HEADER TRANSFERASE/TRANSFERASE INHIBITOR 04-AUG-11 3TAM
TITLE CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (K103N MUTANT) IN
TITLE 2 COMPLEX WITH INHIBITOR M06
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REVERSE TRANSCRIPTASE/RIBONUCLEASE H;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 590-1147;
COMPND 5 SYNONYM: REVERSE TRANSCRIPTASE/RIBONUCLEASE H, EXORIBONUCLEASE H, P66
COMPND 6 RT;
COMPND 7 EC: 2.7.7.49, 2.7.7.7, 3.1.26.13, 3.1.13.2;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 OTHER_DETAILS: P66 RT;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: P51 RT;
COMPND 13 CHAIN: B;
COMPND 14 FRAGMENT: UNP RESIDUES 588-1027;
COMPND 15 SYNONYM: REVERSE TRANSCRIPTASE/RIBONUCLEASE H, EXORIBONUCLEASE H, P51
COMPND 16 RT;
COMPND 17 EC: 3.4.23.16, 2.7.7.49, 2.7.7.7, 3.1.26.13, 3.1.13.2;
COMPND 18 ENGINEERED: YES;
COMPND 19 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HIV-1 M:B_HXB2R;
SOURCE 3 ORGANISM_COMMON: HIV-1;
SOURCE 4 ORGANISM_TAXID: 11706;
SOURCE 5 STRAIN: HXB2;
SOURCE 6 GENE: GAG-POL, HIV-1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HIV-1 M:B_HXB2R;
SOURCE 11 ORGANISM_COMMON: HIV-1;
SOURCE 12 ORGANISM_TAXID: 11706;
SOURCE 13 STRAIN: HXB2;
SOURCE 14 GENE: GAG-POL, HIV-1;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HIV-1 REVERSE TRANSCRIPTASE, NON-NUCLEOSIDE INHIBITION,
KEYWDS 2 NUCLEOTIDYLTRANFERASE, K103N, HIV-1, TRANSFERASE-TRANSFERASE
KEYWDS 3 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YAN
REVDAT 3 13-SEP-23 3TAM 1 REMARK SEQADV
REVDAT 2 18-JAN-12 3TAM 1 JRNL
REVDAT 1 26-OCT-11 3TAM 0
JRNL AUTH R.GOMEZ,S.JOLLY,T.WILLIAMS,T.TUCKER,R.TYNEBOR,J.VACCA,
JRNL AUTH 2 G.MCGAUGHEY,M.T.LAI,P.FELOCK,V.MUNSHI,D.DESTEFANO,S.TOUCH,
JRNL AUTH 3 M.MILLER,Y.YAN,R.SANCHEZ,Y.LIANG,B.PATON,B.L.WAN,N.ANTHONY
JRNL TITL DESIGN AND SYNTHESIS OF PYRIDONE INHIBITORS OF
JRNL TITL 2 NON-NUCLEOSIDE REVERSE TRANSCRIPTASE.
JRNL REF BIOORG.MED.CHEM.LETT. V. 21 7344 2011
JRNL REFN ISSN 0960-894X
JRNL PMID 22071300
JRNL DOI 10.1016/J.BMCL.2011.10.027
REMARK 2
REMARK 2 RESOLUTION. 2.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.5
REMARK 3 NUMBER OF REFLECTIONS : 42363
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2150
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.51
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.58
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.45
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1045
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2625
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 991
REMARK 3 BIN R VALUE (WORKING SET) : 0.2576
REMARK 3 BIN FREE R VALUE : 0.3603
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.17
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 54
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7837
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 362
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.10890
REMARK 3 B22 (A**2) : -1.09510
REMARK 3 B33 (A**2) : -5.01380
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.340
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.473
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8077 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 10977 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2805 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 230 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1097 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8077 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1041 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 9193 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.25
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.91
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.92
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3TAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067245.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JAN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42589
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.510
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.4
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: BUSTER 2.9.4
REMARK 200 STARTING MODEL: 3LP1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, PH 6.1, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 77.84500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.84500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 58.95500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 76.95000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 58.95500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 76.95000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 77.84500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 58.95500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 76.95000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 77.84500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 58.95500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 76.95000
REMARK 290 SMTRY3 8 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: 5370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 -2
REMARK 465 ASN A -1
REMARK 465 SER A 0
REMARK 465 LYS A 65
REMARK 465 LYS A 66
REMARK 465 ASP A 67
REMARK 465 SER A 68
REMARK 465 LYS A 558
REMARK 465 VAL A 559
REMARK 465 LEU A 560
REMARK 465 MET B -2
REMARK 465 ASN B -1
REMARK 465 SER B 0
REMARK 465 PRO B 1
REMARK 465 ILE B 2
REMARK 465 SER B 3
REMARK 465 PRO B 4
REMARK 465 LYS B 66
REMARK 465 ASP B 67
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 MET B 357
REMARK 465 ARG B 358
REMARK 465 GLY B 359
REMARK 465 ALA B 360
REMARK 465 LEU B 429
REMARK 465 GLU B 430
REMARK 465 LYS B 431
REMARK 465 GLU B 432
REMARK 465 PRO B 433
REMARK 465 ILE B 434
REMARK 465 VAL B 435
REMARK 465 GLY B 436
REMARK 465 ALA B 437
REMARK 465 GLU B 438
REMARK 465 THR B 439
REMARK 465 PHE B 440
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 SER A 3 130.36 -38.91
REMARK 500 PRO A 9 98.31 -67.62
REMARK 500 VAL A 90 -97.43 -22.39
REMARK 500 MET A 184 -119.75 51.35
REMARK 500 ASP A 192 63.73 -102.56
REMARK 500 ILE A 270 -35.67 -136.56
REMARK 500 THR A 286 13.44 51.47
REMARK 500 PRO A 345 108.98 -35.11
REMARK 500 ALA A 355 67.20 -151.77
REMARK 500 PRO A 392 47.57 -81.87
REMARK 500 PRO A 412 -117.29 -61.65
REMARK 500 VAL A 466 119.23 -161.28
REMARK 500 ASP A 471 64.46 -117.83
REMARK 500 HIS A 539 -8.16 67.58
REMARK 500 ASP B 17 -166.11 -124.07
REMARK 500 MET B 184 -125.70 53.50
REMARK 500 GLU B 297 34.15 -84.36
REMARK 500 GLU B 298 -37.42 -130.10
REMARK 500 PRO B 345 -20.83 -32.91
REMARK 500 TYR B 427 78.40 -117.31
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 M06 A 561
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3T19 RELATED DB: PDB
REMARK 900 RELATED ID: 3T1A RELATED DB: PDB
DBREF 3TAM A 3 560 UNP P04585 POL_HV1H2 590 1147
DBREF 3TAM B 1 440 UNP P04585 POL_HV1H2 588 1027
SEQADV 3TAM MET A -2 UNP P04585 EXPRESSION TAG
SEQADV 3TAM ASN A -1 UNP P04585 EXPRESSION TAG
SEQADV 3TAM SER A 0 UNP P04585 EXPRESSION TAG
SEQADV 3TAM PRO A 1 UNP P04585 EXPRESSION TAG
SEQADV 3TAM ILE A 2 UNP P04585 EXPRESSION TAG
SEQADV 3TAM ASN A 103 UNP P04585 LYS 690 ENGINEERED MUTATION
SEQADV 3TAM MET B -2 UNP P04585 EXPRESSION TAG
SEQADV 3TAM ASN B -1 UNP P04585 EXPRESSION TAG
SEQADV 3TAM SER B 0 UNP P04585 EXPRESSION TAG
SEQADV 3TAM ASN B 103 UNP P04585 LYS 690 ENGINEERED MUTATION
SEQRES 1 A 563 MET ASN SER PRO ILE SER PRO ILE GLU THR VAL PRO VAL
SEQRES 2 A 563 LYS LEU LYS PRO GLY MET ASP GLY PRO LYS VAL LYS GLN
SEQRES 3 A 563 TRP PRO LEU THR GLU GLU LYS ILE LYS ALA LEU VAL GLU
SEQRES 4 A 563 ILE CYS THR GLU MET GLU LYS GLU GLY LYS ILE SER LYS
SEQRES 5 A 563 ILE GLY PRO GLU ASN PRO TYR ASN THR PRO VAL PHE ALA
SEQRES 6 A 563 ILE LYS LYS LYS ASP SER THR LYS TRP ARG LYS LEU VAL
SEQRES 7 A 563 ASP PHE ARG GLU LEU ASN LYS ARG THR GLN ASP PHE TRP
SEQRES 8 A 563 GLU VAL GLN LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS
SEQRES 9 A 563 LYS ASN LYS SER VAL THR VAL LEU ASP VAL GLY ASP ALA
SEQRES 10 A 563 TYR PHE SER VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR
SEQRES 11 A 563 THR ALA PHE THR ILE PRO SER ILE ASN ASN GLU THR PRO
SEQRES 12 A 563 GLY ILE ARG TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP
SEQRES 13 A 563 LYS GLY SER PRO ALA ILE PHE GLN SER SER MET THR LYS
SEQRES 14 A 563 ILE LEU GLU PRO PHE ARG LYS GLN ASN PRO ASP ILE VAL
SEQRES 15 A 563 ILE TYR GLN TYR MET ASP ASP LEU TYR VAL GLY SER ASP
SEQRES 16 A 563 LEU GLU ILE GLY GLN HIS ARG THR LYS ILE GLU GLU LEU
SEQRES 17 A 563 ARG GLN HIS LEU LEU ARG TRP GLY LEU THR THR PRO ASP
SEQRES 18 A 563 LYS LYS HIS GLN LYS GLU PRO PRO PHE LEU TRP MET GLY
SEQRES 19 A 563 TYR GLU LEU HIS PRO ASP LYS TRP THR VAL GLN PRO ILE
SEQRES 20 A 563 VAL LEU PRO GLU LYS ASP SER TRP THR VAL ASN ASP ILE
SEQRES 21 A 563 GLN LYS LEU VAL GLY LYS LEU ASN TRP ALA SER GLN ILE
SEQRES 22 A 563 TYR PRO GLY ILE LYS VAL ARG GLN LEU CYS LYS LEU LEU
SEQRES 23 A 563 ARG GLY THR LYS ALA LEU THR GLU VAL ILE PRO LEU THR
SEQRES 24 A 563 GLU GLU ALA GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE
SEQRES 25 A 563 LEU LYS GLU PRO VAL HIS GLY VAL TYR TYR ASP PRO SER
SEQRES 26 A 563 LYS ASP LEU ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY
SEQRES 27 A 563 GLN TRP THR TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN
SEQRES 28 A 563 LEU LYS THR GLY LYS TYR ALA ARG MET ARG GLY ALA HIS
SEQRES 29 A 563 THR ASN ASP VAL LYS GLN LEU THR GLU ALA VAL GLN LYS
SEQRES 30 A 563 ILE THR THR GLU SER ILE VAL ILE TRP GLY LYS THR PRO
SEQRES 31 A 563 LYS PHE LYS LEU PRO ILE GLN LYS GLU THR TRP GLU THR
SEQRES 32 A 563 TRP TRP THR GLU TYR TRP GLN ALA THR TRP ILE PRO GLU
SEQRES 33 A 563 TRP GLU PHE VAL ASN THR PRO PRO LEU VAL LYS LEU TRP
SEQRES 34 A 563 TYR GLN LEU GLU LYS GLU PRO ILE VAL GLY ALA GLU THR
SEQRES 35 A 563 PHE TYR VAL ASP GLY ALA ALA ASN ARG GLU THR LYS LEU
SEQRES 36 A 563 GLY LYS ALA GLY TYR VAL THR ASN ARG GLY ARG GLN LYS
SEQRES 37 A 563 VAL VAL THR LEU THR ASP THR THR ASN GLN LYS THR GLU
SEQRES 38 A 563 LEU GLN ALA ILE TYR LEU ALA LEU GLN ASP SER GLY LEU
SEQRES 39 A 563 GLU VAL ASN ILE VAL THR ASP SER GLN TYR ALA LEU GLY
SEQRES 40 A 563 ILE ILE GLN ALA GLN PRO ASP GLN SER GLU SER GLU LEU
SEQRES 41 A 563 VAL ASN GLN ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS
SEQRES 42 A 563 VAL TYR LEU ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY
SEQRES 43 A 563 GLY ASN GLU GLN VAL ASP LYS LEU VAL SER ALA GLY ILE
SEQRES 44 A 563 ARG LYS VAL LEU
SEQRES 1 B 443 MET ASN SER PRO ILE SER PRO ILE GLU THR VAL PRO VAL
SEQRES 2 B 443 LYS LEU LYS PRO GLY MET ASP GLY PRO LYS VAL LYS GLN
SEQRES 3 B 443 TRP PRO LEU THR GLU GLU LYS ILE LYS ALA LEU VAL GLU
SEQRES 4 B 443 ILE CYS THR GLU MET GLU LYS GLU GLY LYS ILE SER LYS
SEQRES 5 B 443 ILE GLY PRO GLU ASN PRO TYR ASN THR PRO VAL PHE ALA
SEQRES 6 B 443 ILE LYS LYS LYS ASP SER THR LYS TRP ARG LYS LEU VAL
SEQRES 7 B 443 ASP PHE ARG GLU LEU ASN LYS ARG THR GLN ASP PHE TRP
SEQRES 8 B 443 GLU VAL GLN LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS
SEQRES 9 B 443 LYS ASN LYS SER VAL THR VAL LEU ASP VAL GLY ASP ALA
SEQRES 10 B 443 TYR PHE SER VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR
SEQRES 11 B 443 THR ALA PHE THR ILE PRO SER ILE ASN ASN GLU THR PRO
SEQRES 12 B 443 GLY ILE ARG TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP
SEQRES 13 B 443 LYS GLY SER PRO ALA ILE PHE GLN SER SER MET THR LYS
SEQRES 14 B 443 ILE LEU GLU PRO PHE ARG LYS GLN ASN PRO ASP ILE VAL
SEQRES 15 B 443 ILE TYR GLN TYR MET ASP ASP LEU TYR VAL GLY SER ASP
SEQRES 16 B 443 LEU GLU ILE GLY GLN HIS ARG THR LYS ILE GLU GLU LEU
SEQRES 17 B 443 ARG GLN HIS LEU LEU ARG TRP GLY LEU THR THR PRO ASP
SEQRES 18 B 443 LYS LYS HIS GLN LYS GLU PRO PRO PHE LEU TRP MET GLY
SEQRES 19 B 443 TYR GLU LEU HIS PRO ASP LYS TRP THR VAL GLN PRO ILE
SEQRES 20 B 443 VAL LEU PRO GLU LYS ASP SER TRP THR VAL ASN ASP ILE
SEQRES 21 B 443 GLN LYS LEU VAL GLY LYS LEU ASN TRP ALA SER GLN ILE
SEQRES 22 B 443 TYR PRO GLY ILE LYS VAL ARG GLN LEU CYS LYS LEU LEU
SEQRES 23 B 443 ARG GLY THR LYS ALA LEU THR GLU VAL ILE PRO LEU THR
SEQRES 24 B 443 GLU GLU ALA GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE
SEQRES 25 B 443 LEU LYS GLU PRO VAL HIS GLY VAL TYR TYR ASP PRO SER
SEQRES 26 B 443 LYS ASP LEU ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY
SEQRES 27 B 443 GLN TRP THR TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN
SEQRES 28 B 443 LEU LYS THR GLY LYS TYR ALA ARG MET ARG GLY ALA HIS
SEQRES 29 B 443 THR ASN ASP VAL LYS GLN LEU THR GLU ALA VAL GLN LYS
SEQRES 30 B 443 ILE THR THR GLU SER ILE VAL ILE TRP GLY LYS THR PRO
SEQRES 31 B 443 LYS PHE LYS LEU PRO ILE GLN LYS GLU THR TRP GLU THR
SEQRES 32 B 443 TRP TRP THR GLU TYR TRP GLN ALA THR TRP ILE PRO GLU
SEQRES 33 B 443 TRP GLU PHE VAL ASN THR PRO PRO LEU VAL LYS LEU TRP
SEQRES 34 B 443 TYR GLN LEU GLU LYS GLU PRO ILE VAL GLY ALA GLU THR
SEQRES 35 B 443 PHE
HET M06 A 561 28
HETNAM M06 3-CHLORO-5-{[4-METHYL-2-OXO-1-(2H-PYRAZOLO[3,4-
HETNAM 2 M06 B]PYRIDIN-3-YLMETHYL)-1,2-DIHYDROPYRIDIN-3-
HETNAM 3 M06 YL]OXY}BENZONITRILE
FORMUL 3 M06 C20 H14 CL N5 O2
FORMUL 4 HOH *362(H2 O)
HELIX 1 1 THR A 27 GLU A 44 1 18
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 ASP A 121 LYS A 126 1 6
HELIX 6 6 TYR A 127 ALA A 129 5 3
HELIX 7 7 SER A 134 GLU A 138 5 5
HELIX 8 8 GLY A 155 ASN A 175 1 21
HELIX 9 9 GLY A 196 ARG A 211 1 16
HELIX 10 10 THR A 253 SER A 268 1 16
HELIX 11 11 VAL A 276 LEU A 283 1 8
HELIX 12 12 THR A 296 GLU A 297 1 2
HELIX 13 13 GLU A 298 LYS A 311 1 14
HELIX 14 14 ASN A 363 GLY A 384 1 22
HELIX 15 15 GLN A 394 TYR A 405 1 12
HELIX 16 16 THR A 473 SER A 489 1 17
HELIX 17 17 SER A 499 ALA A 508 1 10
HELIX 18 18 SER A 515 LYS A 528 1 14
HELIX 19 19 ILE A 542 ALA A 554 1 13
HELIX 20 20 THR B 27 GLU B 44 1 18
HELIX 21 21 PHE B 77 THR B 84 1 8
HELIX 22 22 THR B 84 VAL B 90 1 7
HELIX 23 23 GLY B 99 ASN B 103 5 5
HELIX 24 24 GLY B 112 VAL B 118 5 7
HELIX 25 25 PHE B 124 ALA B 129 5 6
HELIX 26 26 SER B 134 GLU B 138 5 5
HELIX 27 27 LYS B 154 ASN B 175 1 22
HELIX 28 28 GLU B 194 GLY B 213 1 20
HELIX 29 29 HIS B 235 TRP B 239 5 5
HELIX 30 30 THR B 253 TYR B 271 1 19
HELIX 31 31 VAL B 276 LEU B 282 1 7
HELIX 32 32 GLU B 298 LYS B 311 1 14
HELIX 33 33 ASN B 363 GLY B 384 1 22
HELIX 34 34 GLN B 394 TRP B 402 1 9
HELIX 35 35 THR B 403 TYR B 405 5 3
HELIX 36 36 PRO B 420 TYR B 427 1 8
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 ILE A 63 0
SHEET 2 B 2 ARG A 72 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 VAL A 189 N THR A 107
SHEET 3 C 3 ILE A 178 TYR A 183 -1 N TYR A 181 O TYR A 188
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 TYR A 354 0
SHEET 2 E 5 TRP A 337 GLU A 344 -1 N ILE A 341 O LYS A 350
SHEET 3 E 5 ILE A 326 LYS A 331 -1 N ILE A 326 O TYR A 342
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 GLN A 512 SER A 513 -1 O GLN A 512 N THR A 362
SHEET 1 G 5 GLN A 464 LEU A 469 0
SHEET 2 G 5 GLY A 453 THR A 459 -1 N GLY A 453 O LEU A 469
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 VAL A 496 N PHE A 440
SHEET 5 G 5 LYS A 530 TRP A 535 1 O TYR A 532 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 TYR B 188 N TYR B 181
SHEET 3 J 4 SER B 105 ASP B 110 -1 N THR B 107 O VAL B 189
SHEET 4 J 4 TYR B 232 LEU B 234 -1 O LEU B 234 N VAL B 106
SHEET 1 K 5 LYS B 347 ALA B 355 0
SHEET 2 K 5 GLN B 336 GLU B 344 -1 N TRP B 337 O TYR B 354
SHEET 3 K 5 ILE B 326 GLY B 333 -1 N ILE B 326 O TYR B 342
SHEET 4 K 5 LYS B 388 LEU B 391 1 O LYS B 388 N ALA B 327
SHEET 5 K 5 GLU B 413 PHE B 416 1 O GLU B 413 N PHE B 389
CISPEP 1 PRO A 225 PRO A 226 0 3.58
CISPEP 2 PRO A 420 PRO A 421 0 -1.71
SITE 1 AC1 11 LYS A 101 ASN A 103 VAL A 106 TYR A 188
SITE 2 AC1 11 PRO A 225 PHE A 227 TRP A 229 LEU A 234
SITE 3 AC1 11 HIS A 235 PRO A 236 TYR A 318
CRYST1 117.910 153.900 155.690 90.00 90.00 90.00 C 2 2 21 8
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 0.008481 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006498 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006423 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
