Header list of 1m2e.pdb file
Complete list - 23 20 Bytes
HEADER CIRCADIAN CLOCK PROTEIN 23-JUN-02 1M2E
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNECHOCOCCUS ELONGATUS
TITLE 2 KAIA (KAIA135N); AVERAGE MINIMIZED STRUCTURE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KAIA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (RESIDUES 1-135);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 32046;
SOURCE 4 GENE: KAIA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS ALPHA-BETA-ALPHA SANDWICH, CIRCADIAN CLOCK PROTEIN
EXPDTA SOLUTION NMR
AUTHOR S.B.WILLIAMS,I.VAKONAKIS,S.S.GOLDEN,A.C.LIWANG
REVDAT 4 23-FEB-22 1M2E 1 REMARK
REVDAT 3 24-FEB-09 1M2E 1 VERSN
REVDAT 2 04-DEC-02 1M2E 1 JRNL
REVDAT 1 13-NOV-02 1M2E 0
JRNL AUTH S.B.WILLIAMS,I.VAKONAKIS,S.S.GOLDEN,A.C.LIWANG
JRNL TITL STRUCTURE AND FUNCTION FROM THE CIRCADIAN CLOCK PROTEIN KAIA
JRNL TITL 2 OF SYNECHOCOCCUS ELONGATUS: A POTENTIAL CLOCK INPUT
JRNL TITL 3 MECHANISM
JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 15357 2002
JRNL REFN ISSN 0027-8424
JRNL PMID 12438647
JRNL DOI 10.1073/PNAS.232517099
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, X-PLOR 3.851
REMARK 3 AUTHORS : VARIAN ASSOCIATES (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 2034
REMARK 3 RESTRAINTS: 1816 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 187 ARE
REMARK 3 DIHEDRAL ANGLE RESTRAINTS AND 31 ARE DISTANCE RESTRAINTS FROM
REMARK 3 HYDROGEN BONDS
REMARK 4
REMARK 4 1M2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016511.
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 : 0.17
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM KAIA135N U-15N, 50MM SODIUM
REMARK 210 CHLORIDE, 20MM PHOSPHATE BUFFER;
REMARK 210 3MM KAIA135N U-15N,13C; 50MM
REMARK 210 SODIUM CHLORIDE; 20MM PHOSPHATE
REMARK 210 BUFFER; 3MM KAIA135N U-15N,13C;
REMARK 210 50MM SODIUM CHLORIDE; 20MM
REMARK 210 PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNHA; 4D_13C/15N
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; HNHB; HAHB;
REMARK 210 BRCTCO/BRCTCN
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.8 REV 2001.030.21.27,
REMARK 210 PIPP 4.2.6
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING REGULARIZATION,
REMARK 210 SIMULATED ANNEALING REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: SUBMISSION CORRESPONDS TO THE AVERAGE MINIMIZED STRUCTURE
REMARK 210 BASED ON A 25-LOW-ENERGY-STRUCTURES FAMILY. THE 1H, 15N AND 13C
REMARK 210 CHEMICAL SHIFTS OF KAIA135N ARE DEPOSITED AT THE BMRB DATABASE
REMARK 210 (HTTP://WWW.BMRB.WISC.EDU) UNDER THE ACCESSION NUMBER 5031.
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 VAL A 77 HE2 HIS A 100 1.33
REMARK 500 H ILE A 5 O ARG A 28 1.45
REMARK 500 H VAL A 81 O LEU A 104 1.45
REMARK 500 O GLN A 113 H GLN A 117 1.47
REMARK 500 O GLN A 117 H ALA A 121 1.48
REMARK 500 O ALA A 6 H ASP A 52 1.50
REMARK 500 O LEU A 114 H VAL A 118 1.52
REMARK 500 O THR A 14 H GLN A 18 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 SER A 3 -93.17 45.41
REMARK 500 ALA A 26 142.58 -35.49
REMARK 500 SER A 36 -167.21 -121.84
REMARK 500 HIS A 47 17.94 -151.58
REMARK 500 CYS A 53 124.74 -171.51
REMARK 500 PRO A 61 -72.90 -75.67
REMARK 500 PRO A 78 88.88 -64.18
REMARK 500 PRO A 93 61.12 -68.64
REMARK 500 TYR A 99 -149.88 -147.40
REMARK 500 GLU A 112 -23.33 167.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5031 RELATED DB: BMRB
REMARK 900 1H, 13C AND 15N RESONANCE ASSIGNMENTS
REMARK 900 RELATED ID: 1M2F RELATED DB: PDB
REMARK 900 FAMILY OF 25 STRUCTURES OF KAIA
DBREF 1M2E A 1 135 UNP Q79PF6 KAIA_SYNP7 1 135
SEQRES 1 A 135 MET LEU SER GLN ILE ALA ILE CYS ILE TRP VAL GLU SER
SEQRES 2 A 135 THR ALA ILE LEU GLN ASP CYS GLN ARG ALA LEU SER ALA
SEQRES 3 A 135 ASP ARG TYR GLN LEU GLN VAL CYS GLU SER GLY GLU MET
SEQRES 4 A 135 LEU LEU GLU TYR ALA GLN THR HIS ARG ASP GLN ILE ASP
SEQRES 5 A 135 CYS LEU ILE LEU VAL ALA ALA ASN PRO SER PHE ARG ALA
SEQRES 6 A 135 VAL VAL GLN GLN LEU CYS PHE GLU GLY VAL VAL VAL PRO
SEQRES 7 A 135 ALA ILE VAL VAL GLY ASP ARG ASP SER GLU ASP PRO ASP
SEQRES 8 A 135 GLU PRO ALA LYS GLU GLN LEU TYR HIS SER ALA GLU LEU
SEQRES 9 A 135 HIS LEU GLY ILE HIS GLN LEU GLU GLN LEU PRO TYR GLN
SEQRES 10 A 135 VAL ASP ALA ALA LEU ALA GLU PHE LEU ARG LEU ALA PRO
SEQRES 11 A 135 VAL GLU THR MET ALA
HELIX 1 1 SER A 13 LEU A 24 1 12
HELIX 2 2 GLY A 37 GLN A 45 1 9
HELIX 3 3 SER A 62 GLY A 74 1 13
HELIX 4 4 LYS A 95 TYR A 99 5 5
HELIX 5 5 GLY A 107 LEU A 111 5 5
HELIX 6 6 GLN A 113 LEU A 128 1 16
SHEET 1 A 5 TYR A 29 CYS A 34 0
SHEET 2 A 5 ILE A 5 TRP A 10 1 N ILE A 5 O GLN A 30
SHEET 3 A 5 CYS A 53 VAL A 57 1 O ILE A 55 N CYS A 8
SHEET 4 A 5 ALA A 79 VAL A 82 1 O ILE A 80 N LEU A 54
SHEET 5 A 5 LEU A 104 LEU A 106 1 O LEU A 104 N VAL A 81
CISPEP 1 ALA A 129 PRO A 130 0 -0.14
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
Complete list - 23 20 Bytes