Header list of 1wcl.pdb file
Complete list - r 19 2 Bytes
HEADER RNA-BINDING PROTEIN 17-NOV-04 1WCL
TITLE NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS OF ESCHERICHIA COLI NUSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION ELONGATION PROTEIN NUSA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ACIDIC REPEAT 1, RESIDUES 351-426;
COMPND 5 SYNONYM: N UTILIZATION SUBSTANCE PROTEIN A, L FACTOR;
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 REGULATION,
KEYWDS 2 REGULATION OF RNA BINDING, TRANSCRIPTION ANTITERMINATION AND
KEYWDS 3 TERMINATION, C-TERMINAL REPEAT UNITS
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR A.EISENMANN,S.SCHWARZ,K.SCHWEIMER,P.ROESCH
REVDAT 3 19-APR-17 1WCL 1 REMARK
REVDAT 2 24-FEB-09 1WCL 1 VERSN
REVDAT 1 31-AUG-05 1WCL 0
JRNL AUTH A.EISENMANN,S.SCHWARZ,S.PRASCH,K.SCHWEIMER,P.ROESCH
JRNL TITL THE E. COLI NUSA CARBOXY-TERMINAL DOMAINS ARE STRUCTURALLY
JRNL TITL 2 SIMILAR AND SHOW SPECIFIC RNAP- AND 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 : X-PLOR-NIH 1.2.1
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN JRNL
REMARK 3 CITATION ABOVE
REMARK 4
REMARK 4 1WCL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-NOV-04.
REMARK 100 THE PDBE ID CODE IS EBI-21617.
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 : 50
REMARK 210 PRESSURE : 1.0 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE PUBLICATION
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 700 MHZ; 800 MHZ; 600
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW5.0.4
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 : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 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 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400
REMARK 400 COMPOUND
REMARK 400 PARTICIPATES IN BOTH THE TERMINATION AND ANTITERMINATION
REMARK 400 OF TRANSCRIPTION. NUSA BINDS DIRECTLY TO THE CORE ENZYME
REMARK 400 OF THE DNA-DEPENDENT RNA POLYMERASE.
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 THR A 371 H GLU A 375 1.45
REMARK 500 O GLU A 382 H TYR A 386 1.48
REMARK 500 O ARG A 409 H ALA A 413 1.52
REMARK 500 O MET A 389 H LEU A 393 1.54
REMARK 500 O THR A 416 H GLN A 419 1.59
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 TYR A 362 -64.18 -101.82
REMARK 500 1 ILE A 395 -33.44 -34.48
REMARK 500 1 GLU A 396 -92.10 -177.53
REMARK 500 2 TYR A 362 -64.87 -95.03
REMARK 500 2 ILE A 365 -166.22 -120.78
REMARK 500 2 ILE A 395 -34.74 -33.06
REMARK 500 2 GLU A 396 -90.87 -178.74
REMARK 500 3 TYR A 362 -66.53 -102.99
REMARK 500 3 ILE A 365 -169.27 -121.93
REMARK 500 3 ILE A 395 -33.95 -34.18
REMARK 500 3 GLU A 396 -95.71 -176.21
REMARK 500 3 ALA A 410 -72.19 -44.61
REMARK 500 4 TYR A 362 -60.33 -101.31
REMARK 500 4 ILE A 395 -35.80 -32.61
REMARK 500 4 GLU A 396 -83.64 -176.52
REMARK 500 5 TYR A 362 -65.46 -100.98
REMARK 500 5 GLU A 396 -116.41 -162.01
REMARK 500 6 TYR A 362 -62.99 -104.81
REMARK 500 6 GLU A 396 -107.68 -169.74
REMARK 500 7 TYR A 362 -64.27 -101.69
REMARK 500 7 ILE A 395 -35.60 -32.78
REMARK 500 7 GLU A 396 -83.85 -176.33
REMARK 500 8 TYR A 362 -66.37 -100.50
REMARK 500 8 ILE A 395 -37.01 -33.09
REMARK 500 8 GLU A 396 -89.62 -174.72
REMARK 500 9 ILE A 365 -164.90 -125.96
REMARK 500 9 ILE A 395 -29.93 -38.65
REMARK 500 9 GLU A 396 -105.91 -170.71
REMARK 500 9 ALA A 410 -71.19 -42.33
REMARK 500 10 TYR A 362 -62.46 -102.68
REMARK 500 10 ILE A 365 -166.49 -123.53
REMARK 500 10 ILE A 395 -35.80 -32.62
REMARK 500 10 GLU A 396 -90.40 -174.14
REMARK 500 11 TYR A 362 -69.25 -99.28
REMARK 500 11 GLU A 396 -115.93 -165.46
REMARK 500 12 ILE A 365 -169.13 -125.41
REMARK 500 12 ILE A 395 -37.19 -32.43
REMARK 500 12 GLU A 396 -80.43 -172.23
REMARK 500 13 TYR A 362 -64.11 -102.63
REMARK 500 13 GLU A 396 -112.52 -163.32
REMARK 500 14 ILE A 395 -35.90 -32.12
REMARK 500 14 GLU A 396 -86.50 -173.85
REMARK 500 15 TYR A 362 -71.94 -100.31
REMARK 500 15 ILE A 365 -168.55 -122.53
REMARK 500 15 ILE A 395 -34.94 -33.19
REMARK 500 15 GLU A 396 -98.86 -175.76
REMARK 500 16 TYR A 362 -66.47 -100.21
REMARK 500 16 ILE A 365 -169.05 -126.23
REMARK 500 16 ILE A 395 -34.21 -33.59
REMARK 500 16 GLU A 396 -90.02 -175.49
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
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 407 0.19 SIDE CHAIN
REMARK 500 1 ARG A 409 0.16 SIDE CHAIN
REMARK 500 2 ARG A 407 0.24 SIDE CHAIN
REMARK 500 2 ARG A 409 0.21 SIDE CHAIN
REMARK 500 3 ARG A 407 0.32 SIDE CHAIN
REMARK 500 3 ARG A 409 0.32 SIDE CHAIN
REMARK 500 4 ARG A 407 0.21 SIDE CHAIN
REMARK 500 4 ARG A 409 0.14 SIDE CHAIN
REMARK 500 5 ARG A 407 0.15 SIDE CHAIN
REMARK 500 5 ARG A 409 0.10 SIDE CHAIN
REMARK 500 6 ARG A 407 0.17 SIDE CHAIN
REMARK 500 6 ARG A 409 0.30 SIDE CHAIN
REMARK 500 7 ARG A 407 0.15 SIDE CHAIN
REMARK 500 7 ARG A 409 0.16 SIDE CHAIN
REMARK 500 8 ARG A 407 0.31 SIDE CHAIN
REMARK 500 8 ARG A 409 0.29 SIDE CHAIN
REMARK 500 9 ARG A 407 0.26 SIDE CHAIN
REMARK 500 9 ARG A 409 0.24 SIDE CHAIN
REMARK 500 10 ARG A 407 0.20 SIDE CHAIN
REMARK 500 10 ARG A 409 0.25 SIDE CHAIN
REMARK 500 11 ARG A 407 0.28 SIDE CHAIN
REMARK 500 11 ARG A 409 0.30 SIDE CHAIN
REMARK 500 12 ARG A 407 0.15 SIDE CHAIN
REMARK 500 12 ARG A 409 0.23 SIDE CHAIN
REMARK 500 13 ARG A 407 0.29 SIDE CHAIN
REMARK 500 13 ARG A 409 0.19 SIDE CHAIN
REMARK 500 14 ARG A 407 0.30 SIDE CHAIN
REMARK 500 14 ARG A 409 0.18 SIDE CHAIN
REMARK 500 15 ARG A 407 0.28 SIDE CHAIN
REMARK 500 15 ARG A 409 0.32 SIDE CHAIN
REMARK 500 16 ARG A 407 0.23 SIDE CHAIN
REMARK 500 16 ARG A 409 0.21 SIDE CHAIN
REMARK 500 17 ARG A 407 0.14 SIDE CHAIN
REMARK 500 17 ARG A 409 0.29 SIDE CHAIN
REMARK 500 18 ARG A 407 0.11 SIDE CHAIN
REMARK 500 18 ARG A 409 0.27 SIDE CHAIN
REMARK 500 19 ARG A 407 0.31 SIDE CHAIN
REMARK 500 19 ARG A 409 0.08 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 INTERACTION
REMARK 900 RELATED ID: 1WCN RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS OF ESCHERICHIA COLI
REMARK 900 NUSA
DBREF 1WCL A 351 426 UNP P03003 NUSA_ECOLI 351 426
SEQRES 1 A 76 GLU ALA HIS ALA ALA ILE ASP THR PHE THR LYS TYR LEU
SEQRES 2 A 76 ASP ILE ASP GLU ASP PHE ALA THR VAL LEU VAL GLU GLU
SEQRES 3 A 76 GLY PHE SER THR LEU GLU GLU LEU ALA TYR VAL PRO MET
SEQRES 4 A 76 LYS GLU LEU LEU GLU ILE GLU GLY LEU ASP GLU PRO THR
SEQRES 5 A 76 VAL GLU ALA LEU ARG GLU ARG ALA LYS ASN ALA LEU ALA
SEQRES 6 A 76 THR ILE ALA GLN ALA GLN GLU GLU SER LEU GLY
HELIX 1 1 HIS A 353 TYR A 362 1 10
HELIX 2 2 GLU A 367 GLU A 376 1 10
HELIX 3 3 LEU A 381 TYR A 386 1 6
HELIX 4 4 MET A 389 GLU A 394 1 6
HELIX 5 5 GLU A 400 THR A 416 1 17
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 19 2 Bytes