Header list of 2fuu.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 27-JAN-06 2FUU TITLE NMR SOLUTION STRUCTURE OF THE PHD DOMAIN FROM THE HUMAN BPTF IN TITLE 2 COMPLEX WITH H3(1-15)K4ME3 PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: BROMODOMAIN PHD FINGER TRANSCRIPTION FACTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PHD FINGER DOMAIN (RESIDUES 2583-2639); COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HISTONE H3; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: H3(1-15)K4ME3; COMPND 10 ENGINEERED: YES; COMPND 11 MUTATION: 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: ROSSETA 2; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX6P; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 OTHER_DETAILS: SYNTHETIC. THE SEQUENCE ARTKQTARKSTGGKA OCCURS SOURCE 13 NATURALLY IN HUMANS ON HISTONE 3 KEYWDS BPTF, NURF, PHD DOMAIN, HISTONE RECOGNITION, H3K4ME3, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.ILIN,D.J.PATEL REVDAT 3 09-MAR-22 2FUU 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 2FUU 1 VERSN REVDAT 1 11-JUL-06 2FUU 0 JRNL AUTH H.LI,S.ILIN,W.WANG,E.M.DUNCAN,J.WYSOCKA,C.D.ALLIS,D.J.PATEL JRNL TITL MOLECULAR BASIS FOR SITE-SPECIFIC READ-OUT OF HISTONE JRNL TITL 2 H3K4ME3 BY THE BPTF PHD FINGER OF NURF. JRNL REF NATURE V. 442 91 2006 JRNL REFN ISSN 0028-0836 JRNL PMID 16728978 JRNL DOI 10.1038/NATURE04802 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : TOPSPIN 1.5, X-PLOR 2.13 REMARK 3 AUTHORS : BRUKER (TOPSPIN), G. MARIUS CLORE (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2FUU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-06. REMARK 100 THE DEPOSITION ID IS D_1000036338. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.5 REMARK 210 IONIC STRENGTH : 50 MM KCL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 0.64 MM PHD FINGER U-15N,13C; REMARK 210 3.0 MM H3(1-15)K4ME3; 20 MM REMARK 210 PHOSPHATE BUFFER PH 7.5, 50 MM REMARK 210 KCL, 5 MM DTT; 0.62 MM PHD REMARK 210 FINGER U-15N, 3.0 MM H3(1-15) REMARK 210 K4ME3; 20 MM PHOSPHATE BUFFER PH REMARK 210 7.5, 50 MM KCL, 5 MM DTT REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D FILTER-EDIT REMARK 210 15N-SEPARATED NOESY; 3D FILTER- REMARK 210 EDIT 13C-SEPARATED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ; 900 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 1.6C, CARA 1.5.3, X-PLOR REMARK 210 2.13, NMRPIPE REMARK 210 METHOD USED : THE STRUCTURE WAS SOLVED USING A REMARK 210 TORSION ANGLE SIMULATED REMARK 210 ANNEALING PROTOCOL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 85 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING VARIOUS TRIPLE REMARK 210 -RESONANCE NMR EXPERIMENTS PLUS FILTER EDIT EXPERIMENTS TO REMARK 210 DETERMINE THE STRUCTURE OF THE PEPTIDE. 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 SG CYS A 26 SG CYS A 53 0.64 REMARK 500 SG CYS A 29 SG CYS A 56 0.75 REMARK 500 SG CYS A 11 SG CYS A 13 1.00 REMARK 500 SG CYS A 26 SG CYS A 56 1.15 REMARK 500 SG CYS A 56 ZN ZN A 201 1.24 REMARK 500 SG CYS A 37 ZN ZN A 202 1.28 REMARK 500 O ASP A 18 H LYS A 21 1.32 REMARK 500 HD11 ILE A 48 H ASP A 49 1.34 REMARK 500 H CYS A 26 O ASN A 31 1.37 REMARK 500 SG CYS A 53 ZN ZN A 201 1.39 REMARK 500 SG CYS A 13 ZN ZN A 202 1.41 REMARK 500 O CYS A 26 HH21 ARG B 2 1.45 REMARK 500 O GLU A 44 HB ILE A 48 1.48 REMARK 500 SG CYS A 29 ZN ZN A 201 1.50 REMARK 500 O ASP A 27 HH22 ARG B 2 1.55 REMARK 500 SG CYS A 11 ZN ZN A 202 1.56 REMARK 500 SG CYS A 26 ZN ZN A 201 1.56 REMARK 500 O ARG A 36 H GLY A 39 1.58 REMARK 500 O CYS A 26 H GLN A 30 1.60 REMARK 500 SG CYS A 26 CB CYS A 53 2.04 REMARK 500 SG CYS A 26 CB CYS A 29 2.16 REMARK 500 OD1 ASN A 31 OH TYR A 33 2.18 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 10 -109.68 -67.33 REMARK 500 1 CYS A 11 134.21 -36.39 REMARK 500 1 ILE A 12 -7.39 -59.91 REMARK 500 1 LYS A 14 72.39 42.45 REMARK 500 1 GLU A 19 7.44 -55.15 REMARK 500 1 GLU A 44 -19.76 -44.20 REMARK 500 1 LEU A 47 12.49 -66.74 REMARK 500 1 ASP A 49 27.78 -169.19 REMARK 500 1 GLU A 50 14.76 -161.50 REMARK 500 1 ASP A 61 41.82 31.00 REMARK 500 1 ALA B 7 37.10 -150.10 REMARK 500 1 THR B 11 -70.27 -97.60 REMARK 500 2 LEU A 3 -113.72 -122.06 REMARK 500 2 ASP A 6 -14.10 -156.39 REMARK 500 2 TYR A 10 -124.09 -53.05 REMARK 500 2 CYS A 11 126.52 -33.14 REMARK 500 2 ILE A 12 -6.91 -52.79 REMARK 500 2 LYS A 14 70.97 50.68 REMARK 500 2 PRO A 16 -174.82 -48.75 REMARK 500 2 GLU A 19 8.19 -57.70 REMARK 500 2 GLN A 30 34.93 30.68 REMARK 500 2 ASP A 49 12.76 -161.35 REMARK 500 2 GLU A 50 41.12 -158.28 REMARK 500 2 GLU A 60 103.11 -38.81 REMARK 500 2 ARG B 2 48.87 -95.47 REMARK 500 2 ALA B 7 63.24 34.06 REMARK 500 2 THR B 11 -2.70 57.56 REMARK 500 3 SER A 5 -118.27 -151.93 REMARK 500 3 TYR A 10 -93.92 -114.86 REMARK 500 3 CYS A 11 134.92 -36.24 REMARK 500 3 ILE A 12 -7.15 -51.10 REMARK 500 3 LYS A 14 78.89 83.31 REMARK 500 3 GLU A 19 5.52 -59.60 REMARK 500 3 CYS A 26 108.89 -48.42 REMARK 500 3 ASP A 49 17.73 -160.97 REMARK 500 3 GLU A 50 35.29 -162.28 REMARK 500 3 GLU A 60 -164.61 42.16 REMARK 500 3 ARG B 2 33.51 -88.67 REMARK 500 3 THR B 11 164.29 83.27 REMARK 500 4 TYR A 10 -108.36 -67.93 REMARK 500 4 CYS A 11 131.28 -35.63 REMARK 500 4 ILE A 12 -7.41 -47.78 REMARK 500 4 LYS A 14 78.79 45.73 REMARK 500 4 GLU A 19 7.16 -57.03 REMARK 500 4 ASP A 49 20.21 -161.47 REMARK 500 4 GLU A 50 35.04 -166.16 REMARK 500 4 ARG B 8 16.72 -143.03 REMARK 500 4 LYS B 9 31.19 37.81 REMARK 500 4 SER B 10 -50.21 -145.81 REMARK 500 5 TYR A 10 -110.60 -89.72 REMARK 500 REMARK 500 THIS ENTRY HAS 258 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2FUI RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF PHD FINGER FRAGMENT OF HUMAN BPTF IN FREE REMARK 900 STATE REMARK 900 RELATED ID: 2F6J RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF PHD FINGER-LINKER-BROMODOMAIN FRAGMENT OF REMARK 900 HUMAN BPTF IN THE H3(1-15)K4ME3 BOUND STATE REMARK 900 RELATED ID: 2FSA RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF PHD FINGER-LINKER-BROMODOMAIN FRAGMENT OF REMARK 900 HUMAN BPTF IN THE H3(1-15)K4ME3 BOUND STATE DBREF 2FUU A 6 62 GB 31322942 AAP22284 2583 2639 DBREF 2FUU B 1 15 UNP P61836 H3_ZYGBA 1 15 SEQADV 2FUU GLY A 1 GB 31322942 CLONING ARTIFACT SEQADV 2FUU PRO A 2 GB 31322942 CLONING ARTIFACT SEQADV 2FUU LEU A 3 GB 31322942 CLONING ARTIFACT SEQADV 2FUU GLY A 4 GB 31322942 CLONING ARTIFACT SEQADV 2FUU SER A 5 GB 31322942 CLONING ARTIFACT SEQADV 2FUU M3L B 4 UNP P61836 LYS 4 MODIFIED RESIDUE SEQRES 1 A 62 GLY PRO LEU GLY SER ASP THR LYS LEU TYR CYS ILE CYS SEQRES 2 A 62 LYS THR PRO TYR ASP GLU SER LYS PHE TYR ILE GLY CYS SEQRES 3 A 62 ASP ARG CYS GLN ASN TRP TYR HIS GLY ARG CYS VAL GLY SEQRES 4 A 62 ILE LEU GLN SER GLU ALA GLU LEU ILE ASP GLU TYR VAL SEQRES 5 A 62 CYS PRO GLN CYS GLN SER THR GLU ASP ALA SEQRES 1 B 15 ALA ARG THR M3L GLN THR ALA ARG LYS SER THR GLY GLY SEQRES 2 B 15 LYS ALA MODRES 2FUU M3L B 4 LYS N-TRIMETHYLLYSINE HET M3L B 4 31 HET ZN A 201 1 HET ZN A 202 1 HETNAM M3L N-TRIMETHYLLYSINE HETNAM ZN ZINC ION FORMUL 2 M3L C9 H21 N2 O2 1+ FORMUL 3 ZN 2(ZN 2+) HELIX 1 1 ARG A 36 GLY A 39 5 4 HELIX 2 2 GLN A 42 GLU A 46 5 5 HELIX 3 3 CYS A 53 ASP A 61 1 9 SHEET 1 A 2 TYR A 23 GLY A 25 0 SHEET 2 A 2 TRP A 32 HIS A 34 -1 O TYR A 33 N ILE A 24 SSBOND 1 CYS A 11 CYS A 37 1555 1555 0.94 SSBOND 2 CYS A 13 CYS A 37 1555 1555 0.92 SSBOND 3 CYS A 26 CYS A 29 1555 1555 0.59 SSBOND 4 CYS A 29 CYS A 53 1555 1555 0.69 SSBOND 5 CYS A 53 CYS A 56 1555 1555 0.75 LINK C THR B 3 N M3L B 4 1555 1555 1.33 LINK C M3L B 4 N GLN B 5 1555 1555 1.33 SITE 1 AC1 7 CYS A 26 ASP A 27 ARG A 28 CYS A 29 SITE 2 AC1 7 VAL A 52 CYS A 53 CYS A 56 SITE 1 AC2 4 CYS A 11 CYS A 13 HIS A 34 CYS A 37 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 9 2 Bytes