HEADER HYDROLASE 22-AUG-16 5T1V
TITLE CRYSTAL STRUCTURE OF ZIKA VIRUS NS2B-NS3 PROTEASE IN APO-FORM.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NS2B-NS3 PROTEASE,NS2B-NS3 PROTEASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.21.91,3.6.1.15,3.6.4.13,2.1.1.56,2.1.1.57,2.7.7.48,3.4.21.91,
COMPND 5 3.6.1.15,3.6.4.13,2.1.1.56,2.1.1.57,2.7.7.48;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZIKA VIRUS;
SOURCE 3 ORGANISM_COMMON: ZIKV;
SOURCE 4 ORGANISM_TAXID: 64320;
SOURCE 5 STRAIN: MR 766;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS HYDROLASE, PEPTIDASE S7, FLAVIVIRUS NS3 SERINE PROTEASE., STRUCTURAL
KEYWDS 2 GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES,
KEYWDS 3 CSGID
EXPDTA X-RAY DIFFRACTION
AUTHOR S.NOCADELLO,S.H.LIGHT,G.MINASOV,L.SHUVALOVA,A.A.CARDONA-CORREA,
AUTHOR 2 I.OJEDA,J.VARGAS,M.E.JOHNSON,H.LEE,W.F.ANDERSON,CENTER FOR
AUTHOR 3 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES,CENTER FOR STRUCTURAL
AUTHOR 4 GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 2 04-OCT-23 5T1V 1 REMARK
REVDAT 1 07-SEP-16 5T1V 0
JRNL AUTH S.NOCADELLO,S.H.LIGHT,G.MINASOV,L.A.SHUVALOVA,
JRNL AUTH 2 A.A.CARDONA-CORREA,I.OJEDA,J.VARGAS,M.E.JOHNSON,H.LEE,
JRNL AUTH 3 W.F.ANDERSON,
JRNL AUTH 4 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL TITL CRYSTAL STRUCTURE OF ZIKA VIRUS NS2B-NS3 PROTEASE IN
JRNL TITL 2 APO-FORM.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 6875
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 739
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 483
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 41
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2442
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 79.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 93.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.67000
REMARK 3 B22 (A**2) : 3.67000
REMARK 3 B33 (A**2) : -7.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.550
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.389
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 51.041
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.881
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2491 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2375 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3376 ; 1.247 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5457 ; 0.824 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 316 ; 1.580 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;16.108 ;23.654
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 406 ; 8.947 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ; 6.305 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 370 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2818 ; 0.021 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 548 ; 0.018 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1279 ; 1.583 ; 6.351
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1278 ; 1.583 ; 6.348
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1590 ; 2.817 ; 9.506
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1591 ; 2.816 ; 9.510
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1212 ; 1.212 ; 6.482
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1213 ; 1.212 ; 6.485
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1787 ; 2.134 ; 9.646
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2722 ; 4.839 ;73.449
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2720 ; 4.840 ;73.364
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 6 222 B 6 222 8526 0.14 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 94
REMARK 3 ORIGIN FOR THE GROUP (A): -17.6178 6.3215 -52.6201
REMARK 3 T TENSOR
REMARK 3 T11: 0.1508 T22: 0.3261
REMARK 3 T33: 0.1435 T12: -0.0665
REMARK 3 T13: 0.0502 T23: -0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 4.6969 L22: 9.8439
REMARK 3 L33: 6.0247 L12: -4.7890
REMARK 3 L13: -3.5487 L23: 7.0824
REMARK 3 S TENSOR
REMARK 3 S11: -0.1261 S12: -0.2103 S13: 0.2807
REMARK 3 S21: -0.4059 S22: 0.3281 S23: -0.3954
REMARK 3 S31: -0.4692 S32: 0.4839 S33: -0.2020
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 95 A 157
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2815 3.8241 -51.4747
REMARK 3 T TENSOR
REMARK 3 T11: 0.2267 T22: 0.1353
REMARK 3 T33: 0.1319 T12: 0.0177
REMARK 3 T13: -0.0758 T23: -0.0622
REMARK 3 L TENSOR
REMARK 3 L11: 3.5253 L22: 3.4958
REMARK 3 L33: 5.8278 L12: -1.6388
REMARK 3 L13: -1.0051 L23: 2.5759
REMARK 3 S TENSOR
REMARK 3 S11: -0.1014 S12: 0.1873 S13: 0.0821
REMARK 3 S21: -0.6576 S22: -0.1437 S23: 0.2758
REMARK 3 S31: -0.2235 S32: -0.4142 S33: 0.2451
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 158 A 222
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9985 -9.4647 -53.1820
REMARK 3 T TENSOR
REMARK 3 T11: 0.3602 T22: 0.3009
REMARK 3 T33: 0.3799 T12: 0.0893
REMARK 3 T13: -0.0980 T23: -0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 1.1506 L22: 7.2568
REMARK 3 L33: 5.5562 L12: -1.1536
REMARK 3 L13: -1.7149 L23: 2.5589
REMARK 3 S TENSOR
REMARK 3 S11: -0.0599 S12: -0.0738 S13: -0.4207
REMARK 3 S21: 0.2756 S22: 0.2101 S23: 0.1625
REMARK 3 S31: 0.8058 S32: 0.3471 S33: -0.1501
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 6 B 95
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7902 -3.2499 -25.2501
REMARK 3 T TENSOR
REMARK 3 T11: 0.4749 T22: 0.1728
REMARK 3 T33: 0.4678 T12: 0.0017
REMARK 3 T13: -0.0474 T23: 0.1440
REMARK 3 L TENSOR
REMARK 3 L11: 6.3256 L22: 6.3463
REMARK 3 L33: 5.8254 L12: 2.8383
REMARK 3 L13: -0.8598 L23: 2.8046
REMARK 3 S TENSOR
REMARK 3 S11: 0.4263 S12: -0.3245 S13: -0.9757
REMARK 3 S21: 0.3933 S22: -0.0903 S23: -0.1105
REMARK 3 S31: 1.0300 S32: -0.1092 S33: -0.3360
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 96 B 171
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0596 4.4868 -26.1134
REMARK 3 T TENSOR
REMARK 3 T11: 0.0228 T22: 0.1821
REMARK 3 T33: 0.0802 T12: -0.0186
REMARK 3 T13: 0.0250 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 5.8626 L22: 3.2107
REMARK 3 L33: 6.1058 L12: 0.1240
REMARK 3 L13: 0.9438 L23: 1.6941
REMARK 3 S TENSOR
REMARK 3 S11: -0.0515 S12: -0.3867 S13: -0.3106
REMARK 3 S21: 0.0800 S22: -0.1337 S23: 0.3823
REMARK 3 S31: 0.2932 S32: -0.6324 S33: 0.1853
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 172 B 223
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9703 12.0572 -23.2641
REMARK 3 T TENSOR
REMARK 3 T11: 0.0273 T22: 0.1987
REMARK 3 T33: 0.0706 T12: 0.0051
REMARK 3 T13: 0.0105 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 5.8563 L22: 5.6485
REMARK 3 L33: 6.9539 L12: 1.9305
REMARK 3 L13: -0.3882 L23: -0.2075
REMARK 3 S TENSOR
REMARK 3 S11: 0.0720 S12: -0.2713 S13: 0.5419
REMARK 3 S21: -0.1428 S22: -0.0180 S23: 0.3194
REMARK 3 S31: -0.3392 S32: 0.0769 S33: -0.0540
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5T1V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223483.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUN-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 : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : BERRYLIUM LENSES
REMARK 200 OPTICS : C(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7675
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : 0.11500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.8000
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) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.73200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.740
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: PDB-5LC0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 24.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 12.8MG/ML, 1M SODIUM
REMARK 280 CHLORIDE, 0.05M TRIS-HCL PH=8.5; SCRREN: CLASSICS II (H3), 0.24M
REMARK 280 SODIUM MALONATE PH=7.0, 20% (W/V) PEG 3350, PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 124.60000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 27.54300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 27.54300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 62.30000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 27.54300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 27.54300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 186.90000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 27.54300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 27.54300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 62.30000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 27.54300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 27.54300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 186.90000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 124.60000
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: 1810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ALA A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 GLY A 1
REMARK 465 PRO A 2
REMARK 465 GLY A 3
REMARK 465 LYS A 4
REMARK 465 SER A 5
REMARK 465 GLU A 23
REMARK 465 VAL A 24
REMARK 465 THR A 25
REMARK 465 GLY A 26
REMARK 465 ASN A 27
REMARK 465 SER A 28
REMARK 465 PRO A 29
REMARK 465 ARG A 30
REMARK 465 LEU A 31
REMARK 465 ASP A 32
REMARK 465 VAL A 33
REMARK 465 ALA A 34
REMARK 465 LEU A 35
REMARK 465 ASP A 36
REMARK 465 GLU A 37
REMARK 465 SER A 38
REMARK 465 GLY A 39
REMARK 465 ASP A 40
REMARK 465 PHE A 41
REMARK 465 SER A 42
REMARK 465 LEU A 43
REMARK 465 VAL A 44
REMARK 465 GLU A 45
REMARK 465 GLU A 46
REMARK 465 ASP A 47
REMARK 465 GLY A 48
REMARK 465 PRO A 49
REMARK 465 PRO A 50
REMARK 465 MET A 51
REMARK 465 ARG A 52
REMARK 465 GLU A 53
REMARK 465 ILE A 54
REMARK 465 ILE A 55
REMARK 465 LEU A 56
REMARK 465 GLY A 57
REMARK 465 GLY A 58
REMARK 465 GLY A 59
REMARK 465 GLY A 60
REMARK 465 SER A 61
REMARK 465 GLY A 62
REMARK 465 GLY A 63
REMARK 465 GLY A 64
REMARK 465 GLY A 65
REMARK 465 SER A 66
REMARK 465 GLY A 67
REMARK 465 ALA A 68
REMARK 465 LEU A 69
REMARK 465 TRP A 70
REMARK 465 ASP A 71
REMARK 465 VAL A 72
REMARK 465 PRO A 73
REMARK 465 ALA A 74
REMARK 465 PRO A 75
REMARK 465 LYS A 76
REMARK 465 GLU A 77
REMARK 465 VAL A 78
REMARK 465 LYS A 79
REMARK 465 LYS A 80
REMARK 465 GLY A 81
REMARK 465 ASN A 223
REMARK 465 GLY A 224
REMARK 465 SER A 225
REMARK 465 TYR A 226
REMARK 465 VAL A 227
REMARK 465 SER A 228
REMARK 465 ALA A 229
REMARK 465 ILE A 230
REMARK 465 THR A 231
REMARK 465 GLN A 232
REMARK 465 GLY A 233
REMARK 465 LYS A 234
REMARK 465 ARG A 235
REMARK 465 GLU A 236
REMARK 465 GLU A 237
REMARK 465 GLU A 238
REMARK 465 THR A 239
REMARK 465 PRO A 240
REMARK 465 VAL A 241
REMARK 465 GLU A 242
REMARK 465 CYS A 243
REMARK 465 PHE A 244
REMARK 465 GLU A 245
REMARK 465 PRO A 246
REMARK 465 SER A 247
REMARK 465 MET A 248
REMARK 465 LEU A 249
REMARK 465 LYS A 250
REMARK 465 LYS A 251
REMARK 465 LYS A 252
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 LEU B -7
REMARK 465 VAL B -6
REMARK 465 PRO B -5
REMARK 465 ALA B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 GLY B 3
REMARK 465 LYS B 4
REMARK 465 SER B 5
REMARK 465 ASN B 27
REMARK 465 SER B 28
REMARK 465 PRO B 29
REMARK 465 ARG B 30
REMARK 465 LEU B 31
REMARK 465 ASP B 32
REMARK 465 VAL B 33
REMARK 465 ALA B 34
REMARK 465 LEU B 35
REMARK 465 ASP B 36
REMARK 465 GLU B 37
REMARK 465 SER B 38
REMARK 465 GLY B 39
REMARK 465 ASP B 40
REMARK 465 PHE B 41
REMARK 465 SER B 42
REMARK 465 LEU B 43
REMARK 465 VAL B 44
REMARK 465 GLU B 45
REMARK 465 GLU B 46
REMARK 465 ASP B 47
REMARK 465 GLY B 48
REMARK 465 PRO B 49
REMARK 465 PRO B 50
REMARK 465 MET B 51
REMARK 465 ARG B 52
REMARK 465 GLU B 53
REMARK 465 ILE B 54
REMARK 465 ILE B 55
REMARK 465 LEU B 56
REMARK 465 GLY B 57
REMARK 465 GLY B 58
REMARK 465 GLY B 59
REMARK 465 GLY B 60
REMARK 465 SER B 61
REMARK 465 GLY B 62
REMARK 465 GLY B 63
REMARK 465 GLY B 64
REMARK 465 GLY B 65
REMARK 465 SER B 66
REMARK 465 GLY B 67
REMARK 465 ALA B 68
REMARK 465 LEU B 69
REMARK 465 TRP B 70
REMARK 465 ASP B 71
REMARK 465 VAL B 72
REMARK 465 PRO B 73
REMARK 465 ALA B 74
REMARK 465 PRO B 75
REMARK 465 LYS B 76
REMARK 465 GLU B 77
REMARK 465 VAL B 78
REMARK 465 LYS B 79
REMARK 465 THR B 183
REMARK 465 LYS B 184
REMARK 465 GLY B 224
REMARK 465 SER B 225
REMARK 465 TYR B 226
REMARK 465 VAL B 227
REMARK 465 SER B 228
REMARK 465 ALA B 229
REMARK 465 ILE B 230
REMARK 465 THR B 231
REMARK 465 GLN B 232
REMARK 465 GLY B 233
REMARK 465 LYS B 234
REMARK 465 ARG B 235
REMARK 465 GLU B 236
REMARK 465 GLU B 237
REMARK 465 GLU B 238
REMARK 465 THR B 239
REMARK 465 PRO B 240
REMARK 465 VAL B 241
REMARK 465 GLU B 242
REMARK 465 CYS B 243
REMARK 465 PHE B 244
REMARK 465 GLU B 245
REMARK 465 PRO B 246
REMARK 465 SER B 247
REMARK 465 MET B 248
REMARK 465 LEU B 249
REMARK 465 LYS B 250
REMARK 465 LYS B 251
REMARK 465 LYS B 252
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 172 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 21 57.31 -142.33
REMARK 500 THR A 83 43.50 -143.79
REMARK 500 LEU A 96 70.44 -111.41
REMARK 500 CYS A 145 -12.32 75.94
REMARK 500 LEU A 157 -56.01 -147.96
REMARK 500 LYS A 182 58.06 -110.38
REMARK 500 ASP B 7 69.80 -115.19
REMARK 500 ASP B 21 56.81 -149.40
REMARK 500 THR B 83 43.51 -143.25
REMARK 500 LEU B 96 63.56 -111.26
REMARK 500 CYS B 145 -12.51 76.28
REMARK 500 LEU B 157 -55.70 -148.33
REMARK 500 LYS B 222 107.54 -54.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP95745 RELATED DB: TARGETTRACK
DBREF 5T1V A 3 56 UNP Q32ZE1 POLG_ZIKV 1414 1467
DBREF 5T1V A 66 252 UNP Q32ZE1 POLG_ZIKV 1499 1685
DBREF 5T1V B 3 56 UNP Q32ZE1 POLG_ZIKV 1414 1467
DBREF 5T1V B 66 252 UNP Q32ZE1 POLG_ZIKV 1499 1685
SEQADV 5T1V MET A -20 UNP Q32ZE1 INITIATING METHIONINE
SEQADV 5T1V GLY A -19 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V SER A -18 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V SER A -17 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS A -16 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS A -15 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS A -14 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS A -13 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS A -12 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS A -11 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V SER A -10 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V SER A -9 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V GLY A -8 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V LEU A -7 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V VAL A -6 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V PRO A -5 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V ALA A -4 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V GLY A -3 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V SER A -2 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS A -1 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V MET A 0 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V GLY A 1 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V PRO A 2 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V GLY A 57 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY A 58 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY A 59 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY A 60 UNP Q32ZE1 LINKER
SEQADV 5T1V SER A 61 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY A 62 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY A 63 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY A 64 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY A 65 UNP Q32ZE1 LINKER
SEQADV 5T1V MET B -20 UNP Q32ZE1 INITIATING METHIONINE
SEQADV 5T1V GLY B -19 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V SER B -18 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V SER B -17 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS B -16 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS B -15 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS B -14 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS B -13 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS B -12 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS B -11 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V SER B -10 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V SER B -9 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V GLY B -8 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V LEU B -7 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V VAL B -6 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V PRO B -5 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V ALA B -4 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V GLY B -3 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V SER B -2 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V HIS B -1 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V MET B 0 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V GLY B 1 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V PRO B 2 UNP Q32ZE1 EXPRESSION TAG
SEQADV 5T1V GLY B 57 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY B 58 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY B 59 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY B 60 UNP Q32ZE1 LINKER
SEQADV 5T1V SER B 61 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY B 62 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY B 63 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY B 64 UNP Q32ZE1 LINKER
SEQADV 5T1V GLY B 65 UNP Q32ZE1 LINKER
SEQRES 1 A 273 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 273 LEU VAL PRO ALA GLY SER HIS MET GLY PRO GLY LYS SER
SEQRES 3 A 273 VAL ASP MET TYR ILE GLU ARG ALA GLY ASP ILE THR TRP
SEQRES 4 A 273 GLU LYS ASP ALA GLU VAL THR GLY ASN SER PRO ARG LEU
SEQRES 5 A 273 ASP VAL ALA LEU ASP GLU SER GLY ASP PHE SER LEU VAL
SEQRES 6 A 273 GLU GLU ASP GLY PRO PRO MET ARG GLU ILE ILE LEU GLY
SEQRES 7 A 273 GLY GLY GLY SER GLY GLY GLY GLY SER GLY ALA LEU TRP
SEQRES 8 A 273 ASP VAL PRO ALA PRO LYS GLU VAL LYS LYS GLY GLU THR
SEQRES 9 A 273 THR ASP GLY VAL TYR ARG VAL MET THR ARG ARG LEU LEU
SEQRES 10 A 273 GLY SER THR GLN VAL GLY VAL GLY VAL MET GLN GLU GLY
SEQRES 11 A 273 VAL PHE HIS THR MET TRP HIS VAL THR LYS GLY ALA ALA
SEQRES 12 A 273 LEU ARG SER GLY GLU GLY ARG LEU ASP PRO TYR TRP GLY
SEQRES 13 A 273 ASP VAL LYS GLN ASP LEU VAL SER TYR CYS GLY PRO TRP
SEQRES 14 A 273 LYS LEU ASP ALA ALA TRP ASP GLY LEU SER GLU VAL GLN
SEQRES 15 A 273 LEU LEU ALA VAL PRO PRO GLY GLU ARG ALA ARG ASN ILE
SEQRES 16 A 273 GLN THR LEU PRO GLY ILE PHE LYS THR LYS ASP GLY ASP
SEQRES 17 A 273 ILE GLY ALA VAL ALA LEU ASP TYR PRO ALA GLY THR SER
SEQRES 18 A 273 GLY SER PRO ILE LEU ASP LYS CYS GLY ARG VAL ILE GLY
SEQRES 19 A 273 LEU TYR GLY ASN GLY VAL VAL ILE LYS ASN GLY SER TYR
SEQRES 20 A 273 VAL SER ALA ILE THR GLN GLY LYS ARG GLU GLU GLU THR
SEQRES 21 A 273 PRO VAL GLU CYS PHE GLU PRO SER MET LEU LYS LYS LYS
SEQRES 1 B 273 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 273 LEU VAL PRO ALA GLY SER HIS MET GLY PRO GLY LYS SER
SEQRES 3 B 273 VAL ASP MET TYR ILE GLU ARG ALA GLY ASP ILE THR TRP
SEQRES 4 B 273 GLU LYS ASP ALA GLU VAL THR GLY ASN SER PRO ARG LEU
SEQRES 5 B 273 ASP VAL ALA LEU ASP GLU SER GLY ASP PHE SER LEU VAL
SEQRES 6 B 273 GLU GLU ASP GLY PRO PRO MET ARG GLU ILE ILE LEU GLY
SEQRES 7 B 273 GLY GLY GLY SER GLY GLY GLY GLY SER GLY ALA LEU TRP
SEQRES 8 B 273 ASP VAL PRO ALA PRO LYS GLU VAL LYS LYS GLY GLU THR
SEQRES 9 B 273 THR ASP GLY VAL TYR ARG VAL MET THR ARG ARG LEU LEU
SEQRES 10 B 273 GLY SER THR GLN VAL GLY VAL GLY VAL MET GLN GLU GLY
SEQRES 11 B 273 VAL PHE HIS THR MET TRP HIS VAL THR LYS GLY ALA ALA
SEQRES 12 B 273 LEU ARG SER GLY GLU GLY ARG LEU ASP PRO TYR TRP GLY
SEQRES 13 B 273 ASP VAL LYS GLN ASP LEU VAL SER TYR CYS GLY PRO TRP
SEQRES 14 B 273 LYS LEU ASP ALA ALA TRP ASP GLY LEU SER GLU VAL GLN
SEQRES 15 B 273 LEU LEU ALA VAL PRO PRO GLY GLU ARG ALA ARG ASN ILE
SEQRES 16 B 273 GLN THR LEU PRO GLY ILE PHE LYS THR LYS ASP GLY ASP
SEQRES 17 B 273 ILE GLY ALA VAL ALA LEU ASP TYR PRO ALA GLY THR SER
SEQRES 18 B 273 GLY SER PRO ILE LEU ASP LYS CYS GLY ARG VAL ILE GLY
SEQRES 19 B 273 LEU TYR GLY ASN GLY VAL VAL ILE LYS ASN GLY SER TYR
SEQRES 20 B 273 VAL SER ALA ILE THR GLN GLY LYS ARG GLU GLU GLU THR
SEQRES 21 B 273 PRO VAL GLU CYS PHE GLU PRO SER MET LEU LYS LYS LYS
HELIX 1 AA1 MET A 114 LYS A 119 1 6
HELIX 2 AA2 PRO A 196 SER A 200 5 5
HELIX 3 AA3 MET B 114 LYS B 119 1 6
HELIX 4 AA4 PRO B 196 SER B 200 5 5
SHEET 1 AA1 6 MET A 8 GLY A 14 0
SHEET 2 AA1 6 GLY A 86 ARG A 94 -1 O VAL A 87 N ALA A 13
SHEET 3 AA1 6 GLY A 97 GLN A 107 -1 O GLY A 102 N VAL A 90
SHEET 4 AA1 6 VAL A 110 THR A 113 -1 O HIS A 112 N VAL A 105
SHEET 5 AA1 6 LEU A 141 TYR A 144 -1 O VAL A 142 N THR A 113
SHEET 6 AA1 6 PRO A 132 ASP A 136 -1 N TRP A 134 O SER A 143
SHEET 1 AA2 2 LEU A 123 SER A 125 0
SHEET 2 AA2 2 GLY A 128 LEU A 130 -1 O LEU A 130 N LEU A 123
SHEET 1 AA3 4 GLN A 175 THR A 176 0
SHEET 2 AA3 4 VAL A 160 LEU A 162 -1 N VAL A 160 O THR A 176
SHEET 3 AA3 4 PRO A 203 LEU A 205 -1 O LEU A 205 N GLN A 161
SHEET 4 AA3 4 VAL A 211 LEU A 214 -1 O ILE A 212 N ILE A 204
SHEET 1 AA4 2 GLY A 179 PHE A 181 0
SHEET 2 AA4 2 ILE A 188 ALA A 190 -1 O ALA A 190 N GLY A 179
SHEET 1 AA5 6 MET B 8 GLY B 14 0
SHEET 2 AA5 6 GLY B 86 ARG B 94 -1 O VAL B 87 N ALA B 13
SHEET 3 AA5 6 GLY B 97 GLN B 107 -1 O GLY B 102 N VAL B 90
SHEET 4 AA5 6 VAL B 110 THR B 113 -1 O HIS B 112 N VAL B 105
SHEET 5 AA5 6 LEU B 141 TYR B 144 -1 O VAL B 142 N THR B 113
SHEET 6 AA5 6 PRO B 132 ASP B 136 -1 N TRP B 134 O SER B 143
SHEET 1 AA6 5 GLU B 23 VAL B 24 0
SHEET 2 AA6 5 ILE B 174 THR B 176 1 O GLN B 175 N GLU B 23
SHEET 3 AA6 5 VAL B 160 LEU B 162 -1 N VAL B 160 O THR B 176
SHEET 4 AA6 5 PRO B 203 LEU B 205 -1 O LEU B 205 N GLN B 161
SHEET 5 AA6 5 VAL B 211 LEU B 214 -1 O ILE B 212 N ILE B 204
SHEET 1 AA7 2 LEU B 123 SER B 125 0
SHEET 2 AA7 2 GLY B 128 LEU B 130 -1 O LEU B 130 N LEU B 123
SHEET 1 AA8 3 GLY B 179 ILE B 180 0
SHEET 2 AA8 3 ILE B 188 ALA B 190 -1 O ALA B 190 N GLY B 179
SHEET 3 AA8 3 VAL B 219 VAL B 220 -1 O VAL B 219 N GLY B 189
CRYST1 55.086 55.086 249.200 90.00 90.00 90.00 P 41 21 2 16
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 0.018153 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018153 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004013 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
