Header list of 1hn3.pdb file
Complete list - b 23 2 Bytes
HEADER ANTITUMOR PROTEIN 05-DEC-00 1HN3
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL 37 AMINO ACIDS OF THE MOUSE ARF
TITLE 2 TUMOR SUPPRESSOR PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P19 ARF PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-37;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
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: PET28A-POLYHIS-SYN-ARF N37
KEYWDS ARF, P19ARF, TUMOR SUPPRESSOR, P53, MDM2, ANTITUMOR PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.L.DIGIAMMARINO,I.FILIPPOV,J.D.WEBER,B.BOTHNER,R.W.KRIWACKI
REVDAT 3 23-FEB-22 1HN3 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1HN3 1 VERSN
REVDAT 1 05-DEC-01 1HN3 0
JRNL AUTH E.L.DIGIAMMARINO,I.FILIPPOV,J.D.WEBER,B.BOTHNER,R.W.KRIWACKI
JRNL TITL SOLUTION STRUCTURE OF THE P53 REGULATORY DOMAIN OF THE
JRNL TITL 2 P19ARF TUMOR SUPPRESSOR PROTEIN.
JRNL REF BIOCHEMISTRY V. 40 2379 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11327858
JRNL DOI 10.1021/BI0024005
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, CNS 1.0
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER, A.T. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HN3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000012456.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 60
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM MARFN37 15N OR 15N/13C; 10MM
REMARK 210 POTASSIUM PHOSPHATE, PH 5.0;
REMARK 210 50MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
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 : NMRPIPE 1.7, FELIX 98, CNS 1.0
REMARK 210 METHOD USED : CNS WAS USED FOR STRUCTURE
REMARK 210 CALCULATIONS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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 : 11
REMARK 210
REMARK 210 REMARK: BACKBONE DIHEDRAL ANGLE RESTRAINTS WERE OBTAINED USING THE
REMARK 210 PROGRAM TALOS DEVELOPED BY CORNILESCU, G., DELAGLIO, F. AND BAX,
REMARK 210 A.
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 SER A 2 -67.21 -105.05
REMARK 500 1 HIS A 3 -175.73 60.43
REMARK 500 1 ARG A 6 20.94 -144.09
REMARK 500 1 GLN A 22 -38.43 -179.77
REMARK 500 2 SER A 2 65.61 -163.99
REMARK 500 2 LEU A 21 -43.12 -160.49
REMARK 500 2 THR A 38 -56.17 -137.15
REMARK 500 2 ALA A 39 70.48 60.70
REMARK 500 3 SER A 2 -54.10 -143.28
REMARK 500 3 HIS A 3 -41.92 -172.27
REMARK 500 3 MET A 4 95.27 62.91
REMARK 500 3 ARG A 34 162.66 60.12
REMARK 500 3 ALA A 39 31.41 -163.90
REMARK 500 4 HIS A 3 144.19 63.17
REMARK 500 4 MET A 4 124.76 -170.79
REMARK 500 4 ARG A 6 -51.62 -142.80
REMARK 500 4 GLN A 22 -36.76 179.15
REMARK 500 4 ARG A 35 76.98 -110.31
REMARK 500 5 HIS A 3 93.66 -163.21
REMARK 500 5 GLN A 22 -41.40 -167.23
REMARK 500 6 ARG A 6 -66.37 -163.40
REMARK 500 6 GLN A 22 -37.29 -179.06
REMARK 500 6 PRO A 36 174.32 -55.42
REMARK 500 7 ARG A 19 87.89 62.10
REMARK 500 7 LEU A 21 108.51 -58.29
REMARK 500 7 GLN A 22 -42.45 -159.62
REMARK 500 7 THR A 38 -46.40 -154.10
REMARK 500 7 ALA A 39 -46.84 -136.32
REMARK 500 8 SER A 2 101.31 -165.98
REMARK 500 8 MET A 4 106.66 60.32
REMARK 500 8 GLN A 22 -42.87 -133.52
REMARK 500 8 ARG A 34 65.60 -153.91
REMARK 500 8 ARG A 35 99.19 56.89
REMARK 500 9 HIS A 3 167.51 60.08
REMARK 500 9 MET A 4 93.58 -164.40
REMARK 500 9 ARG A 19 78.01 -166.99
REMARK 500 9 LEU A 21 -72.19 66.61
REMARK 500 9 ARG A 34 -40.12 -177.33
REMARK 500 9 ARG A 35 63.62 -157.57
REMARK 500 9 ARG A 37 114.35 61.12
REMARK 500 9 THR A 38 -47.11 -162.74
REMARK 500 10 SER A 2 77.35 53.96
REMARK 500 10 HIS A 3 -64.07 -105.82
REMARK 500 10 ARG A 6 24.42 -151.66
REMARK 500 10 GLN A 22 -47.99 -178.61
REMARK 500 10 ALA A 39 -77.32 65.47
REMARK 500 11 HIS A 3 87.59 -66.58
REMARK 500 11 ARG A 6 -67.40 68.69
REMARK 500 11 LEU A 21 -68.61 -178.57
REMARK 500 11 SER A 33 91.36 -59.67
REMARK 500
REMARK 500 THIS ENTRY HAS 99 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1HN3 A 4 40 UNP Q64364 CD2A2_MOUSE 1 37
SEQADV 1HN3 GLY A 1 UNP Q64364 CLONING ARTIFACT
SEQADV 1HN3 SER A 2 UNP Q64364 CLONING ARTIFACT
SEQADV 1HN3 HIS A 3 UNP Q64364 CLONING ARTIFACT
SEQRES 1 A 40 GLY SER HIS MET GLY ARG ARG PHE LEU VAL THR VAL ARG
SEQRES 2 A 40 ILE GLN ARG ALA GLY ARG PRO LEU GLN GLU ARG VAL PHE
SEQRES 3 A 40 LEU VAL LYS PHE VAL ARG SER ARG ARG PRO ARG THR ALA
SEQRES 4 A 40 SER
HELIX 1 1 ARG A 6 GLY A 18 1 13
HELIX 2 2 GLN A 22 SER A 33 1 12
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