Header list of 1qvx.pdb file
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HEADER TRANSFERASE 29-AUG-03 1QVX TITLE SOLUTION STRUCTURE OF THE FAT DOMAIN OF FOCAL ADHESION KINASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: FOCAL ADHESION KINASE 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FAT DOMAIN (RESIDUES 920-1053); COMPND 5 SYNONYM: FADK 1, PP125FAK; COMPND 6 EC: 2.7.1.112; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031; SOURCE 5 GENE: FAK; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX KEYWDS FOCAL ADHESION KINASE, FAK, FOCAL ADHENSION TARGETING DOMAIN, FAT, KEYWDS 2 HELIX BUNDLE, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR G.GAO,K.C.PRUTZMAN,M.L.KING,E.F.DEROSE,R.E.LONDON,M.D.SCHALLER, AUTHOR 2 S.L.CAMPBELL REVDAT 4 14-JUN-23 1QVX 1 REMARK REVDAT 3 05-FEB-20 1QVX 1 REMARK ATOM REVDAT 2 24-FEB-09 1QVX 1 VERSN REVDAT 1 02-MAR-04 1QVX 0 JRNL AUTH G.GAO,K.C.PRUTZMAN,M.L.KING,D.M.SCHESWOHL,E.F.DEROSE, JRNL AUTH 2 R.E.LONDON,M.D.SCHALLER,S.L.CAMPBELL JRNL TITL NMR SOLUTION STRUCTURE OF THE FOCAL ADHESION TARGETING JRNL TITL 2 DOMAIN OF FOCAL ADHESION KINASE IN COMPLEX WITH A PAXILLIN JRNL TITL 3 LD PEPTIDE: EVIDENCE FOR A TWO-SITE BINDING MODEL. JRNL REF J.BIOL.CHEM. V. 279 8441 2004 JRNL REFN ISSN 0021-9258 JRNL PMID 14662767 JRNL DOI 10.1074/JBC.M309808200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1, ARIA 1.2 REMARK 3 AUTHORS : BRUNGER, A.T. ET AL. (CNS), LINGE, J.P. ET AL. REMARK 3 (ARIA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURAL RESTRAINTS INCLUDED NOE, HYDROGEN BOND, DIHEDRAL REMARK 3 ANGLE, AND RDC RESTRAINTS. THE NOE DISTANCE RESTRAINTS WERE REMARK 3 DERIVED FROM A 3D SIMULTANEOUS 13C/15N EDITED NOESY PEAK LISTS REMARK 3 WITH 75 MS MIXING TIME. THE PEAK LISTS WERE GENERATED REMARK 3 AUTOMATICALLY BY NMRVIEW AND EDITED MANUALLY TO REMOVE ANY OBVIOUS REMARK 3 WATER AND APODIZATION ARTIFACTS. THE PEAK LISTS WERE UNASSIGNED REMARK 3 AND UNCALIBRATED WITH RESPECT TO DISTANCE. TO CALIBRATE THE NOE REMARK 3 DISTANCES, THE ROTATIONAL CORRELATION TIME OF THE COMPLEX WAS SET REMARK 3 TO 10 NS AND WAS BASED ON VALUES OBTAINED ON PROTEINS OF THIS SIZE REMARK 3 AT SIMILAR TEMPERATURE. THE DEFAULT PARAMETERS FOR ARIA PRODUCED REMARK 3 STRUCTURES WITH POOR CONVERGENCE. SEVERAL PARAMETERS WERE REMARK 3 OPTIMIZED, INCLUDING THE AMBIGUOUS CUTOFF (RHO), THE VIOLATION REMARK 3 TOLERANCE (VTOL), AND MAXIMUM NUMBER OF AMBIGUITIES PER PEAK (MAXN) REMARK 3 , TO PROVIDE BETTER NOISE DISCRIMINATION. THE FOLLOWING SCHEME LED REMARK 3 TO THE BEST CONVERGENCE OVER 9 ITERATIONS: RHO = (0.95, 0.95, 0.95, REMARK 3 0.94, 0.93, 0.92, 0.91, 0.90, 0 REMARK 3 80), VTOL = (5.0, 2.0, 1.0, 0.5, 0.25, 1.0, 0.1, 0.1, 0.1), MAXN = REMARK 3 5 FOR ALL ITERATIONS. AN ENSEMBLE OF 25 CALCULATED NMR STRUCTURES REMARK 3 OF THE AVIAN FAT DOMAIN WAS SELECTED FOR FURTHER ANALYSIS. REMARK 4 REMARK 4 1QVX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-03. REMARK 100 THE DEPOSITION ID IS D_1000020133. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 50 MM NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 0.6MM 13C,15N LABELED FAT WITH REMARK 210 4.8MM LD2 PEPTIDE, 25MM TRIS- REMARK 210 MALEATE, 0.1% NAN3, 1.0UM PPACK, REMARK 210 0.5MG/ML PEFABLOC, 90% H2O, 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D SIMULTANEOUS 13C/15N EDITED REMARK 210 NOESY; 3D CBCA(CO)NH; 3D HNCA; REMARK 210 3D HNCACB; 3D H(CCO)-TOCSY-NNH; REMARK 210 3D (H)C(CO)-TOCSY-NNH REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.1, VNMR 6.1, NMRVIEW REMARK 210 5.0.4 REMARK 210 METHOD USED : THE PROGRAM CNS VERSION 1.1 WITH REMARK 210 ARIA VERSION 1.2 MODULE WAS USED REMARK 210 TO CALCULATE THE STRUCTURES OF REMARK 210 THE AVIAN FAT DOMAIN. REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: AROMATIC SIDECHAIN ASSIGNMENTS WERE OBTAINED FROM 2D REMARK 210 (HB)CB(CGCDCE)HE AND 2D (HB)CB(CGCD)HD EXPERIMENTS. 1H-15N REMARK 210 RESIDUAL DIPOLAR COUPLING VALUES WERE MEASURED USING 7.5 MG/ML REMARK 210 PF1 PHAGE AS ALIGNING MEDIUM 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 HA LEU A 973 HD12 LEU A 976 1.09 REMARK 500 HA VAL A 952 HB2 MET A 1002 1.10 REMARK 500 HA VAL A 929 HD12 LEU A 932 1.19 REMARK 500 HA LEU A 966 HG22 VAL A 969 1.23 REMARK 500 HD13 LEU A 932 HB2 LEU A 965 1.24 REMARK 500 HG12 VAL A 952 HD3 PRO A 953 1.25 REMARK 500 HA LEU A 995 HD13 LEU A 1028 1.33 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 SER A 921 47.48 -82.49 REMARK 500 1 ASN A 922 72.03 46.84 REMARK 500 1 ASP A 923 -175.50 -45.44 REMARK 500 1 SER A 979 -26.43 179.63 REMARK 500 1 VAL A1009 97.75 -46.17 REMARK 500 2 ASN A 922 82.02 -67.32 REMARK 500 2 ASP A 923 -174.84 -46.23 REMARK 500 2 LYS A 924 -19.38 -42.97 REMARK 500 2 SER A 979 -32.31 -165.76 REMARK 500 2 VAL A1009 115.94 -28.95 REMARK 500 2 MET A1010 -82.55 -99.25 REMARK 500 2 THR A1011 -82.07 -155.83 REMARK 500 2 SER A1050 32.07 -94.89 REMARK 500 3 ASP A 923 -171.63 -46.77 REMARK 500 3 LYS A 924 -21.16 -36.40 REMARK 500 3 SER A 979 -32.76 -161.38 REMARK 500 3 TYR A1008 -76.87 -74.04 REMARK 500 3 VAL A1009 77.08 32.33 REMARK 500 3 MET A1010 -103.71 -139.60 REMARK 500 3 ARG A1051 98.24 -173.39 REMARK 500 3 PRO A1052 -71.87 -67.46 REMARK 500 4 ASP A 923 -173.54 -47.33 REMARK 500 4 LYS A 924 -25.05 -37.78 REMARK 500 4 SER A 979 -39.86 -168.74 REMARK 500 5 ASP A 923 -174.81 -47.05 REMARK 500 5 PRO A 945 34.80 -97.37 REMARK 500 5 SER A 979 -42.04 -162.70 REMARK 500 5 VAL A1009 67.25 34.39 REMARK 500 5 ARG A1051 92.70 63.44 REMARK 500 6 ASP A 923 -171.93 -47.68 REMARK 500 6 LYS A 924 -26.90 -27.92 REMARK 500 6 PRO A 945 31.59 -99.89 REMARK 500 6 SER A 979 -39.03 -163.90 REMARK 500 6 MET A1010 -78.50 -132.49 REMARK 500 6 THR A1011 -97.74 -144.19 REMARK 500 7 ASP A 923 -174.02 -45.58 REMARK 500 7 LYS A 924 -14.18 -44.82 REMARK 500 7 PRO A 948 -15.56 -48.69 REMARK 500 7 SER A 979 -38.32 -169.33 REMARK 500 7 HIS A 981 -18.84 -48.60 REMARK 500 7 VAL A1009 78.54 34.15 REMARK 500 7 SER A1050 29.56 -176.35 REMARK 500 8 ASP A 923 -173.27 -47.01 REMARK 500 8 LYS A 924 -22.74 -39.01 REMARK 500 8 SER A 979 -48.64 -162.57 REMARK 500 8 SER A1012 -47.21 -135.32 REMARK 500 8 ARG A1051 106.44 66.03 REMARK 500 8 PRO A1052 -82.55 -77.24 REMARK 500 9 ASP A 923 -173.92 -47.87 REMARK 500 9 LYS A 924 -19.76 -39.27 REMARK 500 REMARK 500 THIS ENTRY HAS 168 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER A 1012 LEU A 1013 3 -149.71 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 9 ARG A1043 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5924 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT ASSIGNMENTS DBREF 1QVX A 920 1053 UNP Q00944 FAK1_CHICK 920 1053 SEQRES 1 A 134 ARG SER ASN ASP LYS VAL TYR GLU ASN VAL THR GLY LEU SEQRES 2 A 134 VAL LYS ALA VAL ILE GLU MET SER SER LYS ILE GLN PRO SEQRES 3 A 134 ALA PRO PRO GLU GLU TYR VAL PRO MET VAL LYS GLU VAL SEQRES 4 A 134 GLY LEU ALA LEU ARG THR LEU LEU ALA THR VAL ASP GLU SEQRES 5 A 134 SER LEU PRO VAL LEU PRO ALA SER THR HIS ARG GLU ILE SEQRES 6 A 134 GLU MET ALA GLN LYS LEU LEU ASN SER ASP LEU ALA GLU SEQRES 7 A 134 LEU ILE ASN LYS MET LYS LEU ALA GLN GLN TYR VAL MET SEQRES 8 A 134 THR SER LEU GLN GLN GLU TYR LYS LYS GLN MET LEU THR SEQRES 9 A 134 ALA ALA HIS ALA LEU ALA VAL ASP ALA LYS ASN LEU LEU SEQRES 10 A 134 ASP VAL ILE ASP GLN ALA ARG LEU LYS MET ILE SER GLN SEQRES 11 A 134 SER ARG PRO HIS HELIX 1 1 ASP A 923 GLN A 944 1 22 HELIX 2 2 GLU A 950 SER A 979 1 30 HELIX 3 3 ARG A 982 VAL A 1009 1 28 HELIX 4 4 LEU A 1013 ARG A 1051 1 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 - g 9 2 Bytes