Header list of 1v32.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 24-OCT-03 1V32
TITLE SOLUTION STRUCTURE OF THE SWIB/MDM2 DOMAIN OF THE HYPOTHETICAL PROTEIN
TITLE 2 AT5G08430 FROM ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN RAFL09-47-K03;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SWIB/MDM2 DOMAIN;
COMPND 5 SYNONYM: AT5G08430;
COMPND 6 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 GENE: RAFL09-47-K03;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030128-16;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SWI-SNF COMPLEX SUBUNIT, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.YONEYAMA,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1V32 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1V32 1 VERSN
REVDAT 1 24-APR-04 1V32 0
JRNL AUTH M.YONEYAMA,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SWIB/MDM2 DOMAIN OF THE
JRNL TITL 2 HYPOTHETICAL PROTEIN AT5G08430 FROM ARABIDOPSIS THALIANA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V32 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000006144.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4MM SWIB/MDM2 DOMAIN U-15N,
REMARK 210 13C; 20MM PHOSPHATE BUFFER NA;
REMARK 210 100MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.815, CYANA 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : 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 : 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 O LYS A 46 H LYS A 50 1.51
REMARK 500 O LYS A 81 H LEU A 85 1.52
REMARK 500 O ILE A 48 H LEU A 53 1.53
REMARK 500 O LEU A 68 H PHE A 72 1.59
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 SER A 2 98.19 -179.39
REMARK 500 1 SER A 5 -58.03 -157.13
REMARK 500 1 SER A 6 133.60 177.96
REMARK 500 1 LYS A 8 81.74 63.21
REMARK 500 1 PHE A 12 -178.04 58.20
REMARK 500 1 ILE A 21 -73.04 -53.39
REMARK 500 1 MET A 34 111.85 -38.06
REMARK 500 1 LEU A 54 162.49 -45.03
REMARK 500 1 ASN A 58 106.39 -171.53
REMARK 500 1 LYS A 66 -64.50 -159.40
REMARK 500 1 LYS A 91 -139.91 -81.43
REMARK 500 1 GLU A 92 114.11 67.04
REMARK 500 1 SER A 99 153.32 73.96
REMARK 500 2 SER A 5 159.84 -47.33
REMARK 500 2 PHE A 10 -168.03 -127.30
REMARK 500 2 ASP A 30 109.32 -50.90
REMARK 500 2 THR A 31 47.93 -87.84
REMARK 500 2 SER A 32 -76.01 -76.03
REMARK 500 2 MET A 34 102.11 -39.57
REMARK 500 2 LEU A 54 167.08 -45.65
REMARK 500 2 ASN A 58 105.19 -165.54
REMARK 500 2 LYS A 66 -65.97 -167.44
REMARK 500 2 GLU A 87 -46.74 -160.67
REMARK 500 2 LYS A 91 -141.36 -102.48
REMARK 500 2 GLU A 92 90.11 56.76
REMARK 500 2 ASP A 95 94.50 -49.81
REMARK 500 2 SER A 100 -64.54 -161.99
REMARK 500 3 SER A 2 89.82 53.89
REMARK 500 3 SER A 6 -72.99 66.34
REMARK 500 3 GLN A 19 -92.68 -48.01
REMARK 500 3 ILE A 35 104.60 56.26
REMARK 500 3 ASN A 58 105.27 -168.67
REMARK 500 3 LYS A 66 -56.49 -173.13
REMARK 500 3 LEU A 71 -71.53 -87.46
REMARK 500 3 ARG A 79 -29.61 -39.12
REMARK 500 3 HIS A 89 41.82 -102.37
REMARK 500 3 LYS A 91 -141.55 -100.98
REMARK 500 3 GLU A 92 77.96 50.70
REMARK 500 3 SER A 99 103.42 56.17
REMARK 500 3 SER A 100 117.37 -176.01
REMARK 500 4 SER A 2 102.76 -175.18
REMARK 500 4 SER A 5 109.08 -45.21
REMARK 500 4 LYS A 8 70.11 56.97
REMARK 500 4 PHE A 12 147.37 59.42
REMARK 500 4 GLN A 19 -93.11 -44.38
REMARK 500 4 THR A 31 46.09 -89.49
REMARK 500 4 MET A 34 98.32 -37.93
REMARK 500 4 LEU A 54 167.51 -47.43
REMARK 500 4 ASN A 58 101.95 -165.77
REMARK 500 4 LYS A 66 -49.59 -168.79
REMARK 500
REMARK 500 THIS ENTRY HAS 308 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ATR001006188.1 RELATED DB: TARGETDB
DBREF 1V32 A 8 95 UNP Q9FT92 Y5843_ARATH 25 112
SEQADV 1V32 GLY A 1 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 SER A 2 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 SER A 3 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 GLY A 4 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 SER A 5 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 SER A 6 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 GLY A 7 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 SER A 96 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 GLY A 97 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 PRO A 98 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 SER A 99 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 SER A 100 UNP Q9FT92 CLONING ARTIFACT
SEQADV 1V32 GLY A 101 UNP Q9FT92 CLONING ARTIFACT
SEQRES 1 A 101 GLY SER SER GLY SER SER GLY LYS ARG PHE GLU PHE VAL
SEQRES 2 A 101 GLY TRP GLY SER ARG GLN LEU ILE GLU PHE LEU HIS SER
SEQRES 3 A 101 LEU GLY LYS ASP THR SER GLU MET ILE SER ARG TYR ASP
SEQRES 4 A 101 VAL SER ASP THR ILE ALA LYS TYR ILE SER LYS GLU GLY
SEQRES 5 A 101 LEU LEU ASP PRO SER ASN LYS LYS LYS VAL VAL CYS ASP
SEQRES 6 A 101 LYS ARG LEU VAL LEU LEU PHE GLY THR ARG THR ILE PHE
SEQRES 7 A 101 ARG MET LYS VAL TYR ASP LEU LEU GLU LYS HIS TYR LYS
SEQRES 8 A 101 GLU ASN GLN ASP SER GLY PRO SER SER GLY
HELIX 1 1 ARG A 18 LEU A 27 1 10
HELIX 2 2 ARG A 37 GLY A 52 1 16
HELIX 3 3 LYS A 66 PHE A 72 1 7
HELIX 4 4 MET A 80 HIS A 89 1 10
SHEET 1 A 2 LYS A 61 VAL A 63 0
SHEET 2 A 2 THR A 76 PHE A 78 -1 O ILE A 77 N VAL A 62
CISPEP 1 GLY A 97 PRO A 98 1 0.08
CISPEP 2 GLY A 97 PRO A 98 2 0.09
CISPEP 3 GLY A 97 PRO A 98 3 -0.03
CISPEP 4 GLY A 97 PRO A 98 4 -0.01
CISPEP 5 GLY A 97 PRO A 98 5 0.00
CISPEP 6 GLY A 97 PRO A 98 6 -0.01
CISPEP 7 GLY A 97 PRO A 98 7 0.02
CISPEP 8 GLY A 97 PRO A 98 8 -0.02
CISPEP 9 GLY A 97 PRO A 98 9 -0.04
CISPEP 10 GLY A 97 PRO A 98 10 0.06
CISPEP 11 GLY A 97 PRO A 98 11 0.01
CISPEP 12 GLY A 97 PRO A 98 12 -0.03
CISPEP 13 GLY A 97 PRO A 98 13 0.02
CISPEP 14 GLY A 97 PRO A 98 14 -0.06
CISPEP 15 GLY A 97 PRO A 98 15 0.04
CISPEP 16 GLY A 97 PRO A 98 16 0.04
CISPEP 17 GLY A 97 PRO A 98 17 -0.03
CISPEP 18 GLY A 97 PRO A 98 18 0.02
CISPEP 19 GLY A 97 PRO A 98 19 0.00
CISPEP 20 GLY A 97 PRO A 98 20 0.07
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