HEADER LIGASE/DNA 29-MAY-07 2Q2T
TITLE STRUCTURE OF CHLORELLA VIRUS DNA LIGASE-ADENYLATE BOUND TO A 5'
TITLE 2 PHOSPHORYLATED NICK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*TP*TP*CP*CP*GP*AP*TP*AP*GP*TP*GP*GP*GP*GP*TP*CP*GP*CP
COMPND 3 *AP*AP*T)-3';
COMPND 4 CHAIN: B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 5'-D(*AP*TP*TP*GP*CP*GP*AP*CP*(OMC)P*C)-3';
COMPND 8 CHAIN: C;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: 5'-D(P*CP*AP*CP*TP*AP*TP*CP*GP*GP*AP*A)-3';
COMPND 12 CHAIN: D;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: CHLORELLA VIRUS DNA LIGASE;
COMPND 16 CHAIN: A;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: CHEMICALLY SYNTHESIZED.;
SOURCE 4 MOL_ID: 2;
SOURCE 5 SYNTHETIC: YES;
SOURCE 6 OTHER_DETAILS: CHEMICALLY SYNTHESIZED.;
SOURCE 7 MOL_ID: 3;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 OTHER_DETAILS: CHEMICALLY SYNTHESIZED.;
SOURCE 10 MOL_ID: 4;
SOURCE 11 ORGANISM_SCIENTIFIC: PARAMECIUM BURSARIA CHLORELLA VIRUS 1;
SOURCE 12 ORGANISM_TAXID: 10506;
SOURCE 13 STRAIN: CHLORELLA VIRUS;
SOURCE 14 GENE: A544R;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PET16B
KEYWDS LIGASE, LYSINE ADENYLATE, PROTEIN-DNA COMPLEX, LIGASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.LIMA,J.NANDAKUMAR,P.A.NAIR,P.SMITH,S.SHUMAN
REVDAT 5 30-AUG-23 2Q2T 1 REMARK SEQADV LINK
REVDAT 4 18-OCT-17 2Q2T 1 REMARK
REVDAT 3 24-FEB-09 2Q2T 1 VERSN
REVDAT 2 30-OCT-07 2Q2T 1 JRNL
REVDAT 1 10-JUL-07 2Q2T 0
JRNL AUTH P.A.NAIR,J.NANDAKUMAR,P.SMITH,M.ODELL,C.D.LIMA,S.SHUMAN
JRNL TITL STRUCTURAL BASIS FOR NICK RECOGNITION BY A MINIMAL
JRNL TITL 2 PLURIPOTENT DNA LIGASE.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 14 770 2007
JRNL REFN ISSN 1545-9993
JRNL PMID 17618295
JRNL DOI 10.1038/NSMB1266
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1201398.750
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 23077
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 SET) : 0.214
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1151
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3574
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE : 0.3850
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 162
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2360
REMARK 3 NUCLEIC ACID ATOMS : 858
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 145
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -14.03000
REMARK 3 B22 (A**2) : 6.90000
REMARK 3 B33 (A**2) : 7.13000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.33
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) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.45
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.140
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.410 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.340 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.170 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.310 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 33.82
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 : PROTEIN_REP-APL.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA-APC_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : DNA-RNA-APC.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : PROTEIN-APL.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2Q2T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000043077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23105
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.33200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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: 1FVI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: A MIXTURE OF CHVLIG (230 MICROM),
REMARK 280 NICKED DUPLEX DNA (220 MICROM) AND 2 MM EDTA WAS ADDED TO AN
REMARK 280 EQUAL VOLUME OF A WELL SOLUTION CONTAINING 100 MM BIS-TRIS-HCL
REMARK 280 (PH 6.5), 30 MM AMMONIUM ACETATE, 22% PEG-4000. CRYSTALS WERE
REMARK 280 GROWN AT 22 C BY THE SITTING-DROP VAPOR DIFFUSION METHOD.
REMARK 280 CRYSTALS APPEARED AFTER 3 DAYS. THE CRYSTALS WERE TRANSFERRED TO
REMARK 280 BUFFER CONTAINING 100 MM BIS-TRIS-HCL (PH 6.5), 30 MM AMMONIUM
REMARK 280 ACETATE, 22% PEG-4000, 15% GLYCEROL PRIOR TO FLASH-FREEZING IN
REMARK 280 LIQUID NITROGEN. , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 295K
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 33.15050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.20900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.64500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.20900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.15050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.64500
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, A
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 -20
REMARK 465 GLY A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 SER A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 HIS A -5
REMARK 465 ILE A -4
REMARK 465 GLU A -3
REMARK 465 GLY A -2
REMARK 465 ARG A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 294
REMARK 465 GLU A 295
REMARK 465 GLU A 296
REMARK 465 ASP A 297
REMARK 465 ARG A 298
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 O ASN A 49 O HOH A 403 2.03
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 DC D 32 P DC D 32 OP3 -0.088
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 THR A 37 -53.92 78.50
REMARK 500 ASN A 49 76.52 -69.00
REMARK 500 SER A 50 -33.25 -36.36
REMARK 500 THR A 102 -90.99 -91.22
REMARK 500 THR A 211 -145.89 -113.07
REMARK 500 ASP A 231 44.44 -93.64
REMARK 500 ASP A 241 48.77 39.64
REMARK 500 LYS A 281 -77.67 -99.32
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 DT B 10 0.09 SIDE CHAIN
REMARK 500 DG B 11 0.09 SIDE CHAIN
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 AMP A 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FVI RELATED DB: PDB
REMARK 900 RELATED ID: 2Q2U RELATED DB: PDB
DBREF 2Q2T A 1 298 UNP O41026 O41026_PBCV1 1 298
DBREF 2Q2T B 1 21 PDB 2Q2T 2Q2T 1 21
DBREF 2Q2T C 22 31 PDB 2Q2T 2Q2T 22 31
DBREF 2Q2T D 32 42 PDB 2Q2T 2Q2T 32 42
SEQADV 2Q2T MET A -20 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T GLY A -19 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A -18 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A -17 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A -16 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A -15 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A -14 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A -13 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A -12 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A -11 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A -10 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A -9 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T SER A -8 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T SER A -7 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T GLY A -6 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A -5 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T ILE A -4 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T GLU A -3 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T GLY A -2 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T ARG A -1 UNP O41026 EXPRESSION TAG
SEQADV 2Q2T HIS A 0 UNP O41026 EXPRESSION TAG
SEQRES 1 B 21 DT DT DC DC DG DA DT DA DG DT DG DG DG
SEQRES 2 B 21 DG DT DC DG DC DA DA DT
SEQRES 1 C 10 DA DT DT DG DC DG DA DC OMC DC
SEQRES 1 D 11 DC DA DC DT DA DT DC DG DG DA DA
SEQRES 1 A 319 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 319 SER GLY HIS ILE GLU GLY ARG HIS MET ALA ILE THR LYS
SEQRES 3 A 319 PRO LEU LEU ALA ALA THR LEU GLU ASN ILE GLU ASP VAL
SEQRES 4 A 319 GLN PHE PRO CYS LEU ALA THR PRO LYS ILE ASP GLY ILE
SEQRES 5 A 319 ARG SER VAL LYS GLN THR GLN MET LEU SER ARG THR PHE
SEQRES 6 A 319 LYS PRO ILE ARG ASN SER VAL MET ASN ARG LEU LEU THR
SEQRES 7 A 319 GLU LEU LEU PRO GLU GLY SER ASP GLY GLU ILE SER ILE
SEQRES 8 A 319 GLU GLY ALA THR PHE GLN ASP THR THR SER ALA VAL MET
SEQRES 9 A 319 THR GLY HIS LYS MET TYR ASN ALA LYS PHE SER TYR TYR
SEQRES 10 A 319 TRP PHE ASP TYR VAL THR ASP ASP PRO LEU LYS LYS TYR
SEQRES 11 A 319 ILE ASP ARG VAL GLU ASP MET LYS ASN TYR ILE THR VAL
SEQRES 12 A 319 HIS PRO HIS ILE LEU GLU HIS ALA GLN VAL LYS ILE ILE
SEQRES 13 A 319 PRO LEU ILE PRO VAL GLU ILE ASN ASN ILE THR GLU LEU
SEQRES 14 A 319 LEU GLN TYR GLU ARG ASP VAL LEU SER LYS GLY PHE GLU
SEQRES 15 A 319 GLY VAL MET ILE ARG LYS PRO ASP GLY LYS TYR LYS PHE
SEQRES 16 A 319 GLY ARG SER THR LEU LYS GLU GLY ILE LEU LEU LYS MET
SEQRES 17 A 319 LYS GLN PHE LYS ASP ALA GLU ALA THR ILE ILE SER MET
SEQRES 18 A 319 THR ALA LEU PHE LYS ASN THR ASN THR LYS THR LYS ASP
SEQRES 19 A 319 ASN PHE GLY TYR SER LYS ARG SER THR HIS LYS SER GLY
SEQRES 20 A 319 LYS VAL GLU GLU ASP VAL MET GLY SER ILE GLU VAL ASP
SEQRES 21 A 319 TYR ASP GLY VAL VAL PHE SER ILE GLY THR GLY PHE ASP
SEQRES 22 A 319 ALA ASP GLN ARG ARG ASP PHE TRP GLN ASN LYS GLU SER
SEQRES 23 A 319 TYR ILE GLY LYS MET VAL LYS PHE LYS TYR PHE GLU MET
SEQRES 24 A 319 GLY SER LYS ASP CYS PRO ARG PHE PRO VAL PHE ILE GLY
SEQRES 25 A 319 ILE ARG HIS GLU GLU ASP ARG
MODRES 2Q2T OMC C 30 C O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE
HET OMC C 30 21
HET AMP A 300 22
HETNAM OMC O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE
HETNAM AMP ADENOSINE MONOPHOSPHATE
FORMUL 2 OMC C10 H16 N3 O8 P
FORMUL 5 AMP C10 H14 N5 O7 P
FORMUL 6 HOH *145(H2 O)
HELIX 1 1 ASN A 14 VAL A 18 5 5
HELIX 2 2 ASN A 49 LEU A 60 1 12
HELIX 3 3 THR A 74 THR A 84 1 11
HELIX 4 4 LYS A 108 HIS A 123 1 16
HELIX 5 5 PRO A 124 GLU A 128 5 5
HELIX 6 6 ASN A 144 LYS A 158 1 15
HELIX 7 7 HIS A 223 SER A 225 5 3
HELIX 8 8 ASP A 252 ASN A 262 1 11
HELIX 9 9 ASN A 262 ILE A 267 1 6
SHEET 1 A 2 LEU A 7 LEU A 8 0
SHEET 2 A 2 GLY A 175 ARG A 176 1 O GLY A 175 N LEU A 8
SHEET 1 B 5 ALA A 10 THR A 11 0
SHEET 2 B 5 LEU A 184 MET A 187 1 O LEU A 184 N ALA A 10
SHEET 3 B 5 GLY A 162 ARG A 166 -1 N ILE A 165 O LEU A 185
SHEET 4 B 5 CYS A 22 LYS A 27 -1 N THR A 25 O MET A 164
SHEET 5 B 5 VAL A 140 ILE A 142 -1 O VAL A 140 N ALA A 24
SHEET 1 C 5 MET A 39 LEU A 40 0
SHEET 2 C 5 ILE A 31 LYS A 35 -1 N VAL A 34 O LEU A 40
SHEET 3 C 5 SER A 64 SER A 69 -1 O ILE A 68 N ILE A 31
SHEET 4 C 5 PHE A 93 TYR A 100 -1 O TYR A 96 N GLU A 67
SHEET 5 C 5 VAL A 132 PRO A 136 1 O ILE A 135 N TYR A 95
SHEET 1 D 5 VAL A 243 ILE A 247 0
SHEET 2 D 5 LYS A 227 TYR A 240 -1 N TYR A 240 O VAL A 243
SHEET 3 D 5 LYS A 191 ASN A 206 -1 N THR A 201 O GLY A 234
SHEET 4 D 5 MET A 270 PHE A 276 -1 O VAL A 271 N ALA A 195
SHEET 5 D 5 ARG A 285 ILE A 292 -1 O GLY A 291 N LYS A 272
SHEET 1 E 2 THR A 211 LYS A 212 0
SHEET 2 E 2 SER A 218 LYS A 219 -1 O LYS A 219 N THR A 211
LINK NZ LYS A 27 P AMP A 300 1555 1555 1.47
CISPEP 1 PHE A 20 PRO A 21 0 -0.11
SITE 1 AC1 18 THR A 25 PRO A 26 LYS A 27 ILE A 28
SITE 2 AC1 18 ARG A 32 GLU A 67 PHE A 98 LEU A 137
SITE 3 AC1 18 GLU A 161 MET A 164 LYS A 186 LYS A 188
SITE 4 AC1 18 HOH A 319 HOH A 336 HOH A 367 HOH A 370
SITE 5 AC1 18 DC C 31 DC D 32
CRYST1 66.301 81.290 96.418 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 0.015083 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012302 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010372 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
