Header list of 1ntc.pdb file
Complete list - v 3 2 Bytes
HEADER TRANSCRIPTION REGULATION 26-MAY-99 1NTC
TITLE SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF NTRC WITH THREE
TITLE 2 ALANINE SUBSTITUTIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (NITROGEN REGULATION PROTEIN (NTRC));
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: PLYS-S;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PJES1092
KEYWDS HELIX-TURN-HELIX, FIS, FOUR-HELIX BUNDLE, TRANSCRIPTION REGULATION
EXPDTA SOLUTION NMR
NUMMDL 28
AUTHOR J.G.PELTON,S.KUSTU,D.E.WEMMER
REVDAT 4 03-NOV-21 1NTC 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1NTC 1 VERSN
REVDAT 2 29-DEC-99 1NTC 1 JRNL COMPND REMARK DBREF
REVDAT 2 2 1 SEQADV HEADER
REVDAT 1 04-JUN-99 1NTC 0
JRNL AUTH J.G.PELTON,S.KUSTU,D.E.WEMMER
JRNL TITL SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF NTRC WITH
JRNL TITL 2 THREE ALANINE SUBSTITUTIONS.
JRNL REF J.MOL.BIOL. V. 292 1095 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10512705
JRNL DOI 10.1006/JMBI.1999.3140
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 JOURNAL CITATION ABOVE
REMARK 4
REMARK 4 1NTC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000001114.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 307
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : 0.07
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 28
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 LOW ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON THE 13C,15N-LABELED C-TERMINAL FRAGMENT OF NTRC
REMARK 210 (WITH 3 ALA SUBSTITUTIONS)
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 THR B 458 H LYS B 462 1.59
REMARK 500 O THR A 458 H LYS A 462 1.59
REMARK 500 O ALA B 457 H ALA B 461 1.59
REMARK 500 O ALA A 457 H ALA A 461 1.60
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 SER A 416 -80.81 -129.01
REMARK 500 1 GLN A 419 -77.69 -160.31
REMARK 500 1 ASN A 420 55.69 -90.01
REMARK 500 1 LEU A 421 -80.71 -58.91
REMARK 500 1 TRP A 454 -167.07 -103.35
REMARK 500 1 SER B 416 -80.92 -129.30
REMARK 500 1 GLN B 419 -77.66 -160.45
REMARK 500 1 LEU B 421 -81.28 -58.43
REMARK 500 1 TRP B 454 -167.20 -103.61
REMARK 500 2 ASP A 380 147.64 -175.09
REMARK 500 2 LEU A 381 90.87 53.38
REMARK 500 2 PHE A 386 -68.67 -131.48
REMARK 500 2 PRO A 391 -169.86 -73.53
REMARK 500 2 SER A 393 85.30 52.80
REMARK 500 2 SER A 395 144.28 -171.44
REMARK 500 2 ARG A 415 49.75 -86.56
REMARK 500 2 SER A 416 -66.65 -166.03
REMARK 500 2 GLN A 419 -75.30 -167.12
REMARK 500 2 ASN A 420 51.29 -90.17
REMARK 500 2 LEU A 421 -77.07 -52.93
REMARK 500 2 TRP A 454 -77.68 -112.97
REMARK 500 2 ASP B 380 147.57 -175.26
REMARK 500 2 LEU B 381 90.91 53.35
REMARK 500 2 PHE B 386 -68.61 -131.52
REMARK 500 2 PRO B 391 -169.95 -73.43
REMARK 500 2 SER B 393 85.35 52.78
REMARK 500 2 SER B 395 144.27 -171.49
REMARK 500 2 ARG B 415 49.60 -86.64
REMARK 500 2 SER B 416 -66.70 -166.03
REMARK 500 2 GLN B 419 -75.47 -167.03
REMARK 500 2 ASN B 420 51.32 -90.08
REMARK 500 2 LEU B 421 -76.92 -52.94
REMARK 500 2 TRP B 454 -77.69 -112.99
REMARK 500 3 GLU A 384 59.86 -115.77
REMARK 500 3 PHE A 386 86.27 53.05
REMARK 500 3 ALA A 388 -171.39 -173.75
REMARK 500 3 THR A 390 53.66 -158.37
REMARK 500 3 HIS A 396 -158.28 -146.10
REMARK 500 3 LEU A 397 91.43 53.37
REMARK 500 3 SER A 416 -63.37 -171.79
REMARK 500 3 GLN A 419 -76.50 -171.12
REMARK 500 3 GLN A 442 117.80 -37.79
REMARK 500 3 ALA A 449 -71.87 -52.83
REMARK 500 3 TRP A 454 -77.25 -106.76
REMARK 500 3 GLU B 384 59.91 -115.76
REMARK 500 3 PHE B 386 86.32 53.06
REMARK 500 3 ALA B 388 -171.40 -173.60
REMARK 500 3 THR B 390 53.66 -158.35
REMARK 500 3 HIS B 396 -158.51 -146.28
REMARK 500 3 LEU B 397 91.36 53.50
REMARK 500
REMARK 500 THIS ENTRY HAS 549 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 412 0.22 SIDE CHAIN
REMARK 500 1 ARG A 415 0.29 SIDE CHAIN
REMARK 500 1 ARG A 431 0.19 SIDE CHAIN
REMARK 500 1 ARG A 439 0.25 SIDE CHAIN
REMARK 500 1 ARG A 450 0.29 SIDE CHAIN
REMARK 500 1 ARG B 412 0.22 SIDE CHAIN
REMARK 500 1 ARG B 415 0.29 SIDE CHAIN
REMARK 500 1 ARG B 431 0.19 SIDE CHAIN
REMARK 500 1 ARG B 439 0.25 SIDE CHAIN
REMARK 500 1 ARG B 450 0.29 SIDE CHAIN
REMARK 500 2 ARG A 412 0.32 SIDE CHAIN
REMARK 500 2 ARG A 415 0.25 SIDE CHAIN
REMARK 500 2 ARG A 431 0.23 SIDE CHAIN
REMARK 500 2 ARG A 439 0.31 SIDE CHAIN
REMARK 500 2 ARG A 450 0.23 SIDE CHAIN
REMARK 500 2 ARG B 412 0.32 SIDE CHAIN
REMARK 500 2 ARG B 415 0.25 SIDE CHAIN
REMARK 500 2 ARG B 431 0.23 SIDE CHAIN
REMARK 500 2 ARG B 439 0.31 SIDE CHAIN
REMARK 500 2 ARG B 450 0.23 SIDE CHAIN
REMARK 500 3 ARG A 412 0.29 SIDE CHAIN
REMARK 500 3 ARG A 415 0.32 SIDE CHAIN
REMARK 500 3 ARG A 431 0.25 SIDE CHAIN
REMARK 500 3 ARG A 439 0.27 SIDE CHAIN
REMARK 500 3 ARG A 450 0.29 SIDE CHAIN
REMARK 500 3 ARG B 412 0.29 SIDE CHAIN
REMARK 500 3 ARG B 415 0.32 SIDE CHAIN
REMARK 500 3 ARG B 431 0.25 SIDE CHAIN
REMARK 500 3 ARG B 439 0.27 SIDE CHAIN
REMARK 500 3 ARG B 450 0.29 SIDE CHAIN
REMARK 500 4 ARG A 412 0.31 SIDE CHAIN
REMARK 500 4 ARG A 415 0.15 SIDE CHAIN
REMARK 500 4 ARG A 431 0.28 SIDE CHAIN
REMARK 500 4 ARG A 439 0.23 SIDE CHAIN
REMARK 500 4 ARG A 450 0.22 SIDE CHAIN
REMARK 500 4 ARG B 412 0.31 SIDE CHAIN
REMARK 500 4 ARG B 415 0.15 SIDE CHAIN
REMARK 500 4 ARG B 431 0.28 SIDE CHAIN
REMARK 500 4 ARG B 439 0.23 SIDE CHAIN
REMARK 500 4 ARG B 450 0.22 SIDE CHAIN
REMARK 500 5 ARG A 412 0.27 SIDE CHAIN
REMARK 500 5 ARG A 415 0.25 SIDE CHAIN
REMARK 500 5 ARG A 431 0.19 SIDE CHAIN
REMARK 500 5 ARG A 439 0.23 SIDE CHAIN
REMARK 500 5 ARG A 450 0.32 SIDE CHAIN
REMARK 500 5 ARG B 412 0.27 SIDE CHAIN
REMARK 500 5 ARG B 415 0.25 SIDE CHAIN
REMARK 500 5 ARG B 431 0.19 SIDE CHAIN
REMARK 500 5 ARG B 439 0.23 SIDE CHAIN
REMARK 500 5 ARG B 450 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 280 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NTC A 379 469 UNP P41789 NTRC_SALTY 379 469
DBREF 1NTC B 379 469 UNP P41789 NTRC_SALTY 379 469
SEQADV 1NTC MET A 379 UNP P41789 GLN 379 CLONING ARTIFACT
SEQADV 1NTC MET B 379 UNP P41789 GLN 379 CLONING ARTIFACT
SEQADV 1NTC ALA A 456 UNP P41789 ARG 456 ENGINEERED MUTATION
SEQADV 1NTC ALA B 456 UNP P41789 ARG 456 ENGINEERED MUTATION
SEQADV 1NTC ALA A 457 UNP P41789 ASN 457 ENGINEERED MUTATION
SEQADV 1NTC ALA B 457 UNP P41789 ASN 457 ENGINEERED MUTATION
SEQADV 1NTC ALA A 461 UNP P41789 ARG 461 ENGINEERED MUTATION
SEQADV 1NTC ALA B 461 UNP P41789 ARG 461 ENGINEERED MUTATION
SEQRES 1 A 91 MET ASP LEU PRO GLY GLU LEU PHE GLU ALA SER THR PRO
SEQRES 2 A 91 ASP SER PRO SER HIS LEU PRO PRO ASP SER TRP ALA THR
SEQRES 3 A 91 LEU LEU ALA GLN TRP ALA ASP ARG ALA LEU ARG SER GLY
SEQRES 4 A 91 HIS GLN ASN LEU LEU SER GLU ALA GLN PRO GLU LEU GLU
SEQRES 5 A 91 ARG THR LEU LEU THR THR ALA LEU ARG HIS THR GLN GLY
SEQRES 6 A 91 HIS LYS GLN GLU ALA ALA ARG LEU LEU GLY TRP GLY ALA
SEQRES 7 A 91 ALA THR LEU THR ALA LYS LEU LYS GLU LEU GLY MET GLU
SEQRES 1 B 91 MET ASP LEU PRO GLY GLU LEU PHE GLU ALA SER THR PRO
SEQRES 2 B 91 ASP SER PRO SER HIS LEU PRO PRO ASP SER TRP ALA THR
SEQRES 3 B 91 LEU LEU ALA GLN TRP ALA ASP ARG ALA LEU ARG SER GLY
SEQRES 4 B 91 HIS GLN ASN LEU LEU SER GLU ALA GLN PRO GLU LEU GLU
SEQRES 5 B 91 ARG THR LEU LEU THR THR ALA LEU ARG HIS THR GLN GLY
SEQRES 6 B 91 HIS LYS GLN GLU ALA ALA ARG LEU LEU GLY TRP GLY ALA
SEQRES 7 B 91 ALA THR LEU THR ALA LYS LEU LYS GLU LEU GLY MET GLU
HELIX 1 1 TRP A 402 LEU A 414 1 13
HELIX 2 2 LEU A 421 THR A 441 1 21
HELIX 3 3 GLU A 447 LEU A 452 1 6
HELIX 4 4 ALA A 456 GLY A 467 1 12
HELIX 5 5 TRP B 402 LEU B 414 1 13
HELIX 6 6 LEU B 421 THR B 441 1 21
HELIX 7 7 GLU B 447 LEU B 452 1 6
HELIX 8 8 ALA B 456 GLY B 467 1 12
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 - v 3 2 Bytes