HEADER VIRAL PROTEIN 27-NOV-17 5YVV
TITLE CRYSTAL STRUCTURE OF FULL LENGTH NS3 PROTEIN (GD4NS2BNS3) FROM DENV4
TITLE 2 IN CLOSED CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENOME POLYPROTEIN;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: UNP RESIDUES 1494-2092;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GENOME POLYPROTEIN;
COMPND 9 CHAIN: A;
COMPND 10 FRAGMENT: UNP RESIDUES 1393-1439;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DENGUE VIRUS 4;
SOURCE 3 ORGANISM_TAXID: 11070;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: DENGUE VIRUS 4;
SOURCE 8 ORGANISM_TAXID: 11070;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SERINE PROTEASE, NON-STRUCTURAL PROTEIN 3, DEAH HELICASE, ATPASE,
KEYWDS 2 DENGUE VIRUS, FLAVIVIRUS, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.W.PHOO,A.E.SAHILI
REVDAT 2 22-NOV-23 5YVV 1 REMARK
REVDAT 1 05-DEC-18 5YVV 0
JRNL AUTH W.W.PHOO,A.E.SAHILI,Z.Z.ZHANG,M.W.CHEN,J.LESCAR,S.VASUDEVAN,
JRNL AUTH 2 D.LUO
JRNL TITL CRYSTAL STRUCTURES OF UNLINKED FULL LENGTH NS3 FROM DENGUE
JRNL TITL 2 VIRUS PROVIDE INSIGHTS INTO DYNAMICS OF PROTEASE DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 13693
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.260
REMARK 3 FREE R VALUE TEST SET COUNT : 583
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 45.4190 - 4.9142 1.00 3342 143 0.2088 0.2396
REMARK 3 2 4.9142 - 3.9012 1.00 3297 147 0.2110 0.2700
REMARK 3 3 3.9012 - 3.4083 1.00 3281 140 0.2652 0.3245
REMARK 3 4 3.4083 - 3.0968 0.98 3190 153 0.3202 0.3495
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) : 0.510
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.360
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 : 0.003 4877
REMARK 3 ANGLE : 0.651 6628
REMARK 3 CHIRALITY : 0.024 743
REMARK 3 PLANARITY : 0.003 868
REMARK 3 DIHEDRAL : 10.846 1773
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.3498 17.9644 128.8457
REMARK 3 T TENSOR
REMARK 3 T11: 1.2717 T22: 0.8614
REMARK 3 T33: 1.0520 T12: -0.0199
REMARK 3 T13: -0.3160 T23: 0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 1.0700 L22: 0.9746
REMARK 3 L33: 1.6384 L12: -1.2853
REMARK 3 L13: 0.7842 L23: -0.2625
REMARK 3 S TENSOR
REMARK 3 S11: -0.4039 S12: -0.3906 S13: 0.1129
REMARK 3 S21: -0.0694 S22: 0.1525 S23: 0.1470
REMARK 3 S31: -0.2264 S32: -0.1326 S33: 0.2898
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 181 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2538 23.4653 98.7503
REMARK 3 T TENSOR
REMARK 3 T11: 0.3115 T22: 0.4169
REMARK 3 T33: 0.3977 T12: -0.0504
REMARK 3 T13: 0.1051 T23: -0.1077
REMARK 3 L TENSOR
REMARK 3 L11: 5.0826 L22: 5.2277
REMARK 3 L33: 4.2420 L12: -0.6507
REMARK 3 L13: -1.2136 L23: 1.3980
REMARK 3 S TENSOR
REMARK 3 S11: 0.1949 S12: -0.3562 S13: 0.0254
REMARK 3 S21: 0.3213 S22: -0.7247 S23: 0.4549
REMARK 3 S31: -0.0998 S32: -0.5150 S33: 0.3877
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 325 THROUGH 618 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.1841 10.2243 83.2594
REMARK 3 T TENSOR
REMARK 3 T11: 0.3952 T22: 0.3666
REMARK 3 T33: 0.3600 T12: -0.0407
REMARK 3 T13: 0.0954 T23: 0.0431
REMARK 3 L TENSOR
REMARK 3 L11: 2.9488 L22: 2.8366
REMARK 3 L33: 3.8684 L12: 0.1115
REMARK 3 L13: 1.7966 L23: 1.9469
REMARK 3 S TENSOR
REMARK 3 S11: 0.3778 S12: -0.2861 S13: -0.0563
REMARK 3 S21: -0.2108 S22: -0.2903 S23: -0.1182
REMARK 3 S31: 0.1549 S32: -0.4007 S33: -0.1098
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 49 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.5479 5.4369 127.5572
REMARK 3 T TENSOR
REMARK 3 T11: 1.0583 T22: 1.8052
REMARK 3 T33: 1.4641 T12: 0.2049
REMARK 3 T13: 0.1343 T23: 0.2910
REMARK 3 L TENSOR
REMARK 3 L11: 2.1471 L22: 5.8658
REMARK 3 L33: 0.3665 L12: 3.3692
REMARK 3 L13: -0.0992 L23: 0.2966
REMARK 3 S TENSOR
REMARK 3 S11: 0.1097 S12: -0.2269 S13: -0.4206
REMARK 3 S21: 0.4232 S22: -0.5209 S23: 1.0558
REMARK 3 S31: 0.2818 S32: -1.5217 S33: 0.5260
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 54 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.4292 13.9889 137.6337
REMARK 3 T TENSOR
REMARK 3 T11: 1.5795 T22: 1.0405
REMARK 3 T33: 1.5551 T12: -0.1533
REMARK 3 T13: -0.0845 T23: 0.1608
REMARK 3 L TENSOR
REMARK 3 L11: 0.1424 L22: 2.7703
REMARK 3 L33: 4.7870 L12: 0.6216
REMARK 3 L13: -0.8119 L23: -3.6217
REMARK 3 S TENSOR
REMARK 3 S11: -0.8704 S12: 0.3808 S13: 0.3325
REMARK 3 S21: 0.9299 S22: 0.3072 S23: 0.6940
REMARK 3 S31: -0.2885 S32: 0.1696 S33: 0.4633
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 59 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.3569 25.4506 143.1310
REMARK 3 T TENSOR
REMARK 3 T11: 1.6658 T22: 1.2414
REMARK 3 T33: 1.7468 T12: 0.2573
REMARK 3 T13: -0.2424 T23: -0.2626
REMARK 3 L TENSOR
REMARK 3 L11: 0.9878 L22: 3.9201
REMARK 3 L33: 9.4043 L12: -1.5092
REMARK 3 L13: -1.4488 L23: -1.2029
REMARK 3 S TENSOR
REMARK 3 S11: -0.7668 S12: -0.1690 S13: 0.6747
REMARK 3 S21: 0.5097 S22: 0.3039 S23: 0.9006
REMARK 3 S31: -0.7108 S32: -0.0319 S33: 0.5534
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): 78.3356 22.3951 142.7754
REMARK 3 T TENSOR
REMARK 3 T11: 0.7612 T22: 1.4601
REMARK 3 T33: 0.8182 T12: 0.1618
REMARK 3 T13: -0.3451 T23: -0.1303
REMARK 3 L TENSOR
REMARK 3 L11: 0.2862 L22: 4.5213
REMARK 3 L33: 3.8646 L12: -0.7432
REMARK 3 L13: 0.5542 L23: 1.2414
REMARK 3 S TENSOR
REMARK 3 S11: -0.9159 S12: 0.5348 S13: 0.7160
REMARK 3 S21: -0.5483 S22: 0.3542 S23: 0.3096
REMARK 3 S31: -0.6949 S32: 0.9184 S33: 0.3627
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 74 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 85.4767 19.8137 122.7417
REMARK 3 T TENSOR
REMARK 3 T11: 1.9537 T22: 1.1343
REMARK 3 T33: 1.5527 T12: -0.4183
REMARK 3 T13: -0.8554 T23: 0.2228
REMARK 3 L TENSOR
REMARK 3 L11: 9.3768 L22: 6.7697
REMARK 3 L33: 3.4662 L12: -6.5398
REMARK 3 L13: -5.6813 L23: 3.7203
REMARK 3 S TENSOR
REMARK 3 S11: 0.7119 S12: 1.6131 S13: -0.7241
REMARK 3 S21: -2.2942 S22: -0.3558 S23: 1.4779
REMARK 3 S31: -1.4900 S32: -0.8936 S33: -0.1135
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): 83.9332 14.8757 120.0143
REMARK 3 T TENSOR
REMARK 3 T11: 2.3346 T22: 1.1649
REMARK 3 T33: 1.7467 T12: -0.2560
REMARK 3 T13: -0.1880 T23: 0.1848
REMARK 3 L TENSOR
REMARK 3 L11: 0.5147 L22: 3.6975
REMARK 3 L33: 1.8745 L12: 0.7621
REMARK 3 L13: -0.3195 L23: 1.6040
REMARK 3 S TENSOR
REMARK 3 S11: 0.7615 S12: -0.1504 S13: -0.8865
REMARK 3 S21: -1.0520 S22: -1.3697 S23: 0.3327
REMARK 3 S31: 0.2002 S32: 0.6888 S33: 0.5800
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 5YVV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1300005990.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13710
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 45.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.40600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: 2VBC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5, 12% PEG6000, PH 6.0,
REMARK 280 VAPOR DIFFUSION, HANGING 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 44.35750
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A
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 ARG B 28
REMARK 465 GLY B 29
REMARK 465 SER B 30
REMARK 465 ILE B 171
REMARK 465 GLY B 172
REMARK 465 GLU B 173
REMARK 465 PRO B 174
REMARK 465 ASP B 175
REMARK 465 TYR B 176
REMARK 465 VAL A 89
REMARK 465 GLU A 90
REMARK 465 GLU A 91
REMARK 465 THR A 92
REMARK 465 ASN A 93
REMARK 465 MET A 94
REMARK 465 ILE A 95
REMARK 465 GLY A 96
REMARK 465 GLY A 97
REMARK 465 GLY A 98
REMARK 465 GLY A 99
REMARK 465 SER A 100
REMARK 465 GLY A 101
REMARK 465 GLY A 102
REMARK 465 GLY A 103
REMARK 465 GLY A 104
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 B 20 CG CD OE1 OE2
REMARK 470 TYR B 23 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 24 CG CD NE CZ NH1 NH2
REMARK 470 SER B 31 OG
REMARK 470 LYS B 33 CG CD CE NZ
REMARK 470 THR B 34 OG1 CG2
REMARK 470 HIS B 41 CG ND1 CD2 CE1 NE2
REMARK 470 MET B 42 CG SD CE
REMARK 470 GLU B 43 CG CD OE1 OE2
REMARK 470 ARG B 54 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 64 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 65 CG CD1 CD2
REMARK 470 ARG B 73 CG CD NE CZ NH1 NH2
REMARK 470 TRP B 83 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 83 CZ3 CH2
REMARK 470 LYS B 88 CG CD CE NZ
REMARK 470 LYS B 91 CG CD CE NZ
REMARK 470 LEU B 98 CG CD1 CD2
REMARK 470 GLU B 101 CG CD OE1 OE2
REMARK 470 PHE B 116 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 117 CG CD CE NZ
REMARK 470 THR B 118 OG1 CG2
REMARK 470 GLU B 122 CG CD OE1 OE2
REMARK 470 ASP B 129 CG OD1 OD2
REMARK 470 LYS B 142 CG CD CE NZ
REMARK 470 LYS B 143 CG CD CE NZ
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 ASP B 160 CG OD1 OD2
REMARK 470 ARG B 170 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 184 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 202 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 217 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 236 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 254 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 342 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 514 CG CD OE1 OE2
REMARK 470 LYS B 531 CG CD CE NZ
REMARK 470 ARG B 568 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 589 CG CD CE NZ
REMARK 470 LEU A 51 CG CD1 CD2
REMARK 470 LEU A 53 CG CD1 CD2
REMARK 470 GLU A 54 CG CD OE1 OE2
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 ASN A 58 CG OD1 ND2
REMARK 470 ILE A 73 CG1 CG2 CD1
REMARK 470 GLU A 75 CG CD OE1 OE2
REMARK 470 GLU A 80 CG CD OE1 OE2
REMARK 470 ARG A 87 CG CD NE CZ NH1 NH2
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 THR B 48 -156.32 -142.59
REMARK 500 SER B 56 -155.71 -163.18
REMARK 500 ARG B 84 164.33 75.72
REMARK 500 ASP B 87 -163.32 -106.58
REMARK 500 PRO B 132 129.15 -37.01
REMARK 500 SER B 158 -62.96 -93.33
REMARK 500 ILE B 165 97.73 -64.91
REMARK 500 ASP B 192 85.37 -65.97
REMARK 500 PRO B 239 90.47 -65.73
REMARK 500 GLU B 255 76.84 54.90
REMARK 500 ARG B 274 31.47 -99.81
REMARK 500 ALA B 286 22.46 -78.03
REMARK 500 ARG B 342 -163.79 -123.67
REMARK 500 ASN B 345 -54.81 -124.86
REMARK 500 PHE B 348 56.12 -103.90
REMARK 500 LEU B 443 78.70 -109.01
REMARK 500 ARG B 463 -76.20 -93.50
REMARK 500 THR B 565 39.99 -99.95
REMARK 500 TYR B 601 26.55 -140.64
REMARK 500 ASN A 58 -151.54 -115.81
REMARK 500 VAL A 59 60.90 -105.23
REMARK 500 SER A 70 -109.31 -174.25
REMARK 500 SER A 83 -157.07 -107.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE STRUCTURE IS SPLIT IN TWO CHAINS DUE TO THE FACT THAT ONE CHAIN
REMARK 999 COMES FOR THE COFACTOR AND THE OTHER FROM THE NS3 PROTEIN.
DBREF 5YVV B 20 618 UNP F8TEL4 F8TEL4_9FLAV 1494 2092
DBREF 5YVV A 49 95 UNP F8TEL4 F8TEL4_9FLAV 1393 1439
SEQADV 5YVV SER B 30 UNP F8TEL4 LEU 1504 ENGINEERED MUTATION
SEQADV 5YVV SER B 31 UNP F8TEL4 PHE 1505 ENGINEERED MUTATION
SEQADV 5YVV GLY A 96 UNP F8TEL4 EXPRESSION TAG
SEQADV 5YVV GLY A 97 UNP F8TEL4 EXPRESSION TAG
SEQADV 5YVV GLY A 98 UNP F8TEL4 EXPRESSION TAG
SEQADV 5YVV GLY A 99 UNP F8TEL4 EXPRESSION TAG
SEQADV 5YVV SER A 100 UNP F8TEL4 EXPRESSION TAG
SEQADV 5YVV GLY A 101 UNP F8TEL4 EXPRESSION TAG
SEQADV 5YVV GLY A 102 UNP F8TEL4 EXPRESSION TAG
SEQADV 5YVV GLY A 103 UNP F8TEL4 EXPRESSION TAG
SEQADV 5YVV GLY A 104 UNP F8TEL4 EXPRESSION TAG
SEQRES 1 B 599 GLU GLY VAL TYR ARG ILE MET GLN ARG GLY SER SER GLY
SEQRES 2 B 599 LYS THR GLN VAL GLY VAL GLY ILE HIS MET GLU GLY VAL
SEQRES 3 B 599 PHE HIS THR MET TRP HIS VAL THR ARG GLY SER VAL ILE
SEQRES 4 B 599 CYS HIS GLU THR GLY ARG LEU GLU PRO SER TRP ALA ASP
SEQRES 5 B 599 VAL ARG ASN ASP MET ILE SER TYR GLY GLY GLY TRP ARG
SEQRES 6 B 599 LEU GLY ASP LYS TRP ASP LYS GLU GLU ASP VAL GLN VAL
SEQRES 7 B 599 LEU ALA ILE GLU PRO GLY LYS ASN PRO LYS HIS VAL GLN
SEQRES 8 B 599 THR LYS PRO GLY LEU PHE LYS THR LEU THR GLY GLU ILE
SEQRES 9 B 599 GLY ALA VAL THR LEU ASP PHE LYS PRO GLY THR SER GLY
SEQRES 10 B 599 SER PRO ILE ILE ASN LYS LYS GLY LYS VAL ILE GLY LEU
SEQRES 11 B 599 TYR GLY ASN GLY VAL VAL THR LYS SER GLY ASP TYR VAL
SEQRES 12 B 599 SER ALA ILE THR GLN ALA GLU ARG ILE GLY GLU PRO ASP
SEQRES 13 B 599 TYR GLU VAL ASP GLU ASP ILE PHE ARG LYS LYS ARG LEU
SEQRES 14 B 599 THR ILE MET ASP LEU HIS PRO GLY ALA GLY LYS THR LYS
SEQRES 15 B 599 ARG ILE LEU PRO SER ILE VAL ARG GLU ALA LEU LYS ARG
SEQRES 16 B 599 ARG LEU ARG THR LEU ILE LEU ALA PRO THR ARG VAL VAL
SEQRES 17 B 599 ALA ALA GLU MET GLU GLU ALA LEU ARG GLY LEU PRO ILE
SEQRES 18 B 599 ARG TYR GLN THR PRO ALA VAL LYS SER GLU HIS THR GLY
SEQRES 19 B 599 ARG GLU ILE VAL ASP LEU MET CYS HIS ALA THR PHE THR
SEQRES 20 B 599 THR ARG LEU LEU SER SER THR ARG VAL PRO ASN TYR ASN
SEQRES 21 B 599 LEU ILE VAL MET ASP GLU ALA HIS PHE THR ASP PRO CYS
SEQRES 22 B 599 SER VAL ALA ALA ARG GLY TYR ILE SER THR ARG VAL GLU
SEQRES 23 B 599 MET GLY GLU ALA ALA ALA ILE PHE MET THR ALA THR PRO
SEQRES 24 B 599 PRO GLY SER ILE ASP PRO PHE PRO GLN SER ASN SER PRO
SEQRES 25 B 599 ILE GLU ASP ILE GLU ARG GLU ILE PRO GLU ARG SER TRP
SEQRES 26 B 599 ASN THR GLY PHE ASP TRP ILE THR ASP TYR GLN GLY LYS
SEQRES 27 B 599 THR VAL TRP PHE VAL PRO SER ILE LYS ALA GLY ASN ASP
SEQRES 28 B 599 ILE ALA ASN CYS LEU ARG LYS SER GLY LYS LYS VAL ILE
SEQRES 29 B 599 GLN LEU SER ARG LYS THR PHE ASP THR GLU TYR PRO LYS
SEQRES 30 B 599 THR LYS LEU THR ASP TRP ASP PHE VAL VAL THR THR ASP
SEQRES 31 B 599 ILE SER GLU MET GLY ALA ASN PHE ARG ALA GLY ARG VAL
SEQRES 32 B 599 ILE ASP PRO ARG ARG CYS LEU LYS PRO VAL ILE LEU THR
SEQRES 33 B 599 ASP GLY PRO GLU ARG VAL ILE LEU ALA GLY PRO ILE PRO
SEQRES 34 B 599 VAL THR PRO ALA SER ALA ALA GLN ARG ARG GLY ARG ILE
SEQRES 35 B 599 GLY ARG ASN PRO ALA GLN GLU ASP ASP GLN TYR VAL PHE
SEQRES 36 B 599 SER GLY ASP PRO LEU LYS ASN ASP GLU ASP HIS ALA HIS
SEQRES 37 B 599 TRP THR GLU ALA LYS MET LEU LEU ASP ASN ILE TYR THR
SEQRES 38 B 599 PRO GLU GLY ILE ILE PRO THR LEU PHE GLY PRO GLU ARG
SEQRES 39 B 599 GLU LYS THR GLN ALA ILE ASP GLY GLU PHE ARG LEU ARG
SEQRES 40 B 599 GLY GLU GLN ARG LYS THR PHE VAL GLU LEU MET ARG ARG
SEQRES 41 B 599 GLY ASP LEU PRO VAL TRP LEU SER TYR LYS VAL ALA SER
SEQRES 42 B 599 ALA GLY ILE SER TYR LYS ASP ARG GLU TRP CYS PHE THR
SEQRES 43 B 599 GLY GLU ARG ASN ASN GLN ILE LEU GLU GLU ASN MET GLU
SEQRES 44 B 599 VAL GLU ILE TRP THR ARG GLU GLY GLU LYS LYS LYS LEU
SEQRES 45 B 599 ARG PRO LYS TRP LEU ASP ALA ARG VAL TYR ALA ASP PRO
SEQRES 46 B 599 MET ALA LEU LYS ASP PHE LYS GLU PHE ALA SER GLY ARG
SEQRES 47 B 599 LYS
SEQRES 1 A 56 ALA ASP LEU SER LEU GLU LYS ALA ALA ASN VAL GLN TRP
SEQRES 2 A 56 ASP GLU MET ALA ASP ILE THR GLY SER SER PRO ILE ILE
SEQRES 3 A 56 GLU VAL LYS GLN ASP GLU ASP GLY SER PHE SER ILE ARG
SEQRES 4 A 56 ASP VAL GLU GLU THR ASN MET ILE GLY GLY GLY GLY SER
SEQRES 5 A 56 GLY GLY GLY GLY
HELIX 1 AA1 MET B 49 ARG B 54 1 6
HELIX 2 AA2 GLU B 180 ARG B 184 5 5
HELIX 3 AA3 ARG B 202 ARG B 214 1 13
HELIX 4 AA4 THR B 224 LEU B 235 1 12
HELIX 5 AA5 HIS B 262 SER B 272 1 11
HELIX 6 AA6 ASP B 290 MET B 306 1 17
HELIX 7 AA7 PHE B 348 TYR B 354 1 7
HELIX 8 AA8 SER B 364 SER B 378 1 15
HELIX 9 AA9 THR B 389 TYR B 394 1 6
HELIX 10 AB1 PRO B 395 THR B 400 1 6
HELIX 11 AB2 ASP B 409 MET B 413 5 5
HELIX 12 AB3 THR B 450 GLY B 459 1 10
HELIX 13 AB4 HIS B 485 ASP B 496 1 12
HELIX 14 AB5 PHE B 509 GLU B 514 1 6
HELIX 15 AB6 GLY B 527 ARG B 539 1 13
HELIX 16 AB7 PRO B 543 SER B 552 1 10
HELIX 17 AB8 ARG B 560 PHE B 564 5 5
HELIX 18 AB9 GLU B 567 GLN B 571 5 5
HELIX 19 AC1 ASP B 597 TYR B 601 5 5
HELIX 20 AC2 ASP B 603 SER B 615 1 13
SHEET 1 AA1 6 PRO B 67 ASP B 71 0
SHEET 2 AA1 6 MET B 76 TYR B 79 -1 O SER B 78 N SER B 68
SHEET 3 AA1 6 VAL B 45 THR B 48 -1 N PHE B 46 O TYR B 79
SHEET 4 AA1 6 THR B 34 MET B 42 -1 N ILE B 40 O HIS B 47
SHEET 5 AA1 6 GLY B 21 GLN B 27 -1 N TYR B 23 O GLY B 39
SHEET 6 AA1 6 GLU A 54 ALA A 57 -1 O GLU A 54 N ARG B 24
SHEET 1 AA2 2 ILE B 58 CYS B 59 0
SHEET 2 AA2 2 ARG B 64 LEU B 65 -1 O LEU B 65 N ILE B 58
SHEET 1 AA3 5 VAL B 146 TYR B 150 0
SHEET 2 AA3 5 SER B 137 ILE B 140 -1 N ILE B 139 O GLY B 148
SHEET 3 AA3 5 GLN B 96 VAL B 97 -1 N GLN B 96 O ILE B 140
SHEET 4 AA3 5 VAL B 109 THR B 111 -1 O VAL B 109 N VAL B 97
SHEET 5 AA3 5 ASP A 66 THR A 68 1 O ASP A 66 N GLN B 110
SHEET 1 AA4 2 LEU B 115 LYS B 117 0
SHEET 2 AA4 2 ILE A 73 GLU A 75 1 O ILE A 74 N LEU B 115
SHEET 1 AA5 2 ALA B 125 VAL B 126 0
SHEET 2 AA5 2 SER B 163 ALA B 164 -1 O SER B 163 N VAL B 126
SHEET 1 AA6 6 ARG B 187 MET B 191 0
SHEET 2 AA6 6 ALA B 310 MET B 314 1 O ALA B 311 N THR B 189
SHEET 3 AA6 6 LEU B 280 ASP B 284 1 N MET B 283 O MET B 314
SHEET 4 AA6 6 THR B 218 ALA B 222 1 N LEU B 219 O VAL B 282
SHEET 5 AA6 6 VAL B 257 CYS B 261 1 O ASP B 258 N ILE B 220
SHEET 6 AA6 6 ILE B 240 TYR B 242 1 N ARG B 241 O VAL B 257
SHEET 1 AA7 6 ILE B 332 GLU B 336 0
SHEET 2 AA7 6 ASP B 470 PHE B 474 1 O ASP B 470 N GLU B 333
SHEET 3 AA7 6 ARG B 421 ASP B 424 1 N ASP B 424 O VAL B 473
SHEET 4 AA7 6 THR B 358 PHE B 361 1 N PHE B 361 O ILE B 423
SHEET 5 AA7 6 PHE B 404 THR B 407 1 O THR B 407 N TRP B 360
SHEET 6 AA7 6 VAL B 382 LEU B 385 1 N ILE B 383 O PHE B 404
SHEET 1 AA8 2 ARG B 427 LEU B 434 0
SHEET 2 AA8 2 ARG B 440 PRO B 448 -1 O ILE B 447 N CYS B 428
SHEET 1 AA9 2 GLU B 580 TRP B 582 0
SHEET 2 AA9 2 LYS B 588 LYS B 590 -1 O LYS B 589 N ILE B 581
CISPEP 1 GLY B 82 TRP B 83 0 -0.85
CISPEP 2 TRP B 83 ARG B 84 0 13.59
CISPEP 3 ARG B 84 LEU B 85 0 -1.69
CISPEP 4 LEU B 85 GLY B 86 0 -0.03
CISPEP 5 PRO B 195 GLY B 196 0 1.54
CISPEP 6 GLY B 445 PRO B 446 0 -0.49
CISPEP 7 GLU B 502 GLY B 503 0 4.16
CRYST1 52.917 88.715 81.295 90.00 93.08 90.00 P 1 21 1 2
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 0.018898 0.000000 0.001016 0.00000
SCALE2 0.000000 0.011272 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012319 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
