Header list of 1ddm.pdb file
Complete list - b 16 2 Bytes
HEADER SIGNALING PROTEIN/TRANSFERASE 11-NOV-99 1DDM
TITLE SOLUTION STRUCTURE OF THE NUMB PTB DOMAIN COMPLEXED TO A NAK PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUMB PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PHOSPHOTYROSINE BINDING DOMAIN (PTB);
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: CELL FATE DETERMINANT PROTEIN;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NUMB ASSOCIATE KINASE;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: C-TERMINAL NAK 1437-1447;
COMPND 11 SYNONYM: NAK;
COMPND 12 EC: 2.7.1.37
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX4T2;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 10 ORGANISM_COMMON: FRUIT FLY;
SOURCE 11 ORGANISM_TAXID: 7227
KEYWDS COMPLEX, SIGNAL TRANSDUCTION, PHOSPHOTYROSINE BINDING DOMAIN (PTB),
KEYWDS 2 ASYMMETRIC CELL DIVISION, SIGNALING PROTEIN-TRANSFERASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.ZWAHLEN,S.C.LI,L.E.KAY,T.PAWSON,J.D.FORMAN-KAY
REVDAT 4 16-FEB-22 1DDM 1 REMARK
REVDAT 3 24-FEB-09 1DDM 1 VERSN
REVDAT 2 01-APR-03 1DDM 1 JRNL
REVDAT 1 10-APR-00 1DDM 0
JRNL AUTH C.ZWAHLEN,S.C.LI,L.E.KAY,T.PAWSON,J.D.FORMAN-KAY
JRNL TITL MULTIPLE MODES OF PEPTIDE RECOGNITION BY THE PTB DOMAIN OF
JRNL TITL 2 THE CELL FATE DETERMINANT NUMB.
JRNL REF EMBO J. V. 19 1505 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 10747019
JRNL DOI 10.1093/EMBOJ/19.7.1505
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.C.LI,C.ZWAHLEN,S.J.VINCENT,C.J.MCGLADE,L.E.KAY,T.PAWSON,
REMARK 1 AUTH 2 J.D.FORMAN-KAY
REMARK 1 TITL STRUCTURE OF A NUMB PTB DOMAIN-PEPTIDE COMPLEX SUGGESTS A
REMARK 1 TITL 2 BASIS FOR DIVERSE BINDING SPECIFICITY
REMARK 1 REF NAT.STRUCT.BIOL. V. 5 1075 1998
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/4185
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 4, CNS 0.3
REMARK 3 AUTHORS : VARIAN INC. (VNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2088 NOE, 50 DISTANCE RETRAINTS FORM HYDROGEN BONDS, 94 CHEMICAL
REMARK 3 SHIFT-DERIVED DIHEDRAL RESTRAINTS
REMARK 4
REMARK 4 1DDM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000009998.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.00
REMARK 210 IONIC STRENGTH : 50MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM PTB U-15N; 1MM NAK NA; 50MM
REMARK 210 PHOSPHATE BUFFER NA; 1MM PTB U-
REMARK 210 15N, 10% 13C; 1MM NAK NA; 50MM
REMARK 210 PHOSPHATE BUFFER NA; 1MM PTB U-
REMARK 210 15N, U-13C; 1MM NAK NA; 50MM
REMARK 210 PHOSPHATE BUFFER NA; 1MM PTB NA;
REMARK 210 1MM NAK (G1 F2 F7 F10) 15N, 13C;;
REMARK 210 50MM PHOSPHATE BUFFER NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D_13C
REMARK 210 -HSQC; 3D_15N/13C-SEPARATED_NOESY; HNCO/CBCACONNH/HAHBCBCACONNH/
REMARK 210 HNCACB/CCCTOCSYCONNH/HCCTOCSYCONNH/HCCHTOCSY/HALF- FILTER-NOESY;
REMARK 210 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, NMRVIEW 3.1, CNS
REMARK 210 0.3
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS USING
REMARK 210 ARIA PROTOCOLS FOR AMBIGUOUS
REMARK 210 RESTRAINTS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
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
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 SER A 78 -92.36 -85.66
REMARK 500 1 ALA A 79 34.14 -175.94
REMARK 500 1 THR A 80 97.22 -174.41
REMARK 500 1 SER A 82 -153.38 -113.15
REMARK 500 1 TYR A 87 101.53 -58.30
REMARK 500 1 GLU A 95 -68.81 -168.95
REMARK 500 1 ARG A 97 25.96 -146.91
REMARK 500 1 SER A 112 -169.14 -177.73
REMARK 500 1 ARG A 113 -71.95 69.87
REMARK 500 1 VAL A 123 94.45 -62.80
REMARK 500 1 THR A 135 -26.46 -148.89
REMARK 500 1 LEU A 138 149.52 66.26
REMARK 500 1 ILE A 139 -35.91 -138.49
REMARK 500 1 GLN A 142 -164.82 -76.65
REMARK 500 1 PHE A 149 141.51 -174.33
REMARK 500 1 ALA A 151 124.54 -170.09
REMARK 500 1 PRO A 152 -158.98 -82.10
REMARK 500 1 HIS A 156 14.54 -154.46
REMARK 500 1 ARG A 165 -153.14 -72.44
REMARK 500 1 ASP A 166 -178.23 -58.52
REMARK 500 1 THR A 168 -9.10 -171.97
REMARK 500 1 ARG A 170 16.91 59.09
REMARK 500 1 ASP A 182 81.19 56.98
REMARK 500 1 SER A 183 -33.52 -159.89
REMARK 500 1 GLU A 185 -32.24 -151.47
REMARK 500 1 LEU A 187 -43.93 -135.29
REMARK 500 1 SER A 188 -75.61 -57.22
REMARK 500 1 ASP B 9 81.75 59.26
REMARK 500 2 SER A 78 -92.44 -77.09
REMARK 500 2 ALA A 79 35.72 179.54
REMARK 500 2 THR A 80 100.81 -173.03
REMARK 500 2 CYS A 81 -149.45 -124.29
REMARK 500 2 SER A 82 -153.33 53.74
REMARK 500 2 TYR A 87 107.68 -58.31
REMARK 500 2 PHE A 94 64.96 -102.14
REMARK 500 2 GLU A 95 -81.81 -147.89
REMARK 500 2 SER A 112 -163.05 -109.70
REMARK 500 2 VAL A 123 95.45 -60.82
REMARK 500 2 THR A 135 -21.36 -141.83
REMARK 500 2 LEU A 138 119.41 -169.78
REMARK 500 2 GLN A 142 -166.63 -73.29
REMARK 500 2 ALA A 151 101.20 -169.30
REMARK 500 2 PRO A 152 -90.37 -68.41
REMARK 500 2 ASP A 153 -164.03 -173.49
REMARK 500 2 ARG A 154 -83.64 -80.73
REMARK 500 2 ASN A 155 48.17 -176.00
REMARK 500 2 HIS A 156 -17.46 -169.27
REMARK 500 2 ARG A 158 15.16 58.99
REMARK 500 2 ARG A 165 -151.22 -88.73
REMARK 500 2 ASP A 166 -149.51 -65.70
REMARK 500
REMARK 500 THIS ENTRY HAS 504 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NMB RELATED DB: PDB
REMARK 900 2NMB CONTAINS THE SAME PROTEIN COMPLEXED WITH THE GPPY PEPTIDE
DBREF 1DDM A 67 201 UNP P16554 NUMB_DROME 67 201
DBREF 1DDM B 1 11 PDB 1DDM 1DDM 1 11
SEQRES 1 A 135 HIS GLN TRP GLN ALA ASP GLU GLU ALA VAL ARG SER ALA
SEQRES 2 A 135 THR CYS SER PHE SER VAL LYS TYR LEU GLY CYS VAL GLU
SEQRES 3 A 135 VAL PHE GLU SER ARG GLY MET GLN VAL CYS GLU GLU ALA
SEQRES 4 A 135 LEU LYS VAL LEU ARG GLN SER ARG ARG ARG PRO VAL ARG
SEQRES 5 A 135 GLY LEU LEU HIS VAL SER GLY ASP GLY LEU ARG VAL VAL
SEQRES 6 A 135 ASP ASP GLU THR LYS GLY LEU ILE VAL ASP GLN THR ILE
SEQRES 7 A 135 GLU LYS VAL SER PHE CYS ALA PRO ASP ARG ASN HIS GLU
SEQRES 8 A 135 ARG GLY PHE SER TYR ILE CYS ARG ASP GLY THR THR ARG
SEQRES 9 A 135 ARG TRP MET CYS HIS GLY PHE LEU ALA CYS LYS ASP SER
SEQRES 10 A 135 GLY GLU ARG LEU SER HIS ALA VAL GLY CYS ALA PHE ALA
SEQRES 11 A 135 VAL CYS LEU GLU ARG
SEQRES 1 B 11 GLY PHE SER ASN MET SER PHE GLU ASP PHE PRO
HELIX 1 1 GLN A 68 GLU A 73 1 6
HELIX 2 2 GLU A 74 ALA A 79 1 6
HELIX 3 3 GLN A 100 SER A 112 1 13
HELIX 4 4 LEU A 187 LEU A 199 1 13
SHEET 1 A 3 SER A 84 LYS A 86 0
SHEET 2 A 3 ARG A 118 LEU A 121 -1 O GLY A 119 N VAL A 85
SHEET 3 A 3 VAL A 130 ASP A 132 -1 N VAL A 131 O LEU A 120
SHEET 1 B 4 GLY A 89 GLU A 92 0
SHEET 2 B 4 MET A 173 LEU A 178 -1 O CYS A 174 N VAL A 91
SHEET 3 B 4 GLY A 159 CYS A 164 -1 O PHE A 160 N PHE A 177
SHEET 4 B 4 PHE A 149 ALA A 151 -1 O PHE A 149 N ILE A 163
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 16 2 Bytes