Header list of 1c07.pdb file
Complete list - b 16 2 Bytes
HEADER SIGNALING PROTEIN 14-JUL-99 1C07 TITLE STRUCTURE OF THE THIRD EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE COMPND 3 15); COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: EPS15 HOMOLOGY (EH) DOMAIN 3; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834 (DE3); SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSETA KEYWDS CALCIUM BINDING, SIGNALING DOMAIN, NPF BINDING, FW BINDING, EF-HAND, KEYWDS 2 EH DOMAIN, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.L.ENMON,T.DE BEER,M.OVERDUIN REVDAT 4 16-FEB-22 1C07 1 REMARK LINK REVDAT 3 24-FEB-09 1C07 1 VERSN REVDAT 2 01-APR-03 1C07 1 JRNL REVDAT 1 19-JUL-00 1C07 0 JRNL AUTH J.L.ENMON,T.DE BEER,M.OVERDUIN JRNL TITL SOLUTION STRUCTURE OF EPS15'S THIRD EH DOMAIN REVEALS JRNL TITL 2 COINCIDENT PHE-TRP AND ASN-PRO-PHE BINDING SITES. JRNL REF BIOCHEMISTRY V. 39 4309 2000 JRNL REFN ISSN 0006-2960 JRNL PMID 10757979 JRNL DOI 10.1021/BI9927383 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.84, X-PLOR 3.84 REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1C07 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-99. REMARK 100 THE DEPOSITION ID IS D_1000009343. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.00 REMARK 210 PH : 7.80 REMARK 210 IONIC STRENGTH : 100MM KCL, 2MM CACL2, 2MM NAN3 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5-1MM EH3; 20MM D-TRIS, 100MM REMARK 210 KCL, 2MM CACL2, 2MM NAN3, 0.1MM REMARK 210 D-DTT; 95% H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 4D_13C/15N- REMARK 210 SEPARATED_ NOESY; 4D_13C- REMARK 210 SEPARATED_ NOESY; HNHA; HMQC-J 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 : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST NOE REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8 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 O VAL A 40 H PHE A 44 1.53 REMARK 500 O TRP A 58 H ASP A 62 1.53 REMARK 500 O VAL A 35 H LEU A 69 1.56 REMARK 500 O ARG A 41 H LEU A 45 1.56 REMARK 500 O CYS A 61 H THR A 63 1.56 REMARK 500 O ALA A 15 H LYS A 19 1.58 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 TRP A 10 129.17 -175.00 REMARK 500 1 SER A 13 -54.60 174.36 REMARK 500 1 PRO A 14 -145.66 -67.43 REMARK 500 1 ALA A 15 -49.67 -29.20 REMARK 500 1 ASP A 28 71.77 -63.13 REMARK 500 1 GLU A 39 -61.70 -91.05 REMARK 500 1 ARG A 41 -75.77 -42.21 REMARK 500 1 ASP A 62 56.90 -66.61 REMARK 500 1 ASP A 65 51.19 39.84 REMARK 500 1 SER A 70 -179.74 -49.13 REMARK 500 1 LEU A 80 -60.82 -99.67 REMARK 500 1 PRO A 92 63.91 -68.78 REMARK 500 1 HIS A 93 -109.63 35.94 REMARK 500 1 VAL A 94 -165.21 -102.71 REMARK 500 2 VAL A 11 -168.77 -69.67 REMARK 500 2 VAL A 12 66.07 36.76 REMARK 500 2 PRO A 14 -147.69 -77.13 REMARK 500 2 ALA A 15 -59.13 -27.78 REMARK 500 2 MET A 31 26.44 43.16 REMARK 500 2 ARG A 41 -78.99 -44.92 REMARK 500 2 PRO A 50 -153.11 -67.86 REMARK 500 2 SER A 51 -65.11 -104.58 REMARK 500 2 LYS A 71 -84.51 -53.51 REMARK 500 2 HIS A 93 -67.53 -28.14 REMARK 500 2 VAL A 94 -165.61 -115.36 REMARK 500 2 PRO A 102 -160.58 -71.91 REMARK 500 3 VAL A 12 99.11 31.27 REMARK 500 3 SER A 13 -62.18 -134.25 REMARK 500 3 PRO A 14 -143.73 -61.98 REMARK 500 3 ALA A 15 -60.74 -27.65 REMARK 500 3 ASP A 28 80.39 -65.30 REMARK 500 3 LEU A 38 -41.08 -139.93 REMARK 500 3 GLU A 39 -61.67 -91.08 REMARK 500 3 SER A 70 -171.14 -57.85 REMARK 500 3 LYS A 71 -81.77 -66.32 REMARK 500 3 HIS A 93 -83.12 -64.08 REMARK 500 3 VAL A 94 -165.64 -117.74 REMARK 500 4 VAL A 11 -158.61 -80.10 REMARK 500 4 VAL A 12 80.53 21.48 REMARK 500 4 PRO A 14 -152.84 -80.05 REMARK 500 4 ALA A 15 -54.40 -27.94 REMARK 500 4 ARG A 41 -73.15 -46.81 REMARK 500 4 ASP A 62 59.36 -65.50 REMARK 500 4 SER A 70 -178.44 -61.70 REMARK 500 4 LYS A 71 -80.45 -67.10 REMARK 500 4 PRO A 92 47.01 -72.90 REMARK 500 4 HIS A 93 -77.99 55.89 REMARK 500 4 VAL A 94 -161.75 -117.23 REMARK 500 4 PRO A 102 -90.36 -76.21 REMARK 500 5 PRO A 14 -150.25 -75.09 REMARK 500 REMARK 500 THIS ENTRY HAS 229 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 41 0.29 SIDE CHAIN REMARK 500 2 ARG A 41 0.14 SIDE CHAIN REMARK 500 3 ARG A 41 0.12 SIDE CHAIN REMARK 500 5 ARG A 41 0.16 SIDE CHAIN REMARK 500 6 ARG A 41 0.31 SIDE CHAIN REMARK 500 7 ARG A 41 0.20 SIDE CHAIN REMARK 500 8 ARG A 41 0.23 SIDE CHAIN REMARK 500 9 ARG A 41 0.30 SIDE CHAIN REMARK 500 10 ARG A 41 0.27 SIDE CHAIN REMARK 500 11 ARG A 41 0.31 SIDE CHAIN REMARK 500 12 ARG A 41 0.17 SIDE CHAIN REMARK 500 13 ARG A 41 0.30 SIDE CHAIN REMARK 500 14 ARG A 41 0.21 SIDE CHAIN REMARK 500 15 ARG A 41 0.26 SIDE CHAIN REMARK 500 16 ARG A 41 0.20 SIDE CHAIN REMARK 500 17 ARG A 41 0.14 SIDE CHAIN REMARK 500 19 ARG A 41 0.30 SIDE CHAIN REMARK 500 20 ARG A 41 0.29 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 110 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 28 OD1 REMARK 620 2 ASP A 30 OD1 124.2 REMARK 620 3 ASP A 32 OD2 81.8 100.4 REMARK 620 4 PHE A 34 O 62.1 170.3 72.4 REMARK 620 5 GLU A 39 OE1 84.7 63.3 146.7 126.3 REMARK 620 6 GLU A 39 OE2 126.1 62.3 151.8 121.4 48.0 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 110 DBREF 1C07 A 9 103 UNP P42566 EP15_HUMAN 217 311 SEQRES 1 A 95 THR TRP VAL VAL SER PRO ALA GLU LYS ALA LYS TYR ASP SEQRES 2 A 95 GLU ILE PHE LEU LYS THR ASP LYS ASP MET ASP GLY PHE SEQRES 3 A 95 VAL SER GLY LEU GLU VAL ARG GLU ILE PHE LEU LYS THR SEQRES 4 A 95 GLY LEU PRO SER THR LEU LEU ALA HIS ILE TRP SER LEU SEQRES 5 A 95 CYS ASP THR LYS ASP CYS GLY LYS LEU SER LYS ASP GLN SEQRES 6 A 95 PHE ALA LEU ALA PHE HIS LEU ILE SER GLN LYS LEU ILE SEQRES 7 A 95 LYS GLY ILE ASP PRO PRO HIS VAL LEU THR PRO GLU MET SEQRES 8 A 95 ILE PRO PRO SER HET CA A 110 1 HETNAM CA CALCIUM ION FORMUL 2 CA CA 2+ HELIX 1 1 ALA A 15 THR A 27 1 13 HELIX 2 2 GLY A 37 LEU A 45 1 9 HELIX 3 3 SER A 51 CYS A 61 1 11 HELIX 4 4 LYS A 71 LEU A 85 1 15 SHEET 1 A 2 PHE A 34 VAL A 35 0 SHEET 2 A 2 LEU A 69 SER A 70 -1 N LEU A 69 O VAL A 35 LINK OD1 ASP A 28 CA CA A 110 1555 1555 2.57 LINK OD1 ASP A 30 CA CA A 110 1555 1555 2.75 LINK OD2 ASP A 32 CA CA A 110 1555 1555 2.80 LINK O PHE A 34 CA CA A 110 1555 1555 2.48 LINK OE1 GLU A 39 CA CA A 110 1555 1555 2.76 LINK OE2 GLU A 39 CA CA A 110 1555 1555 2.50 SITE 1 AC1 7 ASP A 28 ASP A 30 ASP A 32 PHE A 34 SITE 2 AC1 7 VAL A 35 SER A 36 GLU A 39 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 16 2 Bytes