HEADER HYDROLASE/DNA 14-JUN-10 3NH2
TITLE CRYSTAL STRUCTURE OF RNASE T IN COMPLEX WITH A STEM DNA WITH A 3'
TITLE 2 OVERHANG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE T;
COMPND 3 CHAIN: A, B, E, F;
COMPND 4 SYNONYM: RNASE T, EXORIBONUCLEASE T;
COMPND 5 EC: 3.1.13.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 5'-D(P*TP*TP*AP*CP*AP*AP*C)-3';
COMPND 9 CHAIN: C, D, G, H;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: SSDNA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: JM109 / ATCC 53323;
SOURCE 5 GENE: RNT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630
KEYWDS EXORIBONUCLEASE, RNA PROCESSING, RNA MATURATION, PROTEIN-DNA
KEYWDS 2 INTERACTIONS, PROTEIN-DNA COMPLEX, EXO-NUCLEASE, HYDROLASE-DNA
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-Y.HSIAO,H.S.YUAN
REVDAT 5 08-NOV-23 3NH2 1 REMARK
REVDAT 4 31-MAY-23 3NH2 1 SOURCE REMARK SEQADV
REVDAT 3 21-DEC-11 3NH2 1 JRNL VERSN
REVDAT 2 23-FEB-11 3NH2 1 JRNL
REVDAT 1 16-FEB-11 3NH2 0
JRNL AUTH Y.-Y.HSIAO,C.-C.YANG,C.L.LIN,J.L.J.LIN,Y.DUH,H.S.YUAN
JRNL TITL STRUCTURAL BASIS FOR RNA TRIMMING BY RNASE T IN STABLE RNA
JRNL TITL 2 3'-END MATURATION
JRNL REF NAT.CHEM.BIOL. V. 7 236 2011
JRNL REFN ISSN 1552-4450
JRNL PMID 21317904
JRNL DOI 10.1038/NCHEMBIO.524
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 35456
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.600
REMARK 3 FREE R VALUE TEST SET COUNT : 2693
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 26.7623 - 6.1142 0.95 1677 149 0.1963 0.2285
REMARK 3 2 6.1142 - 4.8625 0.94 1674 136 0.1745 0.1832
REMARK 3 3 4.8625 - 4.2506 0.96 1732 154 0.1455 0.1918
REMARK 3 4 4.2506 - 3.8632 0.96 1710 147 0.1662 0.1939
REMARK 3 5 3.8632 - 3.5870 0.95 1723 133 0.1554 0.2112
REMARK 3 6 3.5870 - 3.3760 0.97 1714 147 0.1656 0.2052
REMARK 3 7 3.3760 - 3.2072 0.97 1750 147 0.1714 0.2269
REMARK 3 8 3.2072 - 3.0678 0.97 1735 138 0.1801 0.2378
REMARK 3 9 3.0678 - 2.9498 0.96 1716 149 0.1858 0.2462
REMARK 3 10 2.9498 - 2.8482 0.97 1731 135 0.1922 0.2762
REMARK 3 11 2.8482 - 2.7592 0.97 1755 142 0.2050 0.2988
REMARK 3 12 2.7592 - 2.6804 0.97 1751 143 0.2039 0.2880
REMARK 3 13 2.6804 - 2.6099 0.97 1704 118 0.2020 0.2648
REMARK 3 14 2.6099 - 2.5463 0.97 1761 154 0.2053 0.2744
REMARK 3 15 2.5463 - 2.4884 0.96 1718 137 0.2128 0.3434
REMARK 3 16 2.4884 - 2.4355 0.96 1759 139 0.2025 0.2851
REMARK 3 17 2.4355 - 2.3868 0.97 1723 140 0.2083 0.2640
REMARK 3 18 2.3868 - 2.3418 0.97 1733 146 0.2059 0.3308
REMARK 3 19 2.3418 - 2.3000 0.95 1697 139 0.1983 0.2658
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 40.97
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.15700
REMARK 3 B22 (A**2) : -1.08760
REMARK 3 B33 (A**2) : -0.06940
REMARK 3 B12 (A**2) : -0.55410
REMARK 3 B13 (A**2) : -0.58550
REMARK 3 B23 (A**2) : 2.47370
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 7023
REMARK 3 ANGLE : 0.736 9618
REMARK 3 CHIRALITY : 0.050 1064
REMARK 3 PLANARITY : 0.002 1176
REMARK 3 DIHEDRAL : 17.435 2514
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NH2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059819.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED 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 : 35579
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 (%) : 96.5
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
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 (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.41000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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 ENTRY 3NGY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1% W/V N-OCTYL-BETA-D-GLUCOSIDE,
REMARK 280 0.1M SODIUM CITRATE TRIBASIC DIHYDRATE, PH 5.5, 22% PEG 4000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: A, B, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER 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 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ASP A 3
REMARK 465 ASN A 4
REMARK 465 ALA A 5
REMARK 465 GLN A 6
REMARK 465 LEU A 7
REMARK 465 THR A 8
REMARK 465 SER A 177
REMARK 465 THR A 178
REMARK 465 GLN A 179
REMARK 465 ALA A 180
REMARK 465 HIS A 181
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ASP B 3
REMARK 465 ASN B 4
REMARK 465 ALA B 5
REMARK 465 GLN B 6
REMARK 465 LEU B 7
REMARK 465 THR B 8
REMARK 465 VAL B 215
REMARK 465 DT D 1
REMARK 465 MET E -19
REMARK 465 GLY E -18
REMARK 465 SER E -17
REMARK 465 SER E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 HIS E -10
REMARK 465 SER E -9
REMARK 465 SER E -8
REMARK 465 GLY E -7
REMARK 465 LEU E -6
REMARK 465 VAL E -5
REMARK 465 PRO E -4
REMARK 465 ARG E -3
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 HIS E 0
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 ASP E 3
REMARK 465 ASN E 4
REMARK 465 ALA E 5
REMARK 465 GLN E 6
REMARK 465 LEU E 7
REMARK 465 THR E 8
REMARK 465 VAL E 215
REMARK 465 MET F -19
REMARK 465 GLY F -18
REMARK 465 SER F -17
REMARK 465 SER F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 HIS F -11
REMARK 465 HIS F -10
REMARK 465 SER F -9
REMARK 465 SER F -8
REMARK 465 GLY F -7
REMARK 465 LEU F -6
REMARK 465 VAL F -5
REMARK 465 PRO F -4
REMARK 465 ARG F -3
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 ASP F 3
REMARK 465 ASN F 4
REMARK 465 ALA F 5
REMARK 465 GLN F 6
REMARK 465 LEU F 7
REMARK 465 THR F 8
REMARK 465 SER F 177
REMARK 465 THR F 178
REMARK 465 GLN F 179
REMARK 465 ALA F 180
REMARK 465 HIS F 181
REMARK 465 DT G 1
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 DT C 1 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DA C 5 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA D 5 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DA D 6 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA G 5 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DA G 6 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA H 5 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DA H 6 O4' - C1' - N9 ANGL. DEV. = 2.9 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 ASP A 55 -69.92 -108.60
REMARK 500 ARG A 114 171.35 176.03
REMARK 500 PHE A 146 -7.02 -141.93
REMARK 500 GLU A 213 55.22 -118.39
REMARK 500 ASP B 55 -93.20 -116.01
REMARK 500 PRO B 82 -6.32 -58.22
REMARK 500 PHE B 146 -9.45 -151.82
REMARK 500 ASP E 55 -87.29 -114.43
REMARK 500 PHE E 146 -19.14 -146.04
REMARK 500 ASP F 55 -82.94 -112.76
REMARK 500 ASP F 86 32.15 -97.28
REMARK 500 PHE F 146 -20.52 -147.08
REMARK 500 PHE F 175 119.15 -160.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NGY RELATED DB: PDB
REMARK 900 RNASE T (E92G MUTANT)
REMARK 900 RELATED ID: 3NGZ RELATED DB: PDB
REMARK 900 RNASE T IN COMPLEX WITH A NON-PREFERRED SSDNA (GC) WITH ONE MG IN
REMARK 900 THE ACTIVE SITE
REMARK 900 RELATED ID: 3NH0 RELATED DB: PDB
REMARK 900 RNASE T IN COMPLEX WITH A NON-PREFERRED SSDNA (AAC)
REMARK 900 RELATED ID: 3NH1 RELATED DB: PDB
REMARK 900 RNASE T IN COMPLEX WITH A PREFERRED SSDNA (TAGG) WITH TWO MG IN THE
REMARK 900 ACTIVE SITE
DBREF 3NH2 A 1 215 UNP P30014 RNT_ECOLI 1 215
DBREF 3NH2 B 1 215 UNP P30014 RNT_ECOLI 1 215
DBREF 3NH2 C 1 7 PDB 3NH2 3NH2 1 7
DBREF 3NH2 D 1 7 PDB 3NH2 3NH2 1 7
DBREF 3NH2 E 1 215 UNP P30014 RNT_ECOLI 1 215
DBREF 3NH2 F 1 215 UNP P30014 RNT_ECOLI 1 215
DBREF 3NH2 G 1 7 PDB 3NH2 3NH2 1 7
DBREF 3NH2 H 1 7 PDB 3NH2 3NH2 1 7
SEQADV 3NH2 MET A -19 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY A -18 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER A -17 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER A -16 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS A -15 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS A -14 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS A -13 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS A -12 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS A -11 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS A -10 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER A -9 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER A -8 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY A -7 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 LEU A -6 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 VAL A -5 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 PRO A -4 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 ARG A -3 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY A -2 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER A -1 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS A 0 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 MET B -19 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY B -18 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER B -17 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER B -16 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS B -15 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS B -14 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS B -13 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS B -12 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS B -11 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS B -10 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER B -9 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER B -8 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY B -7 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 LEU B -6 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 VAL B -5 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 PRO B -4 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 ARG B -3 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY B -2 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER B -1 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS B 0 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 MET E -19 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY E -18 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER E -17 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER E -16 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS E -15 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS E -14 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS E -13 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS E -12 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS E -11 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS E -10 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER E -9 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER E -8 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY E -7 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 LEU E -6 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 VAL E -5 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 PRO E -4 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 ARG E -3 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY E -2 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER E -1 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS E 0 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 MET F -19 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY F -18 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER F -17 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER F -16 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS F -15 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS F -14 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS F -13 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS F -12 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS F -11 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS F -10 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER F -9 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER F -8 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY F -7 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 LEU F -6 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 VAL F -5 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 PRO F -4 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 ARG F -3 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 GLY F -2 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 SER F -1 UNP P30014 EXPRESSION TAG
SEQADV 3NH2 HIS F 0 UNP P30014 EXPRESSION TAG
SEQRES 1 A 235 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 235 LEU VAL PRO ARG GLY SER HIS MET SER ASP ASN ALA GLN
SEQRES 3 A 235 LEU THR GLY LEU CYS ASP ARG PHE ARG GLY PHE TYR PRO
SEQRES 4 A 235 VAL VAL ILE ASP VAL GLU THR ALA GLY PHE ASN ALA LYS
SEQRES 5 A 235 THR ASP ALA LEU LEU GLU ILE ALA ALA ILE THR LEU LYS
SEQRES 6 A 235 MET ASP GLU GLN GLY TRP LEU MET PRO ASP THR THR LEU
SEQRES 7 A 235 HIS PHE HIS VAL GLU PRO PHE VAL GLY ALA ASN LEU GLN
SEQRES 8 A 235 PRO GLU ALA LEU ALA PHE ASN GLY ILE ASP PRO ASN ASP
SEQRES 9 A 235 PRO ASP ARG GLY ALA VAL SER GLU TYR GLU ALA LEU HIS
SEQRES 10 A 235 GLU ILE PHE LYS VAL VAL ARG LYS GLY ILE LYS ALA SER
SEQRES 11 A 235 GLY CYS ASN ARG ALA ILE MET VAL ALA HIS ASN ALA ASN
SEQRES 12 A 235 PHE ASP HIS SER PHE MET MET ALA ALA ALA GLU ARG ALA
SEQRES 13 A 235 SER LEU LYS ARG ASN PRO PHE HIS PRO PHE ALA THR PHE
SEQRES 14 A 235 ASP THR ALA ALA LEU ALA GLY LEU ALA LEU GLY GLN THR
SEQRES 15 A 235 VAL LEU SER LYS ALA CYS GLN THR ALA GLY MET ASP PHE
SEQRES 16 A 235 ASP SER THR GLN ALA HIS SER ALA LEU TYR ASP THR GLU
SEQRES 17 A 235 ARG THR ALA VAL LEU PHE CYS GLU ILE VAL ASN ARG TRP
SEQRES 18 A 235 LYS ARG LEU GLY GLY TRP PRO LEU SER ALA ALA GLU GLU
SEQRES 19 A 235 VAL
SEQRES 1 B 235 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 235 LEU VAL PRO ARG GLY SER HIS MET SER ASP ASN ALA GLN
SEQRES 3 B 235 LEU THR GLY LEU CYS ASP ARG PHE ARG GLY PHE TYR PRO
SEQRES 4 B 235 VAL VAL ILE ASP VAL GLU THR ALA GLY PHE ASN ALA LYS
SEQRES 5 B 235 THR ASP ALA LEU LEU GLU ILE ALA ALA ILE THR LEU LYS
SEQRES 6 B 235 MET ASP GLU GLN GLY TRP LEU MET PRO ASP THR THR LEU
SEQRES 7 B 235 HIS PHE HIS VAL GLU PRO PHE VAL GLY ALA ASN LEU GLN
SEQRES 8 B 235 PRO GLU ALA LEU ALA PHE ASN GLY ILE ASP PRO ASN ASP
SEQRES 9 B 235 PRO ASP ARG GLY ALA VAL SER GLU TYR GLU ALA LEU HIS
SEQRES 10 B 235 GLU ILE PHE LYS VAL VAL ARG LYS GLY ILE LYS ALA SER
SEQRES 11 B 235 GLY CYS ASN ARG ALA ILE MET VAL ALA HIS ASN ALA ASN
SEQRES 12 B 235 PHE ASP HIS SER PHE MET MET ALA ALA ALA GLU ARG ALA
SEQRES 13 B 235 SER LEU LYS ARG ASN PRO PHE HIS PRO PHE ALA THR PHE
SEQRES 14 B 235 ASP THR ALA ALA LEU ALA GLY LEU ALA LEU GLY GLN THR
SEQRES 15 B 235 VAL LEU SER LYS ALA CYS GLN THR ALA GLY MET ASP PHE
SEQRES 16 B 235 ASP SER THR GLN ALA HIS SER ALA LEU TYR ASP THR GLU
SEQRES 17 B 235 ARG THR ALA VAL LEU PHE CYS GLU ILE VAL ASN ARG TRP
SEQRES 18 B 235 LYS ARG LEU GLY GLY TRP PRO LEU SER ALA ALA GLU GLU
SEQRES 19 B 235 VAL
SEQRES 1 C 7 DT DT DA DC DA DA DC
SEQRES 1 D 7 DT DT DA DC DA DA DC
SEQRES 1 E 235 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 235 LEU VAL PRO ARG GLY SER HIS MET SER ASP ASN ALA GLN
SEQRES 3 E 235 LEU THR GLY LEU CYS ASP ARG PHE ARG GLY PHE TYR PRO
SEQRES 4 E 235 VAL VAL ILE ASP VAL GLU THR ALA GLY PHE ASN ALA LYS
SEQRES 5 E 235 THR ASP ALA LEU LEU GLU ILE ALA ALA ILE THR LEU LYS
SEQRES 6 E 235 MET ASP GLU GLN GLY TRP LEU MET PRO ASP THR THR LEU
SEQRES 7 E 235 HIS PHE HIS VAL GLU PRO PHE VAL GLY ALA ASN LEU GLN
SEQRES 8 E 235 PRO GLU ALA LEU ALA PHE ASN GLY ILE ASP PRO ASN ASP
SEQRES 9 E 235 PRO ASP ARG GLY ALA VAL SER GLU TYR GLU ALA LEU HIS
SEQRES 10 E 235 GLU ILE PHE LYS VAL VAL ARG LYS GLY ILE LYS ALA SER
SEQRES 11 E 235 GLY CYS ASN ARG ALA ILE MET VAL ALA HIS ASN ALA ASN
SEQRES 12 E 235 PHE ASP HIS SER PHE MET MET ALA ALA ALA GLU ARG ALA
SEQRES 13 E 235 SER LEU LYS ARG ASN PRO PHE HIS PRO PHE ALA THR PHE
SEQRES 14 E 235 ASP THR ALA ALA LEU ALA GLY LEU ALA LEU GLY GLN THR
SEQRES 15 E 235 VAL LEU SER LYS ALA CYS GLN THR ALA GLY MET ASP PHE
SEQRES 16 E 235 ASP SER THR GLN ALA HIS SER ALA LEU TYR ASP THR GLU
SEQRES 17 E 235 ARG THR ALA VAL LEU PHE CYS GLU ILE VAL ASN ARG TRP
SEQRES 18 E 235 LYS ARG LEU GLY GLY TRP PRO LEU SER ALA ALA GLU GLU
SEQRES 19 E 235 VAL
SEQRES 1 F 235 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 235 LEU VAL PRO ARG GLY SER HIS MET SER ASP ASN ALA GLN
SEQRES 3 F 235 LEU THR GLY LEU CYS ASP ARG PHE ARG GLY PHE TYR PRO
SEQRES 4 F 235 VAL VAL ILE ASP VAL GLU THR ALA GLY PHE ASN ALA LYS
SEQRES 5 F 235 THR ASP ALA LEU LEU GLU ILE ALA ALA ILE THR LEU LYS
SEQRES 6 F 235 MET ASP GLU GLN GLY TRP LEU MET PRO ASP THR THR LEU
SEQRES 7 F 235 HIS PHE HIS VAL GLU PRO PHE VAL GLY ALA ASN LEU GLN
SEQRES 8 F 235 PRO GLU ALA LEU ALA PHE ASN GLY ILE ASP PRO ASN ASP
SEQRES 9 F 235 PRO ASP ARG GLY ALA VAL SER GLU TYR GLU ALA LEU HIS
SEQRES 10 F 235 GLU ILE PHE LYS VAL VAL ARG LYS GLY ILE LYS ALA SER
SEQRES 11 F 235 GLY CYS ASN ARG ALA ILE MET VAL ALA HIS ASN ALA ASN
SEQRES 12 F 235 PHE ASP HIS SER PHE MET MET ALA ALA ALA GLU ARG ALA
SEQRES 13 F 235 SER LEU LYS ARG ASN PRO PHE HIS PRO PHE ALA THR PHE
SEQRES 14 F 235 ASP THR ALA ALA LEU ALA GLY LEU ALA LEU GLY GLN THR
SEQRES 15 F 235 VAL LEU SER LYS ALA CYS GLN THR ALA GLY MET ASP PHE
SEQRES 16 F 235 ASP SER THR GLN ALA HIS SER ALA LEU TYR ASP THR GLU
SEQRES 17 F 235 ARG THR ALA VAL LEU PHE CYS GLU ILE VAL ASN ARG TRP
SEQRES 18 F 235 LYS ARG LEU GLY GLY TRP PRO LEU SER ALA ALA GLU GLU
SEQRES 19 F 235 VAL
SEQRES 1 G 7 DT DT DA DC DA DA DC
SEQRES 1 H 7 DT DT DA DC DA DA DC
FORMUL 9 HOH *345(H2 O)
HELIX 1 1 GLY A 9 PHE A 14 1 6
HELIX 2 2 GLN A 71 GLY A 79 1 9
HELIX 3 3 SER A 91 GLY A 111 1 21
HELIX 4 4 ALA A 122 ALA A 136 1 15
HELIX 5 5 THR A 151 LEU A 159 1 9
HELIX 6 6 VAL A 163 ALA A 171 1 9
HELIX 7 7 SER A 182 LEU A 204 1 23
HELIX 8 8 PRO A 208 GLU A 214 5 7
HELIX 9 9 GLY B 9 PHE B 14 1 6
HELIX 10 10 GLN B 71 GLY B 79 1 9
HELIX 11 11 SER B 91 GLY B 111 1 21
HELIX 12 12 ALA B 122 ALA B 136 1 15
HELIX 13 13 THR B 151 GLY B 160 1 10
HELIX 14 14 VAL B 163 ALA B 171 1 9
HELIX 15 15 SER B 182 LEU B 204 1 23
HELIX 16 16 SER B 210 GLU B 214 5 5
HELIX 17 17 GLY E 9 PHE E 14 1 6
HELIX 18 18 GLN E 71 GLY E 79 1 9
HELIX 19 19 SER E 91 GLY E 111 1 21
HELIX 20 20 ALA E 122 ALA E 136 1 15
HELIX 21 21 THR E 151 LEU E 159 1 9
HELIX 22 22 VAL E 163 ALA E 171 1 9
HELIX 23 23 ASP E 176 ALA E 180 5 5
HELIX 24 24 SER E 182 LEU E 204 1 23
HELIX 25 25 GLY F 9 PHE F 14 1 6
HELIX 26 26 GLN F 71 GLY F 79 1 9
HELIX 27 27 ASP F 84 GLY F 88 5 5
HELIX 28 28 SER F 91 GLY F 111 1 21
HELIX 29 29 ALA F 122 ALA F 136 1 15
HELIX 30 30 THR F 151 LEU F 159 1 9
HELIX 31 31 VAL F 163 ALA F 171 1 9
HELIX 32 32 SER F 182 LEU F 204 1 23
HELIX 33 33 SER F 210 GLU F 214 5 5
SHEET 1 A 5 LEU A 52 HIS A 61 0
SHEET 2 A 5 LEU A 36 MET A 46 -1 N THR A 43 O ASP A 55
SHEET 3 A 5 PHE A 17 THR A 26 -1 N VAL A 21 O ILE A 42
SHEET 4 A 5 ARG A 114 ALA A 119 1 O ARG A 114 N TYR A 18
SHEET 5 A 5 PHE A 143 ASP A 150 1 O PHE A 149 N MET A 117
SHEET 1 B 5 LEU B 52 HIS B 61 0
SHEET 2 B 5 LEU B 36 MET B 46 -1 N THR B 43 O ASP B 55
SHEET 3 B 5 PHE B 17 THR B 26 -1 N VAL B 21 O ILE B 42
SHEET 4 B 5 ARG B 114 ALA B 119 1 O ARG B 114 N TYR B 18
SHEET 5 B 5 PHE B 143 ASP B 150 1 O PHE B 149 N MET B 117
SHEET 1 C 5 LEU E 52 HIS E 61 0
SHEET 2 C 5 LEU E 36 MET E 46 -1 N THR E 43 O ASP E 55
SHEET 3 C 5 PHE E 17 THR E 26 -1 N GLU E 25 O LEU E 37
SHEET 4 C 5 ARG E 114 ALA E 119 1 O ARG E 114 N TYR E 18
SHEET 5 C 5 PHE E 143 ASP E 150 1 O PHE E 149 N MET E 117
SHEET 1 D 5 LEU F 52 HIS F 61 0
SHEET 2 D 5 LEU F 36 MET F 46 -1 N THR F 43 O ASP F 55
SHEET 3 D 5 PHE F 17 THR F 26 -1 N GLU F 25 O LEU F 37
SHEET 4 D 5 ARG F 114 ALA F 119 1 O ARG F 114 N TYR F 18
SHEET 5 D 5 PHE F 143 ASP F 150 1 O PHE F 149 N MET F 117
SSBOND 1 CYS A 11 CYS A 112 1555 1555 2.01
SSBOND 2 CYS E 11 CYS E 112 1555 1555 2.03
SSBOND 3 CYS F 11 CYS F 112 1555 1555 2.03
CISPEP 1 TRP A 207 PRO A 208 0 -2.67
CISPEP 2 TRP B 207 PRO B 208 0 -4.16
CISPEP 3 TRP E 207 PRO E 208 0 -3.82
CISPEP 4 TRP F 207 PRO F 208 0 -2.95
CISPEP 5 GLU F 214 VAL F 215 0 1.66
CRYST1 60.379 62.560 62.657 82.77 82.92 66.13 P 1 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 0.016562 -0.007329 -0.001448 0.00000
SCALE2 0.000000 0.017480 -0.001470 0.00000
SCALE3 0.000000 0.000000 0.016139 0.00000
(ATOM LINES ARE NOT SHOWN.)
END