HEADER TRANSFERASE/RNA 01-FEB-08 2ZH6
TITLE COMPLEX STRUCTURE OF AFCCA WITH TRNAMINIDCU AND ATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA (34-MER);
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CCA-ADDING ENZYME;
COMPND 7 CHAIN: A;
COMPND 8 SYNONYM: TRNA NUCLEOTIDYLTRANSFERASE, TRNA ADENYLYL-/CYTIDYLYL-
COMPND 9 TRANSFERASE, TRNA CCA-PYROPHOSPHORYLASE, TRNA-NT;
COMPND 10 EC: 2.7.7.25, 2.7.7.21;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 5 ORGANISM_TAXID: 2234;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-22B
KEYWDS TRANSFERASE/RNA, ATP-BINDING, MAGNESIUM, METAL-BINDING, NUCLEOTIDE-
KEYWDS 2 BINDING, NUCLEOTIDYLTRANSFERASE, RNA REPAIR, RNA-BINDING, TRNA
KEYWDS 3 PROCESSING, TRANSFERASE-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.TOH,K.TOMITA
REVDAT 3 13-MAR-24 2ZH6 1 REMARK
REVDAT 2 24-FEB-09 2ZH6 1 VERSN
REVDAT 1 05-AUG-08 2ZH6 0
JRNL AUTH Y.TOH,T.NUMATA,K.WATANABE,D.TAKESHITA,O.NUREKI,K.TOMITA
JRNL TITL MOLECULAR BASIS FOR MAINTENANCE OF FIDELITY DURING THE
JRNL TITL 2 CCA-ADDING REACTION BY A CCA-ADDING ENZYME
JRNL REF EMBO J. V. 27 1944 2008
JRNL REFN ISSN 0261-4189
JRNL PMID 18583961
JRNL DOI 10.1038/EMBOJ.2008.124
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3582257.250
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 26831
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) : 0.233
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1303
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4101
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 233
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3630
REMARK 3 NUCLEIC ACID ATOMS : 723
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40000
REMARK 3 B22 (A**2) : -0.40000
REMARK 3 B33 (A**2) : 0.80000
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) : 0.33
REMARK 3 ESD FROM SIGMAA (A) : 0.29
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) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.050
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) : 1.110 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.910 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.580 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.480 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 19.64
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.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : ATP2.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 5 : ION.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZH6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000027966.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26946
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 59.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.15400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 19.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM HEPES, 20% PEG 3550, 0.2M TRI
REMARK 280 -LITHIUM CITRATE, 80MM NH4SO4, PH 7.5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 214.47400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 29.01700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 29.01700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 321.71100
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 29.01700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 29.01700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 107.23700
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 29.01700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 29.01700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 321.71100
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 29.01700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 29.01700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 107.23700
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 214.47400
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: 4130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O PHE A 365 O GLY A 434 7645 2.12
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 LYS A 118 CB - CA - C ANGL. DEV. = 13.0 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 GLU A 4 -73.29 -39.53
REMARK 500 GLU A 96 -59.74 -147.81
REMARK 500 LYS A 105 42.29 39.55
REMARK 500 GLU A 119 116.60 79.56
REMARK 500 PRO A 120 30.20 -69.10
REMARK 500 LYS A 121 -93.60 -57.43
REMARK 500 TYR A 161 -92.06 -70.38
REMARK 500 SER A 250 130.61 -172.95
REMARK 500 LEU A 260 113.66 63.09
REMARK 500 ILE A 262 113.84 8.60
REMARK 500 ARG A 366 105.63 68.61
REMARK 500 LEU A 400 41.85 -95.87
REMARK 500 TYR A 411 139.51 171.27
REMARK 500 PRO A 424 48.14 -75.73
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 U B 19 0.08 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 MG A 438
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4770
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZH1 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZH2 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZH3 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZH4 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZH5 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZH7 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZH8 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZH9 RELATED DB: PDB
REMARK 900 RELATED ID: 2ZHA RELATED DB: PDB
REMARK 900 RELATED ID: 2ZHB RELATED DB: PDB
DBREF 2ZH6 A 1 437 UNP O28126 CCA_ARCFU 1 437
DBREF 2ZH6 B 1 34 PDB 2ZH6 2ZH6 1 34
SEQRES 1 B 34 G G C C C G G G G C G G U
SEQRES 2 B 34 U C G A U U C C G C C C U
SEQRES 3 B 34 G G G C C A C U
SEQRES 1 A 437 MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU
SEQRES 2 A 437 VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU
SEQRES 3 A 437 ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY
SEQRES 4 A 437 VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR
SEQRES 5 A 437 TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU
SEQRES 6 A 437 PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG
SEQRES 7 A 437 GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU
SEQRES 8 A 437 ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL
SEQRES 9 A 437 LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU
SEQRES 10 A 437 LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR
SEQRES 11 A 437 PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY
SEQRES 12 A 437 LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS
SEQRES 13 A 437 ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY
SEQRES 14 A 437 PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR
SEQRES 15 A 437 GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP
SEQRES 16 A 437 THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL
SEQRES 17 A 437 ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP
SEQRES 18 A 437 GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN
SEQRES 19 A 437 LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU
SEQRES 20 A 437 ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU
SEQRES 21 A 437 GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU
SEQRES 22 A 437 ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO
SEQRES 23 A 437 ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG
SEQRES 24 A 437 ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN
SEQRES 25 A 437 PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU
SEQRES 26 A 437 PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE
SEQRES 27 A 437 SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP
SEQRES 28 A 437 GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA
SEQRES 29 A 437 PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE
SEQRES 30 A 437 GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG
SEQRES 31 A 437 SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN
SEQRES 32 A 437 VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER
SEQRES 33 A 437 GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU
SEQRES 34 A 437 CYS GLU MET MET GLY VAL LYS ASP
HET MG A 438 1
HET SO4 A4770 5
HET ATP A 501 31
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 MG MG 2+
FORMUL 4 SO4 O4 S 2-
FORMUL 5 ATP C10 H16 N5 O13 P3
FORMUL 6 HOH *104(H2 O)
HELIX 1 1 LYS A 2 ILE A 15 1 14
HELIX 2 2 ASP A 17 GLU A 37 1 21
HELIX 3 3 GLY A 46 ASN A 51 1 6
HELIX 4 4 SER A 71 LEU A 87 1 17
HELIX 5 5 ARG A 129 GLY A 139 1 11
HELIX 6 6 LYS A 144 ASN A 158 1 15
HELIX 7 7 SER A 171 GLY A 183 1 13
HELIX 8 8 SER A 184 ARG A 193 1 10
HELIX 9 9 ALA A 204 GLY A 206 5 3
HELIX 10 10 SER A 231 ALA A 248 1 18
HELIX 11 11 SER A 250 LYS A 255 5 6
HELIX 12 12 GLU A 263 GLY A 275 1 13
HELIX 13 13 VAL A 289 GLU A 311 1 23
HELIX 14 14 ASP A 351 SER A 360 1 10
HELIX 15 15 THR A 384 HIS A 396 1 13
HELIX 16 16 TRP A 397 LEU A 400 5 4
HELIX 17 17 GLY A 401 TYR A 411 1 11
HELIX 18 18 SER A 416 LYS A 422 1 7
HELIX 19 19 VAL A 425 GLY A 434 1 10
SHEET 1 A 5 TYR A 42 VAL A 45 0
SHEET 2 A 5 GLU A 59 PHE A 66 -1 O PHE A 63 N VAL A 43
SHEET 3 A 5 VAL A 107 TYR A 115 1 O VAL A 112 N LEU A 64
SHEET 4 A 5 VAL A 100 VAL A 104 -1 N VAL A 104 O VAL A 107
SHEET 5 A 5 SER A 89 GLU A 91 -1 N GLU A 91 O HIS A 101
SHEET 1 B 4 GLU A 207 LYS A 210 0
SHEET 2 B 4 THR A 199 ASP A 202 -1 N ASP A 202 O GLU A 207
SHEET 3 B 4 PHE A 215 ASP A 218 1 O PHE A 215 N ILE A 201
SHEET 4 B 4 ASP A 221 ASN A 225 -1 O ARG A 224 N ASP A 218
SHEET 1 C 4 PRO A 315 ALA A 322 0
SHEET 2 C 4 PHE A 326 CYS A 333 -1 O LEU A 330 N ALA A 319
SHEET 3 C 4 ALA A 277 ARG A 284 -1 N PHE A 279 O PHE A 331
SHEET 4 C 4 GLU A 413 ILE A 415 -1 O GLU A 413 N LYS A 282
SHEET 1 D 3 VAL A 341 GLN A 348 0
SHEET 2 D 3 ARG A 373 MET A 379 -1 O TRP A 374 N PRO A 347
SHEET 3 D 3 PHE A 368 GLU A 370 -1 N GLU A 370 O ARG A 373
SITE 1 AC1 2 GLU A 59 ASP A 61
SITE 1 AC2 3 ARG A 299 ARG A 302 LYS A 303
SITE 1 AC3 10 GLY A 46 SER A 47 ARG A 50 GLU A 59
SITE 2 AC3 10 ASP A 61 THR A 130 HIS A 133 LYS A 152
SITE 3 AC3 10 TYR A 161 ARG A 224
CRYST1 58.034 58.034 428.948 90.00 90.00 90.00 P 43 21 2 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 0.017231 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017231 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002331 0.00000
(ATOM LINES ARE NOT SHOWN.)
END