Header list of 1xo8.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 06-OCT-04 1XO8
TITLE SOLUTION STRUCTURE OF AT1G01470 FROM ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AT1G01470;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, CENTER FOR
KEYWDS 2 EUKARYOTIC STRUCTURAL GENOMICS, PSI, CESG, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.SINGH,C.C.CORNILESCU,R.C.TYLER,G.CORNILESCU,M.TONELLI,M.S.LEE,
AUTHOR 2 J.L.MARKLEY,CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS (CESG)
REVDAT 8 02-MAR-22 1XO8 1 REMARK
REVDAT 7 24-FEB-09 1XO8 1 VERSN
REVDAT 6 12-FEB-08 1XO8 1 REMARK
REVDAT 5 12-JUN-07 1XO8 1 AUTHOR
REVDAT 4 25-JUL-06 1XO8 1 JRNL
REVDAT 3 31-MAY-05 1XO8 1 JRNL
REVDAT 2 01-FEB-05 1XO8 1 AUTHOR KEYWDS REMARK
REVDAT 1 19-OCT-04 1XO8 0
JRNL AUTH S.SINGH,C.C.CORNILESCU,R.C.TYLER,G.CORNILESCU,M.TONELLI,
JRNL AUTH 2 M.S.LEE,J.L.MARKLEY
JRNL TITL SOLUTION STRUCTURE OF A LATE EMBRYOGENESIS ABUNDANT PROTEIN
JRNL TITL 2 (LEA14) FROM ARABIDOPSIS THALIANA, A CELLULAR STRESS-RELATED
JRNL TITL 3 PROTEIN
JRNL REF PROTEIN SCI. V. 14 2601 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 16155204
JRNL DOI 10.1110/PS.051579205
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.2, ARIA 1.2
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XO8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030572.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 10MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM 15N,13C-LABELLED AT1G01470,
REMARK 210 10MM PHOSPHATE BUFFER, 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_ROESY; 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 : NMRVIEW 5.1.0, CNS 1.1, ARIA 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, TORSION ANGLE AND
REMARK 210 CARTESIAN COORDINATE DYNAMICS;
REMARK 210 WATER REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 1
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 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 HB3 GLU A 59 HB THR A 123 1.17
REMARK 500 HB3 GLU A 40 HB VAL A 94 1.32
REMARK 500 HE1 TYR A 41 HB1 ALA A 43 1.32
REMARK 500 O HIS A 65 H GLU A 117 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 3 TYR A 98 CZ TYR A 98 CE2 0.082
REMARK 500 4 TYR A 98 CE1 TYR A 98 CZ 0.099
REMARK 500 4 TYR A 98 CZ TYR A 98 CE2 -0.106
REMARK 500 8 TYR A 41 CZ TYR A 41 CE2 -0.081
REMARK 500 15 TYR A 98 CE1 TYR A 98 CZ 0.083
REMARK 500 15 TYR A 98 CZ TYR A 98 CE2 -0.090
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 LEU A 4 61.58 -111.04
REMARK 500 1 ASP A 6 131.17 69.92
REMARK 500 1 LYS A 9 -93.61 -107.77
REMARK 500 1 ASP A 10 -85.35 57.47
REMARK 500 1 ALA A 13 -56.35 -177.62
REMARK 500 1 LEU A 16 153.08 69.89
REMARK 500 1 THR A 17 -57.44 -154.87
REMARK 500 1 ALA A 18 -165.58 -161.72
REMARK 500 1 PRO A 20 -91.19 -66.23
REMARK 500 1 LYS A 21 -45.52 167.43
REMARK 500 1 PRO A 22 58.46 -68.72
REMARK 500 1 SER A 25 33.14 -169.51
REMARK 500 1 THR A 27 -45.31 -174.92
REMARK 500 1 LYS A 32 -91.59 -138.68
REMARK 500 1 VAL A 34 -37.93 -166.78
REMARK 500 1 ASN A 35 -81.92 67.16
REMARK 500 1 ARG A 36 14.24 -172.11
REMARK 500 1 ASP A 37 -39.05 -131.33
REMARK 500 1 SER A 52 31.10 -74.88
REMARK 500 1 SER A 54 110.22 -39.88
REMARK 500 1 PRO A 56 -62.83 -92.75
REMARK 500 1 SER A 66 -91.17 -103.84
REMARK 500 1 ARG A 69 -78.31 -100.17
REMARK 500 1 GLU A 70 -177.34 -171.40
REMARK 500 1 ILE A 71 -35.77 -135.18
REMARK 500 1 PRO A 79 82.66 -63.88
REMARK 500 1 LEU A 82 -156.93 -152.81
REMARK 500 1 LYS A 83 -97.54 -63.82
REMARK 500 1 ALA A 84 106.09 169.40
REMARK 500 1 PRO A 93 -121.15 -49.75
REMARK 500 1 VAL A 94 88.86 -157.37
REMARK 500 1 ASP A 111 -90.41 -67.09
REMARK 500 1 TRP A 112 -45.89 172.44
REMARK 500 1 GLU A 131 146.29 -175.75
REMARK 500 1 PRO A 145 172.26 -55.89
REMARK 500 1 LYS A 148 -50.90 -176.55
REMARK 500 1 ASP A 149 39.42 -148.45
REMARK 500 2 PHE A 11 -58.64 -142.74
REMARK 500 2 ASP A 14 -71.27 -54.72
REMARK 500 2 PRO A 20 -94.96 -81.71
REMARK 500 2 LYS A 21 -54.07 167.22
REMARK 500 2 SER A 25 36.94 -166.57
REMARK 500 2 THR A 27 -50.71 -175.12
REMARK 500 2 LYS A 32 -115.21 -135.45
REMARK 500 2 VAL A 34 -34.30 -155.49
REMARK 500 2 ASN A 35 -77.88 68.34
REMARK 500 2 ARG A 36 10.14 -174.60
REMARK 500 2 SER A 52 13.86 84.16
REMARK 500 2 SER A 54 96.70 -41.89
REMARK 500 2 SER A 66 -97.53 -106.78
REMARK 500
REMARK 500 THIS ENTRY HAS 534 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 23 GLY A 24 16 -143.06
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 TYR A 41 0.05 SIDE CHAIN
REMARK 500 3 TYR A 98 0.06 SIDE CHAIN
REMARK 500 17 TYR A 98 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GO.2361 RELATED DB: TARGETDB
DBREF 1XO8 A 1 151 UNP O03983 LEA14_ARATH 1 151
SEQRES 1 A 151 MET ALA SER LEU LEU ASP LYS ALA LYS ASP PHE VAL ALA
SEQRES 2 A 151 ASP LYS LEU THR ALA ILE PRO LYS PRO GLU GLY SER VAL
SEQRES 3 A 151 THR ASP VAL ASP LEU LYS ASP VAL ASN ARG ASP SER VAL
SEQRES 4 A 151 GLU TYR LEU ALA LYS VAL SER VAL THR ASN PRO TYR SER
SEQRES 5 A 151 HIS SER ILE PRO ILE CYS GLU ILE SER PHE THR PHE HIS
SEQRES 6 A 151 SER ALA GLY ARG GLU ILE GLY LYS GLY LYS ILE PRO ASP
SEQRES 7 A 151 PRO GLY SER LEU LYS ALA LYS ASP MET THR ALA LEU ASP
SEQRES 8 A 151 ILE PRO VAL VAL VAL PRO TYR SER ILE LEU PHE ASN LEU
SEQRES 9 A 151 ALA ARG ASP VAL GLY VAL ASP TRP ASP ILE ASP TYR GLU
SEQRES 10 A 151 LEU GLN ILE GLY LEU THR ILE ASP LEU PRO VAL VAL GLY
SEQRES 11 A 151 GLU PHE THR ILE PRO ILE SER SER LYS GLY GLU ILE LYS
SEQRES 12 A 151 LEU PRO THR PHE LYS ASP PHE PHE
HELIX 1 1 TYR A 98 TRP A 112 1 15
SHEET 1 A 3 ASP A 28 LEU A 31 0
SHEET 2 A 3 TYR A 41 THR A 48 -1 O LEU A 42 N ASP A 30
SHEET 3 A 3 MET A 87 ILE A 92 -1 O LEU A 90 N VAL A 45
SHEET 1 B 2 SER A 38 VAL A 39 0
SHEET 2 B 2 VAL A 96 PRO A 97 -1 O VAL A 96 N VAL A 39
SHEET 1 C 4 ILE A 71 ASP A 78 0
SHEET 2 C 4 CYS A 58 HIS A 65 -1 N CYS A 58 O ASP A 78
SHEET 3 C 4 ASP A 113 ILE A 124 -1 O GLU A 117 N HIS A 65
SHEET 4 C 4 PHE A 132 LYS A 143 -1 O ILE A 134 N LEU A 122
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