Header list of 1ukx.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 03-SEP-03 1UKX
TITLE SOLUTION STRUCTURE OF THE RWD DOMAIN OF MOUSE GCN2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GCN2 EIF2ALPHA KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RWD DOMAIN;
COMPND 5 SYNONYM: GCN2;
COMPND 6 EC: 2.7.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RIKEN CDNA 2900069K12;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021021-28;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS EIF2ALPHA KINASE, UBC-LIKE FOLD, TRIPLE BETA-TURNS, STRUCTURAL
KEYWDS 2 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 3 TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.NAMEKI,M.YONEYAMA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1UKX 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UKX 1 VERSN
REVDAT 1 03-AUG-04 1UKX 0
JRNL AUTH N.NAMEKI,M.YONEYAMA,S.KOSHIBA,N.TOCHIO,M.INOUE,E.SEKI,
JRNL AUTH 2 T.MATSUDA,Y.TOMO,T.HARADA,K.SAITO,N.KOBAYASHI,T.YABUKI,
JRNL AUTH 3 M.AOKI,E.NUNOKAWA,N.MATSUDA,N.SAKAGAMI,T.TERADA,M.SHIROUZU,
JRNL AUTH 4 M.YOSHIDA,H.HIROTA,T.OSANAI,A.TANAKA,T.ARAKAWA,P.CARNINCI,
JRNL AUTH 5 J.KAWAI,Y.HAYASHIZAKI,K.KINOSHITA,P.GUNTERT,T.KIGAWA,
JRNL AUTH 6 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE RWD DOMAIN OF THE MOUSE GCN2
JRNL TITL 2 PROTEIN.
JRNL REF PROTEIN SCI. V. 13 2089 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 15273307
JRNL DOI 10.1110/PS.04751804
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, OPALP
REMARK 3 AUTHORS : BRUKER (XWINNMR), KORADI, R., BILLETER, M.,
REMARK 3 GUENTERT, P. (OPALP)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UKX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000005942.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0MM RWD DOMAIN U-15N, 13C,
REMARK 210 20MM D-TRIS-HCL, 100MM NACL, 1MM
REMARK 210 D-DTT, 0.02% NAN3, 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.815, CYANA 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
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
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 1 LEU A 19 CB - CG - CD1 ANGL. DEV. = 10.5 DEGREES
REMARK 500 2 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 2 ARG A 68 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 5 ARG A 34 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 12 TYR A 52 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 12 ARG A 68 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 14 ARG A 68 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 15 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -3.0 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 GLU A 9 -158.69 -86.84
REMARK 500 1 PRO A 45 80.68 -68.84
REMARK 500 1 ALA A 57 -162.94 61.38
REMARK 500 1 GLU A 59 -147.99 -151.88
REMARK 500 1 VAL A 61 165.91 64.65
REMARK 500 1 TYR A 62 -81.05 -128.83
REMARK 500 1 CYS A 71 139.56 58.03
REMARK 500 1 SER A 91 49.36 -80.12
REMARK 500 1 GLU A 93 -93.73 -87.39
REMARK 500 1 SER A 132 175.52 60.88
REMARK 500 1 PRO A 134 -177.21 -65.79
REMARK 500 1 SER A 136 132.54 -171.99
REMARK 500 2 SER A 2 63.96 31.43
REMARK 500 2 SER A 6 -157.31 56.69
REMARK 500 2 GLU A 9 103.58 -52.16
REMARK 500 2 ARG A 40 -172.63 57.77
REMARK 500 2 LEU A 56 -44.92 -142.97
REMARK 500 2 ALA A 57 -145.99 56.73
REMARK 500 2 GLU A 59 -146.22 -147.93
REMARK 500 2 GLU A 60 -73.73 -58.58
REMARK 500 2 VAL A 61 -171.90 59.99
REMARK 500 2 TYR A 62 -62.26 -145.89
REMARK 500 2 CYS A 71 105.38 56.22
REMARK 500 2 LYS A 88 -92.50 -75.47
REMARK 500 2 SER A 91 -85.03 34.67
REMARK 500 2 ASN A 92 23.02 -143.20
REMARK 500 2 GLU A 93 -114.87 -82.05
REMARK 500 2 SER A 94 13.34 -66.42
REMARK 500 2 LYS A 131 54.71 -66.95
REMARK 500 2 SER A 132 -114.15 -85.87
REMARK 500 2 SER A 136 109.86 -163.64
REMARK 500 3 SER A 3 78.88 -113.22
REMARK 500 3 SER A 5 97.95 64.37
REMARK 500 3 MET A 8 69.45 31.25
REMARK 500 3 TYR A 26 -62.27 -107.33
REMARK 500 3 ALA A 37 152.98 127.15
REMARK 500 3 GLU A 60 -72.38 58.59
REMARK 500 3 VAL A 61 -178.09 63.59
REMARK 500 3 TYR A 62 -80.30 -134.93
REMARK 500 3 CYS A 71 110.75 68.51
REMARK 500 3 ASN A 92 56.87 -172.02
REMARK 500 3 GLU A 93 -75.77 -116.07
REMARK 500 3 LYS A 131 -47.73 -133.95
REMARK 500 3 PRO A 134 -165.31 -72.07
REMARK 500 3 SER A 135 -89.00 -133.70
REMARK 500 4 SER A 2 176.21 63.47
REMARK 500 4 MET A 8 -52.88 -160.19
REMARK 500 4 TYR A 26 -65.79 -106.74
REMARK 500 4 LEU A 33 -55.22 -130.97
REMARK 500 4 ARG A 40 -169.33 -79.82
REMARK 500
REMARK 500 THIS ENTRY HAS 312 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 PHE A 30 GLN A 31 1 148.91
REMARK 500 SER A 136 GLY A 137 5 -119.85
REMARK 500 VAL A 41 ARG A 42 7 -149.63
REMARK 500 LYS A 70 CYS A 71 11 -147.54
REMARK 500 SER A 136 GLY A 137 12 144.91
REMARK 500 GLU A 9 SER A 10 14 147.37
REMARK 500 SER A 10 TYR A 11 14 141.51
REMARK 500 SER A 136 GLY A 137 19 131.93
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 52 0.08 SIDE CHAIN
REMARK 500 2 ARG A 14 0.16 SIDE CHAIN
REMARK 500 4 ARG A 34 0.08 SIDE CHAIN
REMARK 500 6 ARG A 34 0.09 SIDE CHAIN
REMARK 500 6 ARG A 68 0.10 SIDE CHAIN
REMARK 500 8 TYR A 26 0.10 SIDE CHAIN
REMARK 500 8 ARG A 34 0.16 SIDE CHAIN
REMARK 500 8 ARG A 42 0.11 SIDE CHAIN
REMARK 500 8 TYR A 52 0.08 SIDE CHAIN
REMARK 500 9 TYR A 52 0.07 SIDE CHAIN
REMARK 500 9 ARG A 68 0.08 SIDE CHAIN
REMARK 500 10 TYR A 52 0.07 SIDE CHAIN
REMARK 500 10 PHE A 125 0.08 SIDE CHAIN
REMARK 500 11 ARG A 34 0.09 SIDE CHAIN
REMARK 500 13 ARG A 14 0.09 SIDE CHAIN
REMARK 500 13 ARG A 34 0.09 SIDE CHAIN
REMARK 500 13 TYR A 75 0.09 SIDE CHAIN
REMARK 500 14 ARG A 40 0.09 SIDE CHAIN
REMARK 500 15 ARG A 14 0.09 SIDE CHAIN
REMARK 500 15 ARG A 42 0.09 SIDE CHAIN
REMARK 500 16 ARG A 40 0.15 SIDE CHAIN
REMARK 500 17 ARG A 34 0.08 SIDE CHAIN
REMARK 500 17 TYR A 52 0.11 SIDE CHAIN
REMARK 500 18 ARG A 14 0.08 SIDE CHAIN
REMARK 500 20 ARG A 34 0.12 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: MMK001004460.1 RELATED DB: TARGETDB
DBREF 1UKX A 9 131 UNP Q9QZ05 E2AK4_MOUSE 17 139
SEQADV 1UKX GLY A 1 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX SER A 2 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX SER A 3 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX GLY A 4 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX SER A 5 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX SER A 6 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX GLY A 7 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX MET A 8 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX SER A 132 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX GLY A 133 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX PRO A 134 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX SER A 135 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX SER A 136 UNP Q9QZ05 CLONING ARTIFACT
SEQADV 1UKX GLY A 137 UNP Q9QZ05 CLONING ARTIFACT
SEQRES 1 A 137 GLY SER SER GLY SER SER GLY MET GLU SER TYR SER GLN
SEQRES 2 A 137 ARG GLN ASP HIS GLU LEU GLN ALA LEU GLU ALA ILE TYR
SEQRES 3 A 137 GLY SER ASP PHE GLN ASP LEU ARG PRO ASP ALA ARG GLY
SEQRES 4 A 137 ARG VAL ARG GLU PRO PRO GLU ILE ASN LEU VAL LEU TYR
SEQRES 5 A 137 PRO GLN GLY LEU ALA GLY GLU GLU VAL TYR VAL GLN VAL
SEQRES 6 A 137 GLU LEU ARG VAL LYS CYS PRO PRO THR TYR PRO ASP VAL
SEQRES 7 A 137 VAL PRO GLU ILE ASP LEU LYS ASN ALA LYS GLY LEU SER
SEQRES 8 A 137 ASN GLU SER VAL ASN LEU LEU LYS SER HIS LEU GLU GLU
SEQRES 9 A 137 LEU ALA LYS LYS GLN CYS GLY GLU VAL MET ILE PHE GLU
SEQRES 10 A 137 LEU ALA HIS HIS VAL GLN SER PHE LEU SER GLU HIS ASN
SEQRES 11 A 137 LYS SER GLY PRO SER SER GLY
HELIX 1 1 SER A 12 ILE A 25 1 14
HELIX 2 2 VAL A 95 GLN A 109 1 15
HELIX 3 3 ILE A 115 HIS A 129 1 15
SHEET 1 A 4 PHE A 30 ASP A 32 0
SHEET 2 A 4 ILE A 47 LEU A 51 -1 O ASN A 48 N GLN A 31
SHEET 3 A 4 GLN A 64 VAL A 69 -1 O LEU A 67 N LEU A 49
SHEET 4 A 4 ASP A 83 LYS A 88 -1 O ASP A 83 N ARG A 68
CISPEP 1 TYR A 75 PRO A 76 1 0.62
CISPEP 2 TYR A 75 PRO A 76 2 0.24
CISPEP 3 TYR A 75 PRO A 76 3 0.28
CISPEP 4 TYR A 75 PRO A 76 4 -14.53
CISPEP 5 TYR A 75 PRO A 76 5 11.75
CISPEP 6 TYR A 75 PRO A 76 6 15.40
CISPEP 7 TYR A 75 PRO A 76 7 7.13
CISPEP 8 TYR A 75 PRO A 76 8 5.48
CISPEP 9 TYR A 75 PRO A 76 9 1.29
CISPEP 10 TYR A 75 PRO A 76 10 3.22
CISPEP 11 TYR A 75 PRO A 76 11 6.79
CISPEP 12 TYR A 75 PRO A 76 12 3.24
CISPEP 13 TYR A 75 PRO A 76 13 3.61
CISPEP 14 TYR A 75 PRO A 76 14 0.72
CISPEP 15 TYR A 75 PRO A 76 15 13.24
CISPEP 16 TYR A 75 PRO A 76 16 -1.57
CISPEP 17 TYR A 75 PRO A 76 17 8.28
CISPEP 18 TYR A 75 PRO A 76 18 5.34
CISPEP 19 TYR A 75 PRO A 76 19 4.56
CISPEP 20 TYR A 75 PRO A 76 20 10.74
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 2 2 Bytes