HEADER NUCLEOTIDYLTRANSFERASE 19-APR-95 1VRU
TITLE HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR RT-
TITLE 2 INHIBITOR COMPLEXES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 REVERSE TRANSCRIPTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HIV-1 RT;
COMPND 5 EC: 2.7.7.49;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HIV-1 REVERSE TRANSCRIPTASE;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: HIV-1 RT;
COMPND 11 EC: 2.7.7.49;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 CELL_LINE: 293;
SOURCE 5 GENE: HIV-1 POL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: 293;
SOURCE 9 EXPRESSION_SYSTEM_GENE: HIV-1 POL;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 12 ORGANISM_TAXID: 11676;
SOURCE 13 STRAIN: HXB2 ISOLATE;
SOURCE 14 CELL_LINE: 293;
SOURCE 15 GENE: HIV-1 POL;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: 293;
SOURCE 19 EXPRESSION_SYSTEM_GENE: HIV-1 POL
KEYWDS HIV-1 REVERSE TRANSCRIPTASE, NUCLEOTIDYLTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.REN,R.ESNOUF,E.GARMAN,D.SOMERS,C.ROSS,I.KIRBY,J.KEELING,
AUTHOR 2 G.DARBY,Y.JONES,D.STUART,D.STAMMERS
REVDAT 3 24-FEB-09 1VRU 1 VERSN
REVDAT 2 01-APR-03 1VRU 1 JRNL
REVDAT 1 03-APR-96 1VRU 0
JRNL AUTH J.REN,R.ESNOUF,E.GARMAN,D.SOMERS,C.ROSS,I.KIRBY,
JRNL AUTH 2 J.KEELING,G.DARBY,Y.JONES,D.STUART
JRNL TITL HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR
JRNL TITL 2 RT-INHIBITOR COMPLEXES.
JRNL REF NAT.STRUCT.BIOL. V. 2 293 1995
JRNL REFN ISSN 1072-8368
JRNL PMID 7540934
JRNL DOI 10.1038/NSB0495-293
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.ESNOUF,J.REN,C.ROSS,Y.JONES,D.STAMMERS,D.STUART
REMARK 1 TITL MECHANISM OF INHIBITION OF HIV-1 REVERSE
REMARK 1 TITL 2 TRANSCRIPTASE BY NON-NUCLEOSIDE INHIBITORS
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 303 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.K.STAMMERS,D.SOMERS,C.K.ROSS,I.KIRBY,P.H.RAY,
REMARK 1 AUTH 2 J.E.WILSON,M.NORMAN,J.S.REN,R.M.ESNOUF,E.F.GARMAN,
REMARK 1 AUTH 3 E.Y.JONES,D.I.STUART
REMARK 1 TITL CRYSTALS OF HIV-1 REVERSE TRANSCRIPTASE
REMARK 1 TITL 2 DIFFRACTING TO 2.2 ANGSTROM RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 242 586 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.5
REMARK 3 NUMBER OF REFLECTIONS : 38354
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 7698
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.00
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 2.00
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.80
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1VRU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAR-94
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : BAS-III
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38354
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.5
REMARK 200 DATA REDUNDANCY : 5.710
REMARK 200 R MERGE (I) : 0.12800
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: DATA WERE COLLECTED USING THE WEISSENBERG METHOD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 71.60000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 71.60000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.40000
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: 5520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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 PRO A 1
REMARK 465 ILE A 2
REMARK 465 GLY A 444
REMARK 465 ALA A 445
REMARK 465 ALA A 446
REMARK 465 ASN A 447
REMARK 465 ARG A 448
REMARK 465 GLU A 449
REMARK 465 THR A 450
REMARK 465 LYS A 451
REMARK 465 LEU A 452
REMARK 465 GLY A 453
REMARK 465 LYS A 454
REMARK 465 LYS A 540
REMARK 465 GLY A 541
REMARK 465 ILE A 542
REMARK 465 GLY A 543
REMARK 465 GLY A 544
REMARK 465 ASN A 545
REMARK 465 GLU A 546
REMARK 465 GLN A 547
REMARK 465 VAL A 548
REMARK 465 ASP A 549
REMARK 465 LYS A 550
REMARK 465 LEU A 551
REMARK 465 VAL A 552
REMARK 465 SER A 553
REMARK 465 ALA A 554
REMARK 465 GLY A 555
REMARK 465 ILE A 556
REMARK 465 ARG A 557
REMARK 465 LYS A 558
REMARK 465 VAL A 559
REMARK 465 LEU A 560
REMARK 465 PRO B 1
REMARK 465 ILE B 2
REMARK 465 SER B 3
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 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: 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 ASN A 54 N - CA - C ANGL. DEV. = -25.3 DEGREES
REMARK 500 ALA A 538 N - CA - C ANGL. DEV. = 18.5 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 ILE A 50 -168.47 -111.12
REMARK 500 LYS A 65 -92.90 -131.41
REMARK 500 SER A 68 159.01 180.00
REMARK 500 GLU A 89 103.16 -35.84
REMARK 500 VAL A 90 101.29 -55.38
REMARK 500 GLN A 91 85.68 38.10
REMARK 500 ASP A 113 21.68 38.71
REMARK 500 ASN A 137 -73.38 -41.75
REMARK 500 PRO A 140 -110.18 -10.62
REMARK 500 VAL A 148 -163.23 -112.68
REMARK 500 MET A 184 -116.35 62.61
REMARK 500 ILE A 195 -56.71 -28.28
REMARK 500 LYS A 219 -70.79 1.56
REMARK 500 PRO A 243 135.65 -36.91
REMARK 500 PRO A 345 118.67 -37.97
REMARK 500 LYS A 347 74.36 -107.24
REMARK 500 ALA A 355 25.27 -141.66
REMARK 500 PRO A 412 -174.10 -50.29
REMARK 500 ARG A 463 154.24 -48.34
REMARK 500 LYS A 465 146.66 -171.54
REMARK 500 ILE B 5 176.87 -59.94
REMARK 500 VAL B 90 67.39 -67.75
REMARK 500 GLN B 91 -54.49 -159.47
REMARK 500 LEU B 92 -35.72 -145.92
REMARK 500 ILE B 94 73.14 31.33
REMARK 500 PRO B 95 -167.10 -68.82
REMARK 500 PRO B 97 85.18 -67.40
REMARK 500 LEU B 168 36.03 -96.80
REMARK 500 ASN B 175 77.45 175.87
REMARK 500 MET B 184 -115.37 56.34
REMARK 500 SER B 191 177.98 177.49
REMARK 500 LEU B 193 162.02 -48.37
REMARK 500 ILE B 195 -32.70 -33.28
REMARK 500 GLU B 204 -71.34 -54.50
REMARK 500 ARG B 211 0.51 -66.60
REMARK 500 LEU B 214 173.23 170.45
REMARK 500 GLU B 233 29.27 -142.25
REMARK 500 LEU B 234 164.57 -45.70
REMARK 500 PHE B 346 -42.86 86.98
REMARK 500 HIS B 361 -77.41 -161.25
REMARK 500 THR B 362 -66.08 -29.83
REMARK 500 ASN B 363 144.29 155.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 146 0.07 SIDE_CHAIN
REMARK 500 TYR A 181 0.07 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASN A 54 48.1 L L OUTSIDE RANGE
REMARK 500 ASN A 137 23.8 L L OUTSIDE RANGE
REMARK 500 LYS A 219 24.3 L L OUTSIDE RANGE
REMARK 500 ALA A 538 20.1 L L OUTSIDE RANGE
REMARK 500 HIS A 539 24.9 L L OUTSIDE RANGE
REMARK 500 PHE B 87 25.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B1087 DISTANCE = 5.09 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AAP A 999
DBREF 1VRU A 1 560 UNP P04585 POL_HV1H2 587 1146
DBREF 1VRU B 1 440 UNP P04585 POL_HV1H2 587 1026
SEQRES 1 A 560 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 A 560 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 A 560 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 A 560 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 A 560 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 A 560 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 A 560 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 A 560 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS
SEQRES 9 A 560 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 A 560 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 A 560 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 A 560 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 A 560 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 A 560 PRO PHE ARG LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 A 560 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 A 560 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 A 560 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 A 560 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 A 560 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 A 560 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 A 560 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 A 560 ILE LYS VAL ARG GLN LEU CSD LYS LEU LEU ARG GLY THR
SEQRES 23 A 560 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 A 560 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 A 560 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 A 560 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 A 560 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 A 560 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 A 560 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 A 560 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 A 560 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 A 560 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 A 560 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 A 560 GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE TYR VAL
SEQRES 35 A 560 ASP GLY ALA ALA ASN ARG GLU THR LYS LEU GLY LYS ALA
SEQRES 36 A 560 GLY TYR VAL THR ASN ARG GLY ARG GLN LYS VAL VAL THR
SEQRES 37 A 560 LEU THR ASP THR THR ASN GLN LYS THR GLU LEU GLN ALA
SEQRES 38 A 560 ILE TYR LEU ALA LEU GLN ASP SER GLY LEU GLU VAL ASN
SEQRES 39 A 560 ILE VAL THR ASP SER GLN TYR ALA LEU GLY ILE ILE GLN
SEQRES 40 A 560 ALA GLN PRO ASP GLN SER GLU SER GLU LEU VAL ASN GLN
SEQRES 41 A 560 ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS VAL TYR LEU
SEQRES 42 A 560 ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY GLY ASN GLU
SEQRES 43 A 560 GLN VAL ASP LYS LEU VAL SER ALA GLY ILE ARG LYS VAL
SEQRES 44 A 560 LEU
SEQRES 1 B 440 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 B 440 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 B 440 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 B 440 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 B 440 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 B 440 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 B 440 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 B 440 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS
SEQRES 9 B 440 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 B 440 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 B 440 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 B 440 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 B 440 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 B 440 PRO PHE ARG LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 B 440 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 B 440 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 B 440 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 B 440 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 B 440 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 B 440 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 B 440 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 B 440 ILE LYS VAL ARG GLN LEU CYS LYS LEU LEU ARG GLY THR
SEQRES 23 B 440 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 B 440 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 B 440 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 B 440 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 B 440 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 B 440 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 B 440 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 B 440 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 B 440 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 B 440 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 B 440 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 B 440 GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE
MODRES 1VRU CSD A 280 CYS 3-SULFINOALANINE
HET CSD A 280 8
HET AAP A 999 23
HETNAM CSD 3-SULFINOALANINE
HETNAM AAP ALPHA-(2,6-DICHLOROPHENYL)-ALPHA-(2-ACETYL-5-
HETNAM 2 AAP METHYLANILINO)ACETAMIDE
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL 1 CSD C3 H7 N O4 S
FORMUL 3 AAP C17 H16 CL2 N2 O2
FORMUL 4 HOH *131(H2 O)
HELIX 1 1 GLU A 28 GLU A 44 1 17
HELIX 2 2 ARG A 78 ARG A 83 1 6
HELIX 3 3 PRO A 97 GLY A 99 5 3
HELIX 4 4 ALA A 114 SER A 117 1 4
HELIX 5 5 ARG A 125 THR A 128 5 4
HELIX 6 6 SER A 156 GLN A 174 1 19
HELIX 7 7 ILE A 195 TRP A 212 1 18
HELIX 8 8 LYS A 219 HIS A 221 5 3
HELIX 9 9 VAL A 254 GLN A 269 1 16
HELIX 10 10 ARG A 277 LEU A 283 1 7
HELIX 11 11 GLU A 297 LYS A 311 1 15
HELIX 12 12 ASP A 364 TRP A 383 1 20
HELIX 13 13 LYS A 395 GLU A 404 1 10
HELIX 14 14 ASN A 474 ASP A 488 1 15
HELIX 15 15 GLN A 500 ALA A 508 1 9
HELIX 16 16 GLU A 516 LYS A 527 1 12
HELIX 17 17 GLU B 28 LYS B 43 1 16
HELIX 18 18 ARG B 78 ARG B 83 1 6
HELIX 19 19 ALA B 98 LYS B 102 5 5
HELIX 20 20 GLY B 112 SER B 117 5 6
HELIX 21 21 ARG B 125 THR B 128 5 4
HELIX 22 22 ILE B 135 ASN B 137 5 3
HELIX 23 23 LYS B 154 ILE B 167 1 14
HELIX 24 24 GLU B 169 GLN B 174 1 6
HELIX 25 25 ILE B 195 GLY B 213 1 19
HELIX 26 26 PRO B 236 LYS B 238 5 3
HELIX 27 27 VAL B 254 GLN B 269 1 16
HELIX 28 28 ARG B 277 LEU B 283 1 7
HELIX 29 29 GLU B 297 LYS B 311 1 15
HELIX 30 30 ASP B 364 TRP B 383 1 20
HELIX 31 31 LYS B 395 TYR B 405 1 11
HELIX 32 32 PRO B 421 LEU B 425 1 5
SHEET 1 A 3 ILE A 47 LYS A 49 0
SHEET 2 A 3 ILE A 142 TYR A 146 -1 N GLN A 145 O 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 N LEU A 74 O 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 N SER A 191 O SER A 105
SHEET 3 C 3 VAL A 179 TYR A 183 -1 N TYR A 183 O ASP A 186
SHEET 1 D 3 PHE A 227 TRP A 229 0
SHEET 2 D 3 TYR A 232 LEU A 234 -1 N LEU A 234 O PHE A 227
SHEET 3 D 3 TRP A 239 VAL A 241 -1 N THR A 240 O GLU A 233
SHEET 1 E 5 TRP A 414 PHE A 416 0
SHEET 2 E 5 LYS A 388 LEU A 391 1 N PHE A 389 O GLU A 415
SHEET 3 E 5 ILE A 326 GLY A 333 1 N ALA A 327 O LYS A 388
SHEET 4 E 5 GLN A 336 TYR A 342 -1 N TYR A 342 O ILE A 326
SHEET 5 E 5 ASN A 348 TYR A 354 -1 N TYR A 354 O TRP A 337
SHEET 1 F 5 GLN A 464 VAL A 466 0
SHEET 2 F 5 GLY A 456 THR A 459 -1 N TYR A 457 O LYS A 465
SHEET 3 F 5 THR A 439 VAL A 442 -1 N TYR A 441 O VAL A 458
SHEET 4 F 5 GLU A 492 THR A 497 1 N ASN A 494 O PHE A 440
SHEET 5 F 5 LYS A 530 TRP A 535 1 N LYS A 530 O VAL A 493
SHEET 1 G 3 ILE B 47 LYS B 49 0
SHEET 2 G 3 ILE B 142 TYR B 146 -1 N GLN B 145 O SER B 48
SHEET 3 G 3 PHE B 130 ILE B 132 -1 N ILE B 132 O ILE B 142
SHEET 1 H 2 VAL B 60 LYS B 64 0
SHEET 2 H 2 TRP B 71 VAL B 75 -1 N LEU B 74 O PHE B 61
SHEET 1 I 3 SER B 105 ASP B 110 0
SHEET 2 I 3 ASP B 186 SER B 191 -1 N SER B 191 O SER B 105
SHEET 3 I 3 VAL B 179 TYR B 183 -1 N TYR B 183 O ASP B 186
SHEET 1 J 5 TRP B 414 PHE B 416 0
SHEET 2 J 5 LYS B 388 LEU B 391 1 N PHE B 389 O GLU B 415
SHEET 3 J 5 ILE B 326 LYS B 331 1 N ALA B 327 O LYS B 388
SHEET 4 J 5 GLN B 336 TYR B 342 -1 N TYR B 342 O ILE B 326
SHEET 5 J 5 ASN B 348 ALA B 355 -1 N TYR B 354 O TRP B 337
LINK C LEU A 279 N CSD A 280 1555 1555 1.33
LINK C CSD A 280 N LYS A 281 1555 1555 1.33
CISPEP 1 PRO A 225 PRO A 226 0 0.16
CISPEP 2 PRO A 420 PRO A 421 0 0.16
SITE 1 AC1 12 LEU A 100 LYS A 101 VAL A 106 VAL A 179
SITE 2 AC1 12 TYR A 181 TYR A 188 GLY A 190 TRP A 229
SITE 3 AC1 12 LEU A 234 TYR A 318 HOH A1017 GLU B 138
CRYST1 143.200 116.800 66.400 90.00 90.00 90.00 P 21 21 21 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 0.006983 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008562 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015060 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
