Header list of 1se9.pdb file
Complete list - r 2 2 Bytes
HEADER PLANT PROTEIN 16-FEB-04 1SE9
TITLE STRUCTURE OF AT3G01050, A UBIQUITIN-FOLD PROTEIN FROM ARABIDOPSIS
TITLE 2 THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN FAMILY;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: AT3G01050
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: AT3G01050;
SOURCE 6 EXPRESSION_SYSTEM: CELL-FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEU-AT3G01050;
SOURCE 9 OTHER_DETAILS: WHEAT GERM CELL-FREE, IN VITRO EXPRESSION
KEYWDS UBIQUITIN-LIKE, CELL-FREE, WHEAT GERM, STRUCTURAL GENOMICS, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, CESG, PSI, CENTER FOR EUKARYOTIC STRUCTURAL
KEYWDS 3 GENOMICS, PLANT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.F.VOLKMAN,B.L.LYTLE,F.C.PETERSON,CENTER FOR EUKARYOTIC STRUCTURAL
AUTHOR 2 GENOMICS (CESG)
REVDAT 8 02-MAR-22 1SE9 1 REMARK SEQADV
REVDAT 7 24-FEB-09 1SE9 1 VERSN
REVDAT 6 29-APR-08 1SE9 1 SOURCE
REVDAT 5 12-FEB-08 1SE9 1 REMARK
REVDAT 4 08-AUG-06 1SE9 1 JRNL
REVDAT 3 01-FEB-05 1SE9 1 AUTHOR KEYWDS REMARK
REVDAT 2 12-OCT-04 1SE9 1 KEYWDS
REVDAT 1 24-FEB-04 1SE9 0
JRNL AUTH D.A.VINAROV,B.L.LYTLE,F.C.PETERSON,E.M.TYLER,B.F.VOLKMAN,
JRNL AUTH 2 J.L.MARKLEY
JRNL TITL CELL-FREE PROTEIN PRODUCTION AND LABELING PROTOCOL FOR
JRNL TITL 2 NMR-BASED STRUCTURAL PROTEOMICS.
JRNL REF NAT.METHODS V. 1 149 2004
JRNL REFN ISSN 1548-7091
JRNL PMID 15782178
JRNL DOI 10.1038/NMETH716
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1.0.6, XPLOR-NIH 2.0.6
REMARK 3 AUTHORS : PETER GUENTERT (CYANA), MARIUS CLORE (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CANDID AUTOMATED REFINEMENT
REMARK 3 CYANA REFINEMENT
REMARK 3 XPLOR WATER REFINEMENT
REMARK 4
REMARK 4 1SE9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000021635.
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 : 50 MM NACL + 10 MM KPO4
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5 MM U-15N,13C AT3G01050; 10MM
REMARK 210 PHOSPHATE BUFFER, 50MM KCL, 1MM
REMARK 210 DTT, PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D 13C-
REMARK 210 SEPARATED NOESY-AROMATIC
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, NMRPIPE 2.1, XEASY
REMARK 210 1.3.1, SPSCAN 1.1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED
REMARK 210 BY CARTESIAN MOLECULAR DYNAMICS
REMARK 210 IN EXPLICIT SOLVENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: CHEMICAL SHIFT ASSIGNMENTS WERE OBTAINED FROM STANDARD 3D
REMARK 210 TRIPLE-RESONANCE EXPERIMENTS, USING THE AUTOMATED METHOD OF
REMARK 210 GARANT (CHRISTIAN BARTELS).
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 -8
REMARK 465 GLY A -7
REMARK 465 HIS 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 LEU A 0
REMARK 465 LYS A 102
REMARK 465 PRO A 103
REMARK 465 LYS A 104
REMARK 465 GLY A 105
REMARK 465 ASP A 106
REMARK 465 PRO A 107
REMARK 465 LYS A 108
REMARK 465 MET A 109
REMARK 465 ASN A 110
REMARK 465 LYS A 111
REMARK 465 CYS A 112
REMARK 465 VAL A 113
REMARK 465 CYS A 114
REMARK 465 SER A 115
REMARK 465 VAL A 116
REMARK 465 MET A 117
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 HG1 THR A 70 OD1 ASP A 73 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 VAL A 4 97.27 49.68
REMARK 500 1 GLN A 7 -168.74 -109.97
REMARK 500 1 ASN A 48 74.47 62.09
REMARK 500 1 PRO A 50 172.06 -55.47
REMARK 500 1 LYS A 51 -16.63 175.98
REMARK 500 1 PRO A 77 -177.63 -63.93
REMARK 500 1 THR A 97 84.86 57.07
REMARK 500 1 LYS A 99 109.56 -174.00
REMARK 500 1 GLU A 100 -94.10 38.64
REMARK 500 2 HIS A 5 -52.16 -135.55
REMARK 500 2 PRO A 50 94.39 -61.19
REMARK 500 2 LYS A 51 -64.60 -93.85
REMARK 500 2 GLU A 98 100.18 172.88
REMARK 500 3 GLU A 3 82.30 43.29
REMARK 500 3 LYS A 51 -35.48 -130.19
REMARK 500 3 GLU A 100 -93.31 -100.63
REMARK 500 4 ASN A 48 69.37 -62.68
REMARK 500 4 LYS A 51 -36.87 -168.36
REMARK 500 4 PRO A 77 136.39 -39.20
REMARK 500 4 VAL A 78 -3.99 74.75
REMARK 500 4 SER A 79 103.01 69.84
REMARK 500 5 ASN A 48 38.78 -70.47
REMARK 500 5 LYS A 51 -20.58 -148.84
REMARK 500 5 VAL A 78 89.14 49.29
REMARK 500 5 ASN A 80 -65.93 -97.00
REMARK 500 5 ALA A 82 91.27 63.57
REMARK 500 5 GLU A 98 99.11 -164.86
REMARK 500 5 LYS A 99 99.87 66.83
REMARK 500 6 GLU A 3 108.77 -43.07
REMARK 500 6 PRO A 43 117.51 -33.70
REMARK 500 6 PRO A 50 47.53 -72.24
REMARK 500 6 PRO A 77 107.92 -56.14
REMARK 500 6 VAL A 78 -75.91 -127.39
REMARK 500 6 LYS A 99 98.95 68.29
REMARK 500 7 ASN A 6 -31.92 179.40
REMARK 500 7 GLU A 47 -160.74 -70.99
REMARK 500 7 PRO A 50 -179.20 -58.61
REMARK 500 7 LYS A 51 -68.92 -167.31
REMARK 500 7 ALA A 82 129.32 -179.17
REMARK 500 7 GLU A 98 94.15 -67.09
REMARK 500 7 LYS A 99 81.28 177.83
REMARK 500 7 GLU A 100 -37.20 -146.12
REMARK 500 8 ALA A 2 120.37 68.36
REMARK 500 8 LYS A 51 -60.71 -159.43
REMARK 500 8 VAL A 78 109.18 58.64
REMARK 500 8 LYS A 99 115.23 72.98
REMARK 500 9 HIS A 5 -9.80 82.27
REMARK 500 9 GLN A 7 -100.39 -73.20
REMARK 500 9 PRO A 50 157.49 -43.70
REMARK 500 9 LYS A 51 -53.46 -135.61
REMARK 500
REMARK 500 THIS ENTRY HAS 115 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GO.15176 RELATED DB: TARGETDB
DBREF 1SE9 A 2 117 UNP Q9MAB9 Y3105_ARATH 2 117
SEQADV 1SE9 MET A -8 UNP Q9MAB9 INSERTION
SEQADV 1SE9 GLY A -7 UNP Q9MAB9 INSERTION
SEQADV 1SE9 HIS A -6 UNP Q9MAB9 INSERTION
SEQADV 1SE9 HIS A -5 UNP Q9MAB9 INSERTION
SEQADV 1SE9 HIS A -4 UNP Q9MAB9 INSERTION
SEQADV 1SE9 HIS A -3 UNP Q9MAB9 INSERTION
SEQADV 1SE9 HIS A -2 UNP Q9MAB9 INSERTION
SEQADV 1SE9 HIS A -1 UNP Q9MAB9 INSERTION
SEQADV 1SE9 LEU A 0 UNP Q9MAB9 INSERTION
SEQADV 1SE9 GLU A 1 UNP Q9MAB9 INSERTION
SEQRES 1 A 126 MET GLY HIS HIS HIS HIS HIS HIS LEU GLU ALA GLU VAL
SEQRES 2 A 126 HIS ASN GLN LEU GLU ILE LYS PHE ARG LEU THR ASP GLY
SEQRES 3 A 126 SER ASP ILE GLY PRO LYS ALA PHE PRO ASP ALA THR THR
SEQRES 4 A 126 VAL SER ALA LEU LYS GLU THR VAL ILE SER GLU TRP PRO
SEQRES 5 A 126 ARG GLU LYS GLU ASN GLY PRO LYS THR VAL LYS GLU VAL
SEQRES 6 A 126 LYS LEU ILE SER ALA GLY LYS VAL LEU GLU ASN SER LYS
SEQRES 7 A 126 THR VAL LYS ASP TYR ARG SER PRO VAL SER ASN LEU ALA
SEQRES 8 A 126 GLY ALA VAL THR THR MET HIS VAL ILE ILE GLN ALA PRO
SEQRES 9 A 126 VAL THR GLU LYS GLU LYS LYS PRO LYS GLY ASP PRO LYS
SEQRES 10 A 126 MET ASN LYS CYS VAL CYS SER VAL MET
HELIX 1 1 THR A 30 TRP A 42 1 13
HELIX 2 2 THR A 52 LYS A 54 5 3
HELIX 3 3 THR A 70 ARG A 75 5 6
SHEET 1 A 5 ASP A 19 PHE A 25 0
SHEET 2 A 5 LEU A 8 LEU A 14 -1 N PHE A 12 O ILE A 20
SHEET 3 A 5 THR A 86 ILE A 92 1 O THR A 86 N GLU A 9
SHEET 4 A 5 VAL A 56 SER A 60 -1 N ILE A 59 O HIS A 89
SHEET 5 A 5 LYS A 63 VAL A 64 -1 O LYS A 63 N SER A 60
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