Header list of 1wfj.pdb file
Complete list - r 2 2 Bytes
HEADER PLANT PROTEIN 26-MAY-04 1WFJ
TITLE C2 DOMAIN-CONTAINING PROTEIN FROM PUTATIVE ELICITOR-RESPONSIVE GENE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ELICITOR-RESPONSIVE GENE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C2 DOMAIN;
COMPND 5 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 RAFL05-11-F09;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P031104-14;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS C2 DOMAIN, ELICITOR-RESPONSIVE GENE, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS, PLANT
KEYWDS 3 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WFJ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WFJ 1 VERSN
REVDAT 1 26-NOV-04 1WFJ 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL C2 DOMAIN-CONTAINING PROTEIN FROM PUTATIVE
JRNL TITL 2 ELICITOR-RESPONSIVE GENE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 1.0.7
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WFJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023522.
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 : 1.19MM 13C/15N-LABELED PROTEIN;
REMARK 210 20MMNAPI, 100MM NACL, 1MM D-DTT,
REMARK 210 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.8992, 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, 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 H LEU A 73 O ILE A 94 1.36
REMARK 500 H CYS A 39 O GLN A 42 1.49
REMARK 500 H ILE A 105 O LEU A 126 1.51
REMARK 500 H TYR A 110 O ILE A 122 1.56
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 5 156.36 -40.79
REMARK 500 1 PRO A 8 -165.99 -75.00
REMARK 500 1 HIS A 9 125.09 -171.79
REMARK 500 1 VAL A 17 -87.22 -67.93
REMARK 500 1 LEU A 22 -169.04 -70.32
REMARK 500 1 ASP A 24 61.37 -117.78
REMARK 500 1 ARG A 40 88.28 60.97
REMARK 500 1 THR A 41 33.85 34.04
REMARK 500 1 ASN A 47 158.26 -48.51
REMARK 500 1 ALA A 49 84.16 -61.35
REMARK 500 1 TRP A 58 -45.85 -157.13
REMARK 500 1 SER A 67 67.00 -165.94
REMARK 500 1 GLU A 68 161.60 58.49
REMARK 500 1 PHE A 78 -147.25 -145.83
REMARK 500 1 VAL A 82 -162.88 -70.08
REMARK 500 1 THR A 84 -37.84 -39.80
REMARK 500 1 GLU A 85 77.18 -107.44
REMARK 500 1 ASP A 86 -68.54 -164.67
REMARK 500 1 ASP A 87 113.19 -160.48
REMARK 500 1 ASP A 115 -22.13 83.48
REMARK 500 1 GLU A 116 -20.54 155.33
REMARK 500 1 SER A 131 89.29 -59.65
REMARK 500 1 SER A 134 -56.59 -125.32
REMARK 500 2 SER A 5 -60.02 -102.48
REMARK 500 2 HIS A 9 118.32 -167.42
REMARK 500 2 VAL A 17 -88.91 -60.38
REMARK 500 2 ALA A 25 111.12 -170.85
REMARK 500 2 ASP A 26 88.62 -65.02
REMARK 500 2 LEU A 28 71.90 75.83
REMARK 500 2 ARG A 40 -84.98 66.46
REMARK 500 2 ASN A 47 159.20 -47.95
REMARK 500 2 ALA A 49 78.52 -62.04
REMARK 500 2 THR A 55 76.73 -150.65
REMARK 500 2 ASN A 59 30.40 39.31
REMARK 500 2 SER A 67 -67.49 -144.33
REMARK 500 2 THR A 70 92.24 -69.27
REMARK 500 2 GLU A 72 143.97 -174.69
REMARK 500 2 THR A 84 -36.44 -35.25
REMARK 500 2 GLU A 85 57.08 -97.52
REMARK 500 2 ASP A 86 -65.77 -142.20
REMARK 500 2 ASP A 87 119.32 175.56
REMARK 500 2 SER A 104 134.93 -172.40
REMARK 500 2 ASP A 115 -27.54 89.16
REMARK 500 2 GLU A 116 -21.83 158.63
REMARK 500 2 SER A 131 86.10 -65.42
REMARK 500 3 SER A 5 141.33 -175.61
REMARK 500 3 PRO A 8 -164.89 -75.02
REMARK 500 3 HIS A 9 140.66 179.07
REMARK 500 3 VAL A 17 -87.00 -60.17
REMARK 500 3 ALA A 19 116.95 -160.09
REMARK 500
REMARK 500 THIS ENTRY HAS 440 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ATR001008092.1 RELATED DB: TARGETDB
DBREF 1WFJ A 8 130 UNP Q9C8S6 Y1322_ARATH 2 124
SEQADV 1WFJ GLY A 1 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ SER A 2 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ SER A 3 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ GLY A 4 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ SER A 5 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ SER A 6 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ GLY A 7 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ SER A 131 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ GLY A 132 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ PRO A 133 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ SER A 134 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ SER A 135 UNP Q9C8S6 CLONING ARTIFACT
SEQADV 1WFJ GLY A 136 UNP Q9C8S6 CLONING ARTIFACT
SEQRES 1 A 136 GLY SER SER GLY SER SER GLY PRO HIS GLY THR LEU GLU
SEQRES 2 A 136 VAL VAL LEU VAL SER ALA LYS GLY LEU GLU ASP ALA ASP
SEQRES 3 A 136 PHE LEU ASN ASN MET ASP PRO TYR VAL GLN LEU THR CYS
SEQRES 4 A 136 ARG THR GLN ASP GLN LYS SER ASN VAL ALA GLU GLY MET
SEQRES 5 A 136 GLY THR THR PRO GLU TRP ASN GLU THR PHE ILE PHE THR
SEQRES 6 A 136 VAL SER GLU GLY THR THR GLU LEU LYS ALA LYS ILE PHE
SEQRES 7 A 136 ASP LYS ASP VAL GLY THR GLU ASP ASP ALA VAL GLY GLU
SEQRES 8 A 136 ALA THR ILE PRO LEU GLU PRO VAL PHE VAL GLU GLY SER
SEQRES 9 A 136 ILE PRO PRO THR ALA TYR ASN VAL VAL LYS ASP GLU GLU
SEQRES 10 A 136 TYR LYS GLY GLU ILE TRP VAL ALA LEU SER PHE LYS PRO
SEQRES 11 A 136 SER GLY PRO SER SER GLY
HELIX 1 1 LEU A 96 GLY A 103 1 8
SHEET 1 A 8 ASP A 43 LYS A 45 0
SHEET 2 A 8 VAL A 35 THR A 38 -1 N LEU A 37 O GLN A 44
SHEET 3 A 8 GLU A 72 ILE A 77 -1 O LYS A 76 N GLN A 36
SHEET 4 A 8 GLY A 90 PRO A 95 -1 O ILE A 94 N LEU A 73
SHEET 5 A 8 SER A 104 LYS A 114 -1 O VAL A 113 N GLU A 91
SHEET 6 A 8 GLU A 117 PRO A 130 -1 O LEU A 126 N ILE A 105
SHEET 7 A 8 HIS A 9 GLY A 21 -1 N SER A 18 O TRP A 123
SHEET 8 A 8 GLU A 57 SER A 67 -1 O PHE A 64 N LEU A 12
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