Header list of 1nr3.pdb file
Complete list - g 9 2 Bytes
HEADER TRANSCRIPTION 23-JAN-03 1NR3
TITLE SOLUTION STRUCTURE OF THE PROTEIN MTH0916: THE NORTHEAST STRUCTURAL
TITLE 2 GENOMICS CONSORTIUM TARGET TT212
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-BINDING PROTEIN TFX;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MTH0916;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 145262;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, REDUCED-DIMENSIONALITY NMR,
KEYWDS 2 PSI, PROTEIN STRUCTURE INITIATIVE, NESG, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.SHEN,G.LIU,R.BHASKARAN,A.YEE,C.ARROWSMITH,T.SZYPERSKI,NORTHEAST
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 5 14-JUN-23 1NR3 1 REMARK
REVDAT 4 05-FEB-20 1NR3 1 REMARK ATOM
REVDAT 3 24-FEB-09 1NR3 1 VERSN
REVDAT 2 25-JAN-05 1NR3 1 AUTHOR KEYWDS REMARK
REVDAT 1 10-JUN-03 1NR3 0
JRNL AUTH Y.SHEN,G.LIU,R.BHASKARAN,A.YEE,C.ARROWSMITH,T.SZYPERSKI
JRNL TITL SOLUTION STRUCTURE OF THE PROTEIN MTH0916: THE NORTHEAST
JRNL TITL 2 STRUCTURAL GENOMICS CONSORTIUM TARGET TT212
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, CYANA 1.0.3
REMARK 3 AUTHORS : GUNTERT, P. (DYANA), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE CALCULATION WAS PERFORMED BY
REMARK 3 TORSION ANGLE DYNAMICS USING DYANA. CYANA WAS USED TO HELP IN
REMARK 3 THE IDENTIFICATION OF AMBIGUOUS NOE ASSIGNMENTS.
REMARK 4
REMARK 4 1NR3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000018133.
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 : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM TT212 U-15N, 13C, 450MM
REMARK 210 NACL, 10MM DTT, 20MM ZNCL2, 0.01%
REMARK 210 AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 3D
REMARK 210 HNCACB; 3D_RD_HCCHTOCSY; 3D_RD_
REMARK 210 HCCHCOSY; 3D_CACBCONH; 3D_RD_
REMARK 210 HNNCAHA; 3D_RD_HABCABCONHN; 2D_
REMARK 210 RD_H-TOCSY-RELAYED-HCH-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PROSA 6.0, XEASY 1.3.13
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING RD TECHNIQUES.
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 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 59 H ILE A 63 1.44
REMARK 500 O THR A 84 H LEU A 88 1.49
REMARK 500 O ARG A 56 H THR A 59 1.54
REMARK 500 OD1 ASN A 72 H VAL A 78 1.58
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 ARG A 2 -68.92 -169.05
REMARK 500 1 TRP A 6 59.77 -101.44
REMARK 500 1 SER A 7 45.41 -97.70
REMARK 500 1 GLN A 8 63.70 79.11
REMARK 500 1 LYS A 9 -75.40 -83.07
REMARK 500 1 LYS A 10 -92.37 -139.09
REMARK 500 1 ALA A 12 -37.38 -38.23
REMARK 500 1 ARG A 19 52.69 178.43
REMARK 500 1 VAL A 22 -139.04 -91.04
REMARK 500 1 ALA A 24 56.27 37.84
REMARK 500 1 GLU A 31 46.34 -79.55
REMARK 500 1 GLU A 34 -65.48 -163.32
REMARK 500 1 LYS A 35 77.40 179.67
REMARK 500 1 SER A 36 -69.87 -147.67
REMARK 500 1 ASN A 38 38.50 81.52
REMARK 500 1 THR A 39 -78.78 -74.85
REMARK 500 1 HIS A 77 99.31 -48.94
REMARK 500 1 ARG A 90 -35.33 -39.17
REMARK 500 1 ALA A 93 80.37 -171.92
REMARK 500 1 HIS A 95 -84.08 -87.56
REMARK 500 1 LYS A 103 -39.32 -178.09
REMARK 500 1 ARG A 112 -50.37 -148.43
REMARK 500 1 ASP A 113 -24.03 158.76
REMARK 500 1 ASN A 121 139.89 61.28
REMARK 500 2 ARG A 4 162.51 -43.08
REMARK 500 2 SER A 7 -75.55 -69.31
REMARK 500 2 GLN A 8 53.78 -156.84
REMARK 500 2 LYS A 9 -75.62 -68.84
REMARK 500 2 LYS A 10 -84.45 -155.45
REMARK 500 2 ARG A 19 61.66 175.41
REMARK 500 2 ASN A 21 27.18 47.47
REMARK 500 2 SER A 23 -79.51 177.41
REMARK 500 2 GLU A 31 46.70 -80.89
REMARK 500 2 GLU A 34 -60.30 -156.90
REMARK 500 2 LYS A 35 75.74 174.47
REMARK 500 2 SER A 36 -56.18 -142.40
REMARK 500 2 THR A 39 -84.02 -75.90
REMARK 500 2 LYS A 47 62.85 67.60
REMARK 500 2 ASN A 72 -33.25 -39.09
REMARK 500 2 HIS A 77 99.98 -40.45
REMARK 500 2 ARG A 90 -34.89 -38.53
REMARK 500 2 ALA A 93 80.68 -174.10
REMARK 500 2 HIS A 95 -84.91 -91.41
REMARK 500 2 LYS A 103 -42.23 -166.65
REMARK 500 2 ARG A 112 -52.30 -150.94
REMARK 500 2 ASP A 113 -26.72 163.64
REMARK 500 2 ASP A 119 122.25 -173.09
REMARK 500 2 ASN A 121 139.13 61.54
REMARK 500 3 ARG A 2 149.85 -176.41
REMARK 500 3 ARG A 4 -172.35 169.47
REMARK 500
REMARK 500 THIS ENTRY HAS 517 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5657 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGNMENT
REMARK 900 RELATED ID: TT212 RELATED DB: TARGETDB
DBREF 1NR3 A 1 122 UNP O27001 TFX_METTH 16 137
SEQRES 1 A 122 MET ARG GLU ARG GLY TRP SER GLN LYS LYS ILE ALA ARG
SEQRES 2 A 122 GLU LEU LYS THR THR ARG GLN ASN VAL SER ALA ILE GLU
SEQRES 3 A 122 ARG LYS ALA MET GLU ASN ILE GLU LYS SER ARG ASN THR
SEQRES 4 A 122 LEU ASP PHE VAL LYS SER LEU LYS SER PRO VAL ARG ILE
SEQRES 5 A 122 LEU CYS ARG ARG GLY ASP THR LEU ASP GLU ILE ILE LYS
SEQRES 6 A 122 ARG LEU LEU GLU GLU SER ASN LYS GLU GLY ILE HIS VAL
SEQRES 7 A 122 ILE HIS ASP SER ILE THR LEU ALA PHE LEU ILE ARG GLU
SEQRES 8 A 122 LYS ALA SER HIS ARG ILE VAL HIS ARG VAL VAL LYS SER
SEQRES 9 A 122 ASP PHE GLU ILE GLY VAL THR ARG ASP GLY GLU ILE ILE
SEQRES 10 A 122 VAL ASP LEU ASN SER
HELIX 1 1 ILE A 11 THR A 18 1 8
HELIX 2 2 ALA A 24 GLU A 31 1 8
HELIX 3 3 ASN A 38 LYS A 47 1 10
HELIX 4 4 ARG A 56 ASP A 58 5 3
HELIX 5 5 THR A 59 GLY A 75 1 17
HELIX 6 6 ASP A 81 ALA A 93 1 13
SHEET 1 A 3 VAL A 50 CYS A 54 0
SHEET 2 A 3 PHE A 106 VAL A 110 -1 O VAL A 110 N VAL A 50
SHEET 3 A 3 ILE A 116 ASP A 119 -1 O ILE A 117 N GLY A 109
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 - g 9 2 Bytes