HEADER HYDROLASE 03-NOV-03 1RC5
TITLE CRYSTAL STRUCTURE OF MG(II)-COMPLEX OF RNASE III ENDONUCLEASE DOMAIN
TITLE 2 FROM AQUIFEX AEOLICUS AT 2.30 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE III;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: N-TERMINAL ENDONUCLEASE DOMAIN (RESIDUES 1-147);
COMPND 5 SYNONYM: RNASE III;
COMPND 6 EC: 3.1.26.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 GENE: RNC, AQ_946;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKM803
KEYWDS RIBONUCLEASE, RNASE III, DOUBLE-STRANDED RNA, RNA INTERFERENCE,
KEYWDS 2 ENDONUCLEASE DOMAIN, ENDONUCLEOLYTIC CLEAVAGE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BLASZCZYK,J.GAN,X.JI
REVDAT 4 30-AUG-23 1RC5 1 AUTHOR JRNL
REVDAT 3 23-AUG-23 1RC5 1 REMARK LINK
REVDAT 2 24-FEB-09 1RC5 1 VERSN
REVDAT 1 30-MAR-04 1RC5 0
JRNL AUTH J.BLASZCZYK,J.GAN,J.E.TROPEA,D.L.COURT,D.S.WAUGH,X.JI
JRNL TITL NONCATALYTIC ASSEMBLY OF RIBONUCLEASE III WITH
JRNL TITL 2 DOUBLE-STRANDED RNA.
JRNL REF STRUCTURE V. 12 457 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15016361
JRNL DOI 10.1016/J.STR.2004.02.004
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.BLASZCZYK,J.E.TROPEA,M.BUBUNENKO,K.M.ROUTZAHN,D.S.WAUGH,
REMARK 1 AUTH 2 D.L.COURT,X.JI
REMARK 1 TITL CRYSTALLOGRAPHIC AND MODELLING STUDIES OF RNASE III SUGGEST
REMARK 1 TITL 2 A MECHANISM FOR DOUBLE-STRANDED RNA CLEAVAGE
REMARK 1 REF STRUCTURE V. 9 1225 2001
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(01)00685-2
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.1
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.215
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.440
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1248
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 22942
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.192
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.580
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1097
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 19661
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4920
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 675
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 5599.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 2
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 20239
REMARK 3 NUMBER OF RESTRAINTS : 20369
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 ANGLE DISTANCES (A) : 0.016
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.018
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.019
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.026
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.019
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.079
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1975) 201-228
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: LEAST-SQUARES REFINEMENT USING THE
REMARK 3 KONNERT-HENDRICKSON CONJUGATE-GRADIENT ALGORITHM. CNS WAS ALSO
REMARK 3 USED FOR REFINEMENT.
REMARK 4
REMARK 4 1RC5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020645.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04500
REMARK 200 MONOCHROMATOR : SILICON 111
REMARK 200 OPTICS : MIRROR
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 : 24431
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 200 DATA REDUNDANCY : 2.822
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8929
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 (%) : 87.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.42
REMARK 200 R MERGE FOR SHELL (I) : 0.27900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.903
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: PDB ID 1I4S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, TRIS-HCL, ACETATE, CHLORIDE,
REMARK 280 PH 8.50, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 70.42800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 2490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 HIS A 148
REMARK 465 HIS A 149
REMARK 465 HIS A 150
REMARK 465 HIS A 151
REMARK 465 HIS A 152
REMARK 465 HIS A 153
REMARK 465 HIS B 349
REMARK 465 HIS B 350
REMARK 465 HIS B 351
REMARK 465 HIS B 352
REMARK 465 HIS B 353
REMARK 465 HIS C 549
REMARK 465 HIS C 550
REMARK 465 HIS C 551
REMARK 465 HIS C 552
REMARK 465 HIS C 553
REMARK 465 HIS D 748
REMARK 465 HIS D 749
REMARK 465 HIS D 750
REMARK 465 HIS D 751
REMARK 465 HIS D 752
REMARK 465 HIS D 753
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 MET A 1 -160.64 51.03
REMARK 500 LYS A 2 48.07 -101.96
REMARK 500 MET A 3 -61.48 -178.47
REMARK 500 GLU A 88 70.45 34.58
REMARK 500 LYS A 96 -134.41 -94.73
REMARK 500 ARG A 97 84.87 -45.07
REMARK 500 LYS A 144 39.97 -79.38
REMARK 500 LYS B 202 97.17 77.37
REMARK 500 MET B 203 -48.76 -142.71
REMARK 500 GLN B 206 -8.28 153.32
REMARK 500 ASN B 261 -146.20 -84.81
REMARK 500 LYS B 262 -14.90 -167.64
REMARK 500 ARG B 297 -162.12 63.95
REMARK 500 ILE B 300 -63.36 -97.37
REMARK 500 ASN B 301 174.45 76.61
REMARK 500 MET C 401 31.29 -162.47
REMARK 500 LYS C 462 43.69 -100.31
REMARK 500 MET D 601 -97.29 27.68
REMARK 500 LYS D 602 98.77 172.06
REMARK 500 LEU D 604 -99.48 -114.38
REMARK 500 GLU D 605 41.75 -95.35
REMARK 500 SER D 631 106.65 -161.27
REMARK 500 HIS D 635 -163.11 -117.75
REMARK 500 PRO D 660 -82.23 -58.93
REMARK 500 ILE D 700 -118.95 -64.79
REMARK 500 ASN D 701 174.89 133.28
REMARK 500 LYS D 744 23.32 -79.07
REMARK 500 GLU D 745 -53.76 -169.34
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 761 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 40 OE2
REMARK 620 2 ASP A 107 OD1 65.1
REMARK 620 3 GLU A 110 OE1 95.1 108.6
REMARK 620 4 HOH A1004 O 96.1 157.7 83.9
REMARK 620 5 HOH A1056 O 88.0 89.8 160.9 77.0
REMARK 620 6 HOH A1136 O 157.8 102.7 106.7 90.7 72.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 762 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 240 OE1
REMARK 620 2 ASP B 307 OD1 69.0
REMARK 620 3 GLU B 310 OE1 68.2 88.5
REMARK 620 4 HOH B1007 O 98.0 88.3 166.0
REMARK 620 5 HOH B1245 O 162.7 113.1 128.2 65.4
REMARK 620 6 HOH B1319 O 126.1 163.0 90.7 96.3 55.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 763 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 440 OE2
REMARK 620 2 ASP C 507 OD1 70.4
REMARK 620 3 GLU C 510 OE1 101.3 98.9
REMARK 620 4 HOH C1008 O 86.2 154.9 94.3
REMARK 620 5 HOH C1015 O 85.1 87.1 172.4 81.9
REMARK 620 6 HOH C1039 O 158.3 130.1 83.9 72.4 88.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 764 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 640 OE1
REMARK 620 2 ASP D 707 OD1 69.3
REMARK 620 3 GLU D 710 OE1 76.4 101.0
REMARK 620 4 HOH D1123 O 119.9 96.0 160.0
REMARK 620 5 HOH D1302 O 129.3 160.0 79.5 80.9
REMARK 620 N 1 2 3 4
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 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 762
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 763
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 764
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I4S RELATED DB: PDB
REMARK 900 1I4S IS THE CRYSTAL STRUCTURE OF UNLIGATED RNASE III ENDONUCLEASE
REMARK 900 DOMAIN FROM AQUIFEX AEOLICUS
REMARK 900 RELATED ID: 1STU RELATED DB: PDB
REMARK 900 1STU IS THE NMR SOLUTION STRUCTURE OF A DOUBLE-STRANDED RNA-BINDING
REMARK 900 DOMAIN FROM DROSOPHILA STAUFEN PROTEIN
REMARK 900 RELATED ID: 1DI2 RELATED DB: PDB
REMARK 900 1DI2 IS THE CRYSTAL STRUCTURE OF A DOUBLE-STRANDED RNA-BINDING
REMARK 900 DOMAIN FROM XENOPUS LAEVIS COMPLEXED WITH DOUBLE-STRANDED RNA
REMARK 900 RELATED ID: 1JFZ RELATED DB: PDB
REMARK 900 1JFZ IS THE CRYSTAL STRUCTURE OF A MN(II)-COMPLEX OF RNASE III
REMARK 900 ENDONUCLEASE DOMAIN FROM AQUIFEX AEOLICUS
REMARK 900 RELATED ID: 1O0W RELATED DB: PDB
REMARK 900 1O0W IS THE CRYSTAL STRUCTURE OF UNLIGATED RIBONUCLEASE III FROM
REMARK 900 THERMOTOGA MARITIMA
REMARK 900 RELATED ID: 1RC7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RNASE III MUTANT E110K FROM AQUIFEX AEOLICUS
REMARK 900 COMPLEXED WITH DS-RNA AT 2.15 ANGSTROM RESOLUTION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 EXPRESSED WITH A N-TERMINAL GLYCINE RESIDUE,
REMARK 999 AND WITH SIX-HISTIDINE-TAGGED C-TERMINUS.
DBREF 1RC5 A 1 147 UNP O67082 RNC_AQUAE 1 147
DBREF 1RC5 B 201 347 UNP O67082 RNC_AQUAE 1 147
DBREF 1RC5 C 401 547 UNP O67082 RNC_AQUAE 1 147
DBREF 1RC5 D 601 747 UNP O67082 RNC_AQUAE 1 147
SEQADV 1RC5 GLY A 0 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS A 148 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS A 149 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS A 150 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS A 151 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS A 152 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS A 153 UNP O67082 SEE REMARK 999
SEQADV 1RC5 GLY B 200 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS B 348 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS B 349 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS B 350 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS B 351 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS B 352 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS B 353 UNP O67082 SEE REMARK 999
SEQADV 1RC5 GLY C 400 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS C 548 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS C 549 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS C 550 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS C 551 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS C 552 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS C 553 UNP O67082 SEE REMARK 999
SEQADV 1RC5 GLY D 600 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS D 748 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS D 749 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS D 750 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS D 751 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS D 752 UNP O67082 SEE REMARK 999
SEQADV 1RC5 HIS D 753 UNP O67082 SEE REMARK 999
SEQRES 1 A 154 GLY MET LYS MET LEU GLU GLN LEU GLU LYS LYS LEU GLY
SEQRES 2 A 154 TYR THR PHE LYS ASP LYS SER LEU LEU GLU LYS ALA LEU
SEQRES 3 A 154 THR HIS VAL SER TYR SER LYS LYS GLU HIS TYR GLU THR
SEQRES 4 A 154 LEU GLU PHE LEU GLY ASP ALA LEU VAL ASN PHE PHE ILE
SEQRES 5 A 154 VAL ASP LEU LEU VAL GLN TYR SER PRO ASN LYS ARG GLU
SEQRES 6 A 154 GLY PHE LEU SER PRO LEU LYS ALA TYR LEU ILE SER GLU
SEQRES 7 A 154 GLU PHE PHE ASN LEU LEU ALA GLN LYS LEU GLU LEU HIS
SEQRES 8 A 154 LYS PHE ILE ARG ILE LYS ARG GLY LYS ILE ASN GLU THR
SEQRES 9 A 154 ILE ILE GLY ASP VAL PHE GLU ALA LEU TRP ALA ALA VAL
SEQRES 10 A 154 TYR ILE ASP SER GLY ARG ASP ALA ASN PHE THR ARG GLU
SEQRES 11 A 154 LEU PHE TYR LYS LEU PHE LYS GLU ASP ILE LEU SER ALA
SEQRES 12 A 154 ILE LYS GLU GLY ARG HIS HIS HIS HIS HIS HIS
SEQRES 1 B 154 GLY MET LYS MET LEU GLU GLN LEU GLU LYS LYS LEU GLY
SEQRES 2 B 154 TYR THR PHE LYS ASP LYS SER LEU LEU GLU LYS ALA LEU
SEQRES 3 B 154 THR HIS VAL SER TYR SER LYS LYS GLU HIS TYR GLU THR
SEQRES 4 B 154 LEU GLU PHE LEU GLY ASP ALA LEU VAL ASN PHE PHE ILE
SEQRES 5 B 154 VAL ASP LEU LEU VAL GLN TYR SER PRO ASN LYS ARG GLU
SEQRES 6 B 154 GLY PHE LEU SER PRO LEU LYS ALA TYR LEU ILE SER GLU
SEQRES 7 B 154 GLU PHE PHE ASN LEU LEU ALA GLN LYS LEU GLU LEU HIS
SEQRES 8 B 154 LYS PHE ILE ARG ILE LYS ARG GLY LYS ILE ASN GLU THR
SEQRES 9 B 154 ILE ILE GLY ASP VAL PHE GLU ALA LEU TRP ALA ALA VAL
SEQRES 10 B 154 TYR ILE ASP SER GLY ARG ASP ALA ASN PHE THR ARG GLU
SEQRES 11 B 154 LEU PHE TYR LYS LEU PHE LYS GLU ASP ILE LEU SER ALA
SEQRES 12 B 154 ILE LYS GLU GLY ARG HIS HIS HIS HIS HIS HIS
SEQRES 1 C 154 GLY MET LYS MET LEU GLU GLN LEU GLU LYS LYS LEU GLY
SEQRES 2 C 154 TYR THR PHE LYS ASP LYS SER LEU LEU GLU LYS ALA LEU
SEQRES 3 C 154 THR HIS VAL SER TYR SER LYS LYS GLU HIS TYR GLU THR
SEQRES 4 C 154 LEU GLU PHE LEU GLY ASP ALA LEU VAL ASN PHE PHE ILE
SEQRES 5 C 154 VAL ASP LEU LEU VAL GLN TYR SER PRO ASN LYS ARG GLU
SEQRES 6 C 154 GLY PHE LEU SER PRO LEU LYS ALA TYR LEU ILE SER GLU
SEQRES 7 C 154 GLU PHE PHE ASN LEU LEU ALA GLN LYS LEU GLU LEU HIS
SEQRES 8 C 154 LYS PHE ILE ARG ILE LYS ARG GLY LYS ILE ASN GLU THR
SEQRES 9 C 154 ILE ILE GLY ASP VAL PHE GLU ALA LEU TRP ALA ALA VAL
SEQRES 10 C 154 TYR ILE ASP SER GLY ARG ASP ALA ASN PHE THR ARG GLU
SEQRES 11 C 154 LEU PHE TYR LYS LEU PHE LYS GLU ASP ILE LEU SER ALA
SEQRES 12 C 154 ILE LYS GLU GLY ARG HIS HIS HIS HIS HIS HIS
SEQRES 1 D 154 GLY MET LYS MET LEU GLU GLN LEU GLU LYS LYS LEU GLY
SEQRES 2 D 154 TYR THR PHE LYS ASP LYS SER LEU LEU GLU LYS ALA LEU
SEQRES 3 D 154 THR HIS VAL SER TYR SER LYS LYS GLU HIS TYR GLU THR
SEQRES 4 D 154 LEU GLU PHE LEU GLY ASP ALA LEU VAL ASN PHE PHE ILE
SEQRES 5 D 154 VAL ASP LEU LEU VAL GLN TYR SER PRO ASN LYS ARG GLU
SEQRES 6 D 154 GLY PHE LEU SER PRO LEU LYS ALA TYR LEU ILE SER GLU
SEQRES 7 D 154 GLU PHE PHE ASN LEU LEU ALA GLN LYS LEU GLU LEU HIS
SEQRES 8 D 154 LYS PHE ILE ARG ILE LYS ARG GLY LYS ILE ASN GLU THR
SEQRES 9 D 154 ILE ILE GLY ASP VAL PHE GLU ALA LEU TRP ALA ALA VAL
SEQRES 10 D 154 TYR ILE ASP SER GLY ARG ASP ALA ASN PHE THR ARG GLU
SEQRES 11 D 154 LEU PHE TYR LYS LEU PHE LYS GLU ASP ILE LEU SER ALA
SEQRES 12 D 154 ILE LYS GLU GLY ARG HIS HIS HIS HIS HIS HIS
HET MG A 761 1
HET MG B 762 1
HET MG C 763 1
HET MG D 764 1
HETNAM MG MAGNESIUM ION
FORMUL 5 MG 4(MG 2+)
FORMUL 9 HOH *675(H2 O)
HELIX 1 1 MET A 3 GLY A 12 1 10
HELIX 2 2 ASP A 17 THR A 26 1 10
HELIX 3 3 TYR A 36 SER A 59 1 24
HELIX 4 4 ARG A 63 ILE A 75 1 13
HELIX 5 5 SER A 76 GLN A 85 1 10
HELIX 6 6 LYS A 86 PHE A 92 5 7
HELIX 7 7 ASN A 101 SER A 120 1 20
HELIX 8 8 ASP A 123 LYS A 144 1 22
HELIX 9 9 GLN B 206 GLY B 212 1 7
HELIX 10 10 ASP B 217 LEU B 225 1 9
HELIX 11 11 TYR B 236 SER B 259 1 24
HELIX 12 12 ARG B 263 ILE B 275 1 13
HELIX 13 13 SER B 276 GLN B 285 1 10
HELIX 14 14 LYS B 286 PHE B 292 5 7
HELIX 15 15 ASN B 301 SER B 320 1 20
HELIX 16 16 ASP B 323 GLY B 346 1 24
HELIX 17 17 MET C 403 GLY C 412 1 10
HELIX 18 18 ASP C 417 LEU C 425 1 9
HELIX 19 19 TYR C 436 SER C 459 1 24
HELIX 20 20 ARG C 463 SER C 476 1 14
HELIX 21 21 SER C 476 GLU C 488 1 13
HELIX 22 22 LEU C 489 PHE C 492 5 4
HELIX 23 23 ASN C 501 SER C 520 1 20
HELIX 24 24 ASP C 523 GLY C 546 1 24
HELIX 25 25 GLN D 606 GLY D 612 1 7
HELIX 26 26 ASP D 617 THR D 626 1 10
HELIX 27 27 TYR D 636 VAL D 656 1 21
HELIX 28 28 ARG D 663 ILE D 675 1 13
HELIX 29 29 SER D 676 GLU D 688 1 13
HELIX 30 30 LEU D 689 PHE D 692 5 4
HELIX 31 31 ASN D 701 SER D 720 1 20
HELIX 32 32 ASP D 723 ILE D 743 1 21
LINK OE2 GLU A 40 MG MG A 761 1555 1555 1.97
LINK OD1 ASP A 107 MG MG A 761 1555 1555 2.55
LINK OE1 GLU A 110 MG MG A 761 1555 1555 2.22
LINK MG MG A 761 O HOH A1004 1555 1555 2.58
LINK MG MG A 761 O HOH A1056 1555 1555 2.36
LINK MG MG A 761 O HOH A1136 1555 1555 2.07
LINK OE1 GLU B 240 MG MG B 762 1555 1555 2.55
LINK OD1 ASP B 307 MG MG B 762 1555 1555 2.24
LINK OE1 GLU B 310 MG MG B 762 1555 1555 2.02
LINK MG MG B 762 O HOH B1007 1555 1555 2.53
LINK MG MG B 762 O HOH B1245 1555 1555 3.07
LINK MG MG B 762 O HOH B1319 1555 1555 2.84
LINK OE2 GLU C 440 MG MG C 763 1555 1555 2.12
LINK OD1 ASP C 507 MG MG C 763 1555 1555 2.63
LINK OE1 GLU C 510 MG MG C 763 1555 1555 2.50
LINK MG MG C 763 O HOH C1008 1555 1555 2.53
LINK MG MG C 763 O HOH C1015 1555 1555 2.77
LINK MG MG C 763 O HOH C1039 1555 1555 2.81
LINK OE1 GLU D 640 MG MG D 764 1555 1555 2.33
LINK OD1 ASP D 707 MG MG D 764 1555 1555 1.99
LINK OE1 GLU D 710 MG MG D 764 1555 1555 2.16
LINK MG MG D 764 O HOH D1123 1555 1555 2.30
LINK MG MG D 764 O HOH D1302 1555 1555 3.04
SITE 1 AC1 6 GLU A 40 ASP A 107 GLU A 110 HOH A1004
SITE 2 AC1 6 HOH A1056 HOH A1136
SITE 1 AC2 6 GLU B 240 ASP B 307 GLU B 310 HOH B1007
SITE 2 AC2 6 HOH B1245 HOH B1319
SITE 1 AC3 6 GLU C 440 ASP C 507 GLU C 510 HOH C1008
SITE 2 AC3 6 HOH C1015 HOH C1039
SITE 1 AC4 5 GLU D 640 ASP D 707 GLU D 710 HOH D1123
SITE 2 AC4 5 HOH D1302
CRYST1 49.742 140.856 49.746 90.00 117.29 90.00 P 1 21 1 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 0.020104 0.000000 0.010372 0.00000
SCALE2 0.000000 0.007099 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022620 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
