Header list of 1vee.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 30-MAR-04 1VEE
TITLE NMR STRUCTURE OF THE HYPOTHETICAL RHODANESE DOMAIN AT4G01050 FROM
TITLE 2 ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE-RICH PROTEIN FAMILY;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RHODANESE HYPOTHETICAL DOMAIN;
COMPND 5 SYNONYM: HYPOTHETICAL PROTEIN RAFL06-68-J04;
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: RIKEN CDNA RAFL06-68-J04;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030120-27;
SOURCE 8 OTHER_DETAILS: E.COLI CELL-FREE PROTEIN SYNTHESIS
KEYWDS HYPOTHETICAL PROTEIN, STRUCTURAL GENOMICS, RHODANESE DOMAIN, RIKEN
KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.PANTOJA-UCEDA,B.LOPEZ-MENDEZ,S.KOSHIBA,M.INOUE,T.KIGAWA,T.TERADA,
AUTHOR 2 M.SHIROUZU,A.TANAKA,M.SEKI,K.SHINOZAKI,S.YOKOYAMA,P.GUNTERT,RIKEN
AUTHOR 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1VEE 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1VEE 1 VERSN
REVDAT 2 15-FEB-05 1VEE 1 AUTHOR
REVDAT 1 25-JAN-05 1VEE 0
JRNL AUTH D.PANTOJA-UCEDA,B.LOPEZ-MENDEZ,S.KOSHIBA,M.INOUE,T.KIGAWA,
JRNL AUTH 2 T.TERADA,M.SHIROUZU,A.TANAKA,M.SEKI,K.SHINOZAKI,S.YOKOYAMA,
JRNL AUTH 3 P.GUNTERT
JRNL TITL SOLUTION STRUCTURE OF THE RHODANESE HOMOLOGY DOMAIN
JRNL TITL 2 AT4G01050(175-295) FROM ARABIDOPSIS THALIANA
JRNL REF PROTEIN SCI. V. 14 224 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 15576557
JRNL DOI 10.1110/PS.041138705
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.PANTOJA-UCEDA,B.LOPEZ-MENDEZ,S.KOSHIBA,T.KIGAWA,
REMARK 1 AUTH 2 M.SHIROUZU,T.TERADA,M.INOUE,T.YABUKI,M.AOKI,E.SEKI,
REMARK 1 AUTH 3 T.MATSUDA,H.HIROTA,M.YOSHIDA,A.TANAKA,T.OSANAI,M.SEKI,
REMARK 1 AUTH 4 K.SHINOZAKI,S.YOKOYAMA,P.GUNTERT
REMARK 1 TITL NMR ASSIGNMENT OF THE HYPOTHETICAL RHODANESE DOMAIN
REMARK 1 TITL 2 AT4G01050 FROM ARABIDOPSIS THALIANA
REMARK 1 REF J.BIOMOL.NMR V. 29 207 2004
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 15014235
REMARK 1 DOI 10.1023/B:JNMR.0000019241.66789.C3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPALP 1.3
REMARK 3 AUTHORS : R.KORADI,M.BILLETER,P.GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1VEE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000006524.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1MM 13C, 15N-ARABIDOPSIS
REMARK 210 RHODANESE HYPOTHETICAL DOMAIN;
REMARK 210 20MM PHOSPHATE BUFFER; 100MM NA
REMARK 210 1MM DITHIOTHREITOL; 0.02% NA3N;
REMARK 210 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.0.29
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
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 1 ARG A 113 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 6 ARG A 28 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 14 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 20 TYR A 78 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
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 3 -70.32 -128.83
REMARK 500 1 GLN A 35 -70.26 -90.35
REMARK 500 1 LEU A 44 -71.50 -83.46
REMARK 500 1 PHE A 83 -140.84 -141.77
REMARK 500 1 ASP A 107 -5.07 89.85
REMARK 500 1 ASN A 117 24.96 -75.11
REMARK 500 1 SER A 132 -1.56 -147.35
REMARK 500 2 SER A 2 31.16 -144.41
REMARK 500 2 ASP A 19 -168.72 -126.51
REMARK 500 2 ASP A 20 -43.23 -141.66
REMARK 500 2 PHE A 83 -151.64 -138.58
REMARK 500 2 ALA A 109 -45.50 -135.60
REMARK 500 2 TRP A 115 -56.98 -27.70
REMARK 500 2 ASN A 117 7.21 -69.07
REMARK 500 2 TRP A 122 126.19 -171.83
REMARK 500 2 ILE A 123 88.63 -68.66
REMARK 500 3 SER A 2 -55.57 -122.10
REMARK 500 3 ARG A 28 -102.74 -42.19
REMARK 500 3 GLN A 35 -62.86 -99.50
REMARK 500 3 LYS A 126 35.44 -75.15
REMARK 500 4 SER A 3 40.35 -84.70
REMARK 500 4 SER A 5 93.35 -63.13
REMARK 500 4 ASN A 40 76.25 -108.69
REMARK 500 4 ASP A 84 -57.33 -24.45
REMARK 500 4 TRP A 115 -66.59 -29.84
REMARK 500 5 SER A 5 55.65 -151.98
REMARK 500 5 PHE A 83 -136.51 -131.92
REMARK 500 5 ASN A 86 10.79 -145.82
REMARK 500 5 ALA A 102 115.89 -165.21
REMARK 500 5 ASP A 107 -1.58 75.37
REMARK 500 5 PRO A 125 -159.34 -78.18
REMARK 500 6 GLN A 35 -60.37 -101.11
REMARK 500 6 ASP A 84 -55.50 -23.32
REMARK 500 6 ASN A 86 -0.21 -144.04
REMARK 500 6 SER A 132 25.32 -150.62
REMARK 500 7 SER A 3 1.64 -154.76
REMARK 500 7 ASP A 84 -32.44 -34.35
REMARK 500 7 LYS A 100 -70.15 -50.82
REMARK 500 7 THR A 128 -77.57 -147.14
REMARK 500 7 SER A 132 -72.68 -148.66
REMARK 500 8 ILE A 41 20.35 -145.00
REMARK 500 8 PHE A 83 -143.98 -134.98
REMARK 500 9 SER A 5 116.90 -34.25
REMARK 500 9 ILE A 41 15.49 -140.85
REMARK 500 9 SER A 50 108.71 -58.02
REMARK 500 9 ASP A 57 31.97 -149.44
REMARK 500 9 PHE A 83 -141.20 -131.58
REMARK 500 9 TRP A 115 -62.52 -25.94
REMARK 500 9 THR A 128 44.87 -146.29
REMARK 500 10 SER A 3 -7.73 65.27
REMARK 500
REMARK 500 THIS ENTRY HAS 97 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 TYR A 78 0.08 SIDE CHAIN
REMARK 500 2 ARG A 113 0.11 SIDE CHAIN
REMARK 500 3 TYR A 78 0.09 SIDE CHAIN
REMARK 500 6 TYR A 78 0.09 SIDE CHAIN
REMARK 500 6 ARG A 113 0.12 SIDE CHAIN
REMARK 500 7 TYR A 78 0.10 SIDE CHAIN
REMARK 500 8 ARG A 28 0.07 SIDE CHAIN
REMARK 500 8 ARG A 113 0.08 SIDE CHAIN
REMARK 500 10 ARG A 113 0.09 SIDE CHAIN
REMARK 500 12 TYR A 78 0.07 SIDE CHAIN
REMARK 500 12 TYR A 103 0.09 SIDE CHAIN
REMARK 500 15 TYR A 78 0.12 SIDE CHAIN
REMARK 500 16 ARG A 28 0.10 SIDE CHAIN
REMARK 500 16 ARG A 113 0.10 SIDE CHAIN
REMARK 500 17 ARG A 28 0.10 SIDE CHAIN
REMARK 500 17 TYR A 78 0.08 SIDE CHAIN
REMARK 500 18 ARG A 28 0.10 SIDE CHAIN
REMARK 500 18 TYR A 78 0.09 SIDE CHAIN
REMARK 500 19 TYR A 78 0.10 SIDE CHAIN
REMARK 500 19 ARG A 113 0.12 SIDE CHAIN
REMARK 500 20 TYR A 103 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5929 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS
REMARK 900 RELATED ID: ATR001001566 RELATED DB: TARGETDB
DBREF 1VEE A 8 128 UNP Q9M158 Y4105_ARATH 134 254
SEQADV 1VEE GLY A 1 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE SER A 2 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE SER A 3 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE GLY A 4 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE SER A 5 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE SER A 6 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE GLY A 7 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE SER A 129 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE GLY A 130 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE PRO A 131 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE SER A 132 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE SER A 133 UNP Q9M158 CLONING ARTIFACT
SEQADV 1VEE GLY A 134 UNP Q9M158 CLONING ARTIFACT
SEQRES 1 A 134 GLY SER SER GLY SER SER GLY SER ALA LYS ASN ALA TYR
SEQRES 2 A 134 THR LYS LEU GLY THR ASP ASP ASN ALA GLN LEU LEU ASP
SEQRES 3 A 134 ILE ARG ALA THR ALA ASP PHE ARG GLN VAL GLY SER PRO
SEQRES 4 A 134 ASN ILE LYS GLY LEU GLY LYS LYS ALA VAL SER THR VAL
SEQRES 5 A 134 TYR ASN GLY GLU ASP LYS PRO GLY PHE LEU LYS LYS LEU
SEQRES 6 A 134 SER LEU LYS PHE LYS ASP PRO GLU ASN THR THR LEU TYR
SEQRES 7 A 134 ILE LEU ASP LYS PHE ASP GLY ASN SER GLU LEU VAL ALA
SEQRES 8 A 134 GLU LEU VAL ALA LEU ASN GLY PHE LYS SER ALA TYR ALA
SEQRES 9 A 134 ILE LYS ASP GLY ALA GLU GLY PRO ARG GLY TRP LEU ASN
SEQRES 10 A 134 SER SER LEU PRO TRP ILE GLU PRO LYS LYS THR SER GLY
SEQRES 11 A 134 PRO SER SER GLY
HELIX 1 1 SER A 8 ASP A 19 1 12
HELIX 2 2 ALA A 29 VAL A 36 1 8
HELIX 3 3 ASN A 54 GLU A 56 5 3
HELIX 4 4 ASP A 57 LEU A 67 1 11
HELIX 5 5 ASP A 71 ASN A 74 5 4
HELIX 6 6 ASN A 86 GLY A 98 1 13
HELIX 7 7 TRP A 115 SER A 119 5 5
SHEET 1 A 4 VAL A 49 SER A 50 0
SHEET 2 A 4 ALA A 22 ASP A 26 1 N ASP A 26 O VAL A 49
SHEET 3 A 4 THR A 76 LEU A 80 1 O TYR A 78 N LEU A 25
SHEET 4 A 4 SER A 101 ALA A 104 1 O TYR A 103 N ILE A 79
SHEET 1 B 2 SER A 38 PRO A 39 0
SHEET 2 B 2 TRP A 122 ILE A 123 -1 O ILE A 123 N SER A 38
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