HEADER HYDROLASE/HYDROLASE INHIBITOR 01-DEC-14 4RW7
TITLE CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (K103N, Y181C)
TITLE 2 VARIANT IN COMPLEX WITH (E)-3-(3-CHLORO-5-(2-(2-(2,4-DIOXO-3,4-
TITLE 3 DIHYDROPYRIMIDIN-1(2H)-YL)ETHOXY)PHENOXY)PHENYL)ACRYLONITRILE
TITLE 4 (JLJ532), A NON-NUCLEOSIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REVERSE TRANSCRIPTASE/RIBONUCLEASE H, P66 SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: REVERSE TRANSCRIPTASE/RIBONUCLEASE H, EXORIBONUCLEASE H, P66
COMPND 5 RT;
COMPND 6 EC: 2.7.7.49, 2.7.7.7, 3.1.26.13, 3.1.13.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: REVERSE TRANSCRIPTASE/RIBONUCLEASE H, P51 SUBUNIT;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: P51 RT;
COMPND 13 EC: 2.7.7.49;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 BH10;
SOURCE 3 ORGANISM_COMMON: HIV-1;
SOURCE 4 ORGANISM_TAXID: 11678;
SOURCE 5 STRAIN: BH10 ISOLATE;
SOURCE 6 GENE: GAG-POL;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCDF-2;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 BH10;
SOURCE 14 ORGANISM_COMMON: HIV-1;
SOURCE 15 ORGANISM_TAXID: 11678;
SOURCE 16 STRAIN: BH10 ISOLATE;
SOURCE 17 GENE: GAG-POL;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PCDF-2
KEYWDS POLYMERASE, TRANSFERASE, RNASEH, HYDROLASE, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.FREY,K.S.ANDERSON
REVDAT 3 20-SEP-23 4RW7 1 REMARK SEQADV
REVDAT 2 22-NOV-17 4RW7 1 REMARK
REVDAT 1 29-APR-15 4RW7 0
JRNL AUTH K.M.FREY,D.E.PULEO,K.A.SPASOV,M.BOLLINI,W.L.JORGENSEN,
JRNL AUTH 2 K.S.ANDERSON
JRNL TITL STRUCTURE-BASED EVALUATION OF NON-NUCLEOSIDE INHIBITORS WITH
JRNL TITL 2 IMPROVED POTENCY AND SOLUBILITY THAT TARGET HIV REVERSE
JRNL TITL 3 TRANSCRIPTASE VARIANTS.
JRNL REF J.MED.CHEM. V. 58 2737 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 25700160
JRNL DOI 10.1021/JM501908A
REMARK 2
REMARK 2 RESOLUTION. 3.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 25024
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 34.9673 - 7.2439 0.96 1646 144 0.1954 0.1904
REMARK 3 2 7.2439 - 5.7580 1.00 1679 145 0.2404 0.2970
REMARK 3 3 5.7580 - 5.0326 1.00 1666 145 0.2201 0.2259
REMARK 3 4 5.0326 - 4.5736 1.00 1656 144 0.2055 0.2573
REMARK 3 5 4.5736 - 4.2463 1.00 1654 144 0.2148 0.2558
REMARK 3 6 4.2463 - 3.9964 1.00 1665 143 0.2292 0.2864
REMARK 3 7 3.9964 - 3.7965 1.00 1650 144 0.2359 0.2904
REMARK 3 8 3.7965 - 3.6314 1.00 1636 142 0.2497 0.2917
REMARK 3 9 3.6314 - 3.4917 1.00 1649 144 0.2551 0.3205
REMARK 3 10 3.4917 - 3.3713 1.00 1628 141 0.2736 0.3290
REMARK 3 11 3.3713 - 3.2660 1.00 1636 142 0.2652 0.3328
REMARK 3 12 3.2660 - 3.1727 1.00 1638 142 0.2766 0.3153
REMARK 3 13 3.1727 - 3.0892 1.00 1645 143 0.2712 0.3860
REMARK 3 14 3.0892 - 3.0140 0.96 1576 137 0.2950 0.3322
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) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 85.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.82
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 7954
REMARK 3 ANGLE : 0.724 10813
REMARK 3 CHIRALITY : 0.054 1173
REMARK 3 PLANARITY : 0.004 1361
REMARK 3 DIHEDRAL : 12.477 3007
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4RW7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000087871.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : CRYOGENICALLY COOLED DOUBLE
REMARK 200 CRYSTAL MONOCHROMETER WITH
REMARK 200 HORIZONTAL FOCUSING SAGITTAL
REMARK 200 BEND SECOND MONO CRYSTAL WITH 4:
REMARK 200 1 MAGNIFICATION RATIO AND
REMARK 200 VERTICALLY FOCUSING MIRROR.
REMARK 200 OPTICS : MONOCHROMETER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25032
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.010
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48800
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB CODE: 4H4M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% (W/V) PEG 8000, 100 MM AMMONIUM
REMARK 280 SULFATE, 15 MM MAGNESIUM SULFATE, 5 MM SPERMINE, AND 50 MM
REMARK 280 CITRIC ACID, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 80.97650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.93700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 80.97650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.93700
REMARK 290 SMTRY3 4 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: 5120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 LYS A 64
REMARK 465 LYS A 65
REMARK 465 LYS A 66
REMARK 465 ASP A 67
REMARK 465 SER A 68
REMARK 465 THR A 69
REMARK 465 LYS A 70
REMARK 465 GLU A 89
REMARK 465 VAL A 90
REMARK 465 GLN A 91
REMARK 465 LEU A 92
REMARK 465 ASP A 218
REMARK 465 LYS A 219
REMARK 465 LYS A 220
REMARK 465 HIS A 221
REMARK 465 GLN A 222
REMARK 465 SER A 553
REMARK 465 ALA A 554
REMARK 465 GLY A 555
REMARK 465 PRO B 1
REMARK 465 ILE B 2
REMARK 465 SER B 3
REMARK 465 PRO B 4
REMARK 465 GLY B 213
REMARK 465 LEU B 214
REMARK 465 THR B 215
REMARK 465 THR B 216
REMARK 465 PRO B 217
REMARK 465 ASP B 218
REMARK 465 LYS B 219
REMARK 465 LYS B 220
REMARK 465 HIS B 221
REMARK 465 GLN B 222
REMARK 465 LYS B 223
REMARK 465 GLU B 224
REMARK 465 PRO B 225
REMARK 465 PRO B 226
REMARK 465 PHE B 227
REMARK 465 LEU B 228
REMARK 465 TRP B 229
REMARK 465 MET B 230
REMARK 465 GLY B 231
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 LYS A 102 CG CD CE NZ
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 PRO A 52 C - N - CA ANGL. DEV. = 9.2 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 ASN A 136 -2.81 67.19
REMARK 500 TYR A 183 -77.78 -100.93
REMARK 500 MET A 184 -79.13 -126.45
REMARK 500 ILE A 293 132.73 -171.24
REMARK 500 PHE A 346 -8.87 74.88
REMARK 500 PRO A 412 -175.53 -66.38
REMARK 500 MET B 184 -123.49 54.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3X6 A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4H4M RELATED DB: PDB
REMARK 900 RELATED ID: 4H4O RELATED DB: PDB
REMARK 900 RELATED ID: 4MFB RELATED DB: PDB
REMARK 900 RELATED ID: 1JLA RELATED DB: PDB
REMARK 900 RELATED ID: 1JLC RELATED DB: PDB
REMARK 900 RELATED ID: 1JKH RELATED DB: PDB
REMARK 900 RELATED ID: 4LSL RELATED DB: PDB
REMARK 900 RELATED ID: 3BGR RELATED DB: PDB
REMARK 900 RELATED ID: 4I2Q RELATED DB: PDB
REMARK 900 RELATED ID: 4RW4 RELATED DB: PDB
REMARK 900 RELATED ID: 4RW6 RELATED DB: PDB
REMARK 900 RELATED ID: 4RW8 RELATED DB: PDB
REMARK 900 RELATED ID: 4RW9 RELATED DB: PDB
DBREF 4RW7 A 1 555 UNP P03366 POL_HV1B1 600 1154
DBREF 4RW7 B 1 428 UNP P03366 POL_HV1B1 600 1027
SEQADV 4RW7 MET A -1 UNP P03366 EXPRESSION TAG
SEQADV 4RW7 VAL A 0 UNP P03366 EXPRESSION TAG
SEQADV 4RW7 ASN A 103 UNP P03366 LYS 702 ENGINEERED MUTATION
SEQADV 4RW7 ALA A 172 UNP P03366 LYS 771 ENGINEERED MUTATION
SEQADV 4RW7 ALA A 173 UNP P03366 LYS 772 ENGINEERED MUTATION
SEQADV 4RW7 CYS A 181 UNP P03366 TYR 780 ENGINEERED MUTATION
SEQADV 4RW7 SER A 280 UNP P03366 CYS 879 ENGINEERED MUTATION
SEQADV 4RW7 SER B 280 UNP P03366 CYS 879 ENGINEERED MUTATION
SEQRES 1 A 557 MET VAL PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS
SEQRES 2 A 557 LEU LYS PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP
SEQRES 3 A 557 PRO LEU THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE
SEQRES 4 A 557 CYS THR GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE
SEQRES 5 A 557 GLY PRO GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE
SEQRES 6 A 557 LYS LYS LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP
SEQRES 7 A 557 PHE ARG GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU
SEQRES 8 A 557 VAL GLN LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS
SEQRES 9 A 557 ASN LYS SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR
SEQRES 10 A 557 PHE SER VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR
SEQRES 11 A 557 ALA PHE THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY
SEQRES 12 A 557 ILE ARG TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS
SEQRES 13 A 557 GLY SER PRO ALA ILE PHE GLN SER SER MET THR LYS ILE
SEQRES 14 A 557 LEU GLU PRO PHE ALA ALA GLN ASN PRO ASP ILE VAL ILE
SEQRES 15 A 557 CYS GLN TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU
SEQRES 16 A 557 GLU ILE GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG
SEQRES 17 A 557 GLN HIS LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS
SEQRES 18 A 557 LYS HIS GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR
SEQRES 19 A 557 GLU LEU HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL
SEQRES 20 A 557 LEU PRO GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN
SEQRES 21 A 557 LYS LEU VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR
SEQRES 22 A 557 PRO GLY ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG
SEQRES 23 A 557 GLY THR LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU
SEQRES 24 A 557 GLU ALA GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU
SEQRES 25 A 557 LYS GLU PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS
SEQRES 26 A 557 ASP LEU ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN
SEQRES 27 A 557 TRP THR TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU
SEQRES 28 A 557 LYS THR GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR
SEQRES 29 A 557 ASN ASP VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE
SEQRES 30 A 557 THR THR GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS
SEQRES 31 A 557 PHE LYS LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP
SEQRES 32 A 557 TRP THR GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP
SEQRES 33 A 557 GLU PHE VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR
SEQRES 34 A 557 GLN LEU GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE
SEQRES 35 A 557 TYR VAL ASP GLY ALA ALA ASN ARG GLU THR LYS LEU GLY
SEQRES 36 A 557 LYS ALA GLY TYR VAL THR ASN LYS GLY ARG GLN LYS VAL
SEQRES 37 A 557 VAL PRO LEU THR ASN THR THR ASN GLN LYS THR GLU LEU
SEQRES 38 A 557 GLN ALA ILE TYR LEU ALA LEU GLN ASP SER GLY LEU GLU
SEQRES 39 A 557 VAL ASN ILE VAL THR ASP SER GLN TYR ALA LEU GLY ILE
SEQRES 40 A 557 ILE GLN ALA GLN PRO ASP LYS SER GLU SER GLU LEU VAL
SEQRES 41 A 557 ASN GLN ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS VAL
SEQRES 42 A 557 TYR LEU ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY GLY
SEQRES 43 A 557 ASN GLU GLN VAL ASP LYS LEU VAL SER ALA GLY
SEQRES 1 B 428 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 B 428 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 B 428 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 B 428 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 B 428 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 B 428 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 B 428 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 B 428 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS
SEQRES 9 B 428 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 B 428 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 B 428 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 B 428 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 B 428 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 B 428 PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 B 428 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 B 428 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 B 428 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 B 428 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 B 428 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 B 428 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 B 428 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 B 428 ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG GLY THR
SEQRES 23 B 428 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 B 428 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 B 428 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 B 428 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 B 428 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 B 428 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 B 428 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 B 428 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 B 428 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 B 428 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 B 428 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN
HET 3X6 A 601 29
HETNAM 3X6 (2E)-3-(3-CHLORO-5-{2-[2-(2,4-DIOXO-3,4-
HETNAM 2 3X6 DIHYDROPYRIMIDIN-1(2H)-YL)ETHOXY]PHENOXY}PHENYL)PROP-
HETNAM 3 3X6 2-ENENITRILE
FORMUL 3 3X6 C21 H16 CL N3 O4
HELIX 1 1 THR A 27 GLY A 45 1 19
HELIX 2 2 PHE A 77 THR A 84 1 8
HELIX 3 3 HIS A 96 LEU A 100 5 5
HELIX 4 4 ALA A 114 VAL A 118 5 5
HELIX 5 5 SER A 134 GLU A 138 5 5
HELIX 6 6 GLY A 155 ASN A 175 1 21
HELIX 7 7 GLU A 194 TRP A 212 1 19
HELIX 8 8 THR A 253 SER A 268 1 16
HELIX 9 9 VAL A 276 LEU A 282 1 7
HELIX 10 10 THR A 296 LEU A 310 1 15
HELIX 11 11 ASN A 363 TRP A 383 1 21
HELIX 12 12 GLN A 394 TYR A 405 1 12
HELIX 13 13 THR A 473 ASP A 488 1 16
HELIX 14 14 SER A 499 GLN A 507 1 9
HELIX 15 15 SER A 515 LYS A 528 1 14
HELIX 16 16 THR B 27 GLU B 44 1 18
HELIX 17 17 PHE B 77 THR B 84 1 8
HELIX 18 18 ALA B 114 VAL B 118 5 5
HELIX 19 19 ASP B 121 LYS B 126 1 6
HELIX 20 20 TYR B 127 ALA B 129 5 3
HELIX 21 21 SER B 134 GLU B 138 5 5
HELIX 22 22 LYS B 154 PHE B 160 1 7
HELIX 23 23 PHE B 160 ASN B 175 1 16
HELIX 24 24 GLU B 194 ARG B 211 1 18
HELIX 25 25 HIS B 235 TRP B 239 5 5
HELIX 26 26 THR B 253 TYR B 271 1 19
HELIX 27 27 VAL B 276 LYS B 281 1 6
HELIX 28 28 THR B 296 LYS B 311 1 16
HELIX 29 29 ASN B 363 GLY B 384 1 22
HELIX 30 30 GLN B 394 TRP B 402 1 9
HELIX 31 31 THR B 403 TYR B 405 5 3
HELIX 32 32 LYS B 424 GLN B 428 5 5
SHEET 1 A 3 ILE A 47 LYS A 49 0
SHEET 2 A 3 ILE A 142 TYR A 146 -1 O GLN A 145 N SER A 48
SHEET 3 A 3 PHE A 130 ILE A 132 -1 N ILE A 132 O ILE A 142
SHEET 1 B 2 VAL A 60 ALA A 62 0
SHEET 2 B 2 LYS A 73 VAL A 75 -1 O LEU A 74 N PHE A 61
SHEET 1 C 3 SER A 105 ASP A 110 0
SHEET 2 C 3 ASP A 186 SER A 191 -1 O SER A 191 N SER A 105
SHEET 3 C 3 ILE A 178 GLN A 182 -1 N VAL A 179 O GLY A 190
SHEET 1 D 3 PHE A 227 TRP A 229 0
SHEET 2 D 3 TYR A 232 LEU A 234 -1 O TYR A 232 N TRP A 229
SHEET 3 D 3 TRP A 239 VAL A 241 -1 O THR A 240 N GLU A 233
SHEET 1 E 5 LYS A 347 ALA A 355 0
SHEET 2 E 5 GLN A 336 GLU A 344 -1 N ILE A 341 O LYS A 350
SHEET 3 E 5 ILE A 326 GLY A 333 -1 N GLN A 330 O THR A 338
SHEET 4 E 5 LYS A 388 LEU A 391 1 O LYS A 388 N ALA A 327
SHEET 5 E 5 TRP A 414 PHE A 416 1 O GLU A 415 N LEU A 391
SHEET 1 F 2 HIS A 361 THR A 362 0
SHEET 2 F 2 LYS A 512 SER A 513 -1 O LYS A 512 N THR A 362
SHEET 1 G 5 GLN A 464 THR A 470 0
SHEET 2 G 5 LEU A 452 THR A 459 -1 N ALA A 455 O VAL A 467
SHEET 3 G 5 GLU A 438 ALA A 446 -1 N TYR A 441 O VAL A 458
SHEET 4 G 5 GLU A 492 THR A 497 1 O ASN A 494 N PHE A 440
SHEET 5 G 5 LYS A 530 TRP A 535 1 O ALA A 534 N ILE A 495
SHEET 1 H 3 ILE B 47 LYS B 49 0
SHEET 2 H 3 ILE B 142 TYR B 146 -1 O GLN B 145 N SER B 48
SHEET 3 H 3 PHE B 130 ILE B 132 -1 N ILE B 132 O ILE B 142
SHEET 1 I 2 VAL B 60 LYS B 64 0
SHEET 2 I 2 TRP B 71 VAL B 75 -1 O LEU B 74 N PHE B 61
SHEET 1 J 4 VAL B 179 TYR B 183 0
SHEET 2 J 4 ASP B 186 SER B 191 -1 O ASP B 186 N TYR B 183
SHEET 3 J 4 SER B 105 ASP B 110 -1 N THR B 107 O VAL B 189
SHEET 4 J 4 GLU B 233 LEU B 234 -1 O LEU B 234 N VAL B 106
SHEET 1 K 5 ASN B 348 TYR B 354 0
SHEET 2 K 5 GLN B 336 TYR B 342 -1 N TRP B 337 O TYR B 354
SHEET 3 K 5 ILE B 326 GLY B 333 -1 N GLN B 330 O THR B 338
SHEET 4 K 5 LYS B 388 LEU B 391 1 O LYS B 390 N ALA B 327
SHEET 5 K 5 GLU B 413 PHE B 416 1 O GLU B 415 N LEU B 391
CISPEP 1 PRO A 225 PRO A 226 0 1.69
CISPEP 2 PRO A 420 PRO A 421 0 4.06
SITE 1 AC1 14 PRO A 95 LEU A 100 LYS A 101 LYS A 102
SITE 2 AC1 14 ASN A 103 VAL A 106 VAL A 108 VAL A 179
SITE 3 AC1 14 TYR A 188 GLY A 190 TRP A 229 LEU A 234
SITE 4 AC1 14 PRO A 236 TYR A 318
CRYST1 161.953 73.874 108.457 90.00 99.87 90.00 C 1 2 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 0.006175 0.000000 0.001074 0.00000
SCALE2 0.000000 0.013537 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009359 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
