Header list of 2gaq.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSFERASE 09-MAR-06 2GAQ
TITLE NMR SOLUTION STRUCTURE OF THE FRB DOMAIN OF MTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FKBP12-RAPAMYCIN COMPLEX-ASSOCIATED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FRB DOMAIN;
COMPND 5 SYNONYM: FK506-BINDING PROTEIN 12- RAPAMYCIN COMPLEX-ASSOCIATED
COMPND 6 PROTEIN 1, RAPAMYCIN TARGET PROTEIN, RAPT1, MAMMALIAN TARGET OF
COMPND 7 RAPAMYCIN, MTOR;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FRAP1, FRAP, FRAP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS FOUR HELICAL UP AND DOWN BUNDLE, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR M.LEONE,M.PELLECCHIA
REVDAT 4 09-MAR-22 2GAQ 1 REMARK
REVDAT 3 24-FEB-09 2GAQ 1 VERSN
REVDAT 2 05-SEP-06 2GAQ 1 JRNL
REVDAT 1 08-AUG-06 2GAQ 0
JRNL AUTH M.LEONE,K.J.CROWELL,J.CHEN,D.JUNG,G.G.CHIANG,S.SARETH,
JRNL AUTH 2 R.T.ABRAHAM,M.PELLECCHIA
JRNL TITL THE FRB DOMAIN OF MTOR: NMR SOLUTION STRUCTURE AND INHIBITOR
JRNL TITL 2 DESIGN.
JRNL REF BIOCHEMISTRY V. 45 10294 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16922504
JRNL DOI 10.1021/BI060976+
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, GROMOS 96
REMARK 3 AUTHORS : GUNTERT (DYANA), VAN GUNSTEREN (GROMOS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GAQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000036898.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 20 MM PBS 1 MM DTT
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM FRB U-15N; 0.5 MM FRB U
REMARK 210 -15N; 0.6 MM FRB U-15N, U-13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D-(1H,1H,15N)
REMARK 210 -TOCSY; HNCA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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 GLU A 15 H GLU A 19 1.58
REMARK 500
REMARK 500 REMARK: NULL
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 3 TYR A 74 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 12 TYR A 74 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 13 TYR A 90 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 16 TYR A 90 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 18 TYR A 90 CB - CG - CD2 ANGL. DEV. = -3.6 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 ARG A 4 -70.80 -136.28
REMARK 500 1 ILE A 7 -90.02 -59.33
REMARK 500 1 LEU A 8 147.77 56.56
REMARK 500 1 ALA A 20 -61.70 -94.68
REMARK 500 1 GLN A 49 -87.67 -97.33
REMARK 500 1 THR A 50 -101.30 -64.29
REMARK 500 1 LEU A 51 36.75 -176.92
REMARK 500 1 THR A 54 47.32 -150.18
REMARK 500 1 PHE A 56 -45.56 -134.42
REMARK 500 1 ASP A 63 -145.66 -59.28
REMARK 500 1 TRP A 70 48.03 -72.44
REMARK 500 2 LEU A 2 92.35 -46.03
REMARK 500 2 ARG A 4 -44.84 -162.15
REMARK 500 2 ILE A 7 73.46 27.82
REMARK 500 2 GLN A 49 -109.14 -97.79
REMARK 500 2 THR A 50 -78.88 -49.51
REMARK 500 2 LEU A 51 37.92 156.55
REMARK 500 2 THR A 54 62.87 -162.83
REMARK 500 2 TYR A 60 40.53 -71.39
REMARK 500 2 ASP A 63 -134.10 -77.73
REMARK 500 2 TRP A 70 47.87 -79.68
REMARK 500 2 LYS A 76 -30.21 174.16
REMARK 500 2 ASN A 79 -171.48 56.24
REMARK 500 2 LYS A 99 50.51 -169.00
REMARK 500 3 LEU A 2 66.99 39.77
REMARK 500 3 ARG A 4 -43.05 -167.36
REMARK 500 3 ALA A 6 71.65 70.36
REMARK 500 3 LEU A 8 168.05 55.83
REMARK 500 3 MET A 43 0.72 -69.99
REMARK 500 3 PRO A 48 -170.05 -68.45
REMARK 500 3 GLN A 49 -83.35 -126.39
REMARK 500 3 THR A 50 -93.80 -57.64
REMARK 500 3 LEU A 51 35.72 177.35
REMARK 500 3 THR A 54 46.89 -161.50
REMARK 500 3 PHE A 56 -53.30 -139.47
REMARK 500 3 TYR A 60 81.74 -153.71
REMARK 500 3 ASP A 63 -136.70 -70.32
REMARK 500 3 LEU A 64 -46.96 -24.74
REMARK 500 3 TRP A 70 33.95 -83.63
REMARK 500 4 LEU A 2 156.47 62.16
REMARK 500 4 ARG A 4 -49.32 -154.96
REMARK 500 4 ILE A 7 80.12 30.34
REMARK 500 4 LEU A 8 152.51 -49.96
REMARK 500 4 PRO A 48 -166.62 -75.87
REMARK 500 4 GLN A 49 -152.05 -145.23
REMARK 500 4 THR A 50 -85.24 -35.05
REMARK 500 4 LEU A 51 34.12 -178.87
REMARK 500 4 LYS A 52 -52.13 -121.40
REMARK 500 4 THR A 54 47.66 -155.20
REMARK 500 4 TYR A 60 41.10 -75.21
REMARK 500
REMARK 500 THIS ENTRY HAS 258 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 TYR A 74 0.06 SIDE CHAIN
REMARK 500 3 TYR A 24 0.07 SIDE CHAIN
REMARK 500 3 TYR A 74 0.11 SIDE CHAIN
REMARK 500 3 TYR A 90 0.06 SIDE CHAIN
REMARK 500 4 TYR A 24 0.07 SIDE CHAIN
REMARK 500 5 TYR A 74 0.06 SIDE CHAIN
REMARK 500 8 TYR A 24 0.10 SIDE CHAIN
REMARK 500 9 TYR A 24 0.08 SIDE CHAIN
REMARK 500 9 TYR A 74 0.10 SIDE CHAIN
REMARK 500 10 TYR A 60 0.07 SIDE CHAIN
REMARK 500 11 TYR A 74 0.11 SIDE CHAIN
REMARK 500 11 TYR A 90 0.11 SIDE CHAIN
REMARK 500 12 TYR A 60 0.06 SIDE CHAIN
REMARK 500 15 TYR A 60 0.06 SIDE CHAIN
REMARK 500 17 TYR A 60 0.06 SIDE CHAIN
REMARK 500 18 TYR A 24 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 ALA A 86 -10.16
REMARK 500 2 LEU A 17 -10.01
REMARK 500 3 LEU A 17 -11.91
REMARK 500 3 LEU A 64 -11.82
REMARK 500 4 TRP A 87 -10.14
REMARK 500 5 LEU A 17 -10.27
REMARK 500 5 CYS A 71 -12.13
REMARK 500 5 ALA A 86 -10.74
REMARK 500 5 LEU A 89 -10.81
REMARK 500 7 TRP A 13 -11.77
REMARK 500 8 SER A 21 -11.56
REMARK 500 10 CYS A 71 -11.33
REMARK 500 10 LYS A 73 -10.51
REMARK 500 11 TRP A 13 -10.98
REMARK 500 12 LEU A 2 10.83
REMARK 500 12 PHE A 56 -10.11
REMARK 500 12 LYS A 73 -10.43
REMARK 500 13 PHE A 94 -11.75
REMARK 500 14 LEU A 17 -10.85
REMARK 500 14 ASP A 88 -11.60
REMARK 500 15 SER A 21 -11.57
REMARK 500 16 CYS A 71 -12.10
REMARK 500 17 TRP A 9 -11.83
REMARK 500 17 TRP A 13 -10.42
REMARK 500 17 CYS A 71 -12.50
REMARK 500 17 TRP A 87 -10.90
REMARK 500 19 TRP A 13 -11.90
REMARK 500 19 TRP A 87 -11.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FAP RELATED DB: PDB
REMARK 900 RELATED ID: 1AUE RELATED DB: PDB
REMARK 900 RELATED ID: 3FAP RELATED DB: PDB
DBREF 2GAQ A 1 100 UNP P42345 FRAP_HUMAN 2015 2114
SEQRES 1 A 100 GLU LEU ILE ARG VAL ALA ILE LEU TRP HIS GLU MET TRP
SEQRES 2 A 100 HIS GLU GLY LEU GLU GLU ALA SER ARG LEU TYR PHE GLY
SEQRES 3 A 100 GLU ARG ASN VAL LYS GLY MET PHE GLU VAL LEU GLU PRO
SEQRES 4 A 100 LEU HIS ALA MET MET GLU ARG GLY PRO GLN THR LEU LYS
SEQRES 5 A 100 GLU THR SER PHE ASN GLN ALA TYR GLY ARG ASP LEU MET
SEQRES 6 A 100 GLU ALA GLN GLU TRP CYS ARG LYS TYR MET LYS SER GLY
SEQRES 7 A 100 ASN VAL LYS ASP LEU THR GLN ALA TRP ASP LEU TYR TYR
SEQRES 8 A 100 HIS VAL PHE ARG ARG ILE SER LYS GLN
HELIX 1 1 LEU A 8 GLY A 26 1 19
HELIX 2 2 ASN A 29 ARG A 46 1 18
HELIX 3 3 ASP A 63 TRP A 70 1 8
HELIX 4 4 TRP A 70 SER A 77 1 8
HELIX 5 5 ASN A 79 ILE A 97 1 19
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 9 2 Bytes