Header list of 1l7b.pdb file
Complete list - b 23 2 Bytes
HEADER LIGASE 14-MAR-02 1L7B
TITLE SOLUTION NMR STRUCTURE OF BRCT DOMAIN OF T. THERMOPHILUS: NORTHEAST
TITLE 2 STRUCTURAL GENOMICS CONSORTIUM TARGET WR64TT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA LIGASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BRCT DOMAIN;
COMPND 5 EC: 6.5.1.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 GENE: DNLJ;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS BRCT, DNA LIGASE, AUTOSTRUCTURE, STRUCTURAL GENOMICS, NESG, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR G.SAHOTA,B.L.DIXON,Y.P.HUANG,J.ARAMINI,D.MONLEON,D.BHATTACHARYA,
AUTHOR 2 G.V.T.SWAPNA,C.YIN,R.XIAO,S.ANDERSON,R.TEJERO,G.T.MONTELIONE,
AUTHOR 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 23-FEB-22 1L7B 1 REMARK
REVDAT 3 24-FEB-09 1L7B 1 VERSN
REVDAT 2 25-JAN-05 1L7B 1 AUTHOR KEYWDS REMARK
REVDAT 1 16-SEP-03 1L7B 0
JRNL AUTH G.SAHOTA,B.L.DIXON,Y.P.HUANG,J.ARAMINI,A.BHATTACHARYA,
JRNL AUTH 2 D.MONLEON,G.V.T.SWAPNA,C.YIN,R.XIAO,S.ANDERSON,
JRNL AUTH 3 G.T.MONTELIONE,R.TEJERO
JRNL TITL SOLUTION NMR STRUCTURE OF THE BRCT DOMAIN FROM THERMUS
JRNL TITL 2 THERMOPHILUS DNA LIGASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, DYANA 1.5
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, WUTHRICH, ET AL. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: X-PLOR-NIH VERSION 1.1.2 (G.M. CLORE,J.
REMARK 3 KUSZEWSKY,C. SCHWIETERS,N. TJANDRA) WAS ALSO USED FOR REFINEMENT
REMARK 4
REMARK 4 1L7B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015705.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 300MM NH4OAC
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.3MM U-15N,13C; 300MM NH4OAC;
REMARK 210 95% H20, 10% D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D PFG-[15N]HSQC; 3D PFG- 3D PFG
REMARK 210 -(HA)CA(CO)NH; 3D PFG-HA(CA)(CO)
REMARK 210 NH; 3D PFG-HA(CA)NH; 3D PFG-
REMARK 210 CBCANH; 3D PFG-CBCA(CO)NH; 3D
REMARK 210 PFG-(HA)CANH; 3D PFG-H 3D PFG-
REMARK 210 HBHA(CB)(CA)(CO)NH; 3D PFG-
REMARK 210 HCC(CO)NH-TOCSY; 3D PFG-13C-
REMARK 210 EDITED NOESY; 3D PFG-15N-EDITED
REMARK 210 NOESY; 2D HSQC-J; N-H IPAP
REMARK 210 RESIDUAL DIPOLAR COUPLING
REMARK 210 MEASUREMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, NMRPIPE 97.231.15.18,
REMARK 210 AUTOASSIGN 1.7.6, AUTOSTRUCTURE
REMARK 210 1.0 BETA, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : SET OF ALL STRUCTURES WITHIN 5RT
REMARK 210 OF LOWEST ENERGY STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 LYS A 57 H ALA A 61 1.46
REMARK 500 O THR A 45 HG SER A 46 1.55
REMARK 500 O LEU A 78 H THR A 82 1.56
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 GLU A 6 26.22 -151.15
REMARK 500 1 ALA A 7 -85.44 -42.09
REMARK 500 1 GLU A 18 -0.95 -146.55
REMARK 500 1 LEU A 19 -14.77 67.53
REMARK 500 1 SER A 20 33.30 88.82
REMARK 500 1 PRO A 22 94.53 -65.13
REMARK 500 1 ASP A 39 28.52 -156.79
REMARK 500 1 SER A 42 -32.16 -139.36
REMARK 500 1 ARG A 43 -63.61 165.35
REMARK 500 1 THR A 45 -108.83 -81.74
REMARK 500 1 GLU A 52 -172.36 -65.99
REMARK 500 1 ALA A 63 116.42 41.74
REMARK 500 1 LEU A 64 31.66 -86.70
REMARK 500 1 ARG A 76 -76.29 -70.03
REMARK 500 1 LEU A 89 -125.50 -161.04
REMARK 500 1 VAL A 90 -82.00 63.77
REMARK 500 2 GLU A 6 -65.78 -175.32
REMARK 500 2 ALA A 7 -90.97 79.98
REMARK 500 2 LYS A 9 172.60 -47.04
REMARK 500 2 THR A 16 1.00 -56.56
REMARK 500 2 GLU A 18 28.47 176.84
REMARK 500 2 SER A 20 34.74 89.52
REMARK 500 2 PRO A 22 36.76 -70.95
REMARK 500 2 ARG A 23 -14.81 -43.07
REMARK 500 2 ASP A 39 -0.69 -146.63
REMARK 500 2 SER A 42 -31.65 -152.40
REMARK 500 2 ARG A 43 -70.99 -178.20
REMARK 500 2 SER A 46 65.10 -151.65
REMARK 500 2 VAL A 50 93.65 -64.22
REMARK 500 2 GLU A 52 -164.48 -67.51
REMARK 500 2 ALA A 63 149.83 63.14
REMARK 500 2 ARG A 76 -72.10 -67.65
REMARK 500 2 LEU A 78 -75.09 -58.79
REMARK 500 2 LYS A 85 99.85 -69.97
REMARK 500 2 GLU A 88 11.34 58.63
REMARK 500 3 GLU A 6 33.82 -141.27
REMARK 500 3 ALA A 7 -43.64 79.13
REMARK 500 3 LYS A 9 175.18 -46.18
REMARK 500 3 THR A 16 80.46 -68.81
REMARK 500 3 SER A 20 21.04 87.44
REMARK 500 3 PRO A 22 36.01 -69.24
REMARK 500 3 ARG A 23 -15.46 -45.77
REMARK 500 3 LEU A 33 8.23 -69.88
REMARK 500 3 THR A 38 -168.93 -164.25
REMARK 500 3 SER A 42 -55.04 -139.00
REMARK 500 3 ARG A 43 22.02 -175.75
REMARK 500 3 LYS A 44 24.50 -169.30
REMARK 500 3 THR A 45 35.18 -151.57
REMARK 500 3 GLU A 52 -134.75 -114.12
REMARK 500 3 ASN A 53 -64.02 -122.49
REMARK 500
REMARK 500 THIS ENTRY HAS 186 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 21 0.28 SIDE CHAIN
REMARK 500 1 ARG A 23 0.16 SIDE CHAIN
REMARK 500 1 ARG A 31 0.22 SIDE CHAIN
REMARK 500 1 ARG A 32 0.31 SIDE CHAIN
REMARK 500 1 ARG A 43 0.29 SIDE CHAIN
REMARK 500 1 ARG A 62 0.26 SIDE CHAIN
REMARK 500 1 ARG A 76 0.32 SIDE CHAIN
REMARK 500 1 ARG A 81 0.29 SIDE CHAIN
REMARK 500 2 ARG A 21 0.30 SIDE CHAIN
REMARK 500 2 ARG A 23 0.27 SIDE CHAIN
REMARK 500 2 ARG A 31 0.23 SIDE CHAIN
REMARK 500 2 ARG A 32 0.26 SIDE CHAIN
REMARK 500 2 ARG A 43 0.32 SIDE CHAIN
REMARK 500 2 ARG A 62 0.27 SIDE CHAIN
REMARK 500 2 ARG A 76 0.32 SIDE CHAIN
REMARK 500 2 ARG A 81 0.32 SIDE CHAIN
REMARK 500 3 ARG A 21 0.32 SIDE CHAIN
REMARK 500 3 ARG A 31 0.31 SIDE CHAIN
REMARK 500 3 ARG A 32 0.27 SIDE CHAIN
REMARK 500 3 ARG A 43 0.31 SIDE CHAIN
REMARK 500 3 ARG A 62 0.26 SIDE CHAIN
REMARK 500 3 ARG A 76 0.29 SIDE CHAIN
REMARK 500 3 ARG A 81 0.31 SIDE CHAIN
REMARK 500 4 ARG A 21 0.10 SIDE CHAIN
REMARK 500 4 ARG A 23 0.32 SIDE CHAIN
REMARK 500 4 ARG A 31 0.28 SIDE CHAIN
REMARK 500 4 ARG A 32 0.30 SIDE CHAIN
REMARK 500 4 ARG A 43 0.25 SIDE CHAIN
REMARK 500 4 ARG A 62 0.30 SIDE CHAIN
REMARK 500 4 ARG A 76 0.20 SIDE CHAIN
REMARK 500 4 ARG A 81 0.17 SIDE CHAIN
REMARK 500 5 ARG A 21 0.18 SIDE CHAIN
REMARK 500 5 ARG A 23 0.32 SIDE CHAIN
REMARK 500 5 ARG A 31 0.30 SIDE CHAIN
REMARK 500 5 ARG A 32 0.31 SIDE CHAIN
REMARK 500 5 ARG A 43 0.29 SIDE CHAIN
REMARK 500 5 ARG A 62 0.23 SIDE CHAIN
REMARK 500 5 ARG A 76 0.27 SIDE CHAIN
REMARK 500 5 ARG A 81 0.32 SIDE CHAIN
REMARK 500 6 ARG A 21 0.27 SIDE CHAIN
REMARK 500 6 ARG A 23 0.31 SIDE CHAIN
REMARK 500 6 ARG A 31 0.31 SIDE CHAIN
REMARK 500 6 ARG A 32 0.32 SIDE CHAIN
REMARK 500 6 ARG A 43 0.12 SIDE CHAIN
REMARK 500 6 ARG A 62 0.29 SIDE CHAIN
REMARK 500 6 ARG A 76 0.27 SIDE CHAIN
REMARK 500 6 ARG A 81 0.30 SIDE CHAIN
REMARK 500 7 ARG A 21 0.24 SIDE CHAIN
REMARK 500 7 ARG A 23 0.26 SIDE CHAIN
REMARK 500 7 ARG A 31 0.24 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 79 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: WR64TT RELATED DB: TARGETDB
DBREF 1L7B A 2 90 UNP P26996 DNLJ_THET8 588 676
SEQADV 1L7B MET A 1 UNP P26996 SEE REMARK 999
SEQADV 1L7B GLY A 91 UNP P26996 SEE REMARK 999
SEQADV 1L7B SER A 92 UNP P26996 SEE REMARK 999
SEQRES 1 A 92 MET GLU LYS GLY GLY GLU ALA LEU LYS GLY LEU THR PHE
SEQRES 2 A 92 VAL ILE THR GLY GLU LEU SER ARG PRO ARG GLU GLU VAL
SEQRES 3 A 92 LYS ALA LEU LEU ARG ARG LEU GLY ALA LYS VAL THR ASP
SEQRES 4 A 92 SER VAL SER ARG LYS THR SER TYR LEU VAL VAL GLY GLU
SEQRES 5 A 92 ASN PRO GLY SER LYS LEU GLU LYS ALA ARG ALA LEU GLY
SEQRES 6 A 92 VAL PRO THR LEU THR GLU GLU GLU LEU TYR ARG LEU LEU
SEQRES 7 A 92 GLU ALA ARG THR GLY LYS LYS ALA GLU GLU LEU VAL GLY
SEQRES 8 A 92 SER
HELIX 1 A1 ARG A 23 ARG A 31 1 9
HELIX 2 A2 LYS A 57 ALA A 63 1 7
HELIX 3 A3 GLU A 71 GLY A 83 1 13
SHEET 1 S1 4 ALA A 35 THR A 38 0
SHEET 2 S1 4 LEU A 11 ILE A 15 1 N THR A 38 O PHE A 13
SHEET 3 S1 4 TYR A 47 VAL A 50 1 N VAL A 49 O VAL A 14
SHEET 4 S1 4 THR A 68 THR A 70 1 O LEU A 48 N LEU A 69
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 - b 23 2 Bytes