Header list of 1kcy.pdb file
Complete list - t 27 2 Bytes
HEADER METAL BINDING PROTEIN 12-NOV-01 1KCY TITLE NMR SOLUTION STRUCTURE OF APO CALBINDIN D9K (F36G + P43M MUTANT) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALBINDIN D9K; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CONTAINS EF-HAND 1 (LOW AFFINITY) AND EF-HAND 2 (HIGH COMPND 5 AFFINITY); COMPND 6 SYNONYM: CABP, VITAMIN D-DEPENDENT CALCIUM-BINDING PROTEIN, COMPND 7 INTESTINAL; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRCB1 KEYWDS EF HAND, CALCIUM-BINDING PROTEIN, STRUCTURE PERTURBING MUTATION, FOUR KEYWDS 2 HELIX BUNDLE, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 22 AUTHOR M.R.NELSON,E.THULIN,P.A.FAGAN,S.FORSEN,W.J.CHAZIN REVDAT 4 27-OCT-21 1KCY 1 REMARK SEQADV REVDAT 3 24-FEB-09 1KCY 1 VERSN REVDAT 2 06-FEB-02 1KCY 1 JRNL REMARK REVDAT 1 21-NOV-01 1KCY 0 JRNL AUTH M.R.NELSON,E.THULIN,P.A.FAGAN,S.FORSEN,W.J.CHAZIN JRNL TITL THE EF-HAND DOMAIN: A GLOBALLY COOPERATIVE STRUCTURAL UNIT. JRNL REF PROTEIN SCI. V. 11 198 2002 JRNL REFN ISSN 0961-8368 JRNL PMID 11790829 JRNL DOI 10.1110/PS.33302 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DIANA 2.8, AMBER 4.1 REMARK 3 AUTHORS : GUNTERT (DIANA), PEARLMANN (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1042 NOE REMARK 3 RESTRAINTS (186 INTRARESIDUE, 269 SEQUENTIAL, 289 MEDIUM RANGE REMARK 3 (2-4 RESIDUES APART), 298 LONG RANGE), 18 HYDROGEN BOND REMARK 3 RESTRAINTS (ASSIGNED AS DESCRIBED IN SKELTON ET AL., 1995), AND REMARK 3 115 DIHEDRAL CONSTRAINTS (45 PHI, 42 PSI, AND 28 CHI1). REMARK 4 REMARK 4 1KCY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-01. REMARK 100 THE DEPOSITION ID IS D_1000014823. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : NO ADDED SALTS REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2.5 MM CALBINDIN; 95% H2O; 5% REMARK 210 D2O; 2.5 MM CALBINDIN D9K U-15N; REMARK 210 95% H2O; 5% D2O; 2.5 MM REMARK 210 CALBINDIN D9K; 100% D20 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_COSY; 2D_NOESY; 2D_TOCSY; REMARK 210 2D_15N-1H_HSQC; 3D_15N-SEPARATED_ REMARK 210 TOCSY; 3D_15N-SEPARATED_NOESY; REMARK 210 HNHA; HNHB REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : AMX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AMBER 4.1, FELIX 97, GLOMSA REMARK 210 UNKNOWN, GENXPK 1 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22 REMARK 210 CONFORMERS, SELECTION CRITERIA : THE FULL ENSEMBLE WAS ORDERED BY REMARK 210 LOWEST RESIDUAL CONSTRAINT REMARK 210 VIOLATIONS, THEN THE TOP 22 WITH REMARK 210 FAVORABLE COVALENT GEOMETRIES REMARK 210 AND AMBER ENERGIES WERE SELECTED REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING A COMBINATION OF REMARK 210 STANDARD 2D HOMONUCLEAR AND 15N-BASED 3D METHODS. 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: 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 25 -54.50 -26.34 REMARK 500 1 LYS A 41 28.54 -141.45 REMARK 500 1 SER A 44 -121.94 -145.08 REMARK 500 2 LYS A 25 -65.99 -24.09 REMARK 500 2 SER A 44 -155.43 175.21 REMARK 500 2 ASP A 54 -47.95 -29.97 REMARK 500 3 GLU A 17 27.25 -79.97 REMARK 500 3 LYS A 25 -55.82 -20.11 REMARK 500 3 LEU A 31 -79.44 -68.91 REMARK 500 3 LEU A 32 -60.37 -21.68 REMARK 500 3 GLN A 33 -54.80 -24.85 REMARK 500 3 THR A 34 -62.32 -24.56 REMARK 500 3 SER A 44 -79.34 -134.25 REMARK 500 3 GLU A 60 76.32 48.47 REMARK 500 4 LYS A 25 -78.71 0.88 REMARK 500 4 LEU A 39 25.36 -146.33 REMARK 500 4 MET A 43 -131.66 42.59 REMARK 500 4 SER A 44 -147.96 48.03 REMARK 500 5 MET A 43 -117.52 40.45 REMARK 500 5 SER A 44 -126.08 26.50 REMARK 500 6 SER A 38 -61.25 -101.47 REMARK 500 6 SER A 44 -142.51 -146.10 REMARK 500 6 THR A 45 -59.84 -27.68 REMARK 500 7 LYS A 25 -65.74 -19.98 REMARK 500 7 SER A 44 -169.03 -169.82 REMARK 500 8 GLU A 17 45.63 -75.51 REMARK 500 8 LYS A 25 -59.59 -29.32 REMARK 500 8 SER A 44 -82.51 -171.23 REMARK 500 9 LYS A 25 -62.96 -23.85 REMARK 500 9 MET A 43 -82.86 17.47 REMARK 500 9 SER A 44 -107.61 18.81 REMARK 500 10 SER A 44 -138.42 -146.76 REMARK 500 11 LYS A 25 -62.33 -18.49 REMARK 500 11 SER A 44 -81.61 -94.64 REMARK 500 11 ASP A 58 -63.95 68.98 REMARK 500 11 GLU A 60 84.27 -150.46 REMARK 500 12 LYS A 25 -73.55 -18.77 REMARK 500 12 LEU A 39 13.09 -142.05 REMARK 500 12 MET A 43 -90.49 48.07 REMARK 500 12 SER A 44 -94.43 9.14 REMARK 500 13 LYS A 25 -62.57 -24.39 REMARK 500 13 SER A 44 -151.42 -178.30 REMARK 500 14 LEU A 39 14.44 -144.98 REMARK 500 14 MET A 43 -77.05 68.28 REMARK 500 14 SER A 44 -100.78 7.92 REMARK 500 15 LYS A 25 -61.11 -25.08 REMARK 500 15 SER A 44 -137.82 -148.23 REMARK 500 16 LYS A 25 -63.97 -22.60 REMARK 500 16 LYS A 41 45.88 -144.46 REMARK 500 16 MET A 43 85.56 -66.79 REMARK 500 REMARK 500 THIS ENTRY HAS 74 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 PHE A 50 0.12 SIDE CHAIN REMARK 500 1 PHE A 63 0.07 SIDE CHAIN REMARK 500 3 PHE A 50 0.14 SIDE CHAIN REMARK 500 3 PHE A 63 0.09 SIDE CHAIN REMARK 500 4 PHE A 50 0.10 SIDE CHAIN REMARK 500 6 PHE A 50 0.20 SIDE CHAIN REMARK 500 7 PHE A 50 0.15 SIDE CHAIN REMARK 500 7 PHE A 63 0.08 SIDE CHAIN REMARK 500 8 PHE A 50 0.12 SIDE CHAIN REMARK 500 8 PHE A 63 0.10 SIDE CHAIN REMARK 500 9 PHE A 50 0.09 SIDE CHAIN REMARK 500 10 PHE A 50 0.14 SIDE CHAIN REMARK 500 11 PHE A 63 0.08 SIDE CHAIN REMARK 500 12 PHE A 63 0.08 SIDE CHAIN REMARK 500 13 PHE A 50 0.17 SIDE CHAIN REMARK 500 14 PHE A 50 0.09 SIDE CHAIN REMARK 500 15 PHE A 50 0.12 SIDE CHAIN REMARK 500 15 PHE A 63 0.08 SIDE CHAIN REMARK 500 16 PHE A 50 0.11 SIDE CHAIN REMARK 500 16 PHE A 63 0.09 SIDE CHAIN REMARK 500 17 PHE A 50 0.10 SIDE CHAIN REMARK 500 17 PHE A 63 0.08 SIDE CHAIN REMARK 500 17 PHE A 66 0.09 SIDE CHAIN REMARK 500 18 PHE A 50 0.10 SIDE CHAIN REMARK 500 18 PHE A 63 0.08 SIDE CHAIN REMARK 500 18 PHE A 66 0.08 SIDE CHAIN REMARK 500 20 PHE A 50 0.09 SIDE CHAIN REMARK 500 20 PHE A 63 0.08 SIDE CHAIN REMARK 500 21 PHE A 50 0.11 SIDE CHAIN REMARK 500 21 PHE A 63 0.08 SIDE CHAIN REMARK 500 22 PHE A 50 0.12 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CLB RELATED DB: PDB REMARK 900 1CLB IS THE STRUCTURE OF APO P43G CALBINDIN D9K. P43G IS REMARK 900 ESSENTIALLY "WILDTYPE", AND IS VERY SIMILAR TO THE P43M MUTATION REMARK 900 USED AS A BACKGROUND FOR THE F36G MUTATION. REMARK 999 REMARK 999 SEQUENCE REMARK 999 P43M IS THE BACKGROUND MUTATION USED IN REMARK 999 THE CHAZIN LAB TO STUDY ALL CALBINDIN REMARK 999 D9K MUTANTS. THIS MUTATION REMOVES REMARK 999 SPECTRA-COMPLICATING CIS-TRANS REMARK 999 ISOMERIZATION AT PRO43 BUT DOES NOT REMARK 999 OTHERWISE AFFECT THE STRUCTURE. DBREF 1KCY A 1 75 UNP P02633 S100G_BOVIN 4 78 SEQADV 1KCY GLY A 36 UNP P02633 PHE 39 ENGINEERED MUTATION SEQADV 1KCY MET A 43 UNP P02633 PRO 46 ENGINEERED MUTATION SEQRES 1 A 75 LYS SER PRO GLU GLU LEU LYS GLY ILE PHE GLU LYS TYR SEQRES 2 A 75 ALA ALA LYS GLU GLY ASP PRO ASN GLN LEU SER LYS GLU SEQRES 3 A 75 GLU LEU LYS LEU LEU LEU GLN THR GLU GLY PRO SER LEU SEQRES 4 A 75 LEU LYS GLY MET SER THR LEU ASP GLU LEU PHE GLU GLU SEQRES 5 A 75 LEU ASP LYS ASN GLY ASP GLY GLU VAL SER PHE GLU GLU SEQRES 6 A 75 PHE GLN VAL LEU VAL LYS LYS ILE SER GLN HELIX 1 1 LYS A 1 GLU A 17 1 17 HELIX 2 2 LYS A 25 LEU A 40 1 16 HELIX 3 3 SER A 44 GLY A 57 1 14 HELIX 4 4 PHE A 63 GLN A 75 1 13 SHEET 1 A 2 GLN A 22 SER A 24 0 SHEET 2 A 2 GLU A 60 SER A 62 -1 O VAL A 61 N LEU A 23 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 - t 27 2 Bytes