Header list of 2h7b.pdb file
Complete list - t 20 2 Bytes
HEADER TRANSCRIPTION 01-JUN-06 2H7B
TITLE SOLUTION STRUCTURE OF THE ETAFH DOMAIN FROM THE HUMAN LEUKEMIA-
TITLE 2 ASSOCIATED FUSION PROTEIN AML1-ETO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CORE-BINDING FACTOR, ML1-ETO;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 83-185,;
COMPND 5 SYNONYM: RUNT DOMAIN, ALPHA SUBUNIT 2, TRANSLOCATED TO 1, CYCLIN D-
COMPND 6 RELATED;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ETO;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS 4 HELIX BUNDLE, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.J.PLEVIN,J.ZHANG,C.GUO,R.G.ROEDER,M.IKURA
REVDAT 3 20-OCT-21 2H7B 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2H7B 1 VERSN
REVDAT 1 11-JUL-06 2H7B 0
JRNL AUTH M.J.PLEVIN,J.ZHANG,C.GUO,R.G.ROEDER,M.IKURA
JRNL TITL THE ACUTE MYELOID LEUKEMIA FUSION PROTEIN AML1-ETO TARGETS E
JRNL TITL 2 PROTEINS VIA A PAIRED AMPHIPATHIC HELIX-LIKE TBP-ASSOCIATED
JRNL TITL 3 FACTOR HOMOLOGY DOMAIN
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 10242 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16803958
JRNL DOI 10.1073/PNAS.0603463103
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA
REMARK 3 AUTHORS : GUNTERT, P. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2H7B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038019.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 25
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 70 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7 MM ETAFH U-15N, 13C, 20 MM
REMARK 210 SODIUM PHOSPHATE, PH 6.0, 50 MM
REMARK 210 NACL, 1MM PMSF, 1MM AEBSF, 0.25
REMARK 210 MM SODIUM AZIDE, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; 4D_13C/15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
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 ENTRY IS THE SOLUTION CONFORMATION OF ETAFH BOUND TO
REMARK 210 17 RESIDUE AD1 PEPTIDE FROM HUMAN HEB. STRUCTURE OF THE BOUND
REMARK 210 AD1 PEPTIDE WAS NOT DETERMINED DUE TO CHEMICAL EXCHANGE
REMARK 210 BROADENING OF RESONANCES FROM THIS MOLECULE
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: 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 ALA A 1 -67.27 -93.37
REMARK 500 1 SER A 22 163.52 173.08
REMARK 500 1 GLU A 24 -75.80 -51.48
REMARK 500 1 VAL A 33 -73.18 -49.14
REMARK 500 1 SER A 48 -72.24 -75.50
REMARK 500 1 ASN A 55 -176.72 -57.81
REMARK 500 1 PHE A 56 167.40 59.95
REMARK 500 1 PHE A 61 78.53 63.54
REMARK 500 1 PHE A 65 -73.05 -70.35
REMARK 500 1 LEU A 98 50.62 -90.88
REMARK 500 1 LEU A 99 -74.60 -113.87
REMARK 500 2 ALA A 1 -72.95 -94.60
REMARK 500 2 VAL A 33 -71.26 -50.09
REMARK 500 2 LEU A 58 126.79 179.92
REMARK 500 2 PHE A 61 80.29 57.08
REMARK 500 2 ARG A 82 -70.61 -51.84
REMARK 500 2 LEU A 100 -71.04 -51.84
REMARK 500 3 SER A 0 54.38 -117.44
REMARK 500 3 ALA A 1 -60.98 -93.21
REMARK 500 3 VAL A 33 -71.82 -49.66
REMARK 500 3 SER A 48 -72.27 -73.57
REMARK 500 3 VAL A 62 -63.55 -97.19
REMARK 500 3 PHE A 65 -70.30 -66.13
REMARK 500 3 LEU A 98 53.90 -92.07
REMARK 500 3 ASP A 101 94.05 -64.65
REMARK 500 4 VAL A 33 -73.95 -50.47
REMARK 500 4 THR A 54 -75.24 -48.29
REMARK 500 4 ASN A 55 -62.75 -154.07
REMARK 500 4 PHE A 56 -59.84 179.82
REMARK 500 4 PHE A 61 78.00 65.48
REMARK 500 4 LEU A 99 100.86 -56.17
REMARK 500 4 ASP A 101 86.37 -68.72
REMARK 500 5 SER A 0 -166.42 -179.36
REMARK 500 5 ALA A 1 -72.21 -67.41
REMARK 500 5 SER A 22 163.15 176.87
REMARK 500 5 GLU A 24 -72.67 -53.72
REMARK 500 5 VAL A 33 -71.48 -50.61
REMARK 500 5 PRO A 57 -177.57 -69.75
REMARK 500 5 LEU A 58 108.30 -59.01
REMARK 500 5 VAL A 62 -60.29 -95.58
REMARK 500 5 LEU A 98 53.65 -109.59
REMARK 500 5 ASP A 101 97.95 -65.09
REMARK 500 5 ALA A 102 -62.97 -109.91
REMARK 500 6 SER A 0 55.96 -113.08
REMARK 500 6 ALA A 1 -61.03 -93.45
REMARK 500 6 SER A 22 160.24 178.96
REMARK 500 6 GLU A 24 -76.73 -53.45
REMARK 500 6 VAL A 33 -72.53 -51.25
REMARK 500 6 PHE A 65 -72.64 -61.02
REMARK 500 6 ASP A 101 91.59 -65.42
REMARK 500
REMARK 500 THIS ENTRY HAS 167 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2H7B A 1 103 UNP Q7Z4J5 Q7Z4J5_HUMAN 83 185
SEQADV 2H7B GLY A -1 UNP Q7Z4J5 CLONING ARTIFACT
SEQADV 2H7B SER A 0 UNP Q7Z4J5 CLONING ARTIFACT
SEQADV 2H7B ALA A 80 UNP Q7Z4J5 CYS 162 ENGINEERED MUTATION
SEQRES 1 A 105 GLY SER ALA ARG GLN LEU SER LYS LEU LYS ARG PHE LEU
SEQRES 2 A 105 THR THR LEU GLN GLN PHE GLY ASN ASP ILE SER PRO GLU
SEQRES 3 A 105 ILE GLY GLU ARG VAL ARG THR LEU VAL LEU GLY LEU VAL
SEQRES 4 A 105 ASN SER THR LEU THR ILE GLU GLU PHE HIS SER LYS LEU
SEQRES 5 A 105 GLN GLU ALA THR ASN PHE PRO LEU ARG PRO PHE VAL ILE
SEQRES 6 A 105 PRO PHE LEU LYS ALA ASN LEU PRO LEU LEU GLN ARG GLU
SEQRES 7 A 105 LEU LEU HIS ALA ALA ARG LEU ALA LYS GLN ASN PRO ALA
SEQRES 8 A 105 GLN TYR LEU ALA GLN HIS GLU GLN LEU LEU LEU ASP ALA
SEQRES 9 A 105 SER
HELIX 1 1 ALA A 1 LEU A 4 5 4
HELIX 2 2 SER A 5 PHE A 17 1 13
HELIX 3 3 PHE A 17 SER A 22 1 6
HELIX 4 4 SER A 22 ASN A 38 1 17
HELIX 5 5 THR A 42 THR A 54 1 13
HELIX 6 6 VAL A 62 ALA A 68 1 7
HELIX 7 7 ASN A 69 ALA A 81 1 13
HELIX 8 8 ARG A 82 ALA A 84 5 3
HELIX 9 9 ALA A 89 GLN A 94 1 6
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 - t 20 2 Bytes