Header list of 1psb.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 21-JUN-03 1PSB TITLE SOLUTION STRUCTURE OF CALCIUM LOADED S100B COMPLEXED TO A PEPTIDE FROM TITLE 2 N-TERMINAL REGULATORY DOMAIN OF NDR KINASE. COMPND MOL_ID: 1; COMPND 2 MOLECULE: S-100 PROTEIN, BETA CHAIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NDR SER/THR KINASE-LIKE PROTEIN; COMPND 7 CHAIN: C, D; COMPND 8 FRAGMENT: N-TERMINAL REGULATORY DOMAIN FRAGMENT, SEQUENCE DATABASE COMPND 9 RESIDUE 60-85; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 GENE: S100B; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 CODON PLUS (DE3) RIL; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PH6 TEV; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HOMO SAPIENS. KEYWDS HELIX-LOOP-HELIX, PROTEIN-PEPTIDE COMPLEX, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.BHATTACHARYA,E.LARGE,C.W.HEIZMANN,B.HEMMINGS,W.J.CHAZIN REVDAT 3 02-MAR-22 1PSB 1 REMARK REVDAT 2 24-FEB-09 1PSB 1 VERSN REVDAT 1 16-DEC-03 1PSB 0 JRNL AUTH S.BHATTACHARYA,E.LARGE,C.W.HEIZMANN,B.HEMMINGS,W.J.CHAZIN JRNL TITL STRUCTURE OF THE CA(2+)/S100B/NDR KINASE PEPTIDE COMPLEX: JRNL TITL 2 INSIGHTS INTO S100 TARGET SPECIFICITY AND ACTIVATION OF THE JRNL TITL 3 KINASE. JRNL REF BIOCHEMISTRY V. 42 14416 2003 JRNL REFN ISSN 0006-2960 JRNL PMID 14661952 JRNL DOI 10.1021/BI035089A REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.0, AMBER 7.0 REMARK 3 AUTHORS : BRUKER (XWINNMR), PEARLMAN, CASE, CALDWELL, REMARK 3 SEIBEL, CHANDRA SINGH, WEINER, KOLLMAN (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A REMARK 3 TOTAL OF 3274 RESTRAINTS, 2964 REMARK 3 ARE NOE-DERIVED DISTANCE REMARK 3 CONSTRAINTS AND 310 DIHEDRAL REMARK 3 ANGLE RESTRAINTS. REMARK 4 REMARK 4 1PSB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-03. REMARK 100 THE DEPOSITION ID IS D_1000019542. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310; 310; 310 REMARK 210 PH : 7.5; 7.5; 7.5 REMARK 210 IONIC STRENGTH : 0.045 M/L; 0.045 M/L; 0.045 M/L REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM 1H,15N LABELED PROTEIN 1 MM REMARK 210 UNLABELED PEPTIDE 20 MM D-11 REMARK 210 TRIS AND 10MM D10-DTT 5 MM CACL2 REMARK 210 AND 30MM KCL; 1 MM 1H,13C,15N REMARK 210 LABELED PROTEIN 1 MM UNLABELED REMARK 210 PEPTIDE 20 MM D-11 TRIS AND 10MM REMARK 210 D10-DTT 5 MM CACL2 AND 30MM KCL; REMARK 210 1 MM 1H,13C,15N LABELED PROTEIN REMARK 210 1 MM UNLABELED PEPTIDE 20 MM D- REMARK 210 11 TRIS AND 10MM D10-DTT 5 MM REMARK 210 CACL2 AND 30MM KCL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 2D_15N/13C_F2-FILTERED_NOESY; 3D_13C-F1_ REMARK 210 SEPARATED_13C/15N-F2_FILTERED_HMQC-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 2000, DYANA 1.5 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 RESTRAINED MOLECULAR DYNAMICS, REMARK 210 SIMULATED ANNEALING, REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 128 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: PROTEIN BACKBONE/SIDE-CHAIN ASSIGNMENTS WERE REMARK 210 MADE FROM 3D CBCA(CO)NH, 3D HNCA, 3D HN(CO)CA, 3D HNCO REMARK 210 3D HCCH-TOCSY, 3D HCCH-COSY EXPERIMENTS. REMARK 210 PEPTIDE WAS ASSIGNED FROM 2D-FILTERED COSY/TOCSY EXPERIMENTS. 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D 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: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 7 ARG D 78 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 12 ARG C 71 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 19 ARG D 83 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES 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 ASP A 23 63.50 -160.19 REMARK 500 1 LYS A 24 -45.09 72.63 REMARK 500 1 GLU A 49 85.74 -67.19 REMARK 500 1 ASP A 61 77.28 -67.98 REMARK 500 1 ASP B 23 51.94 -149.38 REMARK 500 1 LYS B 24 -35.76 70.85 REMARK 500 1 LEU B 40 48.52 -89.50 REMARK 500 1 HIS C 69 47.60 -70.45 REMARK 500 1 ARG D 66 177.69 -58.33 REMARK 500 1 HIS D 69 46.73 -79.14 REMARK 500 1 ALA D 70 -66.39 62.80 REMARK 500 1 ARG D 71 -65.17 73.80 REMARK 500 2 ASP A 23 58.11 34.09 REMARK 500 2 LYS A 24 -43.02 72.94 REMARK 500 2 ASP A 61 67.64 -47.76 REMARK 500 2 ASP B 23 61.18 22.53 REMARK 500 2 LYS B 24 -5.33 67.11 REMARK 500 2 LYS B 48 -65.00 68.42 REMARK 500 2 ASP B 61 69.62 -62.55 REMARK 500 2 ARG C 65 -60.25 66.83 REMARK 500 2 ARG D 63 -75.15 63.47 REMARK 500 2 ARG D 65 -39.56 -36.50 REMARK 500 2 HIS D 69 126.57 -170.27 REMARK 500 2 ARG D 71 39.58 -79.30 REMARK 500 3 ASP A 23 64.08 33.94 REMARK 500 3 LYS A 24 -32.90 69.28 REMARK 500 3 LEU A 40 -8.43 -153.16 REMARK 500 3 PHE A 43 -63.53 -108.62 REMARK 500 3 LYS A 48 -70.76 64.10 REMARK 500 3 ASP B 61 69.59 -46.59 REMARK 500 3 HIS B 90 80.59 -61.49 REMARK 500 3 LEU C 64 -159.29 64.81 REMARK 500 3 ARG C 65 -72.37 64.70 REMARK 500 3 ARG C 66 47.36 30.66 REMARK 500 3 ARG D 66 42.09 -77.38 REMARK 500 3 SER D 67 33.40 -157.91 REMARK 500 4 LYS A 24 0.50 -60.95 REMARK 500 4 LYS A 48 -53.71 56.52 REMARK 500 4 GLU A 49 98.03 -59.72 REMARK 500 4 ASP A 61 67.79 -64.39 REMARK 500 4 LYS B 48 -141.20 -103.37 REMARK 500 4 ASP B 61 71.22 -64.13 REMARK 500 4 LEU C 64 -64.10 68.23 REMARK 500 4 ALA C 70 41.81 -75.70 REMARK 500 4 ARG C 71 -30.37 64.40 REMARK 500 4 GLU D 73 0.04 -63.87 REMARK 500 5 ASP A 23 58.31 38.75 REMARK 500 5 LYS A 24 -38.82 65.09 REMARK 500 5 LEU A 40 41.41 -83.82 REMARK 500 5 LYS A 48 -59.51 66.63 REMARK 500 REMARK 500 THIS ENTRY HAS 243 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 C 76 0.08 SIDE CHAIN REMARK 500 1 ARG D 66 0.08 SIDE CHAIN REMARK 500 2 PHE B 70 0.07 SIDE CHAIN REMARK 500 2 PHE C 76 0.12 SIDE CHAIN REMARK 500 2 ARG D 71 0.10 SIDE CHAIN REMARK 500 2 PHE D 76 0.08 SIDE CHAIN REMARK 500 3 TYR A 17 0.13 SIDE CHAIN REMARK 500 3 PHE A 70 0.12 SIDE CHAIN REMARK 500 3 TYR B 17 0.10 SIDE CHAIN REMARK 500 3 ARG D 71 0.10 SIDE CHAIN REMARK 500 3 PHE D 76 0.10 SIDE CHAIN REMARK 500 4 PHE A 70 0.09 SIDE CHAIN REMARK 500 4 ARG C 71 0.08 SIDE CHAIN REMARK 500 5 PHE C 76 0.13 SIDE CHAIN REMARK 500 6 TYR A 17 0.09 SIDE CHAIN REMARK 500 6 ARG D 65 0.10 SIDE CHAIN REMARK 500 7 PHE A 87 0.08 SIDE CHAIN REMARK 500 7 TYR B 17 0.09 SIDE CHAIN REMARK 500 7 PHE B 70 0.11 SIDE CHAIN REMARK 500 7 ARG D 63 0.09 SIDE CHAIN REMARK 500 8 ARG C 65 0.11 SIDE CHAIN REMARK 500 8 PHE D 76 0.07 SIDE CHAIN REMARK 500 9 TYR A 17 0.13 SIDE CHAIN REMARK 500 9 PHE C 76 0.09 SIDE CHAIN REMARK 500 10 TYR A 17 0.10 SIDE CHAIN REMARK 500 10 ARG C 63 0.09 SIDE CHAIN REMARK 500 10 ARG D 66 0.09 SIDE CHAIN REMARK 500 11 PHE A 70 0.10 SIDE CHAIN REMARK 500 11 TYR B 17 0.09 SIDE CHAIN REMARK 500 11 PHE B 70 0.08 SIDE CHAIN REMARK 500 12 TYR A 17 0.11 SIDE CHAIN REMARK 500 12 TYR B 17 0.08 SIDE CHAIN REMARK 500 12 ARG C 63 0.09 SIDE CHAIN REMARK 500 12 PHE C 76 0.08 SIDE CHAIN REMARK 500 12 ARG C 78 0.09 SIDE CHAIN REMARK 500 13 PHE B 70 0.11 SIDE CHAIN REMARK 500 13 ARG D 71 0.14 SIDE CHAIN REMARK 500 14 ARG C 63 0.10 SIDE CHAIN REMARK 500 14 PHE C 76 0.09 SIDE CHAIN REMARK 500 15 PHE C 76 0.08 SIDE CHAIN REMARK 500 15 ARG C 78 0.13 SIDE CHAIN REMARK 500 15 ARG D 81 0.08 SIDE CHAIN REMARK 500 16 PHE A 70 0.14 SIDE CHAIN REMARK 500 16 PHE C 76 0.10 SIDE CHAIN REMARK 500 17 TYR A 17 0.17 SIDE CHAIN REMARK 500 17 PHE A 70 0.11 SIDE CHAIN REMARK 500 17 TYR B 17 0.10 SIDE CHAIN REMARK 500 17 PHE C 76 0.07 SIDE CHAIN REMARK 500 17 ARG D 63 0.09 SIDE CHAIN REMARK 500 17 PHE D 76 0.09 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 63 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1MHO RELATED DB: PDB REMARK 900 CA2+ LOADED BOVINE S100B STRUCTURE REMARK 900 RELATED ID: 1DT7 RELATED DB: PDB REMARK 900 S100B-P53 COMPLEX REMARK 900 RELATED ID: 1MWN RELATED DB: PDB REMARK 900 S100B-TRTK-12 COMPLEX REMARK 900 RELATED ID: 1QLK RELATED DB: PDB REMARK 900 CA2+ LOADED RAT S100B STRUCTURE REMARK 900 RELATED ID: 1UWO RELATED DB: PDB REMARK 900 CA2+ LOADED HUMAN S100B STRUCTURE REMARK 900 RELATED ID: 1MQ1 RELATED DB: PDB REMARK 900 S100B-TRTK-12 COMPLEX DBREF 1PSB A 1 91 UNP P02638 S100B_BOVIN 1 91 DBREF 1PSB B 1 91 UNP P02638 S100B_BOVIN 1 91 DBREF 1PSB C 62 87 UNP Q15208 STK38_HUMAN 62 87 DBREF 1PSB D 62 87 UNP Q15208 STK38_HUMAN 62 87 SEQRES 1 A 91 SER GLU LEU GLU LYS ALA VAL VAL ALA LEU ILE ASP VAL SEQRES 2 A 91 PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS LYS SEQRES 3 A 91 LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN GLU SEQRES 4 A 91 LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU VAL SEQRES 5 A 91 VAL ASP LYS VAL MET GLU THR LEU ASP SER ASP GLY ASP SEQRES 6 A 91 GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL ALA SEQRES 7 A 91 MET ILE THR THR ALA CYS HIS GLU PHE PHE GLU HIS GLU SEQRES 1 B 91 SER GLU LEU GLU LYS ALA VAL VAL ALA LEU ILE ASP VAL SEQRES 2 B 91 PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS LYS SEQRES 3 B 91 LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN GLU SEQRES 4 B 91 LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU VAL SEQRES 5 B 91 VAL ASP LYS VAL MET GLU THR LEU ASP SER ASP GLY ASP SEQRES 6 B 91 GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL ALA SEQRES 7 B 91 MET ILE THR THR ALA CYS HIS GLU PHE PHE GLU HIS GLU SEQRES 1 C 26 LYS ARG LEU ARG ARG SER ALA HIS ALA ARG LYS GLU THR SEQRES 2 C 26 GLU PHE LEU ARG LEU LYS ARG THR ARG LEU GLY LEU GLU SEQRES 1 D 26 LYS ARG LEU ARG ARG SER ALA HIS ALA ARG LYS GLU THR SEQRES 2 D 26 GLU PHE LEU ARG LEU LYS ARG THR ARG LEU GLY LEU GLU HELIX 1 1 SER A 1 GLU A 21 1 21 HELIX 2 2 LYS A 29 LEU A 40 1 12 HELIX 3 3 GLU A 49 ASP A 61 1 13 HELIX 4 4 PHE A 70 HIS A 90 1 21 HELIX 5 5 SER B 1 GLY B 19 1 19 HELIX 6 6 LYS B 29 LEU B 40 1 12 HELIX 7 7 GLU B 49 ASP B 61 1 13 HELIX 8 8 PHE B 70 HIS B 90 1 21 HELIX 9 9 GLU C 73 LEU C 86 1 14 HELIX 10 10 GLU D 73 LEU D 86 1 14 SHEET 1 A 2 LYS A 26 LYS A 28 0 SHEET 2 A 2 GLU A 67 ASP A 69 -1 O CYS A 68 N LEU A 27 SHEET 1 B 2 LYS B 26 LYS B 28 0 SHEET 2 B 2 GLU B 67 ASP B 69 -1 O CYS B 68 N LEU B 27 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 2 2 Bytes