Header list of 1t4z.pdb file
Complete list - r 25 2 Bytes
HEADER TRANSFERASE 30-APR-04 1T4Z
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNECHOCOCCUS ELONGATUS
TITLE 2 SASA (25-STRUCTURES ENSEMBLE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADAPTIVE-RESPONSE SENSORY-KINASE SASA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 EC: 2.7.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 1140;
SOURCE 4 STRAIN: PCC 7942;
SOURCE 5 GENE: SASA, SARS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A+
KEYWDS ALPHA/BETA PROTEIN, THIOREDOXIN FOLD, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR I.VAKONAKIS,D.A.KLEWER,A.C.LIWANG
REVDAT 3 13-JUL-11 1T4Z 1 VERSN
REVDAT 2 24-FEB-09 1T4Z 1 VERSN
REVDAT 1 16-NOV-04 1T4Z 0
JRNL AUTH I.VAKONAKIS,D.A.KLEWER,S.B.WILLIAMS,S.S.GOLDEN,A.C.LIWANG
JRNL TITL STRUCTURE OF THE N-TERMINAL DOMAIN OF THE CIRCADIAN
JRNL TITL 2 CLOCK-ASSOCIATED HISTIDINE KINASE SASA.
JRNL REF J.MOL.BIOL. V. 342 9 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15313603
JRNL DOI 10.1016/J.JMB.2004.07.010
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.9.1
REMARK 3 AUTHORS : CLORE, KUSZEWSKI
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 2267
REMARK 3 RESTRAINTS, 1764 WERE NOE, 197 DIHEDRAL ANGLES, 71 COUPLINGS, 198
REMARK 3 CHEMICAL SHIFTS AND 34 HYDROGEN BONDS
REMARK 4
REMARK 4 1T4Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-04.
REMARK 100 THE RCSB ID CODE IS RCSB022318.
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 : 100 MM NACL, 20 MM NAPI
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM N-SASA U-15N, 13C, 20MM
REMARK 210 PHOSPHATE BUFFER PH 7.0, 100MM
REMARK 210 NACL, 95% H2O, 5% D2O; 0.8MM N-
REMARK 210 SASA U-15N, 13C, 20MM PHOSPHATE
REMARK 210 BUFFER PH 7.0, 100MM NACL, 100%
REMARK 210 D2O; 0.8MM N-SASA U-15N, 20MM
REMARK 210 PHOSPHATE BUFFER PH 7.0, 100MM
REMARK 210 NACL, 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C/15N-SEPARATED_NOESY; 4D_
REMARK 210 13C-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1 REV. C, NMRPIPE 2.1
REMARK 210 REV. 2002.044.17.08, PIPP 4.2.6,
REMARK 210 XPLOR-NIH 2.9.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, SLOW REFINEMENT IN THE
REMARK 210 PRESENCE OF DATABASE POTENTIALS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
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: 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 HG SER A 82 H GLY A 83 1.29
REMARK 500 H LEU A 70 O LEU A 81 1.45
REMARK 500 H LEU A 14 O GLY A 74 1.52
REMARK 500 O LEU A 86 H LEU A 90 1.54
REMARK 500 O ASP A 20 HG1 THR A 21 1.55
REMARK 500 O LEU A 70 H LEU A 81 1.58
REMARK 500 O ALA A 37 OE2 GLU A 40 2.19
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 8 43.92 -179.65
REMARK 500 1 PRO A 12 163.65 -44.56
REMARK 500 1 VAL A 39 -29.09 -151.86
REMARK 500 1 GLU A 40 -96.49 36.56
REMARK 500 1 ALA A 41 -178.36 85.45
REMARK 500 1 VAL A 43 71.45 -118.00
REMARK 500 1 ARG A 63 5.68 57.82
REMARK 500 1 VAL A 65 -11.60 -141.40
REMARK 500 1 ILE A 84 5.27 42.19
REMARK 500 2 SER A 2 -97.48 -133.50
REMARK 500 2 LEU A 4 -76.94 -117.18
REMARK 500 2 GLN A 7 98.09 -5.36
REMARK 500 2 ALA A 10 -163.41 -68.08
REMARK 500 2 VAL A 39 -27.28 -149.86
REMARK 500 2 GLU A 40 -110.79 40.46
REMARK 500 2 ALA A 41 176.53 88.58
REMARK 500 2 VAL A 43 71.34 -119.44
REMARK 500 2 ARG A 63 5.11 57.86
REMARK 500 2 VAL A 65 -13.11 -146.19
REMARK 500 2 PRO A 75 -82.26 -53.66
REMARK 500 2 ILE A 84 6.05 41.95
REMARK 500 2 GLN A 101 165.20 -36.83
REMARK 500 3 PRO A 6 156.36 -49.05
REMARK 500 3 PRO A 12 159.59 -47.95
REMARK 500 3 THR A 21 -3.47 54.81
REMARK 500 3 VAL A 39 -36.30 -150.75
REMARK 500 3 GLU A 40 -87.50 35.55
REMARK 500 3 ALA A 41 -169.74 81.60
REMARK 500 3 GLN A 55 77.70 -152.83
REMARK 500 3 VAL A 65 -5.60 -145.19
REMARK 500 3 ILE A 84 6.78 42.44
REMARK 500 3 GLU A 102 -144.81 57.32
REMARK 500 4 LEU A 4 -74.93 -89.67
REMARK 500 4 SER A 5 58.28 -167.85
REMARK 500 4 ALA A 8 76.26 27.69
REMARK 500 4 VAL A 39 -31.42 -149.72
REMARK 500 4 GLU A 40 -85.43 35.88
REMARK 500 4 ALA A 41 -175.21 85.76
REMARK 500 4 ARG A 63 5.01 57.23
REMARK 500 4 VAL A 65 -12.70 -141.93
REMARK 500 4 ILE A 84 5.19 41.70
REMARK 500 4 VAL A 99 32.12 -86.74
REMARK 500 4 GLN A 101 -93.63 -158.19
REMARK 500 4 GLU A 102 40.84 30.38
REMARK 500 5 SER A 3 -14.94 61.28
REMARK 500 5 ALA A 8 81.20 -16.77
REMARK 500 5 THR A 21 10.05 81.22
REMARK 500 5 GLU A 40 -82.02 45.19
REMARK 500 5 ALA A 41 163.39 48.38
REMARK 500 5 VAL A 43 78.50 -114.18
REMARK 500
REMARK 500 THIS ENTRY HAS 249 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 22 0.12 SIDE CHAIN
REMARK 500 1 ARG A 31 0.28 SIDE CHAIN
REMARK 500 1 ARG A 63 0.26 SIDE CHAIN
REMARK 500 1 ARG A 78 0.30 SIDE CHAIN
REMARK 500 2 ARG A 22 0.08 SIDE CHAIN
REMARK 500 2 ARG A 31 0.31 SIDE CHAIN
REMARK 500 2 ARG A 63 0.28 SIDE CHAIN
REMARK 500 2 ARG A 78 0.22 SIDE CHAIN
REMARK 500 3 ARG A 22 0.27 SIDE CHAIN
REMARK 500 3 ARG A 31 0.30 SIDE CHAIN
REMARK 500 3 ARG A 63 0.26 SIDE CHAIN
REMARK 500 4 ARG A 22 0.28 SIDE CHAIN
REMARK 500 4 ARG A 31 0.26 SIDE CHAIN
REMARK 500 4 ARG A 63 0.27 SIDE CHAIN
REMARK 500 4 ARG A 78 0.16 SIDE CHAIN
REMARK 500 5 ARG A 22 0.13 SIDE CHAIN
REMARK 500 5 ARG A 31 0.28 SIDE CHAIN
REMARK 500 5 ARG A 63 0.09 SIDE CHAIN
REMARK 500 5 ARG A 78 0.16 SIDE CHAIN
REMARK 500 6 ARG A 22 0.30 SIDE CHAIN
REMARK 500 6 ARG A 31 0.31 SIDE CHAIN
REMARK 500 6 ARG A 63 0.08 SIDE CHAIN
REMARK 500 6 ARG A 78 0.18 SIDE CHAIN
REMARK 500 7 ARG A 22 0.08 SIDE CHAIN
REMARK 500 7 ARG A 31 0.26 SIDE CHAIN
REMARK 500 7 ARG A 63 0.10 SIDE CHAIN
REMARK 500 7 ARG A 78 0.19 SIDE CHAIN
REMARK 500 8 ARG A 22 0.27 SIDE CHAIN
REMARK 500 8 ARG A 31 0.29 SIDE CHAIN
REMARK 500 8 ARG A 63 0.23 SIDE CHAIN
REMARK 500 8 ARG A 78 0.23 SIDE CHAIN
REMARK 500 9 ARG A 22 0.23 SIDE CHAIN
REMARK 500 9 ARG A 31 0.30 SIDE CHAIN
REMARK 500 9 ARG A 63 0.22 SIDE CHAIN
REMARK 500 9 ARG A 78 0.27 SIDE CHAIN
REMARK 500 10 ARG A 22 0.31 SIDE CHAIN
REMARK 500 10 ARG A 31 0.09 SIDE CHAIN
REMARK 500 10 ARG A 63 0.08 SIDE CHAIN
REMARK 500 10 ARG A 78 0.08 SIDE CHAIN
REMARK 500 11 ARG A 63 0.14 SIDE CHAIN
REMARK 500 11 ARG A 78 0.30 SIDE CHAIN
REMARK 500 12 ARG A 22 0.30 SIDE CHAIN
REMARK 500 12 ARG A 31 0.31 SIDE CHAIN
REMARK 500 12 ARG A 63 0.28 SIDE CHAIN
REMARK 500 12 ARG A 78 0.26 SIDE CHAIN
REMARK 500 13 ARG A 22 0.25 SIDE CHAIN
REMARK 500 13 ARG A 31 0.20 SIDE CHAIN
REMARK 500 13 ARG A 63 0.30 SIDE CHAIN
REMARK 500 13 ARG A 78 0.26 SIDE CHAIN
REMARK 500 14 ARG A 22 0.23 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 91 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T4Y RELATED DB: PDB
DBREF 1T4Z A 3 102 UNP Q06904 SASA_SYNP7 4 103
SEQADV 1T4Z GLY A 1 UNP Q06904 CLONING ARTIFACT
SEQADV 1T4Z SER A 2 UNP Q06904 CLONING ARTIFACT
SEQADV 1T4Z GLY A 103 UNP Q06904 CLONING ARTIFACT
SEQADV 1T4Z ILE A 104 UNP Q06904 CLONING ARTIFACT
SEQADV 1T4Z PHE A 105 UNP Q06904 CLONING ARTIFACT
SEQRES 1 A 105 GLY SER SER LEU SER PRO GLN ALA LEU ALA GLN PRO LEU
SEQRES 2 A 105 LEU LEU GLN LEU PHE VAL ASP THR ARG PRO LEU SER GLN
SEQRES 3 A 105 HIS ILE VAL GLN ARG VAL LYS ASN ILE LEU ALA ALA VAL
SEQRES 4 A 105 GLU ALA THR VAL PRO ILE SER LEU GLN VAL ILE ASN VAL
SEQRES 5 A 105 ALA ASP GLN PRO GLN LEU VAL GLU TYR TYR ARG LEU VAL
SEQRES 6 A 105 VAL THR PRO ALA LEU VAL LYS ILE GLY PRO GLY SER ARG
SEQRES 7 A 105 GLN VAL LEU SER GLY ILE ASP LEU THR ASP GLN LEU ALA
SEQRES 8 A 105 ASN GLN LEU PRO GLN TRP LEU VAL GLN GLN GLU GLY ILE
SEQRES 9 A 105 PHE
HELIX 1 1 ARG A 22 ALA A 37 1 16
HELIX 2 2 GLN A 55 TYR A 62 1 8
HELIX 3 3 ASP A 85 GLN A 100 1 16
SHEET 1 A 4 ILE A 45 ASN A 51 0
SHEET 2 A 4 LEU A 13 VAL A 19 1 N LEU A 13 O SER A 46
SHEET 3 A 4 ALA A 69 GLY A 74 -1 O GLY A 74 N LEU A 14
SHEET 4 A 4 GLN A 79 SER A 82 -1 O LEU A 81 N LEU A 70
CISPEP 1 THR A 67 PRO A 68 1 0.45
CISPEP 2 GLY A 74 PRO A 75 1 0.49
CISPEP 3 THR A 67 PRO A 68 2 0.69
CISPEP 4 GLY A 74 PRO A 75 2 -0.15
CISPEP 5 THR A 67 PRO A 68 3 0.63
CISPEP 6 GLY A 74 PRO A 75 3 0.27
CISPEP 7 THR A 67 PRO A 68 4 0.46
CISPEP 8 GLY A 74 PRO A 75 4 0.22
CISPEP 9 THR A 67 PRO A 68 5 0.74
CISPEP 10 GLY A 74 PRO A 75 5 0.40
CISPEP 11 THR A 67 PRO A 68 6 0.34
CISPEP 12 GLY A 74 PRO A 75 6 -0.17
CISPEP 13 THR A 67 PRO A 68 7 0.18
CISPEP 14 GLY A 74 PRO A 75 7 0.00
CISPEP 15 THR A 67 PRO A 68 8 1.07
CISPEP 16 GLY A 74 PRO A 75 8 0.52
CISPEP 17 THR A 67 PRO A 68 9 0.86
CISPEP 18 GLY A 74 PRO A 75 9 0.47
CISPEP 19 THR A 67 PRO A 68 10 0.92
CISPEP 20 GLY A 74 PRO A 75 10 0.53
CISPEP 21 THR A 67 PRO A 68 11 0.47
CISPEP 22 GLY A 74 PRO A 75 11 0.30
CISPEP 23 THR A 67 PRO A 68 12 0.40
CISPEP 24 GLY A 74 PRO A 75 12 0.11
CISPEP 25 THR A 67 PRO A 68 13 0.27
CISPEP 26 GLY A 74 PRO A 75 13 0.58
CISPEP 27 THR A 67 PRO A 68 14 0.28
CISPEP 28 GLY A 74 PRO A 75 14 0.36
CISPEP 29 THR A 67 PRO A 68 15 0.72
CISPEP 30 GLY A 74 PRO A 75 15 0.76
CISPEP 31 THR A 67 PRO A 68 16 0.56
CISPEP 32 GLY A 74 PRO A 75 16 0.59
CISPEP 33 THR A 67 PRO A 68 17 0.89
CISPEP 34 GLY A 74 PRO A 75 17 0.08
CISPEP 35 THR A 67 PRO A 68 18 0.92
CISPEP 36 GLY A 74 PRO A 75 18 0.22
CISPEP 37 THR A 67 PRO A 68 19 0.27
CISPEP 38 GLY A 74 PRO A 75 19 0.18
CISPEP 39 THR A 67 PRO A 68 20 0.30
CISPEP 40 GLY A 74 PRO A 75 20 -0.53
CISPEP 41 THR A 67 PRO A 68 21 0.19
CISPEP 42 GLY A 74 PRO A 75 21 0.07
CISPEP 43 THR A 67 PRO A 68 22 0.64
CISPEP 44 GLY A 74 PRO A 75 22 0.44
CISPEP 45 THR A 67 PRO A 68 23 0.19
CISPEP 46 GLY A 74 PRO A 75 23 -0.13
CISPEP 47 THR A 67 PRO A 68 24 0.19
CISPEP 48 GLY A 74 PRO A 75 24 0.34
CISPEP 49 THR A 67 PRO A 68 25 0.15
CISPEP 50 GLY A 74 PRO A 75 25 0.05
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 25 2 Bytes