Header list of 1kkx.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN 10-DEC-01 1KKX
TITLE SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF ADR6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION REGULATORY PROTEIN ADR6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ARID DOMAIN;
COMPND 5 SYNONYM: TRANSCRIPTION REGULATORY PROTEIN SWI1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: ADR6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PREP-4
KEYWDS ARID, ADR6, DNA-BINDING DOMAIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR X.TU,J.WU,Y.XU,Y.SHI
REVDAT 4 23-FEB-22 1KKX 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1KKX 1 VERSN
REVDAT 2 04-DEC-02 1KKX 1 REMARK
REVDAT 1 17-JUL-02 1KKX 0
JRNL AUTH X.TU,J.WU,Y.XU,Y.SHI
JRNL TITL 1H, 13C AND 15N RESONANCE ASSIGNMENTS AND SECONDARY
JRNL TITL 2 STRUCTURE OF ADR6 DNA-BINDING DOMAIN.
JRNL REF J.BIOMOL.NMR V. 21 187 2001
JRNL REFN ISSN 0925-2738
JRNL PMID 11727987
JRNL DOI 10.1023/A:1012434510376
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH X.TU,J.WU,Y.XU,Y.SHI
REMARK 1 TITL 1H, 13C AND 15N RESONANCE ASSIGNMENTS AND SECONDARY
REMARK 1 TITL 2 STRUCTURE OF ADR6 DNA-BINDING DOMAIN
REMARK 1 REF J.BIOMOL.NMR V. 21 187 2001
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1012434510376
REMARK 1 REFERENCE 2
REMARK 1 AUTH X.TU,Y.XIAO,W.ZENG,Y.SHI
REMARK 1 TITL EXPRESSION AND PURIFICATION OF A RECOMBINANT DNA-BINDING
REMARK 1 TITL 2 DOMAIN OF ADR6 PROTEIN FROM ESCHERICHIA COLI AND ITS
REMARK 1 TITL 3 SECONDARY STRUCTURE CHARACTERIZATION
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1481 167 2000
REMARK 1 REFN ISSN 0006-3002
REMARK 1 DOI 10.1016/S0167-4838(00)00095-9
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS V 1.0
REMARK 3 AUTHORS : A.T. BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KKX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015064.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 4.9
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM ADR6 ARID DOMAIN U-15N, U
REMARK 210 -13C, 50MM PHOSPHATE BUFFER AT
REMARK 210 PH4.9, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 MET A -11
REMARK 465 ARG A -10
REMARK 465 GLY A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 SER A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 LEU A 105
REMARK 465 GLN A 106
REMARK 465 PRO A 107
REMARK 465 SER A 108
REMARK 465 LEU A 109
REMARK 465 ILE A 110
REMARK 465 SER A 111
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 O LEU A 75 H ILE A 78 1.53
REMARK 500 HG13 ILE A 78 N TYR A 79 1.57
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 ASN A 22 56.83 71.15
REMARK 500 1 PRO A 24 25.75 -76.30
REMARK 500 1 LEU A 25 128.51 -179.46
REMARK 500 1 SER A 27 123.51 -178.47
REMARK 500 1 ILE A 28 129.11 -37.83
REMARK 500 1 PRO A 29 22.57 -77.93
REMARK 500 1 GLU A 30 70.98 20.73
REMARK 500 1 ASN A 33 -79.28 -174.97
REMARK 500 1 ILE A 36 156.90 56.56
REMARK 500 1 ASN A 37 34.88 -179.29
REMARK 500 1 TYR A 40 -73.73 -59.05
REMARK 500 1 THR A 57 -169.55 -121.65
REMARK 500 1 VAL A 63 -76.70 -60.69
REMARK 500 1 GLN A 68 54.11 81.71
REMARK 500 1 TYR A 72 -32.20 -35.08
REMARK 500 1 LEU A 75 -72.09 -55.81
REMARK 500 1 LEU A 83 58.92 -160.97
REMARK 500 1 LEU A 84 -74.08 -54.29
REMARK 500 1 PRO A 85 -35.25 -39.29
REMARK 500 1 TYR A 86 -81.31 -67.55
REMARK 500 1 GLU A 87 -33.73 -39.81
REMARK 500 1 ILE A 91 -77.04 -54.82
REMARK 500 1 SER A 92 -3.66 69.58
REMARK 500 1 LYS A 97 19.35 -152.39
REMARK 500 1 GLU A 98 105.61 63.71
REMARK 500 2 ASN A 22 5.74 173.90
REMARK 500 2 LEU A 25 -79.56 -117.08
REMARK 500 2 SER A 27 114.64 163.10
REMARK 500 2 PRO A 29 60.90 -66.76
REMARK 500 2 GLU A 30 112.11 -33.38
REMARK 500 2 ASN A 33 56.39 72.58
REMARK 500 2 ARG A 34 -172.21 -177.81
REMARK 500 2 TYR A 40 -75.88 -57.02
REMARK 500 2 THR A 57 -161.67 -124.89
REMARK 500 2 VAL A 63 -75.93 -63.29
REMARK 500 2 ASP A 71 58.66 -117.81
REMARK 500 2 TYR A 72 -31.88 -34.33
REMARK 500 2 LEU A 83 55.83 -164.58
REMARK 500 2 LEU A 84 -73.60 -49.63
REMARK 500 2 MET A 90 45.49 -90.10
REMARK 500 2 SER A 92 -36.24 -177.74
REMARK 500 2 ALA A 101 80.34 -161.24
REMARK 500 2 LYS A 102 -46.82 -147.68
REMARK 500 2 ARG A 103 -46.14 -137.07
REMARK 500 3 ASN A 22 42.58 73.82
REMARK 500 3 LEU A 25 97.14 -167.90
REMARK 500 3 PRO A 29 63.95 -69.81
REMARK 500 3 GLU A 30 60.71 -67.11
REMARK 500 3 ILE A 36 161.13 55.76
REMARK 500 3 ASN A 37 46.45 174.40
REMARK 500
REMARK 500 THIS ENTRY HAS 231 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5061 RELATED DB: BMRB
REMARK 900 5061 IS CHEMICAL_SHIFTS FOR THIS PROTEIN.
REMARK 900 RELATED ID: 1KN5 RELATED DB: PDB
REMARK 900 1KN5 IS MINIMIZED AVERAGE STRUCTURE.
DBREF 1KKX A 3 104 UNP P09547 SWI1_YEAST 405 506
SEQADV 1KKX MET A -11 UNP P09547 EXPRESSION TAG
SEQADV 1KKX ARG A -10 UNP P09547 EXPRESSION TAG
SEQADV 1KKX GLY A -9 UNP P09547 EXPRESSION TAG
SEQADV 1KKX SER A -8 UNP P09547 EXPRESSION TAG
SEQADV 1KKX GLY A -7 UNP P09547 EXPRESSION TAG
SEQADV 1KKX SER A -6 UNP P09547 EXPRESSION TAG
SEQADV 1KKX HIS A -5 UNP P09547 EXPRESSION TAG
SEQADV 1KKX HIS A -4 UNP P09547 EXPRESSION TAG
SEQADV 1KKX HIS A -3 UNP P09547 EXPRESSION TAG
SEQADV 1KKX HIS A -2 UNP P09547 EXPRESSION TAG
SEQADV 1KKX HIS A -1 UNP P09547 EXPRESSION TAG
SEQADV 1KKX HIS A 0 UNP P09547 EXPRESSION TAG
SEQADV 1KKX GLY A 1 UNP P09547 EXPRESSION TAG
SEQADV 1KKX SER A 2 UNP P09547 EXPRESSION TAG
SEQADV 1KKX LEU A 105 UNP P09547 CLONING ARTIFACT
SEQADV 1KKX GLN A 106 UNP P09547 CLONING ARTIFACT
SEQADV 1KKX PRO A 107 UNP P09547 CLONING ARTIFACT
SEQADV 1KKX SER A 108 UNP P09547 CLONING ARTIFACT
SEQADV 1KKX LEU A 109 UNP P09547 CLONING ARTIFACT
SEQADV 1KKX ILE A 110 UNP P09547 CLONING ARTIFACT
SEQADV 1KKX SER A 111 UNP P09547 CLONING ARTIFACT
SEQRES 1 A 123 MET ARG GLY SER GLY SER HIS HIS HIS HIS HIS HIS GLY
SEQRES 2 A 123 SER ASN ASN LYS GLN TYR GLU LEU PHE MET LYS SER LEU
SEQRES 3 A 123 ILE GLU ASN CYS LYS LYS ARG ASN MET PRO LEU GLN SER
SEQRES 4 A 123 ILE PRO GLU ILE GLY ASN ARG LYS ILE ASN LEU PHE TYR
SEQRES 5 A 123 LEU TYR MET LEU VAL GLN LYS PHE GLY GLY ALA ASP GLN
SEQRES 6 A 123 VAL THR ARG THR GLN GLN TRP SER MET VAL ALA GLN ARG
SEQRES 7 A 123 LEU GLN ILE SER ASP TYR GLN GLN LEU GLU SER ILE TYR
SEQRES 8 A 123 PHE ARG ILE LEU LEU PRO TYR GLU ARG HIS MET ILE SER
SEQRES 9 A 123 GLN GLU GLY ILE LYS GLU THR GLN ALA LYS ARG ILE LEU
SEQRES 10 A 123 GLN PRO SER LEU ILE SER
HELIX 1 1 LYS A 5 ARG A 21 1 17
HELIX 2 2 PHE A 39 GLN A 46 1 8
HELIX 3 3 GLY A 50 THR A 55 1 6
HELIX 4 4 THR A 57 GLN A 68 1 12
HELIX 5 5 ASP A 71 MET A 90 1 20
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