Header list of 1q1v.pdb file
Complete list - 2 20 Bytes
HEADER DNA BINDING PROTEIN 22-JUL-03 1Q1V
TITLE STRUCTURE OF THE ONCOPROTEIN DEK: A PUTATIVE DNA-BINDING DOMAIN
TITLE 2 RELATED TO THE WINGED HELIX MOTIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEK PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 309-378;
COMPND 5 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: DEK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28C
KEYWDS WINGED-HELIX MOTIF, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.DEVANY,N.P.KOTHARU,H.MATSUO
REVDAT 3 02-MAR-22 1Q1V 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Q1V 1 VERSN
REVDAT 1 10-AUG-04 1Q1V 0
JRNL AUTH M.DEVANY,N.P.KOTHARU,H.MATSUO
JRNL TITL SOLUTION NMR STRUCTURE OF THE C-TERMINAL DOMAIN OF THE HUMAN
JRNL TITL 2 PROTEIN DEK
JRNL REF PROTEIN SCI. V. 13 2252 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 15238633
JRNL DOI 10.1110/PS.04797104
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE BASED ON 1456 NON-REDUNDANT
REMARK 3 NOES, 33 HYDROGEN BOND RESTRAINTS DERIVED FROM DEUTERIUM EXCHANG
REMARK 3 EXPERIMENTS, AND 46 DIHEDRAL-ANGLE RESTRAINTS DERIVED FROM CA
REMARK 3 CHEMICAL SHIFTS.
REMARK 4
REMARK 4 1Q1V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019811.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.75
REMARK 210 IONIC STRENGTH : 50MM NAPO4, 100MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0MM DEK C-TERMINAL DOMAIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST TOTAL
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: DISTANCE RESTRAINTS COLLECTED FROM A NOESY SPECTRUM WITH
REMARK 210 150MS MIXING TIME.
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
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 GLU A 310 -59.28 -177.64
REMARK 500 1 ILE A 313 -55.57 -137.92
REMARK 500 1 LYS A 314 104.60 59.54
REMARK 500 1 LYS A 317 71.14 -164.01
REMARK 500 1 ASP A 358 54.53 -100.74
REMARK 500 1 LEU A 359 97.54 -57.23
REMARK 500 1 GLU A 377 32.78 -163.67
REMARK 500 2 LYS A 314 30.10 -158.68
REMARK 500 2 LYS A 317 -163.04 -66.43
REMARK 500 2 LYS A 331 -70.98 -78.64
REMARK 500 2 LYS A 348 -70.24 -71.82
REMARK 500 2 ASP A 358 48.81 -91.86
REMARK 500 2 LEU A 359 108.93 -38.79
REMARK 500 3 LEU A 312 -58.88 66.67
REMARK 500 3 ILE A 313 168.80 54.35
REMARK 500 3 LYS A 314 155.25 177.62
REMARK 500 3 LEU A 316 -77.40 -66.93
REMARK 500 3 THR A 321 156.02 -40.97
REMARK 500 3 ASP A 358 52.53 -93.92
REMARK 500 3 LEU A 359 103.42 -47.45
REMARK 500 3 GLU A 377 35.60 -173.92
REMARK 500 4 ILE A 313 76.37 -108.71
REMARK 500 4 LYS A 314 39.92 -153.25
REMARK 500 4 LEU A 316 -87.86 -72.64
REMARK 500 4 LYS A 348 -75.68 -66.64
REMARK 500 4 ASP A 358 42.98 -86.22
REMARK 500 4 LEU A 359 99.32 -43.13
REMARK 500 5 ILE A 313 98.26 60.53
REMARK 500 5 LYS A 314 -165.67 -119.54
REMARK 500 5 LYS A 317 -178.80 -52.46
REMARK 500 5 ASP A 358 51.19 -90.50
REMARK 500 5 GLU A 377 43.30 -148.54
REMARK 500 6 LEU A 312 61.46 -112.12
REMARK 500 6 LYS A 314 104.69 -50.25
REMARK 500 6 LEU A 316 47.64 -146.37
REMARK 500 6 LYS A 317 -163.93 -103.45
REMARK 500 6 THR A 321 159.34 -49.49
REMARK 500 6 ALA A 336 -159.76 -151.63
REMARK 500 6 ASP A 358 51.26 -94.86
REMARK 500 6 LEU A 359 112.98 -39.32
REMARK 500 6 ILE A 366 -70.11 -59.51
REMARK 500 6 GLU A 377 26.19 -159.16
REMARK 500 7 LEU A 316 56.34 -110.80
REMARK 500 7 LYS A 318 55.64 -151.05
REMARK 500 7 THR A 321 161.43 -43.19
REMARK 500 7 THR A 356 46.72 -82.43
REMARK 500 7 THR A 360 -59.60 -120.22
REMARK 500 7 GLU A 377 38.48 173.01
REMARK 500 8 LYS A 317 -159.85 58.99
REMARK 500 8 LYS A 349 -71.03 -70.60
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 362 0.29 SIDE CHAIN
REMARK 500 2 ARG A 362 0.32 SIDE CHAIN
REMARK 500 3 ARG A 362 0.31 SIDE CHAIN
REMARK 500 4 ARG A 362 0.16 SIDE CHAIN
REMARK 500 5 ARG A 362 0.27 SIDE CHAIN
REMARK 500 6 ARG A 362 0.31 SIDE CHAIN
REMARK 500 7 ARG A 362 0.21 SIDE CHAIN
REMARK 500 8 ARG A 362 0.11 SIDE CHAIN
REMARK 500 9 ARG A 362 0.08 SIDE CHAIN
REMARK 500 10 ARG A 362 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Q1V A 309 375 UNP P35659 DEK_HUMAN 309 375
SEQADV 1Q1V LEU A 376 UNP P35659 CLONING ARTIFACT
SEQADV 1Q1V GLU A 377 UNP P35659 CLONING ARTIFACT
SEQADV 1Q1V HIS A 378 UNP P35659 CLONING ARTIFACT
SEQRES 1 A 70 ASP GLU PRO LEU ILE LYS LYS LEU LYS LYS PRO PRO THR
SEQRES 2 A 70 ASP GLU GLU LEU LYS GLU THR ILE LYS LYS LEU LEU ALA
SEQRES 3 A 70 SER ALA ASN LEU GLU GLU VAL THR MET LYS GLN ILE CYS
SEQRES 4 A 70 LYS LYS VAL TYR GLU ASN TYR PRO THR TYR ASP LEU THR
SEQRES 5 A 70 GLU ARG LYS ASP PHE ILE LYS THR THR VAL LYS GLU LEU
SEQRES 6 A 70 ILE SER LEU GLU HIS
HELIX 1 1 THR A 321 ALA A 334 1 14
HELIX 2 2 SER A 335 ALA A 336 5 2
HELIX 3 3 ASN A 337 VAL A 341 5 5
HELIX 4 4 THR A 342 TYR A 354 1 13
HELIX 5 5 THR A 360 LEU A 376 1 17
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 309
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 - 2 20 Bytes