Header list of 1lkj.pdb file
Complete list - b 23 2 Bytes
HEADER METAL BINDING PROTEIN 25-APR-02 1LKJ
TITLE NMR STRUCTURE OF APO CALMODULIN FROM YEAST SACCHAROMYCES CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
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: PET30B
KEYWDS YEAST CALMODULIN, SACCHAROMYCES CEREVISIAE, EF-HAND, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 31
AUTHOR H.ISHIDA,K.NAKASHIMA,Y.KUMAKI,M.NAKATA,K.HIKICHI,M.YAZAWA
REVDAT 3 23-FEB-22 1LKJ 1 REMARK
REVDAT 2 24-FEB-09 1LKJ 1 VERSN
REVDAT 1 29-APR-03 1LKJ 0
JRNL AUTH H.ISHIDA,K.NAKASHIMA,Y.KUMAKI,M.NAKATA,K.HIKICHI,M.YAZAWA
JRNL TITL THE SOLUTION STRUCTURE OF APOCALMODULIN FROM SACCHAROMYCES
JRNL TITL 2 CEREVISIAE IMPLIES A MECHANISM FOR ITS UNIQUE CA2+ BINDING
JRNL TITL 3 PROPERTY.
JRNL REF BIOCHEMISTRY V. 41 15536 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12501182
JRNL DOI 10.1021/BI020330R
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER, A. T. (X-PLOR), BRUNGER, A. T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LKJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000016030.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0-1.4MM YEAST CALMUDULIN U
REMARK 210 -15N,13C; 50MM KCL; 1.0-1.4MM
REMARK 210 YEAST CALMUDULIN U-15N; 50MM KCL;
REMARK 210 1.0-1.4MM YEAST CALMODULIN;
REMARK 210 50MM KCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 4D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : A; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : JEOL; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 31
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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
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 LYS A 21 52.68 -118.71
REMARK 500 1 ASP A 22 -98.55 -128.80
REMARK 500 1 ASN A 23 34.08 -174.43
REMARK 500 1 ASN A 24 -75.02 -150.06
REMARK 500 1 SER A 42 64.03 -168.66
REMARK 500 1 LEU A 76 47.89 -95.53
REMARK 500 1 SER A 78 50.58 -167.21
REMARK 500 1 ASP A 80 97.66 -167.85
REMARK 500 1 THR A 117 -167.25 -63.05
REMARK 500 1 SER A 132 -67.92 -132.20
REMARK 500 1 SER A 145 -73.70 -102.61
REMARK 500 2 LYS A 21 67.42 -103.37
REMARK 500 2 ASP A 22 -75.23 -138.41
REMARK 500 2 ASN A 23 -59.90 -164.95
REMARK 500 2 SER A 42 68.66 -168.89
REMARK 500 2 HIS A 61 108.50 56.68
REMARK 500 2 LYS A 77 -158.81 41.36
REMARK 500 2 SER A 78 -52.27 -168.38
REMARK 500 2 LYS A 94 41.17 -108.88
REMARK 500 2 ASN A 95 -43.30 -158.30
REMARK 500 2 THR A 117 -174.17 -62.98
REMARK 500 3 ASN A 3 -170.79 52.56
REMARK 500 3 LYS A 21 -92.74 -79.33
REMARK 500 3 ASP A 22 43.52 -173.07
REMARK 500 3 ASN A 23 -63.76 -101.97
REMARK 500 3 ASN A 24 27.52 -150.57
REMARK 500 3 SER A 42 68.79 -166.34
REMARK 500 3 ASP A 56 92.18 -58.55
REMARK 500 3 ASP A 58 -150.89 -127.43
REMARK 500 3 ASN A 79 42.61 -106.58
REMARK 500 3 ASN A 95 -59.85 -134.32
REMARK 500 4 ASN A 23 25.79 -151.18
REMARK 500 4 ASN A 24 -86.62 55.44
REMARK 500 4 SER A 42 67.19 -167.35
REMARK 500 4 ASP A 56 94.32 -64.59
REMARK 500 4 HIS A 61 116.61 -167.17
REMARK 500 4 ASP A 80 43.89 -158.61
REMARK 500 4 ASP A 130 -37.98 -169.96
REMARK 500 4 SER A 132 -58.40 -124.89
REMARK 500 5 SER A 2 -63.84 -98.84
REMARK 500 5 LYS A 21 -90.47 -64.94
REMARK 500 5 ASP A 22 35.89 -175.79
REMARK 500 5 ASN A 23 -66.19 -151.48
REMARK 500 5 SER A 42 68.21 -167.72
REMARK 500 5 ILE A 55 -62.49 -94.02
REMARK 500 5 LEU A 76 46.48 -92.50
REMARK 500 5 LYS A 77 -158.12 -61.62
REMARK 500 5 SER A 78 89.30 -60.40
REMARK 500 5 SER A 81 -70.46 -59.98
REMARK 500 5 LYS A 94 -65.36 66.15
REMARK 500
REMARK 500 THIS ENTRY HAS 349 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 37 0.20 SIDE CHAIN
REMARK 500 1 ARG A 74 0.22 SIDE CHAIN
REMARK 500 1 ARG A 126 0.32 SIDE CHAIN
REMARK 500 2 ARG A 37 0.26 SIDE CHAIN
REMARK 500 2 ARG A 74 0.28 SIDE CHAIN
REMARK 500 2 ARG A 126 0.22 SIDE CHAIN
REMARK 500 3 ARG A 37 0.24 SIDE CHAIN
REMARK 500 3 ARG A 74 0.21 SIDE CHAIN
REMARK 500 3 ARG A 126 0.32 SIDE CHAIN
REMARK 500 4 ARG A 37 0.31 SIDE CHAIN
REMARK 500 4 ARG A 74 0.24 SIDE CHAIN
REMARK 500 4 ARG A 126 0.30 SIDE CHAIN
REMARK 500 5 ARG A 37 0.23 SIDE CHAIN
REMARK 500 5 ARG A 74 0.30 SIDE CHAIN
REMARK 500 5 ARG A 126 0.31 SIDE CHAIN
REMARK 500 6 ARG A 37 0.30 SIDE CHAIN
REMARK 500 6 ARG A 74 0.22 SIDE CHAIN
REMARK 500 6 ARG A 126 0.22 SIDE CHAIN
REMARK 500 7 ARG A 37 0.28 SIDE CHAIN
REMARK 500 7 ARG A 74 0.22 SIDE CHAIN
REMARK 500 7 ARG A 126 0.22 SIDE CHAIN
REMARK 500 8 ARG A 37 0.31 SIDE CHAIN
REMARK 500 8 ARG A 74 0.29 SIDE CHAIN
REMARK 500 8 ARG A 126 0.25 SIDE CHAIN
REMARK 500 9 ARG A 37 0.32 SIDE CHAIN
REMARK 500 9 ARG A 74 0.26 SIDE CHAIN
REMARK 500 9 ARG A 126 0.22 SIDE CHAIN
REMARK 500 10 ARG A 37 0.26 SIDE CHAIN
REMARK 500 10 ARG A 74 0.32 SIDE CHAIN
REMARK 500 10 ARG A 126 0.25 SIDE CHAIN
REMARK 500 11 ARG A 37 0.25 SIDE CHAIN
REMARK 500 11 ARG A 74 0.24 SIDE CHAIN
REMARK 500 11 ARG A 126 0.26 SIDE CHAIN
REMARK 500 12 ARG A 37 0.23 SIDE CHAIN
REMARK 500 12 ARG A 74 0.31 SIDE CHAIN
REMARK 500 12 ARG A 126 0.27 SIDE CHAIN
REMARK 500 13 ARG A 37 0.21 SIDE CHAIN
REMARK 500 13 ARG A 74 0.32 SIDE CHAIN
REMARK 500 13 ARG A 126 0.31 SIDE CHAIN
REMARK 500 14 ARG A 37 0.31 SIDE CHAIN
REMARK 500 14 ARG A 74 0.27 SIDE CHAIN
REMARK 500 14 ARG A 126 0.31 SIDE CHAIN
REMARK 500 15 ARG A 37 0.29 SIDE CHAIN
REMARK 500 15 ARG A 74 0.21 SIDE CHAIN
REMARK 500 15 ARG A 126 0.27 SIDE CHAIN
REMARK 500 16 ARG A 37 0.26 SIDE CHAIN
REMARK 500 16 ARG A 74 0.22 SIDE CHAIN
REMARK 500 16 ARG A 126 0.23 SIDE CHAIN
REMARK 500 17 ARG A 37 0.27 SIDE CHAIN
REMARK 500 17 ARG A 74 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 93 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F54 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE APO N-TERMINAL DOMAIN OF YEAST CALMODULIN
REMARK 900 RELATED ID: 1F55 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE CALCIUM BOUND N-TERMINAL DOMAIN OF YEAST
REMARK 900 CALMODULIN
DBREF 1LKJ A 1 146 UNP P06787 CALM_YEAST 2 147
SEQRES 1 A 146 SER SER ASN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 146 GLU ALA PHE ALA LEU PHE ASP LYS ASP ASN ASN GLY SER
SEQRES 3 A 146 ILE SER SER SER GLU LEU ALA THR VAL MET ARG SER LEU
SEQRES 4 A 146 GLY LEU SER PRO SER GLU ALA GLU VAL ASN ASP LEU MET
SEQRES 5 A 146 ASN GLU ILE ASP VAL ASP GLY ASN HIS GLN ILE GLU PHE
SEQRES 6 A 146 SER GLU PHE LEU ALA LEU MET SER ARG GLN LEU LYS SER
SEQRES 7 A 146 ASN ASP SER GLU GLN GLU LEU LEU GLU ALA PHE LYS VAL
SEQRES 8 A 146 PHE ASP LYS ASN GLY ASP GLY LEU ILE SER ALA ALA GLU
SEQRES 9 A 146 LEU LYS HIS VAL LEU THR SER ILE GLY GLU LYS LEU THR
SEQRES 10 A 146 ASP ALA GLU VAL ASP ASP MET LEU ARG GLU VAL SER ASP
SEQRES 11 A 146 GLY SER GLY GLU ILE ASN ILE GLN GLN PHE ALA ALA LEU
SEQRES 12 A 146 LEU SER LYS
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 SER A 29 GLY A 40 1 12
HELIX 3 3 SER A 44 ASP A 56 1 13
HELIX 4 4 PHE A 65 LEU A 76 1 12
HELIX 5 5 ASP A 80 ASP A 93 1 14
HELIX 6 6 ALA A 102 GLY A 113 1 12
HELIX 7 7 THR A 117 SER A 129 1 13
HELIX 8 8 ILE A 137 SER A 145 1 9
SHEET 1 A 2 SER A 26 SER A 28 0
SHEET 2 A 2 GLN A 62 GLU A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 B 2 LEU A 99 SER A 101 0
SHEET 2 B 2 GLU A 134 ASN A 136 -1 O ILE A 135 N ILE A 100
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