Header list of 1jjr.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN 09-JUL-01 1JJR
TITLE THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL DNA BINDING DOMAIN
TITLE 2 OF HUMAN KU70
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYROID AUTOANTIGEN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: KU70;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: KU70;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS DNA REPAIR PROTEIN, PROTEIN-DNA INTERACTION, KU70, SOLUTION
KEYWDS 2 STRUCTURE, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Z.ZHANG,Y.CHEN
REVDAT 4 23-FEB-22 1JJR 1 REMARK
REVDAT 3 24-FEB-09 1JJR 1 VERSN
REVDAT 2 24-OCT-01 1JJR 1 JRNL
REVDAT 1 03-OCT-01 1JJR 0
JRNL AUTH Z.ZHANG,L.ZHU,D.LIN,F.CHEN,D.J.CHEN,Y.CHEN
JRNL TITL THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL
JRNL TITL 2 DNA-BINDING DOMAIN OF HUMAN KU70.
JRNL REF J.BIOL.CHEM. V. 276 38231 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11457852
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 98, X-PLOR CNS 1.0
REMARK 3 AUTHORS : MSI (FELIX), A.T.BRUNGER, P.D.ADAMS, G.M.CLORE,
REMARK 3 W.L.DELANO, P.GROS, R.W.GROSSE-KUNSTLEVE, (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JJR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013854.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 100 MM NA PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.0 MM KU70_CTD 15N,13C: 100MM
REMARK 210 PHOSPHATE BUFFER PH6.0; 1.0 MM
REMARK 210 KU70_CTD 15N,13C; 100MM
REMARK 210 PHOSPHATE BUFFER PH6.0; 0.8 MM
REMARK 210 KU70_CTD 15N; 100MM PHOSPHATE
REMARK 210 BUFFER PH6.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, DYANA 1.5, X-PLOR CNS
REMARK 210 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 GLU A 49 H LYS A 53 1.59
REMARK 500 O LEU A 88 H THR A 92 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 TYR A 47 44.45 70.81
REMARK 500 1 GLU A 49 -42.84 163.11
REMARK 500 1 SER A 57 -77.01 -53.26
REMARK 500 1 PHE A 64 158.27 -49.42
REMARK 500 1 THR A 65 -168.00 -73.89
REMARK 500 1 SER A 80 176.58 68.23
REMARK 500 1 LYS A 83 -73.38 -157.39
REMARK 500 1 LYS A 84 -83.77 168.90
REMARK 500 1 PHE A 95 27.66 -148.50
REMARK 500 2 VAL A 45 34.71 -78.43
REMARK 500 2 TYR A 47 50.99 70.42
REMARK 500 2 GLU A 49 -42.16 167.39
REMARK 500 2 SER A 57 -74.37 -53.70
REMARK 500 2 LYS A 58 -74.77 -61.79
REMARK 500 2 PHE A 64 155.80 -49.92
REMARK 500 2 THR A 65 -169.53 -74.40
REMARK 500 2 LYS A 79 24.40 -141.64
REMARK 500 2 SER A 80 -166.99 -77.83
REMARK 500 2 LEU A 82 -86.17 -158.86
REMARK 500 2 LYS A 84 -65.63 169.13
REMARK 500 3 GLU A 49 -43.43 168.16
REMARK 500 3 THR A 65 -168.20 -74.13
REMARK 500 3 SER A 80 -166.89 45.29
REMARK 500 3 LEU A 82 13.09 -153.31
REMARK 500 3 LYS A 84 -79.35 71.39
REMARK 500 3 PHE A 95 34.84 -147.19
REMARK 500 4 VAL A 45 -54.16 -160.52
REMARK 500 4 GLU A 46 -70.49 -164.25
REMARK 500 4 TYR A 47 75.50 -156.17
REMARK 500 4 GLU A 49 -37.22 168.66
REMARK 500 4 SER A 57 -72.75 -54.48
REMARK 500 4 LYS A 58 -74.34 -61.53
REMARK 500 4 PHE A 64 151.79 -49.82
REMARK 500 4 THR A 65 -165.49 -73.87
REMARK 500 4 LYS A 79 75.58 -100.29
REMARK 500 4 SER A 80 -169.07 -75.85
REMARK 500 4 LEU A 82 11.23 -155.40
REMARK 500 4 LYS A 84 -76.82 69.43
REMARK 500 4 PHE A 95 27.96 -147.65
REMARK 500 5 TYR A 47 83.05 64.42
REMARK 500 5 GLU A 49 -39.47 164.83
REMARK 500 5 SER A 57 -76.11 -52.78
REMARK 500 5 PHE A 64 157.26 -49.84
REMARK 500 5 THR A 65 -169.40 -73.86
REMARK 500 5 SER A 80 169.30 65.63
REMARK 500 5 LYS A 83 8.33 -155.88
REMARK 500 5 LYS A 84 -76.48 65.99
REMARK 500 5 PHE A 95 19.75 -147.64
REMARK 500 6 GLU A 49 -39.46 168.24
REMARK 500 6 SER A 57 -75.70 -53.54
REMARK 500
REMARK 500 THIS ENTRY HAS 176 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JJR A 44 97 GB 339667 AAA61177 556 609
SEQRES 1 A 151 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 151 LEU VAL PRO ARG GLY SER HIS MET ALA SER PRO GLU GLY
SEQRES 3 A 151 LYS VAL THR LYS ARG LYS HIS ASP ASN GLU GLY SER GLY
SEQRES 4 A 151 SER LYS ARG PRO LYS VAL GLU TYR SER GLU GLU GLU LEU
SEQRES 5 A 151 LYS THR HIS ILE SER LYS GLY THR LEU GLY LYS PHE THR
SEQRES 6 A 151 VAL PRO MET LEU LYS GLU ALA CYS ARG ALA TYR GLY LEU
SEQRES 7 A 151 LYS SER GLY LEU LYS LYS GLN GLU LEU LEU GLU ALA LEU
SEQRES 8 A 151 THR LYS HIS PHE GLN ASP LYS VAL GLU TYR SER GLU GLU
SEQRES 9 A 151 GLU LEU LYS THR HIS ILE SER LYS GLY THR LEU GLY LYS
SEQRES 10 A 151 PHE THR VAL PRO MET LEU LYS GLU ALA CYS ARG ALA TYR
SEQRES 11 A 151 GLY LEU LYS SER GLY LEU LYS LYS GLN GLU LEU LEU GLU
SEQRES 12 A 151 ALA LEU THR LYS HIS PHE GLN ASP
HELIX 1 1 GLU A 49 GLY A 59 1 11
HELIX 2 2 THR A 65 GLY A 77 1 13
HELIX 3 3 LYS A 84 HIS A 94 1 11
CRYST1 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