HEADER TRANSFERASE/DNA 07-APR-04 1T05
TITLE HIV-1 REVERSE TRANSCRIPTASE CROSSLINKED TO TEMPLATE-PRIMER WITH
TITLE 2 TENOFOVIR-DIPHOSPHATE BOUND AS THE INCOMING NUCLEOTIDE SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OLIGONUCLEOTIDE TEMPLATE;
COMPND 3 CHAIN: T;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: OLIGONUCLEOTIDE PRIMER;
COMPND 7 CHAIN: P;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: POL POLYPROTEIN;
COMPND 11 CHAIN: A;
COMPND 12 FRAGMENT: HIV-1 REVERSE TRANSCRIPTASE P66 SUBUNIT;
COMPND 13 EC: 2.7.7.49;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: POL POLYPROTEIN;
COMPND 18 CHAIN: B;
COMPND 19 FRAGMENT: HIV-1 REVERSE TRANSCRIPTASE P51 SUBUNIT;
COMPND 20 EC: 2.7.7.49;
COMPND 21 ENGINEERED: YES;
COMPND 22 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 OTHER_DETAILS: CHEMICALLY MODIFIED WITH THIOL-DGMP AND ENZYMATICALLY
SOURCE 6 TERMINATED WITH DDGTP;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 9 ORGANISM_TAXID: 11676;
SOURCE 10 STRAIN: BH10;
SOURCE 11 GENE: POL;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 15 MOL_ID: 4;
SOURCE 16 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 17 ORGANISM_TAXID: 11676;
SOURCE 18 STRAIN: BH10;
SOURCE 19 GENE: POL;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 22 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA
KEYWDS HIV-1 REVERSE TRANSCRIPTASE, TENOFOVIR, RT-DNA COMPLEX, TRANSFERASE-
KEYWDS 2 DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.TUSKE,S.G.SARAFIANOS,J.DING,E.ARNOLD
REVDAT 5 23-AUG-23 1T05 1 REMARK
REVDAT 4 27-OCT-21 1T05 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1T05 1 VERSN
REVDAT 2 24-FEB-09 1T05 1 VERSN
REVDAT 1 11-MAY-04 1T05 0
JRNL AUTH S.TUSKE,S.G.SARAFIANOS,A.D.CLARK JR.,J.DING,L.K.NAEGER,
JRNL AUTH 2 K.L.WHITE,M.D.MILLER,C.S.GIBBS,P.L.BOYER,P.CLARK,G.WANG,
JRNL AUTH 3 B.L.GAFFNEY,R.A.JONES,D.M.JERINA,S.H.HUGHES,E.ARNOLD
JRNL TITL STRUCTURES OF HIV-1 RT-DNA COMPLEXES BEFORE AND AFTER
JRNL TITL 2 INCORPORATION OF THE ANTI-AIDS DRUG TENOFOVIR
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 469 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 15107837
JRNL DOI 10.1038/NSMB760
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.100
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.8
REMARK 3 NUMBER OF REFLECTIONS : 42950
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.253
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1720
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.05
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4750
REMARK 3 BIN FREE R VALUE : 0.5630
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 25
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 : 7921
REMARK 3 NUCLEIC ACID ATOMS : 897
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 21
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.56300
REMARK 3 B22 (A**2) : -9.56300
REMARK 3 B33 (A**2) : 19.12700
REMARK 3 B12 (A**2) : -31.38200
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) : 0.51
REMARK 3 ESD FROM SIGMAA (A) : 1.03
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.58
REMARK 3 ESD FROM C-V SIGMAA (A) : 1.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1T05 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JAN-02
REMARK 200 TEMPERATURE (KELVIN) : 108
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.950
REMARK 200 MONOCHROMATOR : WIGGLER
REMARK 200 OPTICS : WIGGLER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52624
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 50.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1RTD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES, PH 6.4, 100 MM AMMONIUM
REMARK 280 SULFATE, 5% SUCROSE, 5% GLYCEROL, 10% PEG 8000, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 1 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -Y,-X,-Z+2/3
REMARK 290 5555 -X+Y,Y,-Z+1/3
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 52.09000
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 104.18000
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 104.18000
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 52.09000
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, P, 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 DA T 701
REMARK 465 DT T 726
REMARK 465 DG T 727
REMARK 465 DA P 802
REMARK 465 GLY A 555
REMARK 465 ILE A 556
REMARK 465 ARG A 557
REMARK 465 LYS A 558
REMARK 465 PRO B 1
REMARK 465 ILE B 2
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 430
REMARK 465 GLY B 431
REMARK 465 HIS B 432
REMARK 465 HIS B 433
REMARK 465 HIS B 434
REMARK 465 HIS B 435
REMARK 465 HIS B 436
REMARK 465 HIS B 437
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 DT T 702 P OP1 OP2
REMARK 470 DC P 803 P OP1 OP2
REMARK 470 MRG P 817 C21 C22 C23 S24
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 C SER B 3 CD PRO B 4 1.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 478 CD GLU A 478 OE2 0.080
REMARK 500
REMARK 500 REMARK: NULL
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 DA T 716 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DA T 718 N9 - C1' - C2' ANGL. DEV. = 10.4 DEGREES
REMARK 500 DG T 719 N9 - C1' - C2' ANGL. DEV. = 8.9 DEGREES
REMARK 500 DG T 719 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DG T 721 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG P 805 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DC P 809 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 DC P 814 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DG P 815 N9 - C1' - C2' ANGL. DEV. = 10.0 DEGREES
REMARK 500 DG P 815 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 PRO A 9 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 LEU A 100 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 PRO A 345 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 PRO A 392 C - N - CA ANGL. DEV. = 10.5 DEGREES
REMARK 500 PRO A 412 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 PRO B 4 C - N - CA ANGL. DEV. = 24.5 DEGREES
REMARK 500 PRO B 4 C - N - CD ANGL. DEV. = -52.0 DEGREES
REMARK 500 PRO B 52 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 LEU B 295 N - CA - C ANGL. DEV. = 18.3 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 5 132.04 -25.18
REMARK 500 PRO A 14 123.10 -17.96
REMARK 500 LYS A 20 20.91 -154.76
REMARK 500 LYS A 22 -169.16 -75.04
REMARK 500 PRO A 55 34.41 -78.61
REMARK 500 ASN A 57 131.29 -174.65
REMARK 500 PHE A 61 -177.26 -173.45
REMARK 500 LYS A 66 -72.24 -29.38
REMARK 500 SER A 68 -159.02 82.89
REMARK 500 THR A 69 -27.88 66.79
REMARK 500 ASP A 76 36.88 -72.32
REMARK 500 PHE A 77 20.57 -47.63
REMARK 500 GLN A 85 -175.04 -68.02
REMARK 500 GLU A 89 136.21 -36.37
REMARK 500 PRO A 97 -35.99 -39.97
REMARK 500 LEU A 109 107.34 -174.60
REMARK 500 PHE A 116 28.98 -76.96
REMARK 500 ASP A 121 126.03 -23.15
REMARK 500 ARG A 125 -32.78 -39.06
REMARK 500 THR A 128 6.14 -59.60
REMARK 500 ILE A 135 -72.35 -65.66
REMARK 500 GLU A 138 -70.23 -81.65
REMARK 500 LYS A 154 -16.61 -33.56
REMARK 500 SER A 156 -61.47 -26.61
REMARK 500 PRO A 157 -77.15 -44.68
REMARK 500 TYR A 181 85.51 -69.08
REMARK 500 MET A 184 -95.82 72.25
REMARK 500 ILE A 195 -36.29 -34.40
REMARK 500 THR A 216 77.16 -115.35
REMARK 500 LYS A 219 34.40 -168.46
REMARK 500 GLN A 222 -117.29 -92.42
REMARK 500 LYS A 223 47.66 -74.39
REMARK 500 THR A 240 170.83 177.97
REMARK 500 ASP A 250 -50.57 -123.50
REMARK 500 LEU A 260 -73.65 -82.70
REMARK 500 SER A 268 -11.87 -34.63
REMARK 500 ILE A 270 -41.33 -132.89
REMARK 500 VAL A 276 -4.48 -141.66
REMARK 500 LEU A 282 5.21 -69.04
REMARK 500 LEU A 289 8.94 -69.63
REMARK 500 GLU A 298 -41.89 -29.37
REMARK 500 GLU A 302 -36.49 -38.34
REMARK 500 LEU A 303 -76.21 -68.58
REMARK 500 GLN A 334 79.96 -58.51
REMARK 500 TYR A 342 -175.97 -175.85
REMARK 500 PRO A 345 -65.03 -3.65
REMARK 500 TYR A 354 106.85 -168.59
REMARK 500 LEU A 368 -7.80 -51.61
REMARK 500 GLU A 370 -4.79 -59.55
REMARK 500 THR A 377 -75.32 -49.38
REMARK 500
REMARK 500 THIS ENTRY HAS 157 RAMACHANDRAN OUTLIERS.
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 PHE A 160 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 600 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 110 OD1
REMARK 620 2 VAL A 111 O 115.4
REMARK 620 3 ASP A 185 OD2 68.0 87.3
REMARK 620 4 TNV A 823 O2B 137.2 79.0 73.0
REMARK 620 5 TNV A 823 O1G 140.9 84.3 150.1 77.3
REMARK 620 6 TNV A 823 O1A 91.9 147.2 86.7 68.5 85.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 443 OD1
REMARK 620 2 ASP A 443 OD2 49.9
REMARK 620 3 ASP A 498 OD2 122.7 72.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TNV A 823
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 824
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 825
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 826
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 438
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 439
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RTD RELATED DB: PDB
REMARK 900 STRUCTURE OF A CATALYTIC COMPLEX OF HIV-1 REVERSE TRANSCRIPTASE:
REMARK 900 IMPLICATIONS FOR NUCLEOSIDE ANALOG RESISTANCE
REMARK 900 RELATED ID: 1T03 RELATED DB: PDB
REMARK 900 HIV-1 REVERSE TRANSCRIPTASE CROSSLINKED TO TENOFOVIR TERMINATED
REMARK 900 TEMPLATE-PRIMER (COMPLEX P)
REMARK 999
REMARK 999 SEQUENCE RESIDUE MRG 817 OF THE P CHAIN IS CROSSLINKED TO CHAIN
REMARK 999 A RESIDUE C258.
DBREF 1T05 A 1 558 UNP P03366 POL_HV1B1 168 725
DBREF 1T05 B 1 429 UNP P04585 POL_HV1H2 156 584
DBREF 1T05 T 701 727 PDB 1T05 1T05 701 727
DBREF 1T05 P 802 822 PDB 1T05 1T05 802 822
SEQADV 1T05 CYS A 258 UNP P03366 GLN 425 ENGINEERED MUTATION
SEQADV 1T05 SER A 280 UNP P03366 CYS 447 ENGINEERED MUTATION
SEQADV 1T05 SER B 280 UNP P04585 CYS 435 ENGINEERED MUTATION
SEQADV 1T05 GLY B 430 UNP P04585 CLONING ARTIFACT
SEQADV 1T05 GLY B 431 UNP P04585 CLONING ARTIFACT
SEQADV 1T05 HIS B 432 UNP P04585 EXPRESSION TAG
SEQADV 1T05 HIS B 433 UNP P04585 EXPRESSION TAG
SEQADV 1T05 HIS B 434 UNP P04585 EXPRESSION TAG
SEQADV 1T05 HIS B 435 UNP P04585 EXPRESSION TAG
SEQADV 1T05 HIS B 436 UNP P04585 EXPRESSION TAG
SEQADV 1T05 HIS B 437 UNP P04585 EXPRESSION TAG
SEQRES 1 T 27 DA DT DG DG DT DC DG DG DC DG DC DC DC
SEQRES 2 T 27 DG DA DA DC DA DG DG DG DA DC DT DG DT
SEQRES 3 T 27 DG
SEQRES 1 P 21 DA DC DA DG DT DC DC DC DT DG DT DT DC
SEQRES 2 P 21 DG DG MRG DC DG DC DC DDG
SEQRES 1 A 558 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 A 558 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 A 558 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 A 558 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 A 558 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 A 558 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 A 558 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 A 558 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS
SEQRES 9 A 558 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 A 558 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 A 558 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 A 558 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 A 558 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 A 558 PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 A 558 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 A 558 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 A 558 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 A 558 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 A 558 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 A 558 GLU LYS ASP SER TRP THR VAL ASN ASP ILE CYS LYS LEU
SEQRES 21 A 558 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 A 558 ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG GLY THR
SEQRES 23 A 558 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 A 558 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 A 558 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 A 558 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 A 558 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 A 558 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 A 558 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 A 558 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 A 558 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 A 558 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 A 558 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 A 558 GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE TYR VAL
SEQRES 35 A 558 ASP GLY ALA ALA ASN ARG GLU THR LYS LEU GLY LYS ALA
SEQRES 36 A 558 GLY TYR VAL THR ASN LYS GLY ARG GLN LYS VAL VAL PRO
SEQRES 37 A 558 LEU THR ASN THR THR ASN GLN LYS THR GLU LEU GLN ALA
SEQRES 38 A 558 ILE TYR LEU ALA LEU GLN ASP SER GLY LEU GLU VAL ASN
SEQRES 39 A 558 ILE VAL THR ASP SER GLN TYR ALA LEU GLY ILE ILE GLN
SEQRES 40 A 558 ALA GLN PRO ASP LYS SER GLU SER GLU LEU VAL ASN GLN
SEQRES 41 A 558 ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS VAL TYR LEU
SEQRES 42 A 558 ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY GLY ASN GLU
SEQRES 43 A 558 GLN VAL ASP LYS LEU VAL SER ALA GLY ILE ARG LYS
SEQRES 1 B 437 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 B 437 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 B 437 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 B 437 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 B 437 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 B 437 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 B 437 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 B 437 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS
SEQRES 9 B 437 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 B 437 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 B 437 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 B 437 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 B 437 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 B 437 PRO PHE ARG LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 B 437 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 B 437 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 B 437 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 B 437 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 B 437 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 B 437 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 B 437 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 B 437 ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG GLY THR
SEQRES 23 B 437 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 B 437 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 B 437 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 B 437 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 B 437 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 B 437 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 B 437 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 B 437 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 B 437 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 B 437 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 B 437 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 B 437 GLY GLY HIS HIS HIS HIS HIS HIS
MODRES 1T05 MRG P 817 DG
MODRES 1T05 DDG P 822 DG
HET MRG P 817 22
HET DDG P 822 21
HET MG A 600 1
HET MG A 601 1
HET TNV A 823 27
HET GOL A 824 6
HET GOL A 825 6
HET GOL A 826 6
HET GOL B 438 6
HET GOL B 439 6
HETNAM MRG N2-(3-MERCAPTOPROPYL)-2'-DEOXYGUANOSINE-5'-
HETNAM 2 MRG MONOPHOSPHATE
HETNAM DDG 2',3'-DIDEOXY-GUANOSINE-5'-MONOPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM TNV [2-(6-AMINO-9H-PURIN-9-YL)-1-METHYLETHOXY]METHYL-
HETNAM 2 TNV TRIPHOSPHATE
HETNAM GOL GLYCEROL
HETSYN TNV TENOFOVIR-DIPHOSPHATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 MRG C13 H20 N5 O7 P S
FORMUL 2 DDG C10 H14 N5 O6 P
FORMUL 5 MG 2(MG 2+)
FORMUL 7 TNV C9 H16 N5 O10 P3
FORMUL 8 GOL 5(C3 H8 O3)
FORMUL 13 HOH *21(H2 O)
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 ASP A 123 TYR A 127 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 GLY A 384 1 22
HELIX 12 12 GLN A 394 GLU A 404 1 11
HELIX 13 13 THR A 473 ASP A 488 1 16
HELIX 14 14 SER A 499 ALA A 508 1 10
HELIX 15 15 SER A 515 LYS A 528 1 14
HELIX 16 16 GLY A 544 VAL A 552 1 9
HELIX 17 17 THR B 27 MET B 41 1 15
HELIX 18 18 PHE B 77 LYS B 82 1 6
HELIX 19 19 THR B 84 GLU B 89 1 6
HELIX 20 20 ALA B 98 LYS B 103 1 6
HELIX 21 21 GLY B 112 VAL B 118 5 7
HELIX 22 22 ASP B 121 LYS B 126 1 6
HELIX 23 23 SER B 134 GLU B 138 5 5
HELIX 24 24 LYS B 154 LYS B 173 1 20
HELIX 25 25 GLU B 194 ARG B 211 1 18
HELIX 26 26 VAL B 254 TYR B 271 1 18
HELIX 27 27 VAL B 276 LYS B 281 1 6
HELIX 28 28 THR B 296 LEU B 310 1 15
HELIX 29 29 ASN B 363 ILE B 382 1 20
HELIX 30 30 GLN B 394 TRP B 406 1 13
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 LYS A 64 0
SHEET 2 B 2 TRP A 71 VAL A 75 -1 O LEU A 74 N PHE A 61
SHEET 1 C 3 SER A 105 LEU A 109 0
SHEET 2 C 3 ASP A 186 SER A 191 -1 O VAL A 189 N THR A 107
SHEET 3 C 3 VAL A 179 TYR A 183 -1 N TYR A 183 O ASP A 186
SHEET 1 D 2 PHE A 227 TRP A 229 0
SHEET 2 D 2 TYR A 232 LEU A 234 -1 O LEU A 234 N PHE A 227
SHEET 1 E 5 LYS A 347 TYR A 354 0
SHEET 2 E 5 TRP A 337 GLU A 344 -1 N TYR A 339 O GLY A 352
SHEET 3 E 5 ILE A 326 GLN A 330 -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 LYS A 512 SER A 513 -1 O LYS A 512 N THR A 362
SHEET 1 G 3 PHE A 440 TYR A 441 0
SHEET 2 G 3 ILE A 495 THR A 497 1 O VAL A 496 N PHE A 440
SHEET 3 G 3 LEU A 533 TRP A 535 1 O ALA A 534 N THR A 497
SHEET 1 H 3 ASP A 443 ASN A 447 0
SHEET 2 H 3 LEU A 452 TYR A 457 -1 O GLY A 456 N ASP A 443
SHEET 3 H 3 LYS A 465 THR A 470 -1 O LEU A 469 N GLY A 453
SHEET 1 I 4 VAL B 179 TYR B 183 0
SHEET 2 I 4 ASP B 186 GLY B 190 -1 O ASP B 186 N TYR B 183
SHEET 3 I 4 VAL B 106 ASP B 110 -1 N LEU B 109 O LEU B 187
SHEET 4 I 4 GLU B 233 LEU B 234 -1 O LEU B 234 N VAL B 106
SHEET 1 J 5 LYS B 350 TYR B 354 0
SHEET 2 J 5 TRP B 337 TYR B 342 -1 N TRP B 337 O TYR B 354
SHEET 3 J 5 ILE B 326 LYS B 331 -1 N ILE B 326 O TYR B 342
SHEET 4 J 5 LYS B 388 LEU B 391 1 O LYS B 390 N ALA B 327
SHEET 5 J 5 TRP B 414 PHE B 416 1 O GLU B 415 N PHE B 389
LINK O3' DG P 816 P MRG P 817 1555 1555 1.61
LINK O3' MRG P 817 P DC P 818 1555 1555 1.60
LINK O3' DC P 821 P DDG P 822 1555 1555 1.60
LINK OD1 ASP A 110 MG MG A 600 1555 1555 2.22
LINK O VAL A 111 MG MG A 600 1555 1555 2.28
LINK OD2 ASP A 185 MG MG A 600 1555 1555 2.48
LINK OD1 ASP A 443 MG MG A 601 1555 1555 2.69
LINK OD2 ASP A 443 MG MG A 601 1555 1555 2.52
LINK OD2 ASP A 498 MG MG A 601 1555 1555 2.62
LINK MG MG A 600 O2B TNV A 823 1555 1555 2.28
LINK MG MG A 600 O1G TNV A 823 1555 1555 2.47
LINK MG MG A 600 O1A TNV A 823 1555 1555 2.41
CISPEP 1 PRO A 225 PRO A 226 0 0.44
CISPEP 2 PRO A 420 PRO A 421 0 -0.86
SITE 1 AC1 4 ASP A 110 VAL A 111 ASP A 185 TNV A 823
SITE 1 AC2 2 ASP A 443 ASP A 498
SITE 1 AC3 14 LYS A 65 ARG A 72 ASP A 110 VAL A 111
SITE 2 AC3 14 GLY A 112 ASP A 113 ALA A 114 GLN A 151
SITE 3 AC3 14 ASP A 185 LYS A 219 MG A 600 DDG P 822
SITE 4 AC3 14 DT T 705 DC T 706
SITE 1 AC4 8 LYS A 101 LYS A 103 VAL A 106 TYR A 188
SITE 2 AC4 8 HIS A 235 PRO A 236 TYR A 318 HOH A 827
SITE 1 AC5 6 GLU A 328 GLN A 340 TYR A 342 PRO A 345
SITE 2 AC5 6 GOL A 826 HOH A 829
SITE 1 AC6 3 GLN A 330 GLN A 340 GOL A 825
SITE 1 AC7 6 ASP B 76 ARG B 78 GLU B 79 LYS B 82
SITE 2 AC7 6 GLU B 413 GOL B 439
SITE 1 AC8 1 GOL B 438
CRYST1 171.570 171.570 156.270 90.00 90.00 120.00 P 31 1 2 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 0.005829 0.003365 0.000000 0.00000
SCALE2 0.000000 0.006730 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006399 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
