Header list of 1t4l.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN/RNA 29-APR-04 1T4L
TITLE SOLUTION STRUCTURE OF DOUBLE-STRANDED RNA BINDING DOMAIN OF S.
TITLE 2 CEREVISIAE RNASE III (RNT1P) IN COMPLEX WITH THE 5' TERMINAL RNA
TITLE 3 HAIRPIN OF SNR47 PRECURSOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5' TERMINAL HAIRPIN OF SNR47 PRECURSOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AGAA TETRALOOP RNA HAIRPIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RIBONUCLEASE III;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: DOUBLE-STRANDED RNA BINDING DOMAIN;
COMPND 10 SYNONYM: RNASE III;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 5 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 6 ORGANISM_TAXID: 4932;
SOURCE 7 GENE: RNT1, YMR239C, YM9408.01C, YM9959.21;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS DSRBD, RNASE III, AGNN TETRALOOP, PROTEIN-RNA COMPLEX, RNA BINDING
KEYWDS 2 PROTEIN-RNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR H.WU,A.HENRAS,G.CHANFREAU,J.FEIGON
REVDAT 4 02-MAR-22 1T4L 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1T4L 1 VERSN
REVDAT 2 08-JUN-04 1T4L 1 JRNL
REVDAT 1 01-JUN-04 1T4L 0
JRNL AUTH H.WU,A.HENRAS,G.CHANFREAU,J.FEIGON
JRNL TITL STRUCTURAL BASIS FOR RECOGNITION OF THE AGNN TETRALOOP RNA
JRNL TITL 2 FOLD BY THE DOUBLE-STRANDED RNA-BINDING DOMAIN OF RNT1P
JRNL TITL 3 RNASE III.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 8307 2004
JRNL REFN ISSN 0027-8424
JRNL PMID 15150409
JRNL DOI 10.1073/PNAS.0402627101
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 2359 DISTANCE RESTRAINTS
REMARK 3 225 DIHEDRAL RESTRAINTS
REMARK 3 43 RESIDUAL DIPOLAR COUPLINGS
REMARK 4
REMARK 4 1T4L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022304.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 20MM NAPI, 150 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 15N-LABELED RNT1P
REMARK 210 DSRBD/UNLABELED SNR47H;
REMARK 210 UNLABELED RNT1P DSRBD/UNLABELED
REMARK 210 SNR47H; UNIFORMALLY 13C,15N-
REMARK 210 LABELED RNT1P DSRBD/UNLABELED
REMARK 210 SNR47H; UNIFORMALLY 13C,15N-
REMARK 210 LABELED RNT1P DSRBD/UNLABELED
REMARK 210 SNR47H; UNLABELED RNT1P DSRBD/
REMARK 210 13C,15N-A,U,G,C-SLECTIVELY
REMARK 210 LABELED SNR47H SNR47H; UNLABELED
REMARK 210 RNT1P DSRBD/UNIFORMALLY 13C,15N-
REMARK 210 LABELED SNR47H SNR47H
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D
REMARK 210 CBCA(CO)NH; 3D CBCANH; 3D
REMARK 210 HBHA(CO)NH; 3D 15N-NOESY-HSQC;
REMARK 210 3D 13C-NOESY-HMQC; 2D 13C-
REMARK 210 FILTERED/EDITED NOESY; 3D HCCH-
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, XWINNMR 2.6
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 B 419 H LYS B 421 1.39
REMARK 500 O VAL B 406 H GLY B 409 1.51
REMARK 500 O ASP B 434 H LEU B 438 1.60
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 1 G A 1 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 1 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G A 3 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 3 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 A A 4 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A A 6 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A A 9 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G A 11 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 11 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 A A 15 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G A 16 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 16 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 A A 17 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A A 18 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G A 19 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 19 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 A A 20 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A A 21 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G A 23 N7 - C8 - N9 ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 G A 23 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES
REMARK 500 1 G A 25 N7 - C8 - N9 ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 G A 26 N7 - C8 - N9 ANGL. DEV. = 4.7 DEGREES
REMARK 500 1 G A 26 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 A A 28 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G A 1 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 1 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 G A 3 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 3 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES
REMARK 500 2 A A 4 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A A 6 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A A 9 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 G A 11 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G A 11 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 A A 15 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G A 16 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 16 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 A A 17 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A A 18 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G A 19 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G A 19 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 A A 20 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A A 21 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 G A 23 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G A 23 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 25 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G A 25 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 400 ANGLE DEVIATIONS.
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 1 ALA B 370 -79.28 -54.86
REMARK 500 1 LYS B 371 -45.15 -29.33
REMARK 500 1 LEU B 374 -80.90 -68.29
REMARK 500 1 SER B 376 -31.57 -135.92
REMARK 500 1 ILE B 378 -62.50 -129.50
REMARK 500 1 SER B 382 45.26 79.13
REMARK 500 1 ARG B 384 -6.16 84.56
REMARK 500 1 LEU B 385 129.50 -36.02
REMARK 500 1 LYS B 391 56.23 95.68
REMARK 500 1 LYS B 392 107.41 -31.21
REMARK 500 1 PRO B 393 159.53 -44.98
REMARK 500 1 ASP B 397 61.56 166.45
REMARK 500 1 ASN B 399 127.21 -30.67
REMARK 500 1 ILE B 420 -46.09 48.79
REMARK 500 1 ALA B 447 -78.00 -72.58
REMARK 500 1 ILE B 448 103.90 -0.39
REMARK 500 1 SER B 451 -177.36 -176.57
REMARK 500 2 ALA B 370 -74.26 -68.54
REMARK 500 2 LEU B 374 -72.79 -64.69
REMARK 500 2 ILE B 378 -121.05 -141.99
REMARK 500 2 ALA B 381 34.56 155.28
REMARK 500 2 SER B 382 16.95 -151.98
REMARK 500 2 ARG B 384 41.28 36.79
REMARK 500 2 LYS B 391 55.97 80.82
REMARK 500 2 LYS B 392 131.33 -33.88
REMARK 500 2 PRO B 393 174.42 -53.74
REMARK 500 2 ASP B 397 63.19 179.18
REMARK 500 2 ASN B 399 116.60 7.71
REMARK 500 2 ILE B 420 -41.88 98.14
REMARK 500 2 ILE B 448 133.03 -39.01
REMARK 500 2 PRO B 449 -164.44 -50.06
REMARK 500 3 SER B 365 56.93 36.67
REMARK 500 3 ALA B 370 -75.28 -62.33
REMARK 500 3 LEU B 374 -71.09 -67.66
REMARK 500 3 ILE B 378 33.58 -142.07
REMARK 500 3 SER B 382 44.94 90.42
REMARK 500 3 ARG B 384 -8.95 81.78
REMARK 500 3 LYS B 391 62.60 85.99
REMARK 500 3 LYS B 392 125.92 -29.47
REMARK 500 3 ASP B 397 54.63 163.82
REMARK 500 3 ASN B 399 148.41 -30.99
REMARK 500 3 ARG B 405 -156.68 -145.59
REMARK 500 3 THR B 414 155.30 176.09
REMARK 500 3 ILE B 420 -45.93 48.33
REMARK 500 3 ALA B 447 57.11 -117.06
REMARK 500 3 PRO B 449 -146.55 -59.51
REMARK 500 3 ARG B 450 -169.95 -54.76
REMARK 500 4 ALA B 370 -78.83 -61.35
REMARK 500 4 ILE B 378 -151.42 -126.91
REMARK 500 4 ALA B 381 71.36 160.15
REMARK 500
REMARK 500 THIS ENTRY HAS 247 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1T4L B 366 453 UNP Q02555 RNT1_YEAST 366 453
DBREF 1T4L A 1 32 PDB 1T4L 1T4L 1 32
SEQADV 1T4L GLY B 364 UNP Q02555 CLONING ARTIFACT
SEQADV 1T4L SER B 365 UNP Q02555 CLONING ARTIFACT
SEQRES 1 A 32 G G G A U A C C A U G U U
SEQRES 2 A 32 C A G A A G A A C G U G G
SEQRES 3 A 32 U A U C U C
SEQRES 1 B 90 GLY SER LEU ASP MET ASN ALA LYS ARG GLN LEU TYR SER
SEQRES 2 B 90 LEU ILE GLY TYR ALA SER LEU ARG LEU HIS TYR VAL THR
SEQRES 3 B 90 VAL LYS LYS PRO THR ALA VAL ASP PRO ASN SER ILE VAL
SEQRES 4 B 90 GLU CYS ARG VAL GLY ASP GLY THR VAL LEU GLY THR GLY
SEQRES 5 B 90 VAL GLY ARG ASN ILE LYS ILE ALA GLY ILE ARG ALA ALA
SEQRES 6 B 90 GLU ASN ALA LEU ARG ASP LYS LYS MET LEU ASP PHE TYR
SEQRES 7 B 90 ALA LYS GLN ARG ALA ALA ILE PRO ARG SER GLU SER
HELIX 1 1 LEU B 366 ILE B 378 1 13
HELIX 2 2 ILE B 420 LEU B 432 1 13
HELIX 3 3 ASP B 434 ILE B 448 1 15
SHEET 1 A 3 HIS B 386 VAL B 390 0
SHEET 2 A 3 SER B 400 VAL B 406 -1 O ARG B 405 N HIS B 386
SHEET 3 A 3 THR B 410 GLY B 417 -1 O GLY B 415 N VAL B 402
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes