Header list of 1m2f.pdb file
Complete list - b 23 2 Bytes
HEADER CIRCADIAN CLOCK PROTEIN 23-JUN-02 1M2F TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNECHOCOCCUS ELONGATUS TITLE 2 KAIA (KAIA135N); FAMILY OF 25 STRUCTURES 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 NUMMDL 25 AUTHOR S.B.WILLIAMS,I.VAKONAKIS,S.S.GOLDEN,A.C.LIWANG REVDAT 4 23-FEB-22 1M2F 1 REMARK REVDAT 3 24-FEB-09 1M2F 1 VERSN REVDAT 2 04-DEC-02 1M2F 1 JRNL REVDAT 1 13-NOV-02 1M2F 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 REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 31 DISTANCE RESTRAINTS FROM HYDROGEN REMARK 3 BONDS REMARK 4 REMARK 4 1M2F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-02. REMARK 100 THE DEPOSITION ID IS D_1000016512. 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 : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 REMARK 210 REMARK 210 REMARK: SUBMISSION CORRESPONDS TO FAMILY OF 25-LOW-ENERGY REMARK 210 -STRUCTURES. THE 1H, 15N AND 13C CHEMICAL SHIFTS OF KAIA135N ARE REMARK 210 DEPOSITED AT THE BMRB DATABASE (HTTP://WWW.BMRB.WISC.EDU) UNDER REMARK 210 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 H ILE A 5 O ARG A 28 1.44 REMARK 500 O GLN A 117 H ALA A 121 1.46 REMARK 500 O GLN A 113 H GLN A 117 1.46 REMARK 500 O THR A 14 H GLN A 18 1.51 REMARK 500 H VAL A 81 O LEU A 104 1.53 REMARK 500 O LEU A 114 H VAL A 118 1.57 REMARK 500 O ALA A 6 H ASP A 52 1.57 REMARK 500 O GLN A 18 H ARG A 22 1.57 REMARK 500 O GLN A 68 H PHE A 72 1.57 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 ALA A 26 145.08 -35.28 REMARK 500 1 SER A 36 -166.81 -130.00 REMARK 500 1 HIS A 47 30.21 -166.46 REMARK 500 1 PRO A 78 85.46 -65.15 REMARK 500 1 ALA A 94 89.01 65.70 REMARK 500 1 GLU A 96 34.03 -99.30 REMARK 500 1 TYR A 99 -139.62 -156.48 REMARK 500 1 GLU A 112 -27.26 172.17 REMARK 500 1 THR A 133 67.35 -108.56 REMARK 500 2 SER A 3 -129.70 49.47 REMARK 500 2 HIS A 47 20.94 -146.83 REMARK 500 2 PRO A 78 97.89 -68.16 REMARK 500 2 ASP A 89 74.00 42.07 REMARK 500 2 PRO A 93 -89.15 -84.27 REMARK 500 2 ALA A 94 21.19 47.91 REMARK 500 2 GLU A 96 24.46 -147.48 REMARK 500 2 TYR A 99 -142.92 -176.09 REMARK 500 2 GLN A 110 31.55 -95.08 REMARK 500 2 GLU A 112 -28.03 170.23 REMARK 500 3 SER A 3 -63.09 -96.11 REMARK 500 3 SER A 36 -167.68 -106.21 REMARK 500 3 HIS A 47 29.45 -142.17 REMARK 500 3 CYS A 53 128.47 -176.11 REMARK 500 3 PRO A 78 89.22 -66.37 REMARK 500 3 ARG A 85 -75.66 -81.38 REMARK 500 3 ASP A 86 115.90 68.18 REMARK 500 3 PRO A 93 46.35 -84.08 REMARK 500 3 TYR A 99 -146.63 -154.85 REMARK 500 3 GLU A 112 -27.08 167.36 REMARK 500 3 THR A 133 59.73 -98.64 REMARK 500 4 LEU A 2 105.83 -46.63 REMARK 500 4 SER A 3 -86.93 -49.26 REMARK 500 4 SER A 25 81.33 -48.17 REMARK 500 4 ARG A 28 44.30 -144.01 REMARK 500 4 SER A 36 -166.54 -123.10 REMARK 500 4 HIS A 47 22.15 -151.10 REMARK 500 4 PRO A 61 -88.22 -72.74 REMARK 500 4 PRO A 78 90.83 -63.46 REMARK 500 4 GLU A 92 154.74 -47.79 REMARK 500 4 TYR A 99 -133.15 -157.14 REMARK 500 4 GLU A 112 -28.27 165.72 REMARK 500 5 SER A 3 -87.66 43.81 REMARK 500 5 SER A 25 78.22 2.76 REMARK 500 5 PRO A 61 -73.94 -71.75 REMARK 500 5 PRO A 78 86.43 -66.27 REMARK 500 5 TYR A 99 -132.27 -162.19 REMARK 500 5 GLU A 112 -23.73 167.94 REMARK 500 5 THR A 133 52.80 -100.85 REMARK 500 6 ALA A 26 136.88 -34.46 REMARK 500 6 GLN A 30 78.77 -111.05 REMARK 500 REMARK 500 THIS ENTRY HAS 242 RAMACHANDRAN OUTLIERS. 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: 1M2E RELATED DB: PDB REMARK 900 MINIMIZED AVERAGE STRUCTURE OF KAIA DBREF 1M2F 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 GLY A 107 LEU A 111 5 5 HELIX 5 5 GLN A 113 ALA A 129 1 17 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 TRP A 10 SHEET 4 A 5 ALA A 79 VAL A 82 1 O ILE A 80 N LEU A 56 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 1 -0.26 CISPEP 2 ALA A 129 PRO A 130 2 -1.70 CISPEP 3 ALA A 129 PRO A 130 3 -1.17 CISPEP 4 ALA A 129 PRO A 130 4 -0.13 CISPEP 5 ALA A 129 PRO A 130 5 -0.78 CISPEP 6 ALA A 129 PRO A 130 6 -0.04 CISPEP 7 ALA A 129 PRO A 130 7 -0.55 CISPEP 8 ALA A 129 PRO A 130 8 -1.52 CISPEP 9 ALA A 129 PRO A 130 9 -0.37 CISPEP 10 ALA A 129 PRO A 130 10 -0.37 CISPEP 11 ALA A 129 PRO A 130 11 -0.76 CISPEP 12 ALA A 129 PRO A 130 12 -0.52 CISPEP 13 ALA A 129 PRO A 130 13 -0.23 CISPEP 14 ALA A 129 PRO A 130 14 -0.18 CISPEP 15 ALA A 129 PRO A 130 15 -0.45 CISPEP 16 ALA A 129 PRO A 130 16 -1.48 CISPEP 17 ALA A 129 PRO A 130 17 0.14 CISPEP 18 ALA A 129 PRO A 130 18 -0.50 CISPEP 19 ALA A 129 PRO A 130 19 -0.15 CISPEP 20 ALA A 129 PRO A 130 20 -0.34 CISPEP 21 ALA A 129 PRO A 130 21 -0.60 CISPEP 22 ALA A 129 PRO A 130 22 -0.43 CISPEP 23 ALA A 129 PRO A 130 23 -0.13 CISPEP 24 ALA A 129 PRO A 130 24 -0.51 CISPEP 25 ALA A 129 PRO A 130 25 -0.79 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 - b 23 2 Bytes