Header list of 1qfq.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION/RNA 12-APR-99 1QFQ
TITLE BACTERIOPHAGE LAMBDA N-PROTEIN-NUTBOXB-RNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 15-MER NUTRBOXB RNA HAIRPIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BACTERIOPHAGE LAMBDA NUT BOXB-RNA;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: NUTBOXB FROM THE NUTR-SEQUENCE;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 36-MER N-TERMINAL PEPTIDE OF THE N PROTEIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: N-TERMINAL BINDING-DOMAIN, RESIDUES 2-36;
COMPND 11 SYNONYM: N36;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SEQUENCE FROM BACTERIOPHAGE LAMBDA. RNA WAS UNIFORMLY
SOURCE 4 LABELLED WITH (13)C AND (15)N;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE LAMBDA;
SOURCE 7 ORGANISM_TAXID: 10710;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BACTERIOPHAGE LAMBDA; ANTITERMINATION; PEPTIDE-RNA-COMPLEX; N-NUT;
KEYWDS 2 GNRA TETRALOOP; BENT-ALPHA-HELIX; PEPTIDE-RNA-RECOGNITION,
KEYWDS 3 TRANSCRIPTION-RNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 29
AUTHOR M.SCHAERPF,H.STICHT,P.ROESCH
REVDAT 4 02-MAR-22 1QFQ 1 REMARK
REVDAT 3 24-FEB-09 1QFQ 1 VERSN
REVDAT 2 04-JAN-05 1QFQ 1 HEADER COMPND SOURCE JRNL
REVDAT 2 2 1 KEYWDS REMARK
REVDAT 1 20-APR-99 1QFQ 0
JRNL AUTH M.SCHAERPF,H.STICHT,K.SCHWEIMER,M.BOEHM,S.HOFFMANN,P.ROESCH
JRNL TITL ANTITERMINATION IN BACTERIOPHAGE LAMBDA. THE STRUCTURE OF
JRNL TITL 2 THE N36 PEPTIDE-BOXB RNA COMPLEX
JRNL REF EUR.J.BIOCHEM. V. 267 2397 2000
JRNL REFN ISSN 0014-2956
JRNL PMID 10759866
JRNL DOI 10.1046/J.1432-1327.2000.01251.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1QFQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000841.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0 MM
REMARK 210 PRESSURE : 1.0 ATM
REMARK 210 SAMPLE CONTENTS : 10% H2O/90% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : (1)H-(31)P-COSY; (1)H-(13)C-CT-
REMARK 210 HSQC; (1)H-(15)N-HSQC; (1)H-(1)H-
REMARK 210 COSY; (1)H-(1)H-TOCSY; (1)H-(1)H-
REMARK 210 NOESY WITH 75 AND 150 MS MIXING
REMARK 210 TIME; '(13)C-ED.-NOESY; (1)H-(15)
REMARK 210 N-(1)H-NOESY-HSQC; (1)H-(15)N-(1)
REMARK 210 H-TOCSY-HSQC; HNHA; (13)C-NOESY-
REMARK 210 HSQC; HCCH-TOCSY; HCCH-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE, XNDEE, X-PLOR
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 29
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY, AGREEMENT WITH
REMARK 210 EXPERIMENTAL DATA
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 GLN B 15 H LYS B 19 1.50
REMARK 500 O ARG B 11 H GLN B 15 1.51
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 ASN B 22 49.83 -153.46
REMARK 500 1 ARG B 35 70.69 -153.10
REMARK 500 2 ASN B 22 50.63 -155.23
REMARK 500 2 LEU B 25 33.82 -99.71
REMARK 500 2 SER B 29 -172.29 52.01
REMARK 500 3 ALA B 3 -41.38 -164.92
REMARK 500 3 ASN B 22 51.58 -154.37
REMARK 500 3 ASN B 34 54.60 -113.65
REMARK 500 4 ALA B 3 -39.75 -148.33
REMARK 500 4 ASN B 22 50.72 -154.96
REMARK 500 4 VAL B 28 172.87 -49.56
REMARK 500 4 SER B 29 79.79 -55.44
REMARK 500 4 ALA B 30 42.00 -175.40
REMARK 500 4 ARG B 35 54.63 -152.44
REMARK 500 5 ALA B 3 -39.64 -161.70
REMARK 500 5 ASN B 22 50.29 -155.08
REMARK 500 5 LEU B 25 35.12 -97.22
REMARK 500 5 LYS B 31 94.34 -162.83
REMARK 500 6 ALA B 3 -39.54 -145.59
REMARK 500 6 ASN B 22 51.91 -154.28
REMARK 500 6 LEU B 25 31.73 -99.39
REMARK 500 6 SER B 29 -167.84 52.06
REMARK 500 6 ALA B 30 78.31 51.44
REMARK 500 6 ARG B 35 108.45 -51.08
REMARK 500 7 ASN B 22 52.42 -155.40
REMARK 500 7 VAL B 28 170.35 -49.88
REMARK 500 7 SER B 29 42.83 -84.03
REMARK 500 7 ALA B 30 50.17 26.12
REMARK 500 7 PRO B 32 -168.32 -75.51
REMARK 500 8 ASN B 22 52.40 -155.35
REMARK 500 8 VAL B 28 171.19 -49.68
REMARK 500 8 SER B 29 49.49 -74.13
REMARK 500 8 ALA B 30 65.52 28.89
REMARK 500 8 VAL B 33 -93.24 -142.33
REMARK 500 9 ASN B 22 52.40 -154.10
REMARK 500 9 VAL B 28 171.51 50.93
REMARK 500 9 ASN B 34 178.63 55.71
REMARK 500 9 ARG B 35 -173.84 47.82
REMARK 500 10 ASN B 22 51.31 -155.08
REMARK 500 10 VAL B 28 -154.25 36.00
REMARK 500 10 SER B 29 46.37 -92.71
REMARK 500 11 ALA B 3 -40.00 -135.52
REMARK 500 11 ASN B 22 50.00 -155.14
REMARK 500 11 SER B 29 -161.36 51.97
REMARK 500 11 LYS B 31 77.08 -159.04
REMARK 500 11 ASN B 34 80.42 -67.41
REMARK 500 12 ASN B 22 52.76 -156.23
REMARK 500 12 LEU B 25 35.22 -96.93
REMARK 500 12 VAL B 28 157.36 -35.83
REMARK 500 12 ALA B 30 69.39 12.91
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QFQ B 2 36 UNP P03045 REGN_LAMBD 2 36
DBREF 1QFQ A 1 15 PDB 1QFQ 1QFQ 1 15
SEQRES 1 A 15 G C C C U G A A A A A G G
SEQRES 2 A 15 G C
SEQRES 1 B 35 ASP ALA GLN THR ARG ARG ARG GLU ARG ARG ALA GLU LYS
SEQRES 2 B 35 GLN ALA GLN TRP LYS ALA ALA ASN PRO LEU LEU VAL GLY
SEQRES 3 B 35 VAL SER ALA LYS PRO VAL ASN ARG PRO
HELIX 1 1 GLN B 4 ALA B 21 1 18
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