Header list of 1wcn.pdb file
Complete list - r 25 2 Bytes
HEADER RNA-BINDING PROTEIN 18-NOV-04 1WCN
TITLE NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS OF ESCHERICHIA
TITLE 2 COLI NUSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION ELONGATION PROTEIN NUSA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ACIDIC REPEAT 2, RESIDUES 426-495;
COMPND 5 SYNONYM: N UTILIZATION SUBSTANCE PROTEIN A, L FACTOR NUSA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PTKK19
KEYWDS RNA-BINDING PROTEIN, ESCHERICHIA COLI NUSA, TRANSCRIPTION
KEYWDS 2 REGULATION, REGULATION OF RNA BINDING, TRANSCRIPTION
KEYWDS 3 ANTITERMINATION AND TERMINATION, C-TERMINAL REPEAT UNITS,
KEYWDS 4 DIRECT PROTEIN SEQUENCING, RNA-BINDING,
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR A.EISENMANN,S.SCHWARZ,K.SCHWEIMER,P.ROESCH
REVDAT 2 24-FEB-09 1WCN 1 VERSN
REVDAT 1 31-AUG-05 1WCN 0
JRNL AUTH A.EISENMANN,S.SCHWARZ,S.PRASCH,K.SCHWEIMER,P.ROESCH
JRNL TITL THE E. COLI NUSA CARBOXY-TERMINAL DOMAINS ARE
JRNL TITL 2 STRUCTURALLY SIMILAR AND SHOW SPECIFIC RNAP- AND
JRNL TITL 3 LAMBDAN INTERACTIONS
JRNL REF PROTEIN SCI. V. 14 2018 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 15987884
JRNL DOI 10.1110/PS.051372205
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 1.2.1
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JOURNAL CITATION ABOVE
REMARK 4
REMARK 4 1WCN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-04.
REMARK 100 THE PDBE ID CODE IS EBI-21715.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 50MM
REMARK 210 PRESSURE : 1.0
REMARK 210 SAMPLE CONTENTS : 90% WATER / 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE PUBLICATION
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW
REMARK 210 METHOD USED : MANUAL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 90
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 NMR SPECTROSCOPY ON 13C, 15N LABELED GP-NUSA(339-495)
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 400
REMARK 400 COMPOUND
REMARK 400 FUNCTION: PARTICIPATES IN BOTH THE TERMINATION AND ANTITERMINATION
REMARK 400 OF TRANSCRIPTION. NUSA BINDS DIRECTLY TO THE CORE ENZYME OF THE
REMARK 400 DNA-DEPENDENT RNA POLYMERASE. NUSA ALSO INTERACTS WITH LAMBDA N
REMARK 400 PROTEIN, RNA, RHO FACTOR, AND PERHAPS NUSB. BINDS RNA.
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 ARG A 486 - H TRP A 490 1.50
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 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 LYS A 429 125.72 66.56
REMARK 500 1 TRP A 490 -85.93 -94.01
REMARK 500 2 TRP A 490 -85.98 -102.96
REMARK 500 3 ALA A 468 -34.61 -164.18
REMARK 500 3 TRP A 490 -87.02 -101.95
REMARK 500 4 TRP A 490 -93.00 -108.67
REMARK 500 5 TRP A 490 -83.51 -96.70
REMARK 500 6 TRP A 490 -83.05 -101.69
REMARK 500 7 LYS A 429 131.40 73.03
REMARK 500 7 TRP A 490 -85.70 -99.75
REMARK 500 8 TRP A 490 -80.73 -112.32
REMARK 500 9 TRP A 490 -84.94 -95.22
REMARK 500 10 TRP A 490 -85.25 -97.74
REMARK 500 11 TRP A 490 -85.10 -92.70
REMARK 500 12 TRP A 490 -90.38 -103.11
REMARK 500 13 TRP A 490 -83.22 -96.17
REMARK 500 14 TRP A 490 -83.88 -94.99
REMARK 500 15 TRP A 490 -81.45 -93.60
REMARK 500 16 TRP A 490 -84.80 -93.24
REMARK 500 17 ALA A 480 -37.08 -39.71
REMARK 500 17 TRP A 490 -84.13 -93.89
REMARK 500 18 TRP A 490 -83.43 -97.91
REMARK 500 19 TRP A 490 -83.93 -102.78
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 1 ARG A 442 0.31 SIDE CHAIN
REMARK 500 1 ARG A 451 0.30 SIDE CHAIN
REMARK 500 1 ARG A 486 0.24 SIDE CHAIN
REMARK 500 2 ARG A 442 0.22 SIDE CHAIN
REMARK 500 2 ARG A 451 0.31 SIDE CHAIN
REMARK 500 2 ARG A 486 0.11 SIDE CHAIN
REMARK 500 3 ARG A 442 0.32 SIDE CHAIN
REMARK 500 3 ARG A 451 0.26 SIDE CHAIN
REMARK 500 3 ARG A 486 0.24 SIDE CHAIN
REMARK 500 4 ARG A 442 0.30 SIDE CHAIN
REMARK 500 4 ARG A 486 0.30 SIDE CHAIN
REMARK 500 5 ARG A 442 0.30 SIDE CHAIN
REMARK 500 5 ARG A 451 0.29 SIDE CHAIN
REMARK 500 5 ARG A 486 0.30 SIDE CHAIN
REMARK 500 6 ARG A 442 0.32 SIDE CHAIN
REMARK 500 6 ARG A 451 0.31 SIDE CHAIN
REMARK 500 6 ARG A 486 0.29 SIDE CHAIN
REMARK 500 7 ARG A 442 0.30 SIDE CHAIN
REMARK 500 7 ARG A 451 0.09 SIDE CHAIN
REMARK 500 7 ARG A 486 0.27 SIDE CHAIN
REMARK 500 8 ARG A 442 0.09 SIDE CHAIN
REMARK 500 8 ARG A 451 0.32 SIDE CHAIN
REMARK 500 8 ARG A 486 0.26 SIDE CHAIN
REMARK 500 9 ARG A 442 0.18 SIDE CHAIN
REMARK 500 9 ARG A 451 0.20 SIDE CHAIN
REMARK 500 10 ARG A 442 0.25 SIDE CHAIN
REMARK 500 10 ARG A 451 0.30 SIDE CHAIN
REMARK 500 10 ARG A 486 0.13 SIDE CHAIN
REMARK 500 11 ARG A 442 0.10 SIDE CHAIN
REMARK 500 11 ARG A 451 0.12 SIDE CHAIN
REMARK 500 11 ARG A 486 0.15 SIDE CHAIN
REMARK 500 12 ARG A 442 0.28 SIDE CHAIN
REMARK 500 12 ARG A 451 0.19 SIDE CHAIN
REMARK 500 12 ARG A 486 0.27 SIDE CHAIN
REMARK 500 13 ARG A 442 0.30 SIDE CHAIN
REMARK 500 13 ARG A 451 0.27 SIDE CHAIN
REMARK 500 13 ARG A 486 0.09 SIDE CHAIN
REMARK 500 14 ARG A 442 0.31 SIDE CHAIN
REMARK 500 14 ARG A 451 0.18 SIDE CHAIN
REMARK 500 14 ARG A 486 0.09 SIDE CHAIN
REMARK 500 15 ARG A 442 0.23 SIDE CHAIN
REMARK 500 15 ARG A 451 0.31 SIDE CHAIN
REMARK 500 15 ARG A 486 0.31 SIDE CHAIN
REMARK 500 16 ARG A 442 0.31 SIDE CHAIN
REMARK 500 16 ARG A 451 0.31 SIDE CHAIN
REMARK 500 16 ARG A 486 0.20 SIDE CHAIN
REMARK 500 17 ARG A 442 0.32 SIDE CHAIN
REMARK 500 17 ARG A 451 0.29 SIDE CHAIN
REMARK 500 17 ARG A 486 0.31 SIDE CHAIN
REMARK 500 18 ARG A 442 0.32 SIDE CHAIN
REMARK 500 18 ARG A 451 0.30 SIDE CHAIN
REMARK 500 18 ARG A 486 0.29 SIDE CHAIN
REMARK 500 19 ARG A 451 0.32 SIDE CHAIN
REMARK 500 19 ARG A 486 0.23 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U9L RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR A NUSA- PROTEIN N
REMARK 900 INTERACTION
REMARK 900 RELATED ID: 1WCL RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS
REMARK 900 OF ESCHERICHIA COLI NUSA
DBREF 1WCN A 426 495 UNP P03003 NUSA_ECOLI 426 495
SEQRES 1 A 70 GLY ASP ASN LYS PRO ALA ASP ASP LEU LEU ASN LEU GLU
SEQRES 2 A 70 GLY VAL ASP ARG ASP LEU ALA PHE LYS LEU ALA ALA ARG
SEQRES 3 A 70 GLY VAL CYS THR LEU GLU ASP LEU ALA GLU GLN GLY ILE
SEQRES 4 A 70 ASP ASP LEU ALA ASP ILE GLU GLY LEU THR ASP GLU LYS
SEQRES 5 A 70 ALA GLY ALA LEU ILE MET ALA ALA ARG ASN ILE CYS TRP
SEQRES 6 A 70 PHE GLY ASP GLU ALA
HELIX 1 1 ASP A 432 LEU A 435 1 4
HELIX 2 2 ARG A 442 ALA A 449 1 8
HELIX 3 3 LEU A 456 ALA A 460 1 5
HELIX 4 4 ILE A 464 ALA A 468 1 5
HELIX 5 5 ASP A 475 CYS A 489 1 15
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 25 2 Bytes