Header list of 1tey.pdb file
Complete list - r 2 2 Bytes
HEADER CHAPERONE 26-MAY-04 1TEY
TITLE NMR STRUCTURE OF HUMAN HISTONE CHAPERONE, ASF1A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASF1 ANTI-SILENCING FUNCTION 1 HOMOLOG A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (RESIDUES 1-156);
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: ASF1A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM30
KEYWDS BETA-SANDWICH, DISTORTED IMMUNOGLOBULIN-LIKE, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.MOUSSON,A.LAUTRETTE,J.Y.THURET,M.AGEZ,B.AMIGUES,R.COURBEYRETTE,
AUTHOR 2 J.M.NEUMANN,R.GUEROIS,C.MANN,F.OCHSENBEIN
REVDAT 4 02-MAR-22 1TEY 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1TEY 1 VERSN
REVDAT 2 17-MAY-05 1TEY 1 JRNL
REVDAT 1 12-APR-05 1TEY 0
JRNL AUTH F.MOUSSON,A.LAUTRETTE,J.Y.THURET,M.AGEZ,R.COURBEYRETTE,
JRNL AUTH 2 B.AMIGUES,E.BECKER,J.M.NEUMANN,R.GUEROIS,C.MANN,F.OCHSENBEIN
JRNL TITL STRUCTURAL BASIS FOR THE INTERACTION OF ASF1 WITH HISTONE H3
JRNL TITL 2 AND ITS FUNCTIONAL IMPLICATIONS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 5975 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15840725
JRNL DOI 10.1073/PNAS.0500149102
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.MOUSSON,J.COUPRIE,J.Y.THURET,J.M.NEUMANN,C.MANN,
REMARK 1 AUTH 2 F.OCHSENBEIN
REMARK 1 TITL 1H, 13C AND 15N RESONANCE ASSIGNMENTS OF THE CONSERVED CORE
REMARK 1 TITL 2 OF HASF1A
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, ARIA 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), J.LINGE, S.O'DONOGHUE, M.NILGES
REMARK 3 (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 4489 RESTRAINTS, 4257 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 170
REMARK 3 DIHEDRAL ANGLE RESTRAINTS FROM J COUPLING MEASUREMENTS AND TALOS,
REMARK 3 62 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1TEY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022594.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 20 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM ASF1A U-15N,13C; 20MM TRIS
REMARK 210 -D11; 1MM EDTA; 0.1MM DSS; 0.1
REMARK 210 MM NAN3; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.1, SPARKY 3.106
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS FOLLOWED BY
REMARK 210 CARTESIAN DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 GLY A -1
REMARK 465 ALA A 0
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 HH TYR A 44 HH12 ARG A 137 1.16
REMARK 500 HG2 PRO A 85 HB3 ASP A 88 1.25
REMARK 500 HZ3 LYS A 3 OE1 GLU A 154 1.57
REMARK 500 OD1 ASP A 86 HZ1 LYS A 129 1.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 4 TYR A 53 CE1 TYR A 53 CZ 0.091
REMARK 500 4 TYR A 53 CZ TYR A 53 CE2 -0.095
REMARK 500 10 TYR A 101 CZ TYR A 101 CE2 -0.083
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 7 -60.88 -105.54
REMARK 500 1 ASP A 13 -25.81 72.75
REMARK 500 1 PHE A 22 93.71 -69.41
REMARK 500 1 LEU A 57 -63.19 -99.81
REMARK 500 1 VAL A 90 40.16 -86.23
REMARK 500 2 ALA A 2 -84.63 -99.88
REMARK 500 2 ASN A 7 -56.06 -133.94
REMARK 500 2 PRO A 17 154.41 -49.92
REMARK 500 2 VAL A 90 40.51 -95.14
REMARK 500 2 VAL A 128 -34.76 -39.61
REMARK 500 3 ASN A 7 -60.39 -127.45
REMARK 500 3 ASP A 13 34.32 70.16
REMARK 500 3 VAL A 90 40.11 -96.12
REMARK 500 3 LEU A 140 88.29 -67.04
REMARK 500 3 ASP A 155 79.04 -116.02
REMARK 500 4 ASN A 7 -61.62 -132.57
REMARK 500 4 GLU A 51 -34.68 68.11
REMARK 500 4 VAL A 128 -64.70 -23.64
REMARK 500 5 LEU A 140 88.78 -67.07
REMARK 500 6 PHE A 18 -29.86 -39.28
REMARK 500 6 GLU A 51 21.59 -79.16
REMARK 500 7 ASN A 7 -56.21 -124.16
REMARK 500 7 PRO A 17 152.65 -48.59
REMARK 500 9 ALA A 2 -84.47 -101.53
REMARK 500 9 ASN A 7 -75.11 -99.13
REMARK 500 9 PRO A 130 171.83 -57.10
REMARK 500 10 ASN A 7 -72.28 -79.37
REMARK 500 10 ASP A 13 -4.11 70.80
REMARK 500 10 ASP A 77 -166.85 -77.67
REMARK 500 10 GLU A 154 -149.09 -118.68
REMARK 500 12 ASN A 7 -63.92 -102.69
REMARK 500 12 PRO A 79 178.99 -59.64
REMARK 500 13 ASN A 7 -61.37 -134.29
REMARK 500 13 ASP A 13 -1.47 70.00
REMARK 500 13 PHE A 18 -32.00 -38.90
REMARK 500 13 ASP A 77 -163.37 -68.92
REMARK 500 13 VAL A 90 40.24 -95.46
REMARK 500 14 ASN A 7 -67.73 -90.85
REMARK 500 14 ASP A 13 -16.06 73.04
REMARK 500 14 VAL A 90 40.04 -97.25
REMARK 500 15 ASN A 7 -64.90 -106.58
REMARK 500 15 VAL A 90 41.35 -88.54
REMARK 500 15 ASN A 143 76.39 -117.07
REMARK 500 16 ALA A 2 -70.89 -84.73
REMARK 500 16 ASP A 13 -4.29 78.22
REMARK 500 16 VAL A 90 41.75 -91.89
REMARK 500 16 GLU A 154 -149.50 -116.26
REMARK 500 17 PRO A 17 153.46 -48.69
REMARK 500 17 PHE A 22 99.74 -64.56
REMARK 500 17 GLU A 51 -24.25 66.75
REMARK 500
REMARK 500 THIS ENTRY HAS 62 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 17 TYR A 117 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TEY A 1 156 UNP Q9Y294 Q9Y294_HUMAN 1 156
SEQADV 1TEY GLY A -1 UNP Q9Y294 CLONING ARTIFACT
SEQADV 1TEY ALA A 0 UNP Q9Y294 CLONING ARTIFACT
SEQRES 1 A 158 GLY ALA MET ALA LYS VAL GLN VAL ASN ASN VAL VAL VAL
SEQRES 2 A 158 LEU ASP ASN PRO SER PRO PHE TYR ASN PRO PHE GLN PHE
SEQRES 3 A 158 GLU ILE THR PHE GLU CYS ILE GLU ASP LEU SER GLU ASP
SEQRES 4 A 158 LEU GLU TRP LYS ILE ILE TYR VAL GLY SER ALA GLU SER
SEQRES 5 A 158 GLU GLU TYR ASP GLN VAL LEU ASP SER VAL LEU VAL GLY
SEQRES 6 A 158 PRO VAL PRO ALA GLY ARG HIS MET PHE VAL PHE GLN ALA
SEQRES 7 A 158 ASP ALA PRO ASN PRO GLY LEU ILE PRO ASP ALA ASP ALA
SEQRES 8 A 158 VAL GLY VAL THR VAL VAL LEU ILE THR CYS THR TYR ARG
SEQRES 9 A 158 GLY GLN GLU PHE ILE ARG VAL GLY TYR TYR VAL ASN ASN
SEQRES 10 A 158 GLU TYR THR GLU THR GLU LEU ARG GLU ASN PRO PRO VAL
SEQRES 11 A 158 LYS PRO ASP PHE SER LYS LEU GLN ARG ASN ILE LEU ALA
SEQRES 12 A 158 SER ASN PRO ARG VAL THR ARG PHE HIS ILE ASN TRP GLU
SEQRES 13 A 158 ASP ASN
HELIX 1 1 SER A 50 ASP A 54 5 5
HELIX 2 2 PRO A 85 VAL A 90 1 6
HELIX 3 3 GLU A 119 ASN A 125 1 7
SHEET 1 A 3 VAL A 4 LEU A 12 0
SHEET 2 A 3 PHE A 22 CYS A 30 -1 O THR A 27 N ASN A 8
SHEET 3 A 3 GLY A 68 ALA A 76 -1 O GLY A 68 N CYS A 30
SHEET 1 B 6 SER A 16 PRO A 17 0
SHEET 2 B 6 LEU A 135 ARG A 148 -1 O ARG A 137 N SER A 16
SHEET 3 B 6 GLN A 104 TYR A 117 -1 N ASN A 114 O ASN A 138
SHEET 4 B 6 VAL A 92 TYR A 101 -1 N VAL A 95 O TYR A 111
SHEET 5 B 6 LEU A 38 TYR A 44 -1 N GLU A 39 O THR A 100
SHEET 6 B 6 GLN A 55 VAL A 62 -1 O VAL A 60 N TRP A 40
CISPEP 1 ASN A 14 PRO A 15 1 -2.40
CISPEP 2 GLY A 63 PRO A 64 1 -10.83
CISPEP 3 ASN A 14 PRO A 15 2 -9.23
CISPEP 4 GLY A 63 PRO A 64 2 -11.49
CISPEP 5 ASN A 14 PRO A 15 3 -3.16
CISPEP 6 GLY A 63 PRO A 64 3 -14.17
CISPEP 7 ASN A 14 PRO A 15 4 -3.16
CISPEP 8 GLY A 63 PRO A 64 4 -14.20
CISPEP 9 ASN A 14 PRO A 15 5 -11.89
CISPEP 10 GLY A 63 PRO A 64 5 -12.84
CISPEP 11 ASN A 14 PRO A 15 6 -5.67
CISPEP 12 GLY A 63 PRO A 64 6 -7.43
CISPEP 13 ASN A 14 PRO A 15 7 -0.75
CISPEP 14 GLY A 63 PRO A 64 7 -13.72
CISPEP 15 ASN A 14 PRO A 15 8 -5.92
CISPEP 16 GLY A 63 PRO A 64 8 -12.60
CISPEP 17 ASN A 14 PRO A 15 9 -8.79
CISPEP 18 GLY A 63 PRO A 64 9 -14.74
CISPEP 19 ASN A 14 PRO A 15 10 -13.61
CISPEP 20 GLY A 63 PRO A 64 10 -13.33
CISPEP 21 ASN A 14 PRO A 15 11 -3.85
CISPEP 22 GLY A 63 PRO A 64 11 -16.24
CISPEP 23 ASN A 14 PRO A 15 12 -4.88
CISPEP 24 GLY A 63 PRO A 64 12 -18.56
CISPEP 25 ASN A 14 PRO A 15 13 -3.33
CISPEP 26 GLY A 63 PRO A 64 13 -16.23
CISPEP 27 ASN A 14 PRO A 15 14 -7.55
CISPEP 28 GLY A 63 PRO A 64 14 -16.15
CISPEP 29 ASN A 14 PRO A 15 15 -10.00
CISPEP 30 GLY A 63 PRO A 64 15 -16.76
CISPEP 31 ASN A 14 PRO A 15 16 -2.67
CISPEP 32 GLY A 63 PRO A 64 16 -13.68
CISPEP 33 ASN A 14 PRO A 15 17 -5.43
CISPEP 34 GLY A 63 PRO A 64 17 -14.56
CISPEP 35 ASN A 14 PRO A 15 18 -8.40
CISPEP 36 GLY A 63 PRO A 64 18 -11.82
CISPEP 37 ASN A 14 PRO A 15 19 -6.11
CISPEP 38 GLY A 63 PRO A 64 19 -13.63
CISPEP 39 ASN A 14 PRO A 15 20 -6.15
CISPEP 40 GLY A 63 PRO A 64 20 -14.64
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 - r 2 2 Bytes