Header list of 1qtg.pdb file
Complete list - 21 20 Bytes
HEADER GENE REGULATION 27-JUN-99 1QTG
TITLE AVERAGED NMR MODEL OF SWITCH ARC, A DOUBLE MUTANT OF ARC REPRESSOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REPRESSOR ARC;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEDERBERGVIRUS P22;
SOURCE 3 ORGANISM_TAXID: 10754;
SOURCE 4 GENE: ARC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET800-SWITCH_ARC;
SOURCE 9 OTHER_DETAILS: MUTATED SYNTHETIC ARC GENE
KEYWDS BETA-SHEET, RIGHT-HANDED HELIX, STRUCTURAL CHANGE, GENE REGULATION
EXPDTA SOLUTION NMR
AUTHOR M.H.J.CORDES,N.P.WALSH,C.J.MCKNIGHT,R.T.SAUER
REVDAT 5 21-DEC-22 1QTG 1 COMPND SOURCE DBREF SEQADV
REVDAT 4 02-MAR-22 1QTG 1 REMARK
REVDAT 3 24-FEB-09 1QTG 1 VERSN
REVDAT 2 01-APR-03 1QTG 1 JRNL
REVDAT 1 12-JUL-99 1QTG 0
JRNL AUTH M.H.CORDES,N.P.WALSH,C.J.MCKNIGHT,R.T.SAUER
JRNL TITL EVOLUTION OF A PROTEIN FOLD IN VITRO.
JRNL REF SCIENCE V. 284 325 1999
JRNL REFN ISSN 0036-8075
JRNL PMID 10195898
JRNL DOI 10.1126/SCIENCE.284.5412.325
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 GENERATION OF THIS MODEL OF THE SWITCH ARC MUTANT INVOLVED A
REMARK 3 COMBINATION OF EXPERIMENTAL AND SIMU
REMARK 3 LATED DISTANCE RESTRAINTS. FOR RESIDUES 7-14, 81 NOE CROSSPEAKS
REMARK 3 WERE OBTAINED FROM A 50-MS 2D NOES
REMARK 3 Y SPECTRUM AND WERE TRANSLATED INTO STRONG (1.8-2.8 A), MEDIUM
REMARK 3 (1.8-3.3 A), MEDIUM-WEAK (1.8-3.8 A
REMARK 3 ) AND WEAK (1.8-4.3 A) DISTANCE RESTRAINTS.18 ADDITIONAL
REMARK 3 CROSSPEAKS WERE OBTAINED FROM A 150-MS 3D
REMARK 3 NOESY SPECTRUM AND WERE ASSIGNED LOOSER RESTRAINTS (1.8 TO 4.0 A
REMARK 3 OR 1.8 TO 6.0 A)BECAUSE OF THE L
REMARK 3 ONGER MIXING TIME USED IN THIS EXPERIMENT. TO SIMULATE THE
REMARK 3 STRUCTURE OF RESIDUES 14 TO 53 (RESIDUE
REMARK 3 14 WAS DESCRIBED BY BOTH ACTUAL AND COMPUTED RESTRAINTS), A LIST
REMARK 3 OF 1635 DISTANCES WAS GENERATED
REMARK 3 BETWEEN PAIRS OF HEAVY ATOMS WITHIN 4 A OF EACH OTHER IN THE WILD-
REMARK 3 TYPE ARC CRYSTAL STRUCTURE, AND
REMARK 3 THE INTERATOMIC DISTANCES WERE CONSTRAINED TO BE WITHIN + OR - 1.0
REMARK 3 A OF THIS VALUE. 28 INITIAL STR
REMARK 3 UCTURES WITH RANDOM CONFIGURATIONS FOR RESIDUES 1 TO 13 WERE
REMARK 3 GENERATED BY PERFORMING A SET OF CALC
REMARK 3 ULATIONS WITH ONLY THE SIMULATED RESTRAINTS FOR RESIDUES 14 TO 53.
REMARK 3 THEN, 28 MODEL STRUCTURES WERE
REMARK 3 GENERATED BY INCLUDING THE EXPERIMENTAL RESTRAINTS FOR RESIDUES 7
REMARK 3 TO 14. NO RESTRAINTS WERE USED F
REMARK 3 OR RESIDUES 1 TO 6, WHICH APPEAR TO BE DISORDERED. AMBIGUITIES IN
REMARK 3 INTRA- AND INTERMOLECULAR NOE AS
REMARK 3 SIGNMENT RESULTING FROM ARC'S TWOFOLD SYMMETRY WERE RESOLVED
REMARK 3 COMPUTATIONALLY AS DESCRIBED (M. NILG
REMARK 3 ES, PROTEIN STRUCT. FUNCT. GENET. 17, 297 (1993).19 OF 28
REMARK 3 STRUCTURES WERE ACCEPTED WITH NO NOE VIO
REMARK 3 LATIONS GREATER THAN 0.3 A. THE FIVE STRUCTURES WITH THE HIGHEST
REMARK 3 ENERGY, WHICH ALSO CONTAINED BACK
REMARK 3 BONE DIHEDRAL ANGLES IN DISALLOWED REGIONS OF RAMACHANDRAN SPACE,
REMARK 3 WERE DISCARDED. THE REMAINING 14
REMARK 3 STRUCTURES, WHICH HAD PAIRWISE RMSD'S OF 0.6 A (BACKBONE) AND 1.6
REMARK 3 A (HEAVY), WERE USED TO GENERAT
REMARK 3 E A MINIMIZED AVERAGE MODEL.
REMARK 4
REMARK 4 1QTG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000009246.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 HA MET B 1 HB3 SER B 5 1.26
REMARK 500 HA MET A 1 HB3 SER A 5 1.26
REMARK 500 HH11 ARG A 50 HG23 VAL B 25 1.26
REMARK 500 HG23 VAL A 25 HH11 ARG B 50 1.27
REMARK 500 H SER A 5 HZ1 LYS A 6 1.28
REMARK 500 HG3 MET B 1 H LYS B 2 1.28
REMARK 500 HG3 MET A 1 H LYS A 2 1.29
REMARK 500 O LEU B 11 H TRP B 14 1.39
REMARK 500 O LEU A 11 H TRP A 14 1.39
REMARK 500 O MET A 4 H LYS A 6 1.47
REMARK 500 O MET B 4 H LYS B 6 1.47
REMARK 500 O GLY A 3 H SER A 5 1.52
REMARK 500 O GLY B 3 H SER B 5 1.52
REMARK 500 N SER B 5 HZ2 LYS B 6 1.53
REMARK 500 O VAL B 18 H LEU B 21 1.59
REMARK 500 O VAL A 18 H LEU A 21 1.59
REMARK 500 O GLY A 3 N SER A 5 1.69
REMARK 500 O GLY B 3 N SER B 5 1.69
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 LYS A 2 -2.99 -46.53
REMARK 500 MET A 4 35.00 6.62
REMARK 500 SER A 5 60.33 -62.65
REMARK 500 LYS A 6 -87.60 -157.37
REMARK 500 MET A 7 89.47 -35.60
REMARK 500 GLN A 9 9.55 -68.84
REMARK 500 VAL A 18 -73.31 -74.17
REMARK 500 LEU A 19 -60.12 -24.48
REMARK 500 LYS B 2 -2.86 -46.69
REMARK 500 MET B 4 35.24 6.65
REMARK 500 SER B 5 60.33 -62.97
REMARK 500 LYS B 6 -87.64 -157.29
REMARK 500 MET B 7 89.44 -35.48
REMARK 500 GLN B 9 9.67 -69.05
REMARK 500 VAL B 18 -73.32 -74.21
REMARK 500 LEU B 19 -60.04 -24.47
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 ARG A 13 0.32 SIDE CHAIN
REMARK 500 ARG A 16 0.15 SIDE CHAIN
REMARK 500 ARG A 23 0.29 SIDE CHAIN
REMARK 500 ARG A 31 0.19 SIDE CHAIN
REMARK 500 ARG A 50 0.12 SIDE CHAIN
REMARK 500 ARG B 13 0.32 SIDE CHAIN
REMARK 500 ARG B 16 0.15 SIDE CHAIN
REMARK 500 ARG B 23 0.29 SIDE CHAIN
REMARK 500 ARG B 31 0.19 SIDE CHAIN
REMARK 500 ARG B 50 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ARR RELATED DB: PDB
REMARK 900 THE MINIMIZED AVERAGE SOLUTION STRUCTURE OF WILD-TYPE ARC REPRESSOR
REMARK 900 RELATED ID: 1PAR RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF WILD-TYPE ARC BOUND TO OPERATOR DNA
DBREF 1QTG A 1 53 UNP P03050 RARC_BPP22 1 53
DBREF 1QTG B 1 53 UNP P03050 RARC_BPP22 1 53
SEQADV 1QTG LEU A 11 UNP P03050 ASN 11 ENGINEERED MUTATION
SEQADV 1QTG ASN A 12 UNP P03050 LEU 12 ENGINEERED MUTATION
SEQADV 1QTG LEU B 11 UNP P03050 ASN 11 ENGINEERED MUTATION
SEQADV 1QTG ASN B 12 UNP P03050 LEU 12 ENGINEERED MUTATION
SEQRES 1 A 53 MET LYS GLY MET SER LYS MET PRO GLN PHE LEU ASN ARG
SEQRES 2 A 53 TRP PRO ARG GLU VAL LEU ASP LEU VAL ARG LYS VAL ALA
SEQRES 3 A 53 GLU GLU ASN GLY ARG SER VAL ASN SER GLU ILE TYR GLN
SEQRES 4 A 53 ARG VAL MET GLU SER PHE LYS LYS GLU GLY ARG ILE GLY
SEQRES 5 A 53 ALA
SEQRES 1 B 53 MET LYS GLY MET SER LYS MET PRO GLN PHE LEU ASN ARG
SEQRES 2 B 53 TRP PRO ARG GLU VAL LEU ASP LEU VAL ARG LYS VAL ALA
SEQRES 3 B 53 GLU GLU ASN GLY ARG SER VAL ASN SER GLU ILE TYR GLN
SEQRES 4 B 53 ARG VAL MET GLU SER PHE LYS LYS GLU GLY ARG ILE GLY
SEQRES 5 B 53 ALA
HELIX 1 1 PHE A 10 TRP A 14 5 5
HELIX 2 2 PRO A 15 GLY A 30 1 16
HELIX 3 3 SER A 32 GLY A 49 1 18
HELIX 4 4 PHE B 10 TRP B 14 5 5
HELIX 5 5 PRO B 15 GLY B 30 1 16
HELIX 6 6 SER B 32 GLY B 49 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
Complete list - 21 20 Bytes