HEADER HYDROLASE/HYDROLASE INHIBITOR 30-SEP-11 3U1J
TITLE APROTININ BOUND TO DENGUE VIRUS PROTEASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE SUBUNIT NS2B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1393-1438;
COMPND 5 SYNONYM: FLAVIVIRIN PROTEASE NS2B REGULATORY SUBUNIT, NON-STRUCTURAL
COMPND 6 PROTEIN 2B;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SERINE PROTEASE NS3;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 1474-1655;
COMPND 12 SYNONYM: FLAVIVIRIN PROTEASE NS3 CATALYTIC SUBUNIT, NON-STRUCTURAL
COMPND 13 PROTEIN 3;
COMPND 14 EC: 3.4.21.91, 3.6.1.15, 3.6.4.13;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;
COMPND 18 CHAIN: E;
COMPND 19 FRAGMENT: UNP RESIDUES 36-93;
COMPND 20 SYNONYM: APROTININ, BASIC PROTEASE INHIBITOR, BPI, BPTI
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DENGUE VIRUS 3;
SOURCE 3 ORGANISM_COMMON: DENV-3;
SOURCE 4 ORGANISM_TAXID: 408693;
SOURCE 5 STRAIN: SINGAPORE/8120/1995;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: DENGUE VIRUS 3;
SOURCE 13 ORGANISM_COMMON: DENV-3;
SOURCE 14 ORGANISM_TAXID: 408693;
SOURCE 15 STRAIN: SINGAPORE/8120/1995;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX6P1;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 23 ORGANISM_COMMON: BOVINE;
SOURCE 24 ORGANISM_TAXID: 9913
KEYWDS SERINE PROTEASE, BOVINE PANCREATIC TRYPSIN INHIBITOR, ER MEMBRANE,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.G.NOBLE
REVDAT 3 01-NOV-23 3U1J 1 SEQADV
REVDAT 2 05-JUN-13 3U1J 1 JRNL
REVDAT 1 09-NOV-11 3U1J 0
JRNL AUTH C.G.NOBLE,C.C.SEH,A.T.CHAO,P.Y.SHI
JRNL TITL LIGAND-BOUND STRUCTURES OF THE DENGUE VIRUS PROTEASE REVEAL
JRNL TITL 2 THE ACTIVE CONFORMATION
JRNL REF J.VIROL. V. 86 438 2012
JRNL REFN ISSN 0022-538X
JRNL PMID 22031935
JRNL DOI 10.1128/JVI.06225-11
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 24442
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1312
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1771
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 93
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1856
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 193
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.76000
REMARK 3 B22 (A**2) : 0.76000
REMARK 3 B33 (A**2) : -1.15000
REMARK 3 B12 (A**2) : 0.38000
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): 0.109
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.834
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1937 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2629 ; 1.263 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 251 ; 6.076 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;29.086 ;24.368
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 327 ;16.813 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;12.271 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 279 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1487 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1207 ; 0.735 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1943 ; 1.370 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 730 ; 1.948 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 680 ; 3.388 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
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 50 A 69
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1894 -35.9263 -18.3130
REMARK 3 T TENSOR
REMARK 3 T11: 0.0273 T22: 0.0847
REMARK 3 T33: 0.0900 T12: 0.0398
REMARK 3 T13: -0.0108 T23: -0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 4.4224 L22: 3.2029
REMARK 3 L33: 5.5891 L12: 1.6665
REMARK 3 L13: -2.8256 L23: -2.7968
REMARK 3 S TENSOR
REMARK 3 S11: 0.0583 S12: 0.2081 S13: -0.5347
REMARK 3 S21: -0.0785 S22: -0.2758 S23: -0.3397
REMARK 3 S31: 0.1609 S32: 0.3120 S33: 0.2174
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 : B 6 B 171
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4181 -29.4386 -12.1281
REMARK 3 T TENSOR
REMARK 3 T11: 0.0295 T22: 0.0491
REMARK 3 T33: 0.0222 T12: 0.0254
REMARK 3 T13: -0.0074 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.7698 L22: 0.2506
REMARK 3 L33: 1.0470 L12: -0.2567
REMARK 3 L13: -0.3534 L23: -0.0100
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: 0.0146 S13: -0.0340
REMARK 3 S21: -0.0051 S22: -0.0199 S23: -0.0361
REMARK 3 S31: -0.0391 S32: 0.0576 S33: 0.0117
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 : E 1 E 56
REMARK 3 ORIGIN FOR THE GROUP (A): -30.7126 -35.4404 -21.3030
REMARK 3 T TENSOR
REMARK 3 T11: 0.0644 T22: 0.1549
REMARK 3 T33: 0.0949 T12: 0.0579
REMARK 3 T13: -0.0703 T23: -0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 6.1616 L22: 2.7836
REMARK 3 L33: 2.0048 L12: 2.9814
REMARK 3 L13: 2.4210 L23: 0.4123
REMARK 3 S TENSOR
REMARK 3 S11: 0.0490 S12: -0.0965 S13: 0.1089
REMARK 3 S21: -0.1799 S22: -0.0313 S23: 0.3580
REMARK 3 S31: -0.0093 S32: -0.3280 S33: -0.0177
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3U1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068188.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25786
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 49.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <I/SIGMA(I)> 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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2IJO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5, 30% PEG 4000, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 217 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 261 LIES ON A SPECIAL POSITION.
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 45
REMARK 465 PRO A 46
REMARK 465 LEU A 47
REMARK 465 GLY A 48
REMARK 465 SER A 49
REMARK 465 VAL A 70
REMARK 465 SER A 71
REMARK 465 HIS A 72
REMARK 465 ASN A 73
REMARK 465 LEU A 74
REMARK 465 MET A 75
REMARK 465 ILE A 76
REMARK 465 THR A 77
REMARK 465 VAL A 78
REMARK 465 ASP A 79
REMARK 465 ASP A 80
REMARK 465 ASP A 81
REMARK 465 GLY A 82
REMARK 465 THR A 83
REMARK 465 MET A 84
REMARK 465 ARG A 85
REMARK 465 ILE A 86
REMARK 465 LYS A 87
REMARK 465 ASP A 88
REMARK 465 ASP A 89
REMARK 465 GLU A 90
REMARK 465 THR A 91
REMARK 465 GLU A 92
REMARK 465 ASN A 93
REMARK 465 ILE A 94
REMARK 465 LEU A 95
REMARK 465 GLY B -8
REMARK 465 GLY B -7
REMARK 465 GLY B -6
REMARK 465 GLY B -5
REMARK 465 SER B -4
REMARK 465 GLY B -3
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 VAL B 3
REMARK 465 LEU B 4
REMARK 465 TRP B 5
REMARK 465 PRO B 172
REMARK 465 ASP B 173
REMARK 465 GLY B 174
REMARK 465 PRO B 175
REMARK 465 THR B 176
REMARK 465 PRO B 177
REMARK 465 GLU B 178
REMARK 465 LEU B 179
REMARK 465 GLU B 180
REMARK 465 GLU B 181
REMARK 465 GLU B 182
REMARK 465 GLY E 57
REMARK 465 ALA E 58
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 ASP B 6 CG OD1 OD2
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 PHE B 31 -7.31 79.14
REMARK 500 THR B 120 -73.83 -65.29
REMARK 500 ASN E 44 107.50 -166.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3U1I RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHOR STATED THE SEQUENCE CONFLICT OF I115T (UNP RESIDUE NUMBER
REMARK 999 1588) WAS A NATURALLY OCCURRING DIFFERENCE.
DBREF 3U1J A 50 95 UNP Q5UB51 POLG_DEN3I 1393 1438
DBREF 3U1J B 1 182 UNP Q5UB51 POLG_DEN3I 1474 1655
DBREF 3U1J E 1 58 UNP P00974 BPT1_BOVIN 36 93
SEQADV 3U1J GLY A 45 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J PRO A 46 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J LEU A 47 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J GLY A 48 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J SER A 49 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J GLY B -8 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J GLY B -7 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J GLY B -6 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J GLY B -5 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J SER B -4 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J GLY B -3 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J GLY B -2 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J GLY B -1 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J GLY B 0 UNP Q5UB51 EXPRESSION TAG
SEQADV 3U1J THR B 115 UNP Q5UB51 ILE 1588 SEE REMARK 999
SEQRES 1 A 51 GLY PRO LEU GLY SER ASP LEU THR VAL GLU LYS ALA ALA
SEQRES 2 A 51 ASP VAL THR TRP GLU GLU GLU ALA GLU GLN THR GLY VAL
SEQRES 3 A 51 SER HIS ASN LEU MET ILE THR VAL ASP ASP ASP GLY THR
SEQRES 4 A 51 MET ARG ILE LYS ASP ASP GLU THR GLU ASN ILE LEU
SEQRES 1 B 191 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY VAL LEU
SEQRES 2 B 191 TRP ASP VAL PRO SER PRO PRO GLU THR GLN LYS ALA GLU
SEQRES 3 B 191 LEU GLU GLU GLY VAL TYR ARG ILE LYS GLN GLN GLY ILE
SEQRES 4 B 191 PHE GLY LYS THR GLN VAL GLY VAL GLY VAL GLN LYS GLU
SEQRES 5 B 191 GLY VAL PHE HIS THR MET TRP HIS VAL THR ARG GLY ALA
SEQRES 6 B 191 VAL LEU THR HIS ASN GLY LYS ARG LEU GLU PRO ASN TRP
SEQRES 7 B 191 ALA SER VAL LYS LYS ASP LEU ILE SER TYR GLY GLY GLY
SEQRES 8 B 191 TRP ARG LEU SER ALA GLN TRP GLN LYS GLY GLU GLU VAL
SEQRES 9 B 191 GLN VAL ILE ALA VAL GLU PRO GLY LYS ASN PRO LYS ASN
SEQRES 10 B 191 PHE GLN THR MET PRO GLY THR PHE GLN THR THR THR GLY
SEQRES 11 B 191 GLU ILE GLY ALA ILE ALA LEU ASP PHE LYS PRO GLY THR
SEQRES 12 B 191 SER GLY SER PRO ILE ILE ASN ARG GLU GLY LYS VAL VAL
SEQRES 13 B 191 GLY LEU TYR GLY ASN GLY VAL VAL THR LYS ASN GLY GLY
SEQRES 14 B 191 TYR VAL SER GLY ILE ALA GLN THR ASN ALA GLU PRO ASP
SEQRES 15 B 191 GLY PRO THR PRO GLU LEU GLU GLU GLU
SEQRES 1 E 58 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO
SEQRES 2 E 58 CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS
SEQRES 3 E 58 ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG
SEQRES 4 E 58 ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET
SEQRES 5 E 58 ARG THR CYS GLY GLY ALA
FORMUL 4 HOH *193(H2 O)
HELIX 1 1 TRP B 50 ARG B 54 1 5
HELIX 2 2 PRO E 2 GLU E 7 5 6
HELIX 3 3 SER E 47 GLY E 56 1 10
SHEET 1 A 6 LEU A 51 ALA A 57 0
SHEET 2 A 6 GLY B 21 GLY B 29 -1 O VAL B 22 N ALA A 57
SHEET 3 A 6 GLY B 32 LYS B 42 -1 O GLN B 41 N GLY B 21
SHEET 4 A 6 VAL B 45 MET B 49 -1 O HIS B 47 N VAL B 40
SHEET 5 A 6 LEU B 76 TYR B 79 -1 O TYR B 79 N PHE B 46
SHEET 6 A 6 PRO B 67 SER B 71 -1 N TRP B 69 O SER B 78
SHEET 1 B 5 GLU A 66 GLY A 69 0
SHEET 2 B 5 LYS B 107 THR B 111 1 O GLN B 110 N GLU A 66
SHEET 3 B 5 VAL B 95 ALA B 99 -1 N VAL B 97 O PHE B 109
SHEET 4 B 5 PRO B 138 ILE B 140 -1 O ILE B 140 N GLN B 96
SHEET 5 B 5 VAL B 146 LEU B 149 -1 O GLY B 148 N ILE B 139
SHEET 1 C 2 LEU B 58 HIS B 60 0
SHEET 2 C 2 LYS B 63 LEU B 65 -1 O LEU B 65 N LEU B 58
SHEET 1 D 4 GLY B 114 GLN B 117 0
SHEET 2 D 4 GLU B 122 ILE B 126 -1 O ILE B 123 N PHE B 116
SHEET 3 D 4 TYR B 161 GLY B 164 -1 O SER B 163 N ILE B 126
SHEET 4 D 4 GLY B 153 VAL B 155 -1 N VAL B 154 O VAL B 162
SHEET 1 E 2 ILE E 18 ASN E 24 0
SHEET 2 E 2 LEU E 29 TYR E 35 -1 O TYR E 35 N ILE E 18
SSBOND 1 CYS E 5 CYS E 55 1555 1555 2.04
SSBOND 2 CYS E 14 CYS E 38 1555 1555 2.04
SSBOND 3 CYS E 30 CYS E 51 1555 1555 2.04
CISPEP 1 GLN A 67 THR A 68 0 3.99
CISPEP 2 ARG E 1 PRO E 2 0 18.48
CRYST1 84.789 84.789 66.031 90.00 90.00 120.00 P 3 2 1 6
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 0.011794 0.006809 0.000000 0.00000
SCALE2 0.000000 0.013618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015144 0.00000
(ATOM LINES ARE NOT SHOWN.)
END