Header list of 1q53.pdb file
Complete list - r 20 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 06-AUG-03 1Q53
TITLE SOLUTION STRUCTURE OF HYPOTHETICAL ARABIDOPSIS THALIANA PROTEIN
TITLE 2 AT3G17210. CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS TARGET 13081
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXPRESSED PROTEIN: AT3G17210;
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 (NOVAGEN);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS STRUCTURAL GENOMICS, UNKNOWN FUNCTION, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 CESG, PSI, CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.L.LYTLE,F.C.PETERSON,B.F.VOLKMAN,CENTER FOR EUKARYOTIC STRUCTURAL
AUTHOR 2 GENOMICS (CESG)
REVDAT 7 30-JAN-13 1Q53 1 AUTHOR JRNL VERSN
REVDAT 6 24-FEB-09 1Q53 1 VERSN
REVDAT 5 12-FEB-08 1Q53 1 REMARK
REVDAT 4 01-FEB-05 1Q53 1 AUTHOR KEYWDS REMARK
REVDAT 3 12-OCT-04 1Q53 1 KEYWDS
REVDAT 2 09-MAR-04 1Q53 1 JRNL
REVDAT 1 19-AUG-03 1Q53 0
SPRSDE 19-AUG-03 1Q53 1NWJ
JRNL AUTH B.L.LYTLE,F.C.PETERSON,K.L.KJER,R.O.FREDERICK,Q.ZHAO,S.THAO,
JRNL AUTH 2 C.BINGMAN,K.A.JOHNSON,G.N.PHILLIPS JR.,B.F.VOLKMAN
JRNL TITL STRUCTURE OF THE HYPOTHETICAL PROTEIN AT3G17210 FROM
JRNL TITL 2 ARABIDOPSIS THALIANA.
JRNL REF J.BIOMOL.NMR V. 28 397 2004
JRNL REFN ISSN 0925-2738
JRNL PMID 14872131
JRNL DOI 10.1023/B:JNMR.0000015385.54050.19
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1.0.6
REMARK 3 AUTHORS : HERRMANN, T., GUENTERT, P.,
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: INITIAL STRUCTURES WERE GENERATED USING
REMARK 3 THE CANDID MODULE OF THE TORSION ANGLE DYNAMICS PROGRAM CYANA.
REMARK 3 ADDITIONAL NOE ASSIGNMENTS WERE DETERMINED MANUALLY AND PEAK
REMARK 3 INTENSITIES WERE CONVERTED INTO UPPER DISTANCE BOUNDS WITH THE
REMARK 3 CALIBA FUNCTION OF CYANA. THE FINAL STRUCTURES WERE BASED ON THE
REMARK 3 FOLLOWING RESTRAINTS (FOR EACH MONOMER): 2001 NON-TRIVIAL NOE
REMARK 3 DISTANCE CONSTRAINTS (1831 INTRAMOLECULAR AND 170 INTERMOLECULAR)
REMARK 3 AND 141 PHI AND PSI TORSION ANGLE CONSTRAINTS GENERATED FROM
REMARK 3 CHEMICAL SHIFT DATABASE SEARCHING USING THE PROGRAM TALOS.
REMARK 4
REMARK 4 1Q53 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-03.
REMARK 100 THE RCSB ID CODE IS RCSB019926.
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 : 50 MM SODIUM CHLORIDE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM AT3G17210 U-15N,13C, 20 MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 50 MM
REMARK 210 SODIUM CHLORIDE, 90% H20, 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
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.0, NMRPIPE
REMARK 210 97.027.12.56, XEASY 1.4, CYANA
REMARK 210 1.0.6
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 : LOWEST TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 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 TYR A 63 H HIS A 65 1.50
REMARK 500 H VAL A 14 O ILE A 103 1.56
REMARK 500 O LEU A 38 H ILE A 42 1.56
REMARK 500 O TYR A 63 HG1 THR A 64 1.56
REMARK 500 O GLY A 34 H LEU A 38 1.57
REMARK 500 O LYS A 12 H TYR A 105 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 2 130.93 62.16
REMARK 500 1 LYS A 8 -50.73 85.94
REMARK 500 1 LYS A 20 164.11 -42.12
REMARK 500 1 ILE A 42 97.80 -58.10
REMARK 500 1 MET A 45 98.63 -173.39
REMARK 500 1 ASP A 53 108.35 -59.59
REMARK 500 1 SER A 55 79.09 81.80
REMARK 500 1 LEU A 59 70.33 77.27
REMARK 500 1 THR A 64 -58.97 64.71
REMARK 500 1 SER A 73 -163.35 -177.11
REMARK 500 1 ALA A 82 39.80 -96.43
REMARK 500 1 SER A 96 61.83 -151.98
REMARK 500 1 ASP A 98 -68.01 -93.15
REMARK 500 1 HIS B 3 -78.64 64.60
REMARK 500 1 MET B 4 170.91 70.20
REMARK 500 1 ALA B 7 166.59 57.00
REMARK 500 1 LYS B 8 -64.18 -163.58
REMARK 500 1 LYS B 20 170.51 -59.45
REMARK 500 1 ILE B 42 97.10 -47.82
REMARK 500 1 MET B 45 -40.25 -171.30
REMARK 500 1 LYS B 46 -64.68 68.96
REMARK 500 1 ASP B 53 99.15 -49.65
REMARK 500 1 SER B 55 -82.38 163.12
REMARK 500 1 ASN B 58 -59.43 -170.31
REMARK 500 1 LEU B 59 92.62 -51.77
REMARK 500 1 HIS B 60 144.62 -177.61
REMARK 500 1 THR B 64 -55.88 77.13
REMARK 500 1 HIS B 65 173.18 170.96
REMARK 500 1 SER B 73 118.03 -172.65
REMARK 500 1 ALA B 82 34.57 -98.55
REMARK 500 1 SER B 96 64.89 -153.18
REMARK 500 2 SER A 2 -57.12 178.55
REMARK 500 2 MET A 4 94.92 58.41
REMARK 500 2 ILE A 42 101.96 -51.05
REMARK 500 2 MET A 45 153.09 177.29
REMARK 500 2 LYS A 46 -83.02 -101.45
REMARK 500 2 SER A 55 82.53 36.74
REMARK 500 2 ASN A 58 95.54 66.99
REMARK 500 2 LEU A 59 47.14 -179.04
REMARK 500 2 THR A 64 -32.18 -35.82
REMARK 500 2 SER A 73 -175.57 -178.21
REMARK 500 2 HIS B 3 168.21 55.72
REMARK 500 2 LYS B 8 47.75 -106.01
REMARK 500 2 LYS B 20 157.82 -39.49
REMARK 500 2 MET B 45 97.36 -175.82
REMARK 500 2 ASP B 53 106.93 -48.06
REMARK 500 2 GLU B 57 -71.67 67.91
REMARK 500 2 ASN B 58 90.40 171.78
REMARK 500 2 LEU B 59 99.30 178.23
REMARK 500 2 THR B 64 -56.98 72.45
REMARK 500
REMARK 500 THIS ENTRY HAS 504 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GO.13081 RELATED DB: TARGETDB
DBREF 1Q53 A 4 112 UNP Q9LUV2 POP3_ARATH 1 109
DBREF 1Q53 B 4 112 UNP Q9LUV2 POP3_ARATH 1 109
SEQADV 1Q53 GLY A 1 UNP Q9LUV2 CLONING ARTIFACT
SEQADV 1Q53 SER A 2 UNP Q9LUV2 CLONING ARTIFACT
SEQADV 1Q53 HIS A 3 UNP Q9LUV2 CLONING ARTIFACT
SEQADV 1Q53 GLY B 1 UNP Q9LUV2 CLONING ARTIFACT
SEQADV 1Q53 SER B 2 UNP Q9LUV2 CLONING ARTIFACT
SEQADV 1Q53 HIS B 3 UNP Q9LUV2 CLONING ARTIFACT
SEQRES 1 A 112 GLY SER HIS MET GLU GLU ALA LYS GLY PRO VAL LYS HIS
SEQRES 2 A 112 VAL LEU LEU ALA SER PHE LYS ASP GLY VAL SER PRO GLU
SEQRES 3 A 112 LYS ILE GLU GLU LEU ILE LYS GLY TYR ALA ASN LEU VAL
SEQRES 4 A 112 ASN LEU ILE GLU PRO MET LYS ALA PHE HIS TRP GLY LYS
SEQRES 5 A 112 ASP VAL SER ILE GLU ASN LEU HIS GLN GLY TYR THR HIS
SEQRES 6 A 112 ILE PHE GLU SER THR PHE GLU SER LYS GLU ALA VAL ALA
SEQRES 7 A 112 GLU TYR ILE ALA HIS PRO ALA HIS VAL GLU PHE ALA THR
SEQRES 8 A 112 ILE PHE LEU GLY SER LEU ASP LYS VAL LEU VAL ILE ASP
SEQRES 9 A 112 TYR LYS PRO THR SER VAL SER LEU
SEQRES 1 B 112 GLY SER HIS MET GLU GLU ALA LYS GLY PRO VAL LYS HIS
SEQRES 2 B 112 VAL LEU LEU ALA SER PHE LYS ASP GLY VAL SER PRO GLU
SEQRES 3 B 112 LYS ILE GLU GLU LEU ILE LYS GLY TYR ALA ASN LEU VAL
SEQRES 4 B 112 ASN LEU ILE GLU PRO MET LYS ALA PHE HIS TRP GLY LYS
SEQRES 5 B 112 ASP VAL SER ILE GLU ASN LEU HIS GLN GLY TYR THR HIS
SEQRES 6 B 112 ILE PHE GLU SER THR PHE GLU SER LYS GLU ALA VAL ALA
SEQRES 7 B 112 GLU TYR ILE ALA HIS PRO ALA HIS VAL GLU PHE ALA THR
SEQRES 8 B 112 ILE PHE LEU GLY SER LEU ASP LYS VAL LEU VAL ILE ASP
SEQRES 9 B 112 TYR LYS PRO THR SER VAL SER LEU
HELIX 1 1 SER A 24 ILE A 42 1 19
HELIX 2 2 SER A 73 ALA A 82 1 10
HELIX 3 3 HIS A 83 GLY A 95 1 13
HELIX 4 4 SER B 24 ASN B 40 1 17
HELIX 5 5 GLU B 75 ALA B 82 1 8
HELIX 6 6 HIS B 83 GLY B 95 1 13
SHEET 1 A 4 ALA A 47 LYS A 52 0
SHEET 2 A 4 HIS A 65 PHE A 71 -1 O THR A 70 N ALA A 47
SHEET 3 A 4 VAL A 11 SER A 18 -1 N LEU A 15 O PHE A 67
SHEET 4 A 4 LYS A 99 TYR A 105 -1 O ILE A 103 N VAL A 14
SHEET 1 B 4 ALA B 47 GLY B 51 0
SHEET 2 B 4 ILE B 66 THR B 70 -1 O ILE B 66 N GLY B 51
SHEET 3 B 4 LYS B 12 SER B 18 -1 N LEU B 15 O PHE B 67
SHEET 4 B 4 LYS B 99 TYR B 105 -1 O TYR B 105 N LYS B 12
CISPEP 1 GLY A 9 PRO A 10 1 0.05
CISPEP 2 GLY B 9 PRO B 10 1 0.00
CISPEP 3 GLY A 9 PRO A 10 2 0.02
CISPEP 4 GLY B 9 PRO B 10 2 -0.04
CISPEP 5 GLY A 9 PRO A 10 3 0.00
CISPEP 6 GLY B 9 PRO B 10 3 -0.03
CISPEP 7 GLY A 9 PRO A 10 4 -0.08
CISPEP 8 GLY B 9 PRO B 10 4 -0.01
CISPEP 9 GLY A 9 PRO A 10 5 -0.03
CISPEP 10 GLY B 9 PRO B 10 5 0.02
CISPEP 11 GLY A 9 PRO A 10 6 -0.02
CISPEP 12 GLY B 9 PRO B 10 6 0.00
CISPEP 13 GLY A 9 PRO A 10 7 0.04
CISPEP 14 GLY B 9 PRO B 10 7 0.05
CISPEP 15 GLY A 9 PRO A 10 8 -0.01
CISPEP 16 GLY B 9 PRO B 10 8 0.03
CISPEP 17 GLY A 9 PRO A 10 9 -0.05
CISPEP 18 GLY B 9 PRO B 10 9 0.04
CISPEP 19 GLY A 9 PRO A 10 10 0.00
CISPEP 20 GLY B 9 PRO B 10 10 -0.03
CISPEP 21 GLY A 9 PRO A 10 11 -0.01
CISPEP 22 GLY B 9 PRO B 10 11 -0.08
CISPEP 23 GLY A 9 PRO A 10 12 -0.03
CISPEP 24 GLY B 9 PRO B 10 12 0.08
CISPEP 25 GLY A 9 PRO A 10 13 0.07
CISPEP 26 GLY B 9 PRO B 10 13 -0.03
CISPEP 27 GLY A 9 PRO A 10 14 -0.01
CISPEP 28 GLY B 9 PRO B 10 14 0.04
CISPEP 29 GLY A 9 PRO A 10 15 0.03
CISPEP 30 GLY B 9 PRO B 10 15 0.05
CISPEP 31 GLY A 9 PRO A 10 16 -0.04
CISPEP 32 GLY B 9 PRO B 10 16 0.00
CISPEP 33 GLY A 9 PRO A 10 17 0.04
CISPEP 34 GLY B 9 PRO B 10 17 0.04
CISPEP 35 GLY A 9 PRO A 10 18 -0.03
CISPEP 36 GLY B 9 PRO B 10 18 -0.03
CISPEP 37 GLY A 9 PRO A 10 19 0.00
CISPEP 38 GLY B 9 PRO B 10 19 0.01
CISPEP 39 GLY A 9 PRO A 10 20 -0.09
CISPEP 40 GLY B 9 PRO B 10 20 -0.08
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 20 2 Bytes