Header list of 1egx.pdb file
Complete list - l 25 2 Bytes
HEADER SIGNALING PROTEIN 17-FEB-00 1EGX TITLE SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN TITLE 2 VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP) COMPND MOL_ID: 1; COMPND 2 MOLECULE: VASODILATOR-STIMULATED PHOSPHOPROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: EVH1 DOMAIN; COMPND 5 SYNONYM: VASP; 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 BL21; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PGEX-4T-1 KEYWDS EVH1, VASP-ENA, POLY-PROLINE-BINDING DOMAIN, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR L.BALL,R.KUHNE,B.HOFFMANN,A.HAFNER,P.SCHMIEDER,R.VOLKMER-ENGERT, AUTHOR 2 M.HOF,M.WAHL,J.SCHNEIDER-MERGENER,U.WALTER,H.OSCHKINAT,T.JARCHAU REVDAT 4 25-JUL-12 1EGX 1 REMARK VERSN REVDAT 3 24-FEB-09 1EGX 1 VERSN REVDAT 2 01-APR-03 1EGX 1 JRNL REVDAT 1 20-SEP-00 1EGX 0 JRNL AUTH L.J.BALL,R.KUHNE,B.HOFFMANN,A.HAFNER,P.SCHMIEDER, JRNL AUTH 2 R.VOLKMER-ENGERT,M.HOF,M.WAHL,J.SCHNEIDER-MERGENER,U.WALTER, JRNL AUTH 3 H.OSCHKINAT,T.JARCHAU JRNL TITL DUAL EPITOPE RECOGNITION BY THE VASP EVH1 DOMAIN MODULATES JRNL TITL 2 POLYPROLINE LIGAND SPECIFICITY AND BINDING AFFINITY. JRNL REF EMBO J. V. 19 4903 2000 JRNL REFN ISSN 0261-4189 JRNL PMID 10990454 JRNL DOI 10.1093/EMBOJ/19.18.4903 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 09A REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: structures are based on 3043 NOE- REMARK 3 derived distance restraints, 49 dihedral angle restraints, 25 REMARK 3 distance restraints from hydrogen bonds REMARK 4 REMARK 4 1EGX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-00. REMARK 100 THE RCSB ID CODE IS RCSB010559. 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 : 50 MM KCL, 20 MM KH2PO4 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.3 MM VASP EVH1 DOMAIN 15N,13C; REMARK 210 BUFFER CONTAINING 20 MM KH2PO4, REMARK 210 50 MM KCL, 0.2 MM NA3N3; SAMPLES REMARK 210 WERE USED IN BOTH 90% H2O,10% D2O REMARK 210 AND 99.8% D2O 2 MM VASP EVH1 REMARK 210 DOMAIN 15N BUFFER CONTAINING 20 REMARK 210 MM KH2PO4, 50 MM KCL, 0.2 MM REMARK 210 NA3N3;SAMPLE WERE USED IN 90% REMARK 210 H2O,10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; 2D NOESY; DQF- REMARK 210 COSY; HNHA; 3D_HCCH-TOCSY; 3D_ REMARK 210 HNHB; 3D_CBCA(CO)NNH; 3D_CBCANNH; REMARK 210 3D_15N-SEPARATED-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 09A, AZARA 2.1, XWINNMR 1.3, REMARK 210 ANSIG 3.3 REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 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: 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: 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 GLU A 3 -169.22 51.14 REMARK 500 1 ILE A 6 -62.04 -104.80 REMARK 500 1 LYS A 21 76.75 64.33 REMARK 500 1 ARG A 22 174.63 176.14 REMARK 500 1 THR A 28 -160.40 -101.39 REMARK 500 1 PRO A 30 159.84 -46.08 REMARK 500 1 ALA A 32 46.16 171.28 REMARK 500 1 PHE A 33 178.01 61.86 REMARK 500 1 GLN A 58 85.83 61.21 REMARK 500 1 ASN A 63 66.12 -162.92 REMARK 500 1 ARG A 68 46.72 26.92 REMARK 500 1 GLN A 74 79.39 59.04 REMARK 500 1 ASP A 84 -87.55 -93.59 REMARK 500 1 ALA A 85 -69.33 -93.73 REMARK 500 2 LYS A 21 83.78 56.56 REMARK 500 2 ARG A 22 157.03 173.85 REMARK 500 2 PRO A 25 97.28 -44.06 REMARK 500 2 THR A 28 -76.26 -136.86 REMARK 500 2 PRO A 30 164.89 -45.03 REMARK 500 2 GLN A 31 57.54 -149.69 REMARK 500 2 ALA A 32 49.23 -93.22 REMARK 500 2 PHE A 33 -176.83 61.77 REMARK 500 2 SER A 34 149.02 -172.95 REMARK 500 2 MET A 54 45.59 -94.55 REMARK 500 2 GLN A 58 118.16 65.74 REMARK 500 2 ASN A 63 70.02 -163.14 REMARK 500 2 ARG A 68 87.59 -61.19 REMARK 500 2 TYR A 72 106.30 -47.56 REMARK 500 2 GLN A 74 88.67 -66.85 REMARK 500 2 GLN A 81 118.83 177.15 REMARK 500 2 ASP A 84 -102.24 -93.65 REMARK 500 2 ALA A 85 -72.91 -60.96 REMARK 500 2 ARG A 86 -13.01 -140.81 REMARK 500 3 SER A 2 -172.09 -59.27 REMARK 500 3 ILE A 6 -71.20 -101.36 REMARK 500 3 ALA A 11 -178.61 -170.66 REMARK 500 3 LYS A 21 82.11 53.92 REMARK 500 3 ARG A 22 172.79 176.55 REMARK 500 3 PRO A 25 96.20 -44.11 REMARK 500 3 THR A 28 -72.88 -142.70 REMARK 500 3 PRO A 30 160.96 -48.05 REMARK 500 3 GLN A 31 57.42 -142.03 REMARK 500 3 ALA A 32 48.90 -93.39 REMARK 500 3 PHE A 33 -174.51 61.62 REMARK 500 3 SER A 34 148.35 -174.30 REMARK 500 3 ASN A 45 40.78 76.06 REMARK 500 3 MET A 54 45.71 -107.95 REMARK 500 3 GLN A 58 102.19 58.32 REMARK 500 3 ASN A 63 64.00 -160.81 REMARK 500 3 ARG A 68 97.26 -46.44 REMARK 500 REMARK 500 THIS ENTRY HAS 282 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QC6 RELATED DB: PDB REMARK 900 EVH1 DOMAIN FROM ENA/VASP-LIKE PROTEIN IN COMPLEX WITH ACTA REMARK 900 RELATED ID: 1EVH RELATED DB: PDB REMARK 900 EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE REMARK 900 RELATED ID: 18569 RELATED DB: BMRB DBREF 1EGX A 1 115 UNP P50552 VASP_HUMAN 1 115 SEQRES 1 A 115 MET SER GLU THR VAL ILE CYS SER SER ARG ALA THR VAL SEQRES 2 A 115 MET LEU TYR ASP ASP GLY ASN LYS ARG TRP LEU PRO ALA SEQRES 3 A 115 GLY THR GLY PRO GLN ALA PHE SER ARG VAL GLN ILE TYR SEQRES 4 A 115 HIS ASN PRO THR ALA ASN SER PHE ARG VAL VAL GLY ARG SEQRES 5 A 115 LYS MET GLN PRO ASP GLN GLN VAL VAL ILE ASN CYS ALA SEQRES 6 A 115 ILE VAL ARG GLY VAL LYS TYR ASN GLN ALA THR PRO ASN SEQRES 7 A 115 PHE HIS GLN TRP ARG ASP ALA ARG GLN VAL TRP GLY LEU SEQRES 8 A 115 ASN PHE GLY SER LYS GLU ASP ALA ALA GLN PHE ALA ALA SEQRES 9 A 115 GLY MET ALA SER ALA LEU GLU ALA LEU GLU GLY HELIX 1 1 SER A 95 GLY A 115 1 21 SHEET 1 A 6 VAL A 60 ILE A 66 0 SHEET 2 A 6 SER A 46 LYS A 53 -1 O PHE A 47 N ILE A 66 SHEET 3 A 6 SER A 34 ASN A 41 -1 N ARG A 35 O ARG A 52 SHEET 4 A 6 VAL A 5 THR A 12 -1 N ILE A 6 O ILE A 38 SHEET 5 A 6 VAL A 88 PHE A 93 -1 O ASN A 92 N THR A 12 SHEET 6 A 6 LEU A 15 TYR A 16 -1 N TYR A 16 O VAL A 88 SHEET 1 B 6 VAL A 60 ILE A 66 0 SHEET 2 B 6 SER A 46 LYS A 53 -1 O PHE A 47 N ILE A 66 SHEET 3 B 6 SER A 34 ASN A 41 -1 N ARG A 35 O ARG A 52 SHEET 4 B 6 VAL A 5 THR A 12 -1 N ILE A 6 O ILE A 38 SHEET 5 B 6 VAL A 88 PHE A 93 -1 O ASN A 92 N THR A 12 SHEET 6 B 6 PHE A 79 ARG A 83 -1 O HIS A 80 N LEU A 91 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 - l 25 2 Bytes