Header list of 1xg1.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 16-SEP-04 1XG1
TITLE SOLUTION STRUCTURE OF MYB-DOMAIN OF HUMAN TRF2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TELOMERIC REPEAT BINDING FACTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL MYB DOMAIN;
COMPND 5 SYNONYM: HTRF2, TTAGGG REPEAT BINDING FACTOR 2, TELOMERIC DNA BINDING
COMPND 6 PROTEIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-14B
KEYWDS HELIX-TURN-HELIX, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.PAQUET,H.MEUDAL,S.AMIARD,M.DOUDEAU,J.PAOLETTI,M.J.GIRAUD-PANIS,
AUTHOR 2 G.LANCELOT
REVDAT 5 02-MAR-22 1XG1 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1XG1 1 VERSN
REVDAT 3 14-MAR-06 1XG1 1 JRNL
REVDAT 2 04-OCT-05 1XG1 1 JRNL
REVDAT 1 27-SEP-05 1XG1 0
JRNL AUTH Y.BILBILLE,F.PAQUET,H.MEUDAL,M.J.GIRAUD-PANIS,G.LANCELOT
JRNL TITL NMR STUDIES OF TELOMERIC NUCLEOPROTEIN COMPLEXES INVOLVING
JRNL TITL 2 THE MYB-LIKE DOMAIN OF THE HUMAN TELOMERIC PROTEIN TRF2
JRNL REF C.R.CHIMIE V. 9 452 2006
JRNL REFN ISSN 1631-0748
JRNL DOI 10.1016/J.CRCI.2005.06.016
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE LINUX, ARIA 1.1
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), LINGE (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XG1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030322.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.3
REMARK 210 IONIC STRENGTH : 50MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM MYB, 2MM PHOSPHATE BUFFER
REMARK 210 PH6, 50MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA 1.1
REMARK 210 METHOD USED : AUTOMATED ASSIGNMENT OF
REMARK 210 AMBIGUOUS NUCLEAR OVERHAUSER
REMARK 210 EFFECTS WITH ARIA AND NMR
REMARK 210 STRUCTURE CALCULATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
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: 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: 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 HZ3 TRP A 17 HE1 PHE A 46 1.35
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 MET A 4 106.28 -162.26
REMARK 500 1 ASP A 6 -44.55 -174.63
REMARK 500 1 SER A 7 41.77 -148.55
REMARK 500 1 ASN A 10 39.20 -80.57
REMARK 500 1 LYS A 14 83.88 59.17
REMARK 500 1 GLN A 15 -167.72 63.63
REMARK 500 1 PRO A 45 43.12 -66.09
REMARK 500 1 ASN A 48 -41.52 72.97
REMARK 500 2 ASP A 6 -169.38 -167.07
REMARK 500 2 SER A 7 -139.37 -171.26
REMARK 500 2 THR A 8 -51.26 -162.57
REMARK 500 2 ILE A 11 112.23 69.46
REMARK 500 2 THR A 12 -44.13 70.95
REMARK 500 2 LYS A 13 -178.06 71.38
REMARK 500 2 GLN A 15 45.77 -79.28
REMARK 500 2 PRO A 45 44.57 -66.98
REMARK 500 2 ASN A 48 -30.38 67.10
REMARK 500 3 SER A 2 -91.84 62.42
REMARK 500 3 HIS A 3 38.12 -80.09
REMARK 500 3 GLU A 5 38.48 -80.88
REMARK 500 3 ILE A 11 34.26 -140.20
REMARK 500 3 LYS A 14 145.64 76.29
REMARK 500 3 ASN A 36 49.34 -85.65
REMARK 500 3 PRO A 45 48.93 -66.39
REMARK 500 3 ASN A 48 -34.04 69.88
REMARK 500 4 SER A 2 -42.59 66.83
REMARK 500 4 ASN A 10 50.81 -68.19
REMARK 500 4 THR A 12 -51.18 -157.35
REMARK 500 4 LYS A 14 105.47 -58.15
REMARK 500 4 PRO A 45 44.28 -67.47
REMARK 500 4 MET A 66 38.80 -95.58
REMARK 500 5 SER A 2 45.89 -141.92
REMARK 500 5 MET A 4 129.70 -174.51
REMARK 500 5 THR A 8 -51.80 -155.78
REMARK 500 5 THR A 9 -140.56 -147.85
REMARK 500 5 THR A 12 -19.00 100.64
REMARK 500 5 GLU A 34 106.69 -55.15
REMARK 500 5 PRO A 45 46.30 -68.32
REMARK 500 5 ASN A 48 -39.87 73.91
REMARK 500 5 MET A 66 50.38 -91.82
REMARK 500 6 THR A 9 -52.47 -148.34
REMARK 500 6 LYS A 13 49.80 178.44
REMARK 500 6 GLN A 15 138.27 70.16
REMARK 500 6 ASN A 36 48.19 -81.62
REMARK 500 6 PRO A 45 48.27 -67.60
REMARK 500 6 ASN A 48 -30.92 65.84
REMARK 500 7 GLU A 5 104.82 65.14
REMARK 500 7 ILE A 11 27.85 -71.01
REMARK 500 7 PRO A 45 43.02 -66.31
REMARK 500 7 ASN A 48 -40.67 71.33
REMARK 500
REMARK 500 THIS ENTRY HAS 159 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XG1 A 5 67 UNP Q15554 TERF2_HUMAN 438 500
SEQADV 1XG1 GLY A 1 UNP Q15554 CLONING ARTIFACT
SEQADV 1XG1 SER A 2 UNP Q15554 CLONING ARTIFACT
SEQADV 1XG1 HIS A 3 UNP Q15554 CLONING ARTIFACT
SEQADV 1XG1 MET A 4 UNP Q15554 CLONING ARTIFACT
SEQRES 1 A 67 GLY SER HIS MET GLU ASP SER THR THR ASN ILE THR LYS
SEQRES 2 A 67 LYS GLN LYS TRP THR VAL GLU GLU SER GLU TRP VAL LYS
SEQRES 3 A 67 ALA GLY VAL GLN LYS TYR GLY GLU GLY ASN TRP ALA ALA
SEQRES 4 A 67 ILE SER LYS ASN TYR PRO PHE VAL ASN ARG THR ALA VAL
SEQRES 5 A 67 MET ILE LYS ASP ARG TRP ARG THR MET LYS ARG LEU GLY
SEQRES 6 A 67 MET ASN
HELIX 1 1 THR A 18 TYR A 32 1 15
HELIX 2 2 ASN A 36 TYR A 44 1 9
HELIX 3 3 THR A 50 LEU A 64 1 15
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 - r 2 2 Bytes