Header list of 1rjj.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-NOV-03 1RJJ
TITLE SOLUTION STRUCTURE OF A HOMODIMERIC HYPOTHETICAL PROTEIN, AT5G22580, A
TITLE 2 STRUCTURAL GENOMICS TARGET FROM ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXPRESSED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)/PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS BETA BARREL, HOMODIMER, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS, CESG, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.CORNILESCU,C.C.CORNILESCU,Q.ZHAO,R.O.FREDERICK,F.C.PETERSON,S.THAO,
AUTHOR 2 J.L.MARKLEY,CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS (CESG)
REVDAT 7 02-MAR-22 1RJJ 1 REMARK
REVDAT 6 24-FEB-09 1RJJ 1 VERSN
REVDAT 5 12-FEB-08 1RJJ 1 REMARK
REVDAT 4 01-FEB-05 1RJJ 1 AUTHOR KEYWDS REMARK
REVDAT 3 29-JUN-04 1RJJ 1 JRNL
REVDAT 2 23-DEC-03 1RJJ 1 REMARK
REVDAT 1 09-DEC-03 1RJJ 0
JRNL AUTH G.CORNILESCU,C.C.CORNILESCU,Q.ZHAO,R.O.FREDERICK,
JRNL AUTH 2 F.C.PETERSON,S.THAO,J.L.MARKLEY
JRNL TITL SOLUTION STRUCTURE OF A HOMODIMERIC HYPOTHETICAL PROTEIN,
JRNL TITL 2 AT5G22580, A STRUCTURAL GENOMICS TARGET FROM ARABIDOPSIS
JRNL TITL 3 THALIANA.
JRNL REF J.BIOMOL.NMR V. 29 387 2004
JRNL REFN ISSN 0925-2738
JRNL PMID 15213437
JRNL DOI 10.1023/B:JNMR.0000032525.70677.16
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, VNMR, XPLOR-NIH
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA, CLORE (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RJJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000020805.
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 : 50MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ; 600 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRDRAW, PIPP, NMRPIPE, XPLOR
REMARK 210 -NIH
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 PRO A 111 O
REMARK 470 PRO B 111 O
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 VAL A 31 H ILE A 34 1.40
REMARK 500 O VAL B 31 H ILE B 34 1.40
REMARK 500 O GLY B 26 H LEU B 30 1.43
REMARK 500 O GLY A 26 H LEU A 30 1.43
REMARK 500 O THR B 87 H ILE B 90 1.44
REMARK 500 O THR A 87 H ILE A 90 1.44
REMARK 500 O HIS A 49 H ARG A 53 1.53
REMARK 500 O HIS B 49 H ARG B 53 1.53
REMARK 500 O LYS A 104 H SER A 106 1.53
REMARK 500 O LYS B 104 H SER B 106 1.53
REMARK 500 O LEU B 27 H VAL B 31 1.55
REMARK 500 O LEU A 27 H VAL A 31 1.55
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 4 -100.50 -139.64
REMARK 500 1 ASP A 17 64.82 153.83
REMARK 500 1 THR A 18 105.20 -50.93
REMARK 500 1 VAL A 37 21.44 37.83
REMARK 500 1 LYS A 46 80.82 -68.50
REMARK 500 1 GLU A 47 54.66 -96.91
REMARK 500 1 SER A 48 -138.10 -134.14
REMARK 500 1 GLN A 54 -4.00 55.90
REMARK 500 1 PHE A 56 -128.02 -59.26
REMARK 500 1 THR A 57 -36.13 -164.99
REMARK 500 1 ASN A 66 -174.57 -173.75
REMARK 500 1 SER A 75 12.37 -66.81
REMARK 500 1 ALA A 102 74.74 -56.46
REMARK 500 1 VAL A 103 -26.22 -148.36
REMARK 500 1 LYS A 104 -28.26 -38.45
REMARK 500 1 SER A 105 70.72 -57.69
REMARK 500 1 VAL A 107 30.18 -91.73
REMARK 500 1 SER B 4 -100.51 -139.47
REMARK 500 1 ASP B 17 64.68 153.75
REMARK 500 1 THR B 18 105.19 -50.73
REMARK 500 1 VAL B 37 21.38 37.93
REMARK 500 1 LYS B 46 80.89 -68.59
REMARK 500 1 GLU B 47 54.56 -96.95
REMARK 500 1 SER B 48 -138.22 -134.14
REMARK 500 1 GLN B 54 -4.06 55.87
REMARK 500 1 PHE B 56 -128.08 -58.92
REMARK 500 1 THR B 57 -36.25 -164.90
REMARK 500 1 ASN B 66 -174.40 -173.57
REMARK 500 1 SER B 75 12.34 -66.66
REMARK 500 1 ALA B 102 74.74 -56.39
REMARK 500 1 VAL B 103 -26.15 -148.33
REMARK 500 1 LYS B 104 -28.13 -38.60
REMARK 500 1 SER B 105 70.69 -57.77
REMARK 500 1 VAL B 107 30.29 -91.76
REMARK 500 2 ALA A 2 110.68 -38.25
REMARK 500 2 THR A 3 -49.07 -147.64
REMARK 500 2 SER A 4 -103.76 -124.05
REMARK 500 2 ASP A 17 62.51 155.24
REMARK 500 2 THR A 18 105.20 -49.04
REMARK 500 2 ASP A 35 -9.43 -58.91
REMARK 500 2 VAL A 37 45.09 30.26
REMARK 500 2 LYS A 46 81.17 -65.50
REMARK 500 2 SER A 48 73.34 -158.49
REMARK 500 2 HIS A 49 125.12 54.34
REMARK 500 2 GLN A 54 13.71 49.21
REMARK 500 2 PRO A 77 -7.54 -43.78
REMARK 500 2 ALA A 88 -26.57 -38.85
REMARK 500 2 ALA A 102 76.05 -58.88
REMARK 500 2 VAL A 107 51.62 -177.19
REMARK 500 2 VAL A 108 43.42 -168.06
REMARK 500
REMARK 500 THIS ENTRY HAS 651 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8972 RELATED DB: BMRB
REMARK 900 RELATED ID: 1Q53 RELATED DB: PDB
REMARK 900 RELATED ID: 1IUJ RELATED DB: PDB
REMARK 900 RELATED ID: 1LQ9 RELATED DB: PDB
REMARK 900 RELATED ID: GO.22997 RELATED DB: TARGETDB
DBREF 1RJJ A 1 111 UNP Q9FK81 Q9FK81_ARATH 1 111
DBREF 1RJJ B 1 111 UNP Q9FK81 Q9FK81_ARATH 1 111
SEQRES 1 A 111 MET ALA THR SER GLY PHE LYS HIS LEU VAL VAL VAL LYS
SEQRES 2 A 111 PHE LYS GLU ASP THR LYS VAL ASP GLU ILE LEU LYS GLY
SEQRES 3 A 111 LEU GLU ASN LEU VAL SER GLN ILE ASP THR VAL LYS SER
SEQRES 4 A 111 PHE GLU TRP GLY GLU ASP LYS GLU SER HIS ASP MET LEU
SEQRES 5 A 111 ARG GLN GLY PHE THR HIS ALA PHE SER MET THR PHE GLU
SEQRES 6 A 111 ASN LYS ASP GLY TYR VAL ALA PHE THR SER HIS PRO LEU
SEQRES 7 A 111 HIS VAL GLU PHE SER ALA ALA PHE THR ALA VAL ILE ASP
SEQRES 8 A 111 LYS ILE VAL LEU LEU ASP PHE PRO VAL ALA ALA VAL LYS
SEQRES 9 A 111 SER SER VAL VAL ALA THR PRO
SEQRES 1 B 111 MET ALA THR SER GLY PHE LYS HIS LEU VAL VAL VAL LYS
SEQRES 2 B 111 PHE LYS GLU ASP THR LYS VAL ASP GLU ILE LEU LYS GLY
SEQRES 3 B 111 LEU GLU ASN LEU VAL SER GLN ILE ASP THR VAL LYS SER
SEQRES 4 B 111 PHE GLU TRP GLY GLU ASP LYS GLU SER HIS ASP MET LEU
SEQRES 5 B 111 ARG GLN GLY PHE THR HIS ALA PHE SER MET THR PHE GLU
SEQRES 6 B 111 ASN LYS ASP GLY TYR VAL ALA PHE THR SER HIS PRO LEU
SEQRES 7 B 111 HIS VAL GLU PHE SER ALA ALA PHE THR ALA VAL ILE ASP
SEQRES 8 B 111 LYS ILE VAL LEU LEU ASP PHE PRO VAL ALA ALA VAL LYS
SEQRES 9 B 111 SER SER VAL VAL ALA THR PRO
HELIX 1 1 LYS A 19 SER A 32 1 14
HELIX 2 2 GLN A 33 VAL A 37 5 5
HELIX 3 3 ASN A 66 SER A 75 1 10
HELIX 4 4 HIS A 76 VAL A 89 1 14
HELIX 5 5 LYS B 19 SER B 32 1 14
HELIX 6 6 GLN B 33 VAL B 37 5 5
HELIX 7 7 ASN B 66 SER B 75 1 10
HELIX 8 8 HIS B 76 VAL B 89 1 14
SHEET 1 A 4 SER A 39 ASP A 45 0
SHEET 2 A 4 HIS A 58 PHE A 64 -1 O ALA A 59 N GLU A 44
SHEET 3 A 4 GLY A 5 LYS A 13 -1 N HIS A 8 O MET A 62
SHEET 4 A 4 LYS A 92 VAL A 100 -1 O VAL A 100 N GLY A 5
SHEET 1 B 4 SER B 39 ASP B 45 0
SHEET 2 B 4 HIS B 58 PHE B 64 -1 O ALA B 59 N GLU B 44
SHEET 3 B 4 GLY B 5 LYS B 13 -1 N HIS B 8 O MET B 62
SHEET 4 B 4 LYS B 92 VAL B 100 -1 O VAL B 100 N GLY B 5
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