Header list of 1ydu.pdb file
Complete list - t 20 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 26-DEC-04 1YDU
TITLE SOLUTION NMR STRUCTURE OF AT5G01610, AN ARABIDOPSIS THALIANA PROTEIN
TITLE 2 CONTAINING DUF538 DOMAIN
CAVEAT 1YDU CHIRALITY ERROR CHIRAL CENTER CA 73 THR A MODEL 8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AT5G01610;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AT5G01610;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 ARABIDOPSIS, DUF538, STRUCTURAL GENOMICS, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS, CESG, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Q.ZHAO,C.C.CORNILESCU,M.S.LEE,J.L.MARKLEY,CENTER FOR EUKARYOTIC
AUTHOR 2 STRUCTURAL GENOMICS (CESG)
REVDAT 5 20-OCT-21 1YDU 1 REMARK SEQADV
REVDAT 4 06-APR-16 1YDU 1 AUTHOR VERSN
REVDAT 3 24-FEB-09 1YDU 1 VERSN
REVDAT 2 12-FEB-08 1YDU 1 REMARK
REVDAT 1 15-FEB-05 1YDU 0
JRNL AUTH Q.ZHAO,C.CORNILESCU,M.S.LEE,J.L.MARKLEY
JRNL TITL SOLUTION NMR STRUCTURE OF AT5G01610, AN ARABIDOPSIS THALIANA
JRNL TITL 2 PROTEIN CONTAINING DUF538 DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, X-PLOR 2.9.3
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YDU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031413.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.18
REMARK 210 IONIC STRENGTH : 25MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10MG/ML, H2O/7%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
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 : CYANA 1.0.5, SPARKY 3.72,
REMARK 210 NMRPIPE 2.3
REMARK 210 METHOD USED : WATER REFINEMENT WITH XPLOR
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: THE PROTEIN WAS DEGRADING DURING DATA COLLECTION.
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
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 GLN A 3 27.45 -146.30
REMARK 500 1 SER A 30 111.03 -161.27
REMARK 500 1 ILE A 46 89.95 -64.52
REMARK 500 1 LYS A 49 -35.38 -135.32
REMARK 500 1 MET A 50 -87.30 66.88
REMARK 500 1 GLN A 51 -0.18 -143.52
REMARK 500 1 ASP A 62 -162.22 -77.17
REMARK 500 1 ILE A 67 -67.39 64.95
REMARK 500 1 PHE A 68 -56.63 179.61
REMARK 500 1 THR A 73 27.86 83.24
REMARK 500 1 LYS A 97 1.75 -67.99
REMARK 500 1 SER A 99 -68.52 -146.89
REMARK 500 1 SER A 100 -74.19 -164.15
REMARK 500 1 ASP A 119 98.78 54.74
REMARK 500 1 MET A 128 -35.55 -158.94
REMARK 500 1 SER A 141 -77.96 -173.10
REMARK 500 1 THR A 146 93.65 -51.10
REMARK 500 1 ALA A 147 -35.71 163.27
REMARK 500 1 MET A 149 -10.24 72.51
REMARK 500 1 TYR A 158 24.50 -153.19
REMARK 500 1 ASP A 168 -34.01 -144.41
REMARK 500 2 ASP A 2 79.63 57.74
REMARK 500 2 SER A 34 90.95 -163.32
REMARK 500 2 TRP A 41 -77.89 -68.55
REMARK 500 2 LEU A 42 34.72 -170.76
REMARK 500 2 GLN A 51 -46.86 72.53
REMARK 500 2 LYS A 52 92.24 75.07
REMARK 500 2 PRO A 53 3.68 -68.70
REMARK 500 2 ASP A 62 -153.95 -91.93
REMARK 500 2 ILE A 67 -70.78 57.79
REMARK 500 2 PHE A 68 -50.53 176.73
REMARK 500 2 ASP A 71 -39.65 177.43
REMARK 500 2 ALA A 72 166.28 -46.48
REMARK 500 2 THR A 73 26.22 88.11
REMARK 500 2 PRO A 89 98.59 -52.23
REMARK 500 2 SER A 90 141.56 74.03
REMARK 500 2 TYR A 96 -157.10 -127.22
REMARK 500 2 ASP A 98 -53.93 177.93
REMARK 500 2 SER A 100 83.53 -152.77
REMARK 500 2 VAL A 127 -56.57 -139.17
REMARK 500 2 VAL A 133 -78.73 -132.05
REMARK 500 2 THR A 134 -167.01 51.86
REMARK 500 2 SER A 141 -80.29 -174.96
REMARK 500 2 MET A 149 82.86 173.30
REMARK 500 2 LYS A 150 -88.74 -88.84
REMARK 500 2 TYR A 158 21.60 177.95
REMARK 500 2 ASP A 168 -27.49 -160.87
REMARK 500 3 GLN A 3 85.86 -155.52
REMARK 500 3 ILE A 4 87.83 -151.42
REMARK 500 3 LYS A 16 64.48 63.66
REMARK 500
REMARK 500 THIS ENTRY HAS 487 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 2 ARG A 166 0.08 SIDE CHAIN
REMARK 500 10 ARG A 166 0.09 SIDE CHAIN
REMARK 500 12 ARG A 166 0.08 SIDE CHAIN
REMARK 500 14 ARG A 155 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GO.24315 RELATED DB: TARGETDB
DBREF 1YDU A 2 170 UNP Q9M015 Y5161_ARATH 2 170
SEQADV 1YDU SER A 1 UNP Q9M015 CLONING ARTIFACT
SEQADV 1YDU GLY A 159 UNP Q9M015 GLU 159 ENGINEERED MUTATION
SEQRES 1 A 170 SER ASP GLN ILE PHE ASN LYS VAL GLY SER TYR TRP LEU
SEQRES 2 A 170 GLY GLN LYS ALA ASN LYS GLN PHE ASP SER VAL GLY ASN
SEQRES 3 A 170 ASP LEU ASN SER VAL SER THR SER ILE GLU GLY GLY THR
SEQRES 4 A 170 LYS TRP LEU VAL ASN LYS ILE LYS GLY LYS MET GLN LYS
SEQRES 5 A 170 PRO LEU PRO GLU LEU LEU LYS GLU TYR ASP LEU PRO ILE
SEQRES 6 A 170 GLY ILE PHE PRO GLY ASP ALA THR ASN TYR GLU PHE ASP
SEQRES 7 A 170 GLU GLU THR LYS LYS LEU THR VAL LEU ILE PRO SER ILE
SEQRES 8 A 170 CYS GLU VAL GLY TYR LYS ASP SER SER VAL LEU LYS PHE
SEQRES 9 A 170 THR THR THR VAL THR GLY HIS LEU GLU LYS GLY LYS LEU
SEQRES 10 A 170 THR ASP VAL GLU GLY ILE LYS THR LYS VAL MET ILE TRP
SEQRES 11 A 170 VAL LYS VAL THR SER ILE SER THR ASP ALA SER LYS VAL
SEQRES 12 A 170 TYR PHE THR ALA GLY MET LYS LYS SER ARG SER ARG ASP
SEQRES 13 A 170 ALA TYR GLY VAL GLN ARG ASN GLY LEU ARG VAL ASP LYS
SEQRES 14 A 170 PHE
HELIX 1 1 LEU A 54 ASP A 62 1 9
SHEET 1 A 4 ASN A 74 PHE A 77 0
SHEET 2 A 4 LEU A 84 LEU A 87 -1 O THR A 85 N GLU A 76
SHEET 3 A 4 THR A 107 LEU A 112 -1 O VAL A 108 N VAL A 86
SHEET 4 A 4 LEU A 117 GLU A 121 -1 O THR A 118 N HIS A 111
SHEET 1 B 4 CYS A 92 GLY A 95 0
SHEET 2 B 4 VAL A 101 PHE A 104 -1 O PHE A 104 N CYS A 92
SHEET 3 B 4 LYS A 124 LYS A 126 -1 O LYS A 124 N LYS A 103
SHEET 4 B 4 TRP A 130 VAL A 131 -1 O VAL A 131 N THR A 125
SHEET 1 C 2 SER A 137 THR A 138 0
SHEET 2 C 2 VAL A 143 TYR A 144 -1 O TYR A 144 N SER A 137
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 - t 20 2 Bytes