Header list of 1f81.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 28-JUN-00 1F81
TITLE SOLUTION STRUCTURE OF THE TAZ2 DOMAIN OF THE TRANSCRIPTIONAL ADAPTOR
TITLE 2 PROTEIN CBP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CREB-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TAZ2 DOMAIN (1764-1850);
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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZINC FINGER, TAZ2, CBP, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.N.DE GUZMAN,H.L.LIU,M.MARTINEZ-YAMOUT,H.J.DYSON,P.E.WRIGHT
REVDAT 5 23-FEB-22 1F81 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1F81 1 VERSN
REVDAT 3 24-FEB-04 1F81 1 CRYST1
REVDAT 2 01-APR-03 1F81 1 JRNL
REVDAT 1 18-OCT-00 1F81 0
JRNL AUTH R.N.DE GUZMAN,H.Y.LIU,M.MARTINEZ-YAMOUT,H.J.DYSON,P.E.WRIGHT
JRNL TITL SOLUTION STRUCTURE OF THE TAZ2 (CH3) DOMAIN OF THE
JRNL TITL 2 TRANSCRIPTIONAL ADAPTOR PROTEIN CBP.
JRNL REF J.MOL.BIOL. V. 303 243 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11023789
JRNL DOI 10.1006/JMBI.2000.4141
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, AMBER 6
REMARK 3 AUTHORS : PETER GUNTERT (DYANA), CASE, PEARLMAN, (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F81 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011356.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.9
REMARK 210 IONIC STRENGTH : 25 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5 MM TAZ2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; HNCA-J; HNHA;
REMARK 210 CBCA(CO)HN
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AMBER 6, NMRPIPE 4
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210 MATRIX RELAXATION TORSION ANGLE
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY,TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A 0
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 CYS A 23 82.05 -66.01
REMARK 500 1 ARG A 24 47.93 -81.22
REMARK 500 1 LEU A 30 105.29 -38.58
REMARK 500 1 LYS A 49 -129.20 32.58
REMARK 500 1 GLU A 73 91.69 -64.74
REMARK 500 1 ASN A 74 45.92 -78.79
REMARK 500 1 LYS A 75 42.82 -157.49
REMARK 500 1 PHE A 80 -42.97 72.25
REMARK 500 2 CYS A 23 91.71 -60.93
REMARK 500 2 LEU A 30 107.10 -45.77
REMARK 500 2 CYS A 46 74.92 -69.70
REMARK 500 2 LYS A 49 -132.97 35.64
REMARK 500 2 GLU A 73 105.57 -53.73
REMARK 500 2 ASN A 74 44.66 -78.39
REMARK 500 2 LYS A 75 43.39 -170.44
REMARK 500 2 PHE A 80 -37.79 71.75
REMARK 500 3 CYS A 23 86.35 -62.50
REMARK 500 3 LEU A 30 103.04 -36.74
REMARK 500 3 LYS A 49 -137.58 33.29
REMARK 500 3 GLN A 72 -54.42 -120.51
REMARK 500 3 GLU A 73 97.61 -10.62
REMARK 500 3 PHE A 80 -15.93 73.49
REMARK 500 4 CYS A 23 83.53 -64.02
REMARK 500 4 LEU A 30 103.28 -34.32
REMARK 500 4 LYS A 49 -133.89 34.43
REMARK 500 4 LYS A 75 60.12 -113.11
REMARK 500 4 PHE A 80 -41.97 72.95
REMARK 500 5 ARG A 24 52.63 -94.19
REMARK 500 5 LYS A 49 84.18 -69.84
REMARK 500 5 THR A 50 -60.34 75.11
REMARK 500 5 ASN A 51 -61.89 -24.45
REMARK 500 5 GLU A 73 96.54 -56.72
REMARK 500 5 ASN A 74 42.23 -78.20
REMARK 500 5 LYS A 75 42.59 -163.43
REMARK 500 5 PHE A 80 -35.79 70.29
REMARK 500 6 CYS A 23 89.36 -63.52
REMARK 500 6 ARG A 24 49.32 -81.86
REMARK 500 6 CYS A 46 91.03 -67.71
REMARK 500 6 LYS A 49 85.12 -68.90
REMARK 500 6 THR A 50 -36.34 73.57
REMARK 500 6 GLU A 73 103.51 -49.72
REMARK 500 6 LYS A 75 44.98 -174.20
REMARK 500 6 PHE A 80 -41.98 71.20
REMARK 500 7 CYS A 23 78.39 -64.67
REMARK 500 7 LEU A 30 102.80 -32.90
REMARK 500 7 CYS A 46 75.85 -67.82
REMARK 500 7 LYS A 49 -100.24 -2.05
REMARK 500 7 PHE A 80 -44.28 72.57
REMARK 500 7 CYS A 81 -66.75 -28.44
REMARK 500 8 CYS A 23 82.70 -53.24
REMARK 500
REMARK 500 THIS ENTRY HAS 138 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 HIS A 42 0.11 SIDE CHAIN
REMARK 500 1 TYR A 66 0.12 SIDE CHAIN
REMARK 500 2 HIS A 42 0.10 SIDE CHAIN
REMARK 500 3 ARG A 24 0.11 SIDE CHAIN
REMARK 500 3 HIS A 42 0.10 SIDE CHAIN
REMARK 500 3 TYR A 66 0.16 SIDE CHAIN
REMARK 500 3 HIS A 67 0.09 SIDE CHAIN
REMARK 500 4 HIS A 42 0.10 SIDE CHAIN
REMARK 500 4 TYR A 66 0.10 SIDE CHAIN
REMARK 500 4 HIS A 67 0.10 SIDE CHAIN
REMARK 500 5 ARG A 24 0.10 SIDE CHAIN
REMARK 500 5 HIS A 42 0.12 SIDE CHAIN
REMARK 500 5 TYR A 66 0.17 SIDE CHAIN
REMARK 500 6 HIS A 42 0.11 SIDE CHAIN
REMARK 500 6 TYR A 66 0.15 SIDE CHAIN
REMARK 500 7 ARG A 7 0.08 SIDE CHAIN
REMARK 500 7 HIS A 42 0.10 SIDE CHAIN
REMARK 500 7 TYR A 66 0.09 SIDE CHAIN
REMARK 500 8 HIS A 42 0.11 SIDE CHAIN
REMARK 500 8 TYR A 66 0.17 SIDE CHAIN
REMARK 500 9 HIS A 42 0.11 SIDE CHAIN
REMARK 500 9 TYR A 66 0.11 SIDE CHAIN
REMARK 500 10 HIS A 42 0.10 SIDE CHAIN
REMARK 500 10 TYR A 66 0.15 SIDE CHAIN
REMARK 500 11 HIS A 42 0.12 SIDE CHAIN
REMARK 500 11 ARG A 48 0.11 SIDE CHAIN
REMARK 500 11 TYR A 66 0.17 SIDE CHAIN
REMARK 500 12 HIS A 42 0.10 SIDE CHAIN
REMARK 500 12 TYR A 66 0.14 SIDE CHAIN
REMARK 500 13 HIS A 42 0.10 SIDE CHAIN
REMARK 500 13 TYR A 66 0.16 SIDE CHAIN
REMARK 500 13 HIS A 67 0.09 SIDE CHAIN
REMARK 500 14 ARG A 24 0.13 SIDE CHAIN
REMARK 500 14 HIS A 42 0.10 SIDE CHAIN
REMARK 500 14 TYR A 66 0.11 SIDE CHAIN
REMARK 500 15 TYR A 66 0.16 SIDE CHAIN
REMARK 500 16 HIS A 42 0.10 SIDE CHAIN
REMARK 500 16 TYR A 66 0.09 SIDE CHAIN
REMARK 500 17 ARG A 24 0.10 SIDE CHAIN
REMARK 500 17 HIS A 42 0.11 SIDE CHAIN
REMARK 500 17 TYR A 66 0.21 SIDE CHAIN
REMARK 500 18 HIS A 42 0.12 SIDE CHAIN
REMARK 500 18 TYR A 66 0.16 SIDE CHAIN
REMARK 500 19 HIS A 42 0.11 SIDE CHAIN
REMARK 500 19 ARG A 48 0.12 SIDE CHAIN
REMARK 500 19 TYR A 66 0.14 SIDE CHAIN
REMARK 500 20 HIS A 42 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 88 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 19 NE2
REMARK 620 2 CYS A 23 SG 106.6
REMARK 620 3 CYS A 28 SG 111.5 107.0
REMARK 620 4 CYS A 33 SG 110.9 109.5 111.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 89 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 42 NE2
REMARK 620 2 CYS A 46 SG 108.5
REMARK 620 3 CYS A 54 SG 111.4 110.3
REMARK 620 4 CYS A 57 SG 111.3 107.6 107.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 90 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 67 NE2
REMARK 620 2 CYS A 71 SG 106.8
REMARK 620 3 CYS A 76 SG 106.6 109.8
REMARK 620 4 CYS A 81 SG 108.8 110.2 114.4
REMARK 620 N 1 2 3
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 88
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 89
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 90
DBREF 1F81 A 1 87 UNP P45481 CBP_MOUSE 1764 1850
SEQADV 1F81 MET A 0 UNP P45481 CLONING ARTIFACT
SEQADV 1F81 LYS A 87 UNP P45481 ASN 1850 CONFLICT
SEQRES 1 A 88 MET SER PRO GLN GLU SER ARG ARG LEU SER ILE GLN ARG
SEQRES 2 A 88 CYS ILE GLN SER LEU VAL HIS ALA CYS GLN CYS ARG ASN
SEQRES 3 A 88 ALA ASN CYS SER LEU PRO SER CYS GLN LYS MET LYS ARG
SEQRES 4 A 88 VAL VAL GLN HIS THR LYS GLY CYS LYS ARG LYS THR ASN
SEQRES 5 A 88 GLY GLY CYS PRO VAL CYS LYS GLN LEU ILE ALA LEU CYS
SEQRES 6 A 88 CYS TYR HIS ALA LYS HIS CYS GLN GLU ASN LYS CYS PRO
SEQRES 7 A 88 VAL PRO PHE CYS LEU ASN ILE LYS HIS LYS
HET ZN A 88 1
HET ZN A 89 1
HET ZN A 90 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 3(ZN 2+)
HELIX 1 1 SER A 1 CYS A 23 1 23
HELIX 2 2 LEU A 30 CYS A 46 1 17
HELIX 3 3 ARG A 48 GLY A 53 1 6
HELIX 4 4 CYS A 54 CYS A 71 1 18
HELIX 5 5 PHE A 80 LYS A 87 1 8
LINK NE2 HIS A 19 ZN ZN A 88 1555 1555 2.10
LINK SG CYS A 23 ZN ZN A 88 1555 1555 2.30
LINK SG CYS A 28 ZN ZN A 88 1555 1555 2.30
LINK SG CYS A 33 ZN ZN A 88 1555 1555 2.31
LINK NE2 HIS A 42 ZN ZN A 89 1555 1555 2.10
LINK SG CYS A 46 ZN ZN A 89 1555 1555 2.30
LINK SG CYS A 54 ZN ZN A 89 1555 1555 2.29
LINK SG CYS A 57 ZN ZN A 89 1555 1555 2.30
LINK NE2 HIS A 67 ZN ZN A 90 1555 1555 2.08
LINK SG CYS A 71 ZN ZN A 90 1555 1555 2.30
LINK SG CYS A 76 ZN ZN A 90 1555 1555 2.29
LINK SG CYS A 81 ZN ZN A 90 1555 1555 2.30
SITE 1 AC1 4 HIS A 19 CYS A 23 CYS A 28 CYS A 33
SITE 1 AC2 4 HIS A 42 CYS A 46 CYS A 54 CYS A 57
SITE 1 AC3 4 HIS A 67 CYS A 71 CYS A 76 CYS A 81
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