP VAL VAL LEU GLU SEQRES 3 B 415 HIS GLY GLY CYS VAL THR VAL MET ALA GLN ASP LYS PRO SEQRES 4 B 415 THR VAL ASP ILE GLU LEU VAL THR THR THR VAL SER ASN SEQRES 5 B 415 MET ALA GLU VAL ARG SER TYR CYS TYR GLU ALA SER ILE SEQRES 6 B 415 SER ASP MET ALA SER ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 B 415 GLU ALA TYR LEU ASP LYS GLN SER ASP THR GLN TYR VAL SEQRES 8 B 415 CYS LYS ARG THR LEU VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 B 415 CYS GLY LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA SEQRES 10 B 415 LYS PHE ALA CYS SER LYS LYS MET THR GLY LYS SER ILE SEQRES 11 B 415 GLN PRO GLU ASN LEU GLU TYR ARG ILE MET LEU SER VAL SEQRES 12 B 415 HIS GLY SER GLN HIS SER GLY MET ILE VAL ASN ASP THR SEQRES 13 B 415 GLY HIS GLU THR ASP GLU ASN ARG ALA LYS VAL GLU ILE SEQRES 14 B 415 THR PRO ASN SER PRO ARG ALA GLU ALA THR LEU GLY GLY SEQRES 15 B 415 PHE GLY SER LEU GLY LEU ASP CYS GLU PRO ARG THR GLY SEQRES 16 B 415 LEU ASP PHE SER ASP LEU TYR TYR LEU THR MET ASN ASN SEQRES 17 B 415 LYS HIS TRP LEU VAL HIS LYS GLU TRP PHE HIS ASP ILE SEQRES 18 B 415 PRO LEU PRO TRP HIS ALA GLY ALA ASP THR GLY THR PRO SEQRES 19 B 415 HIS TRP ASN ASN LYS GLU ALA LEU VAL GLU PHE LYS ASP SEQRES 20 B 415 ALA HIS ALA LYS ARG GLN THR VAL VAL VAL LEU GLY SER SEQRES 21 B 415 GLN GLU GLY ALA VAL HIS THR ALA LEU ALA GLY ALA LEU SEQRES 22 B 415 GLU ALA GLU MET ASP GLY ALA LYS GLY ARG LEU SER SER SEQRES 23 B 415 GLY HIS LEU LYS CYS ARG LEU LYS MET ASP LYS LEU ARG SEQRES 24 B 415 LEU LYS GLY VAL SER TYR SER LEU CYS THR ALA ALA PHE SEQRES 25 B 415 THR PHE THR LYS ILE PRO ALA GLU THR LEU HIS GLY THR SEQRES 26 B 415 VAL THR VAL GLU VAL GLN TYR ALA GLY THR ASP GLY PRO SEQRES 27 B 415 CYS LYS VAL PRO ALA GLN MET ALA VAL ASP MET GLN THR SEQRES 28 B 415 LEU THR PRO VAL GLY ARG LEU ILE THR ALA ASN PRO VAL SEQRES 29 B 415 ILE THR GLU SER THR GLU ASN SER LYS MET MET LEU GLU SEQRES 30 B 415 LEU ASP PRO PRO PHE GLY ASP SER TYR ILE VAL ILE GLY SEQRES 31 B 415 VAL GLY GLU LYS LYS ILE THR HIS HIS TRP HIS ARG SER SEQRES 32 B 415 GLY SER SER GLY GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 C 240 ARG VAL HIS LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 C 240 PRO GLY ARG SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 C 240 PHE ALA PHE SER ASN TYR HIS MET HIS TRP VAL ARG GLN SEQRES 4 C 240 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ILE ILE TRP SEQRES 5 C 240 ASP ASP GLY SER ASP GLN TYR TYR ALA ASP SER VAL LYS SEQRES 6 C 240 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 C 240 LEU PHE LEU GLN MET ASN ARG LEU ARG ALA GLU ASP THR SEQRES 8 C 240 ALA LEU TYR TYR CYS VAL GLY GLY SER SER ALA TYR ASN SEQRES 9 C 240 GLY ASP ASN GLY TRP ARG GLU ALA ALA SER LEU ASP ASP SEQRES 10 C 240 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER SEQRES 11 C 240 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 C 240 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 C 240 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 C 240 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 C 240 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 C 240 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 C 240 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 C 240 VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR SEQRES 19 C 240 HIS HIS HIS HIS HIS HIS SEQRES 1 D 216 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 D 216 PRO GLY GLN SER ILE THR ILE PHE CYS SER GLY SER SER SEQRES 3 D 216 ASN ASP VAL GLY GLY TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 D 216 GLN TYR PRO GLY LYS VAL PRO LYS LEU LEU ILE TYR ASP SEQRES 5 D 216 VAL ASN SER ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 D 216 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 D 216 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 D 216 SER TYR THR SER ARG ARG THR TRP VAL PHE GLY GLY GLY SEQRES 9 D 216 THR ILE VAL THR VAL LEU GLY GLN PRO LYS ALA ASN PRO SEQRES 10 D 216 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 D 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 D 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP GLY SEQRES 13 D 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 D 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 D 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 D 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 D 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 H 240 ARG VAL HIS LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 240 PRO GLY ARG SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 H 240 PHE ALA PHE SER ASN TYR HIS MET HIS TRP VAL ARG GLN SEQRES 4 H 240 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ILE ILE TRP SEQRES 5 H 240 ASP ASP GLY SER ASP GLN TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 240 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 240 LEU PHE LEU GLN MET ASN ARG LEU ARG ALA GLU ASP THR SEQRES 8 H 240 ALA LEU TYR TYR CYS VAL GLY GLY SER SER ALA TYR ASN SEQRES 9 H 240 GLY ASP ASN GLY TRP ARG GLU ALA ALA SER LEU ASP ASP SEQRES 10 H 240 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER SEQRES 11 H 240 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 H 240 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 H 240 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 H 240 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 H 240 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 H 240 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 H 240 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 H 240 VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR SEQRES 19 H 240 HIS HIS HIS HIS HIS HIS SEQRES 1 L 216 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 L 216 PRO GLY GLN SER ILE THR ILE PHE CYS SER GLY SER SER SEQRES 3 L 216 ASN ASP VAL GLY GLY TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 L 216 GLN TYR PRO GLY LYS VAL PRO LYS LEU LEU ILE TYR ASP SEQRES 5 L 216 VAL ASN SER ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 L 216 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 L 216 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 L 216 SER TYR THR SER ARG ARG THR TRP VAL PHE GLY GLY GLY SEQRES 9 L 216 THR ILE VAL THR VAL LEU GLY GLN PRO LYS ALA ASN PRO SEQRES 10 L 216 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 L 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 L 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP GLY SEQRES 13 L 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 L 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 L 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 L 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 L 216 THR VAL ALA PRO THR GLU CYS SER HELIX 1 AA1 LEU A 82 ASP A 87 5 6 HELIX 2 AA2 GLN A 131 GLU A 133 5 3 HELIX 3 AA3 THR A 156 ASP A 161 5 6 HELIX 4 AA4 GLY A 181 PHE A 183 5 3 HELIX 5 AA5 LYS A 215 ASP A 220 1 6 HELIX 6 AA6 ASN A 238 ALA A 241 5 4 HELIX 7 AA7 GLN A 261 ALA A 268 1 8 HELIX 8 AA8 LEU B 82 ASP B 87 5 6 HELIX 9 AA9 GLN B 131 GLU B 133 5 3 HELIX 10 AB1 GLY B 181 PHE B 183 5 3 HELIX 11 AB2 LYS B 215 ASP B 220 1 6 HELIX 12 AB3 ASN B 238 ALA B 241 5 4 HELIX 13 AB4 GLN B 261 ALA B 268 1 8 HELIX 14 AB5 ALA C 28 SER C 30 5 3 HELIX 15 AB6 ASP C 62 LYS C 65 5 4 HELIX 16 AB7 ARG C 87 THR C 91 5 5 HELIX 17 AB8 SER C 171 ALA C 173 5 3 HELIX 18 AB9 GLN D 81 GLU D 85 5 5 HELIX 19 AC1 SER D 125 ALA D 131 1 7 HELIX 20 AC2 THR D 185 HIS D 192 1 8 HELIX 21 AC3 ALA H 28 SER H 30 5 3 HELIX 22 AC4 ASP H 62 LYS H 65 5 4 HELIX 23 AC5 ASN H 74 LYS H 76 5 3 HELIX 24 AC6 ARG H 87 THR H 91 5 5 HELIX 25 AC7 SER H 171 ALA H 173 5 3 HELIX 26 AC8 GLN L 81 GLU L 85 5 5 HELIX 27 AC9 SER L 125 ALA L 131 1 7 HELIX 28 AD1 THR L 185 HIS L 192 1 8 SHEET 1 AA114 ASN A 8 GLU A 13 0 SHEET 2 AA114 GLY A 29 ALA A 35 1 O THR A 32 N ASP A 10 SHEET 3 AA114 LYS A 38 VAL A 50 -1 O VAL A 41 N VAL A 33 SHEET 4 AA114 GLU A 55 ARG A 73 0 SHEET 5 AA114 TYR A 90 ARG A 99 0 SHEET 6 AA114 GLY A 109 LYS A 128 -1 O ALA A 117 N VAL A 91 SHEET 7 AA114 LEU A 135 VAL A 143 -1 O MET A 140 N GLU A 44 SHEET 8 AA114 ALA A 165 ILE A 169 -1 O ALA A 165 N LEU A 141 SHEET 9 AA114 LEU A 201 MET A 206 -1 O TYR A 203 N LYS A 128 SHEET 10 AA114 LYS A 209 HIS A 214 -1 O LYS A 209 N MET A 206 SHEET 11 AA114 TRP A 225 HIS A 226 -1 O HIS A 226 N SER A 58 SHEET 12 AA114 LEU A 273 GLU A 276 -1 O ALA A 275 N HIS A 210 SHEET 13 AA114 GLY A 282 LEU A 284 -1 O ARG A 283 N GLU A 276 SHEET 14 AA114 GLY H 108 ARG H 110 -1 O TRP H 109 N SER A 70 SHEET 1 AA2 4 TRP A 20 LEU A 25 0 SHEET 2 AA2 4 LEU A 289 LYS A 294 -1 O LEU A 293 N VAL A 21 SHEET 3 AA2 4 SER A 185 GLU A 191 -1 N ASP A 189 O ARG A 292 SHEET 4 AA2 4 ARG A 175 THR A 179 -1 N ALA A 178 O LEU A 186 SHEET 1 AA3 2 VAL A 243 LYS A 246 0 SHEET 2 AA3 2 THR A 254 VAL A 257 -1 O THR A 254 N LYS A 246 SHEET 1 AA4 5 PHE A 312 PHE A 314 0 SHEET 2 AA4 5 ALA A 319 GLU A 320 0 SHEET 3 AA4 5 VAL A 326 TYR A 332 -1 O THR A 327 N ALA A 319 SHEET 4 AA4 5 ARG A 357 LEU A 358 0 SHEET 5 AA4 5 SER A 372 ASP A 379 -1 O ASP A 379 N ARG A 357 SHEET 1 AA5 3 ALA A 343 ALA A 346 0 SHEET 2 AA5 3 GLY A 383 ILE A 389 -1 O VAL A 388 N GLN A 344 SHEET 3 AA5 3 ILE A 396 ARG A 402 -1 O HIS A 398 N ILE A 387 SHEET 1 AA614 ASN B 8 GLU B 13 0 SHEET 2 AA614 GLY B 29 ALA B 35 1 O MET B 34 N VAL B 12 SHEET 3 AA614 LYS B 38 VAL B 50 -1 O VAL B 41 N VAL B 33 SHEET 4 AA614 GLU B 55 ARG B 73 0 SHEET 5 AA614 TYR B 90 ARG B 99 0 SHEET 6 AA614 GLY B 109 SER B 129 -1 O ALA B 117 N VAL B 91 SHEET 7 AA614 LEU B 135 VAL B 143 -1 O GLU B 136 N THR B 49 SHEET 8 AA614 ALA B 165 ILE B 169 -1 O ALA B 165 N LEU B 141 SHEET 9 AA614 LEU B 201 THR B 205 -1 O THR B 205 N THR B 126 SHEET 10 AA614 HIS B 210 HIS B 214 -1 O VAL B 213 N TYR B 202 SHEET 11 AA614 TRP B 225 HIS B 226 -1 O HIS B 226 N SER B 58 SHEET 12 AA614 LEU B 273 MET B 277 -1 O LEU B 273 N LEU B 212 SHEET 13 AA614 GLY B 282 LEU B 284 -1 O ARG B 283 N GLU B 276 SHEET 14 AA614 GLY C 108 ARG C 110 -1 O TRP C 109 N SER B 70 SHEET 1 AA7 4 TRP B 20 LEU B 25 0 SHEET 2 AA7 4 LEU B 289 LYS B 294 -1 O LEU B 293 N VAL B 21 SHEET 3 AA7 4 SER B 185 GLU B 191 -1 N ASP B 189 O ARG B 292 SHEET 4 AA7 4 ARG B 175 THR B 179 -1 N ALA B 178 O LEU B 186 SHEET 1 AA8 2 VAL B 243 LYS B 246 0 SHEET 2 AA8 2 THR B 254 VAL B 257 -1 O THR B 254 N LYS B 246 SHEET 1 AA9 4 PHE B 312 GLU B 320 0 SHEET 2 AA9 4 VAL B 326 TYR B 332 -1 O GLN B 331 N THR B 313 SHEET 3 AA9 4 SER B 372 ASP B 379 -1 O MET B 374 N VAL B 330 SHEET 4 AA9 4 ARG B 357 LEU B 358 -1 N ARG B 357 O ASP B 379 SHEET 1 AB1 3 ALA B 343 ALA B 346 0 SHEET 2 AB1 3 GLY B 383 ILE B 389 -1 O VAL B 388 N GLN B 344 SHEET 3 AB1 3 ILE B 396 ARG B 402 -1 O HIS B 398 N ILE B 387 SHEET 1 AB2 4 HIS C 3 SER C 7 0 SHEET 2 AB2 4 SER C 17 SER C 25 -1 O SER C 25 N HIS C 3 SHEET 3 AB2 4 THR C 78 ASN C 84 -1 O MET C 83 N LEU C 18 SHEET 4 AB2 4 PHE C 68 ASP C 73 -1 N THR C 69 O GLN C 82 SHEET 1 AB3 7 GLY C 10 VAL C 11 0 SHEET 2 AB3 7 TYR C 32 GLN C 39 0 SHEET 3 AB3 7 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 4 AB3 7 GLN C 58 TYR C 60 -1 O TYR C 59 N ILE C 50 SHEET 5 AB3 7 ALA C 92 SER C 100 -1 O TYR C 95 N VAL C 37 SHEET 6 AB3 7 ASP C 117 TRP C 118 -1 O ASP C 117 N GLY C 98 SHEET 7 AB3 7 THR C 122 THR C 125 -1 O THR C 122 N TYR C 94 SHEET 1 AB4 5 SER C 135 LEU C 139 0 SHEET 2 AB4 5 THR C 150 TYR C 160 -1 O LEU C 156 N PHE C 137 SHEET 3 AB4 5 VAL C 178 THR C 180 0 SHEET 4 AB4 5 VAL C 184 LEU C 185 0 SHEET 5 AB4 5 TYR C 191 PRO C 200 -1 O SER C 192 N VAL C 184 SHEET 1 AB5 3 THR C 166 TRP C 169 0 SHEET 2 AB5 3 TYR C 209 ASN C 214 -1 O ASN C 212 N SER C 168 SHEET 3 AB5 3 LYS C 225 VAL C 226 -1 O VAL C 226 N TYR C 209 SHEET 1 AB6 6 SER D 9 GLY D 12 0 SHEET 2 AB6 6 SER D 36 GLN D 40 0 SHEET 3 AB6 6 LYS D 47 ILE D 50 -1 O LYS D 47 N GLN D 39 SHEET 4 AB6 6 ALA D 86 TYR D 93 -1 O ASP D 87 N GLN D 40 SHEET 5 AB6 6 TRP D 99 PHE D 101 -1 O VAL D 100 N SER D 92 SHEET 6 AB6 6 THR D 105 VAL D 109 -1 O VAL D 107 N ALA D 86 SHEET 1 AB7 3 ILE D 18 ILE D 20 0 SHEET 2 AB7 3 THR D 72 ILE D 77 -1 O ILE D 77 N ILE D 18 SHEET 3 AB7 3 PHE D 64 SER D 69 -1 N SER D 65 O THR D 76 SHEET 1 AB8 5 THR D 118 PHE D 122 0 SHEET 2 AB8 5 ALA D 134 PHE D 143 -1 O SER D 141 N THR D 118 SHEET 3 AB8 5 VAL D 163 THR D 165 0 SHEET 4 AB8 5 SER D 169 LYS D 170 0 SHEET 5 AB8 5 TYR D 176 LEU D 184 -1 O ALA D 177 N SER D 169 SHEET 1 AB9 3 THR D 149 LYS D 153 0 SHEET 2 AB9 3 TYR D 195 HIS D 201 -1 O GLN D 198 N ALA D 151 SHEET 3 AB9 3 SER D 204 VAL D 210 -1 O SER D 204 N HIS D 201 SHEET 1 AC1 4 HIS H 3 SER H 7 0 SHEET 2 AC1 4 SER H 17 SER H 25 -1 O SER H 25 N HIS H 3 SHEET 3 AC1 4 THR H 78 ASN H 84 -1 O MET H 83 N LEU H 18 SHEET 4 AC1 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AC2 7 GLY H 10 VAL H 11 0 SHEET 2 AC2 7 TYR H 32 GLN H 39 0 SHEET 3 AC2 7 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 4 AC2 7 GLN H 58 TYR H 60 -1 O TYR H 59 N ILE H 50 SHEET 5 AC2 7 ALA H 92 SER H 100 -1 O TYR H 95 N VAL H 37 SHEET 6 AC2 7 ASP H 117 TRP H 118 -1 O ASP H 117 N GLY H 98 SHEET 7 AC2 7 THR H 122 THR H 125 -1 O THR H 122 N TYR H 94 SHEET 1 AC3 5 SER H 135 LEU H 139 0 SHEET 2 AC3 5 THR H 150 TYR H 160 -1 O LEU H 156 N PHE H 137 SHEET 3 AC3 5 VAL H 178 THR H 180 0 SHEET 4 AC3 5 VAL H 184 LEU H 185 0 SHEET 5 AC3 5 TYR H 191 PRO H 200 -1 O SER H 192 N VAL H 184 SHEET 1 AC4 3 THR H 166 TRP H 169 0 SHEET 2 AC4 3 TYR H 209 ASN H 214 -1 O ASN H 212 N SER H 168 SHEET 3 AC4 3 LYS H 225 VAL H 226 -1 O VAL H 226 N TYR H 209 SHEET 1 AC5 6 SER L 9 GLY L 12 0 SHEET 2 AC5 6 SER L 36 GLN L 40 0 SHEET 3 AC5 6 LYS L 47 ILE L 50 -1 O LYS L 47 N GLN L 39 SHEET 4 AC5 6 ALA L 86 TYR L 93 -1 O ASP L 87 N GLN L 40 SHEET 5 AC5 6 TRP L 99 PHE L 101 -1 O VAL L 100 N SER L 92 SHEET 6 AC5 6 THR L 105 VAL L 109 -1 O VAL L 107 N ALA L 86 SHEET 1 AC6 3 ILE L 18 ILE L 20 0 SHEET 2 AC6 3 THR L 72 ILE L 77 -1 O ILE L 77 N ILE L 18 SHEET 3 AC6 3 PHE L 64 SER L 69 -1 N SER L 65 O THR L 76 SHEET 1 AC7 5 THR L 118 PHE L 122 0 SHEET 2 AC7 5 ALA L 134 PHE L 143 -1 O SER L 141 N THR L 118 SHEET 3 AC7 5 VAL L 163 THR L 165 0 SHEET 4 AC7 5 SER L 169 LYS L 170 0 SHEET 5 AC7 5 TYR L 176 LEU L 184 -1 O ALA L 177 N SER L 169 SHEET 1 AC8 3 THR L 149 LYS L 153 0 SHEET 2 AC8 3 TYR L 195 HIS L 201 -1 O GLN L 198 N ALA L 151 SHEET 3 AC8 3 SER L 204 VAL L 210 -1 O SER L 204 N HIS L 201 SSBOND 1 CYS A 3 CYS A 30 1555 1555 2.02 SSBOND 2 CYS A 60 CYS A 121 1555 1555 2.03 SSBOND 3 CYS A 74 CYS A 105 1555 1555 2.03 SSBOND 4 CYS A 92 CYS A 116 1555 1555 2.03 SSBOND 5 CYS A 190 CYS A 291 1555 1555 2.03 SSBOND 6 CYS A 308 CYS A 339 1555 1555 2.03 SSBOND 7 CYS B 3 CYS B 30 1555 1555 2.02 SSBOND 8 CYS B 60 CYS B 121 1555 1555 2.03 SSBOND 9 CYS B 74 CYS B 105 1555 1555 2.03 SSBOND 10 CYS B 92 CYS B 116 1555 1555 2.03 SSBOND 11 CYS B 190 CYS B 291 1555 1555 2.03 SSBOND 12 CYS B 308 CYS B 339 1555 1555 2.03 SSBOND 13 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 14 CYS C 155 CYS C 211 1555 1555 2.03 SSBOND 15 CYS D 22 CYS D 90 1555 1555 2.03 SSBOND 16 CYS D 138 CYS D 197 1555 1555 2.04 SSBOND 17 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 18 CYS H 155 CYS H 211 1555 1555 2.03 SSBOND 19 CYS L 22 CYS L 90 1555 1555 2.03 SSBOND 20 CYS L 138 CYS L 197 1555 1555 2.04 CISPEP 1 ASP A 278 GLY A 279 0 -0.04 CISPEP 2 GLY A 337 PRO A 338 0 -1.12 CISPEP 3 GLY B 228 ALA B 229 0 -12.37 CISPEP 4 ALA B 229 ASP B 230 0 -5.46 CISPEP 5 ASP B 278 GLY B 279 0 0.75 CISPEP 6 GLY B 337 PRO B 338 0 -1.90 CISPEP 7 PHE C 161 PRO C 162 0 -4.94 CISPEP 8 GLU C 163 PRO C 164 0 -3.39 CISPEP 9 TYR D 144 PRO D 145 0 -1.80 CISPEP 10 PHE H 161 PRO H 162 0 -4.71 CISPEP 11 GLU H 163 PRO H 164 0 -2.29 CISPEP 12 TYR L 144 PRO L 145 0 -1.88 CRYST1 95.041 133.609 105.109 90.00 106.49 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 0.010522 0.000000 0.003115 0.00000 SCALE2 0.000000 0.007485 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009922 0.00000