Header list of 1mjd.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN 27-AUG-02 1MJD
TITLE STRUCTURE OF N-TERMINAL DOMAIN OF HUMAN DOUBLECORTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DOUBLECORTIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES (45-150);
COMPND 5 SYNONYM: LISSENCEPHALIN-X, LIS-X, DOUBLIN;
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 GENE: DCX;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: GSTUNI1
KEYWDS DCX DOMAIN, UBIQUITIN-LIKE FOLD, MICROTUBULE ASSOCIATED PROTEIN,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.H.KIM,T.CIERPICKI,U.DEREWENDA,D.KROWARSCH,Y.FENG,Y.DEVEDJIEV,
AUTHOR 2 Z.DAUTER,C.A.WALSH,J.OTLEWSKI,J.H.BUSHWELLER,Z.S.DEREWENDA
REVDAT 5 23-FEB-22 1MJD 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1MJD 1 VERSN
REVDAT 3 13-MAY-03 1MJD 2 JRNL
REVDAT 2 06-MAY-03 1MJD 1 JRNL
REVDAT 1 29-APR-03 1MJD 0
JRNL AUTH M.H.KIM,T.CIERPICKI,U.DEREWENDA,D.KROWARSCH,Y.FENG,
JRNL AUTH 2 Y.DEVEDJIEV,Z.DAUTER,C.A.WALSH,J.OTLEWSKI,J.H.BUSHWELLER,
JRNL AUTH 3 Z.S.DEREWENDA
JRNL TITL THE DCX-DOMAIN TANDEMS OF DOUBLECORTIN AND DOUBLECORTIN-LIKE
JRNL TITL 2 KINASE
JRNL REF NAT.STRUCT.BIOL. V. 10 324 2003
JRNL REFN ISSN 1072-8368
JRNL PMID 12692530
JRNL DOI 10.1038/NSB918
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.CIERPICKI,M.H.KIM,J.OTLEWSKI,Z.S.DEREWENDA,J.H.BUSHWELLER
REMARK 1 TITL LETTER TO THE EDITOR: ASSIGNMENT OF 1H, 13C AND 15N
REMARK 1 TITL 2 RESONANCES OF THE N-TERMINAL MICROTUBULE-BINDING DOMAIN OF
REMARK 1 TITL 3 HUMAN DOUBLECORTIN
REMARK 1 REF J.BIOMOL.NMR V. 25 81 2003
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1021981207062
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, CNS 1.0
REMARK 3 AUTHORS : DELAGLIO, F., GRZESIEK, S., VUISTER, G.W., ZHU,
REMARK 3 G., PFEIFER, J., BAX, A. (NMRPIPE), BRUNGER, A.T.,
REMARK 3 ADAMS, P.D., CLORE, G.M., DELANO, W.L., GROS, P.,
REMARK 3 GROSSE-KUNSTLEVE, R.W., JIANG, J.S., KUSZEWSKI, J.,
REMARK 3 NILGES, M., PANNU, N.S. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NOESY CROSS-PEAKS WERE ASSIGNED USING
REMARK 3 COMBINATION OF MANUAL AND AUTOMATIC ASSIGNMENT EMPLOYING NOAH/
REMARK 3 DYANA PROGRAM. THE FINAL SET OF STRUCTURES WAS REFINED IN CNS.
REMARK 4
REMARK 4 1MJD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016956.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM DOUBLECORTIN 45-150 U-15N,
REMARK 210 13C; 50MM PHOSPHATE BUFFER; 5MMM
REMARK 210 DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.100, DYANA 1.5
REMARK 210 METHOD USED : AUTOMATIC NOESY CROSS-PEAKS
REMARK 210 ASSIGNMENT, TORSION ANGLE
REMARK 210 DYNAMICS, SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 18
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 ALA A 39 88.61 -156.12
REMARK 500 1 MET A 40 -60.92 -90.52
REMARK 500 1 ASP A 41 88.12 -158.27
REMARK 500 1 PHE A 44 73.78 -156.75
REMARK 500 1 ALA A 45 28.96 -163.69
REMARK 500 1 LEU A 46 88.09 -160.69
REMARK 500 1 SER A 47 130.58 64.48
REMARK 500 1 ALA A 52 -176.78 68.98
REMARK 500 1 ASP A 62 -47.82 -146.81
REMARK 500 1 ARG A 63 -78.23 64.32
REMARK 500 1 ASP A 93 1.81 -150.24
REMARK 500 1 ASN A 94 34.40 34.22
REMARK 500 1 ILE A 95 -76.87 -126.70
REMARK 500 1 GLN A 99 43.32 -95.17
REMARK 500 1 VAL A 101 115.83 -163.45
REMARK 500 1 SER A 129 -50.81 -152.70
REMARK 500 1 ASP A 130 32.85 -149.94
REMARK 500 1 PHE A 133 121.18 66.85
REMARK 500 1 THR A 139 17.52 -150.70
REMARK 500 1 VAL A 148 27.83 -150.72
REMARK 500 2 ASP A 41 85.56 60.73
REMARK 500 2 GLU A 43 -59.51 73.55
REMARK 500 2 PHE A 44 30.84 -86.59
REMARK 500 2 ASN A 48 117.37 68.91
REMARK 500 2 LYS A 51 146.17 63.21
REMARK 500 2 ALA A 52 160.42 62.50
REMARK 500 2 ASP A 62 -46.65 -142.61
REMARK 500 2 ARG A 63 35.27 35.72
REMARK 500 2 TYR A 64 26.81 -152.96
REMARK 500 2 SER A 92 126.97 -34.73
REMARK 500 2 ASN A 94 29.66 -163.89
REMARK 500 2 ILE A 95 -57.20 -130.58
REMARK 500 2 VAL A 101 114.74 -165.89
REMARK 500 2 SER A 129 -48.07 -153.02
REMARK 500 2 ASP A 130 31.98 -149.63
REMARK 500 2 ASN A 131 -163.91 -107.59
REMARK 500 2 PHE A 132 50.79 -151.83
REMARK 500 2 PHE A 133 111.32 42.10
REMARK 500 2 LYS A 135 94.28 37.74
REMARK 500 2 ASN A 143 119.16 76.45
REMARK 500 2 PRO A 144 36.96 -84.97
REMARK 500 2 ASN A 149 54.36 -92.95
REMARK 500 3 ALA A 39 -64.64 -175.20
REMARK 500 3 ASP A 41 -58.26 -159.17
REMARK 500 3 ALA A 45 171.76 76.05
REMARK 500 3 LEU A 46 47.07 -159.06
REMARK 500 3 SER A 47 -78.81 63.43
REMARK 500 3 ASN A 48 -49.69 -158.14
REMARK 500 3 LYS A 51 167.19 63.79
REMARK 500 3 ALA A 52 162.49 71.13
REMARK 500
REMARK 500 THIS ENTRY HAS 401 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5482 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS
REMARK 900 RELATED ID: 1MG4 RELATED DB: PDB
REMARK 900 STRUCTURE OF DCX DOMAINS: IMPLICATIONS FOR MICROTUBULE BUNDLING AND
REMARK 900 CEREBRAL CORTEX DEVELOPMENT
REMARK 900 RELATED ID: 1MFW RELATED DB: PDB
REMARK 900 STRUCTURE OF THE DCX DOMAINS: IMPLICATIONS FOR MICROTUBULE BUNDLING
REMARK 900 AND CEREBRAL CORTEX DEVELOPMENT
DBREF 1MJD A 45 150 UNP O43602 DCX_HUMAN 87 192
SEQADV 1MJD GLY A 38 UNP O43602 CLONING ARTIFACT
SEQADV 1MJD ALA A 39 UNP O43602 CLONING ARTIFACT
SEQADV 1MJD MET A 40 UNP O43602 CLONING ARTIFACT
SEQADV 1MJD ASP A 41 UNP O43602 CLONING ARTIFACT
SEQADV 1MJD PRO A 42 UNP O43602 CLONING ARTIFACT
SEQADV 1MJD GLU A 43 UNP O43602 CLONING ARTIFACT
SEQADV 1MJD PHE A 44 UNP O43602 CLONING ARTIFACT
SEQRES 1 A 113 GLY ALA MET ASP PRO GLU PHE ALA LEU SER ASN GLU LYS
SEQRES 2 A 113 LYS ALA LYS LYS VAL ARG PHE TYR ARG ASN GLY ASP ARG
SEQRES 3 A 113 TYR PHE LYS GLY ILE VAL TYR ALA VAL SER SER ASP ARG
SEQRES 4 A 113 PHE ARG SER PHE ASP ALA LEU LEU ALA ASP LEU THR ARG
SEQRES 5 A 113 SER LEU SER ASP ASN ILE ASN LEU PRO GLN GLY VAL ARG
SEQRES 6 A 113 TYR ILE TYR THR ILE ASP GLY SER ARG LYS ILE GLY SER
SEQRES 7 A 113 MET ASP GLU LEU GLU GLU GLY GLU SER TYR VAL CYS SER
SEQRES 8 A 113 SER ASP ASN PHE PHE LYS LYS VAL GLU TYR THR LYS ASN
SEQRES 9 A 113 VAL ASN PRO ASN TRP SER VAL ASN VAL
HELIX 1 1 SER A 79 SER A 92 1 14
HELIX 2 2 SER A 115 LEU A 119 5 5
SHEET 1 A 5 ILE A 68 VAL A 72 0
SHEET 2 A 5 LYS A 53 ARG A 59 -1 N PHE A 57 O ILE A 68
SHEET 3 A 5 GLU A 123 SER A 128 1 O TYR A 125 N TYR A 58
SHEET 4 A 5 TYR A 103 THR A 106 -1 N TYR A 105 O VAL A 126
SHEET 5 A 5 LYS A 112 ILE A 113 -1 O ILE A 113 N ILE A 104
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 - b 23 2 Bytes