HEADER TRANSFERASE 26-JUN-03 1PV3
TITLE NMR SOLUTION STRUCTURE OF THE AVIAN FAT-DOMAIN OF FOCAL ADHESION
TITLE 2 KINASE
CAVEAT 1PV3 CHIRALITY ERROR AT CA CENTER OF GLN A908
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FOCAL ADHESION KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FOCAL ADHESION TARGETING (FAT) DOMAIN;
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: FAK1 OR FAK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS FOCAL ADHESION KINASE, HELIX BUNDLE, FAT-DOMAIN, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.C.PRUTZMAN,G.GAO,M.L.KING,V.V.IYER,G.A.MUELLER,M.D.SCHALLER,
AUTHOR 2 S.L.CAMPBELL
REVDAT 3 27-APR-16 1PV3 1 ATOM VERSN
REVDAT 2 24-FEB-09 1PV3 1 VERSN
REVDAT 1 25-MAY-04 1PV3 0
JRNL AUTH K.C.PRUTZMAN,G.GAO,M.L.KING,V.V.IYER,G.A.MUELLER,
JRNL AUTH 2 M.D.SCHALLER,S.L.CAMPBELL
JRNL TITL THE FOCAL ADHESION TARGETING DOMAIN OF FOCAL ADHESION KINASE
JRNL TITL 2 CONTAINS A HINGE REGION THAT MODULATES TYROSINE 926
JRNL TITL 3 PHOSPHORYLATION.
JRNL REF STRUCTURE V. 12 881 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15130480
JRNL DOI 10.1016/J.STR.2004.02.028
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.2
REMARK 3 AUTHORS : NILGES, M.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 3049 TOTAL RESTRAINTS: 1627 UNAMBIGUOUS
REMARK 3 NOE-DERIVED DISTANCE CONSTRAINTS, 1078 AMBIGUOUS NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 83 DIHEDRAL ANGLE RESTRAINTS, 97 DISTANCE
REMARK 3 RESTRAINTS FROM HYDROGEN BONDS, 164 RESIDUAL DIPOLAR COUPLING
REMARK 3 RESTRAINTS
REMARK 4
REMARK 4 1PV3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-03.
REMARK 100 THE RCSB ID CODE IS RCSB019594.
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 : 150 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.85 MM FOCAL ADHESION TARGETING
REMARK 210 DOMAIN U-15N,13C, 25 MM TRIS-
REMARK 210 MALEATE, 0.1 % NAN3, 1.0 UM
REMARK 210 PPACK, 0.5 MG/ML PEFABLOC 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.0, NMRVIEW 5.0.4, CNS
REMARK 210 1.1, ARIA 1.2
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: PDB ENTRY 1K40 WAS USED AS A STARTING TEMPLATE FOR
REMARK 210 STRUCTURE CALCULATIONS. THE STRUCTURE WAS DETERMINED USING TRIPLE
REMARK 210 -RESONANCE NMR 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 HIS A1053 O
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 VAL A 1009 HB2 GLN A 1014 1.28
REMARK 500 O ASP A 1031 H LEU A 1035 1.54
REMARK 500 O LEU A 960 HG1 THR A 964 1.55
REMARK 500 O GLU A 950 H VAL A 952 1.56
REMARK 500 O ILE A 937 HG SER A 940 1.57
REMARK 500 HZ3 LYS A 956 OE1 GLU A 957 1.57
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 -50.05 -176.16
REMARK 500 1 GLU A 950 -9.29 72.20
REMARK 500 1 TYR A 951 -46.78 52.18
REMARK 500 1 THR A1011 -153.08 -142.87
REMARK 500 2 SER A 913 -43.79 -130.19
REMARK 500 2 ARG A 920 86.44 79.65
REMARK 500 2 SER A 921 -12.45 -153.73
REMARK 500 2 ASP A 923 -10.53 73.36
REMARK 500 2 VAL A 936 -75.45 -52.85
REMARK 500 2 ALA A 978 103.99 70.28
REMARK 500 2 SER A 979 -59.70 69.17
REMARK 500 2 THR A1011 -77.95 -163.56
REMARK 500 2 SER A1012 -76.43 -50.55
REMARK 500 2 ARG A1051 -54.70 -131.26
REMARK 500 2 PRO A1052 45.99 -69.71
REMARK 500 3 PRO A 910 69.90 -69.05
REMARK 500 3 ILE A 919 81.98 -59.95
REMARK 500 3 ARG A 920 102.60 175.54
REMARK 500 3 ASP A 923 136.01 -174.48
REMARK 500 3 LYS A 924 -14.33 -49.83
REMARK 500 3 VAL A 936 -76.76 -46.73
REMARK 500 3 PRO A 945 57.23 -69.63
REMARK 500 3 PRO A 948 131.14 -34.73
REMARK 500 3 GLU A 949 29.03 -66.67
REMARK 500 3 GLU A 950 66.15 33.53
REMARK 500 3 PRO A 977 -154.96 -87.49
REMARK 500 3 ALA A 978 -93.68 68.04
REMARK 500 3 THR A1011 -86.15 -163.68
REMARK 500 3 GLN A1049 -70.39 -128.54
REMARK 500 3 PRO A1052 130.27 -21.30
REMARK 500 4 ILE A 912 -99.46 41.46
REMARK 500 4 VAL A 936 -75.49 -49.21
REMARK 500 4 PRO A 948 -156.63 -83.13
REMARK 500 4 GLU A 950 0.27 -61.41
REMARK 500 4 ALA A 978 -159.11 -83.94
REMARK 500 4 SER A 979 -36.35 -37.67
REMARK 500 4 THR A1011 -94.18 -160.66
REMARK 500 4 GLN A1049 -77.37 -86.23
REMARK 500 4 SER A1050 -46.62 176.50
REMARK 500 5 PRO A 910 81.03 -67.80
REMARK 500 5 SER A 921 114.67 69.24
REMARK 500 5 ASN A 922 -167.55 73.61
REMARK 500 5 ASP A 923 -177.83 145.82
REMARK 500 5 VAL A 936 -75.83 -58.60
REMARK 500 5 GLN A 944 147.66 67.34
REMARK 500 5 ALA A 946 -58.17 -167.98
REMARK 500 5 GLU A 949 -13.26 60.71
REMARK 500 5 ARG A1051 -74.32 -118.50
REMARK 500 6 ILE A 919 44.77 -57.99
REMARK 500 6 ARG A 920 11.73 -140.11
REMARK 500
REMARK 500 THIS ENTRY HAS 208 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 ALA A 946 PRO A 947 8 149.18
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PV3 A 920 1053 UNP Q00944 FAK1_CHICK 920 1053
SEQADV 1PV3 GLY A 908 UNP Q00944 GLN 908 CLONING ARTIFACT
SEQADV 1PV3 SER A 909 UNP Q00944 GLU 909 CLONING ARTIFACT
SEQADV 1PV3 PRO A 910 UNP Q00944 ILE 910 CLONING ARTIFACT
SEQADV 1PV3 GLY A 911 UNP Q00944 SER 911 CLONING ARTIFACT
SEQADV 1PV3 ILE A 912 UNP Q00944 PRO 912 CLONING ARTIFACT
SEQADV 1PV3 SER A 913 UNP Q00944 PRO 913 CLONING ARTIFACT
SEQADV 1PV3 GLY A 914 UNP Q00944 PRO 914 CLONING ARTIFACT
SEQADV 1PV3 GLY A 915 UNP Q00944 THR 915 CLONING ARTIFACT
SEQADV 1PV3 GLY A 916 UNP Q00944 ALA 916 CLONING ARTIFACT
SEQADV 1PV3 GLY A 917 UNP Q00944 LEU 917 CLONING ARTIFACT
SEQADV 1PV3 GLY A 918 UNP Q00944 ASP 918 CLONING ARTIFACT
SEQADV 1PV3 ILE A 919 UNP Q00944 ASP 919 CLONING ARTIFACT
SEQRES 1 A 146 GLY SER PRO GLY ILE SER GLY GLY GLY GLY GLY ILE ARG
SEQRES 2 A 146 SER ASN ASP LYS VAL TYR GLU ASN VAL THR GLY LEU VAL
SEQRES 3 A 146 LYS ALA VAL ILE GLU MET SER SER LYS ILE GLN PRO ALA
SEQRES 4 A 146 PRO PRO GLU GLU TYR VAL PRO MET VAL LYS GLU VAL GLY
SEQRES 5 A 146 LEU ALA LEU ARG THR LEU LEU ALA THR VAL ASP GLU SER
SEQRES 6 A 146 LEU PRO VAL LEU PRO ALA SER THR HIS ARG GLU ILE GLU
SEQRES 7 A 146 MET ALA GLN LYS LEU LEU ASN SER ASP LEU ALA GLU LEU
SEQRES 8 A 146 ILE ASN LYS MET LYS LEU ALA GLN GLN TYR VAL MET THR
SEQRES 9 A 146 SER LEU GLN GLN GLU TYR LYS LYS GLN MET LEU THR ALA
SEQRES 10 A 146 ALA HIS ALA LEU ALA VAL ASP ALA LYS ASN LEU LEU ASP
SEQRES 11 A 146 VAL ILE ASP GLN ALA ARG LEU LYS MET ILE SER GLN SER
SEQRES 12 A 146 ARG PRO HIS
HELIX 1 1 ASP A 923 ILE A 943 1 21
HELIX 2 2 TYR A 951 LEU A 976 1 26
HELIX 3 3 THR A 980 TYR A 1008 1 29
HELIX 4 4 THR A 1011 GLN A 1049 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
(ATOM LINES ARE NOT SHOWN.)
END
