Header list of 1tce.pdb file
Complete list - 2 20 Bytes
HEADER COMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) 27-MAR-96 1TCE
TITLE SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A
TITLE 2 TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR, MINIMIZED
TITLE 3 AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PHOSPHOPEPTIDE OF THE ZETA CHAIN OF T CELL RECEPTOR;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: BL21 (DE3);
SOURCE 6 CELL_LINE: BL21;
SOURCE 7 GENE: SH2 DOMAIN OF SHC;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET20B;
SOURCE 11 EXPRESSION_SYSTEM_GENE: SH2 DOMAIN OF SHC;
SOURCE 12 MOL_ID: 2
KEYWDS SH2 DOMAIN, COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE), COMPLEX (SIGNAL
KEYWDS 2 TRANSDUCTION-PEPTIDE) COMPLEX
EXPDTA SOLUTION NMR
AUTHOR M.-M.ZHOU,R.P.MEADOWS,T.M.LOGAN,H.S.YOON,W.R.WADE,K.S.RAVICHANDRAN,
AUTHOR 2 S.J.BURAKOFF,S.W.FEISK
REVDAT 3 02-MAR-22 1TCE 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1TCE 1 VERSN
REVDAT 1 15-MAY-97 1TCE 0
JRNL AUTH M.M.ZHOU,R.P.MEADOWS,T.M.LOGAN,H.S.YOON,W.S.WADE,
JRNL AUTH 2 K.S.RAVICHANDRAN,S.J.BURAKOFF,S.W.FESIK
JRNL TITL SOLUTION STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A
JRNL TITL 2 TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 92 7784 1995
JRNL REFN ISSN 0027-8424
JRNL PMID 7544002
JRNL DOI 10.1073/PNAS.92.17.7784
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.M.PASCAL,A.U.SINGER,G.GISH,T.YAMAZAKI,S.E.SHOELSON,
REMARK 1 AUTH 2 T.PAWSON,L.E.KAY,J.D.FORMAN-KAY
REMARK 1 TITL NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF
REMARK 1 TITL 2 PHOSPHOLIPASE C-GAMMA 1 COMPLEXED WITH A HIGH AFFINITY
REMARK 1 TITL 3 BINDING PEPTIDE
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 77 461 1994
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.WAKSMAN,S.E.SHOELSON,N.PANT,D.COWBURN,J.KURIYAN
REMARK 1 TITL BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC
REMARK 1 TITL 2 SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND
REMARK 1 TITL 3 PEPTIDE-FREE FORMS
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 72 779 1993
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.J.ECK,S.E.SHOELSON,S.C.HARRISON
REMARK 1 TITL RECOGNITION OF A HIGH-AFFINITY PHOSPHOTYROSYL PEPTIDE BY THE
REMARK 1 TITL 2 SRC HOMOLOGY-2 DOMAIN OF P56LCK
REMARK 1 REF NATURE V. 362 87 1993
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SET OF IDEAL BOND LENGTHS AND ANGLES
REMARK 3 USED DURING REFINEMENT: PARALLHDG.PRO IN X-PLOR.
REMARK 4
REMARK 4 1TCE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176611.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 GLU A 2 111.23 -163.78
REMARK 500 GLN A 3 -171.04 53.11
REMARK 500 LYS A 13 99.35 -51.75
REMARK 500 ASN A 26 95.43 -66.86
REMARK 500 SER A 48 60.80 178.82
REMARK 500 GLN A 50 84.07 -156.81
REMARK 500 ASP A 67 47.10 -166.78
REMARK 500 ILE A 88 156.96 60.45
REMARK 500 SER A 89 -72.03 -168.61
REMARK 500 LEU A 94 103.06 -58.22
REMARK 500 GLN A 97 -49.57 -141.03
REMARK 500 VAL A 100 -117.76 -66.54
REMARK 500 GLU A 101 126.39 175.38
REMARK 500 ARG A 102 -74.50 -143.55
REMARK 500 LYS A 103 75.00 52.44
REMARK 500 LEU A 104 -39.60 175.25
REMARK 500 LEU A 105 -159.65 -79.73
REMARK 500 GLU A 106 100.99 66.11
REMARK 500 HIS B 202 -106.47 -70.24
REMARK 500 ASP B 203 -150.56 -164.18
REMARK 500 LEU B 205 106.96 1.76
REMARK 500 GLN B 207 -133.18 -104.77
REMARK 500 THR B 211 -147.57 164.69
REMARK 500 ALA B 212 12.26 -151.96
REMARK 500 THR B 213 116.93 -175.48
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 GLY B 201 HIS B 202 -62.36
REMARK 500 HIS B 202 ASP B 203 83.89
REMARK 500 ASP B 203 GLY B 204 135.89
REMARK 500 GLY B 204 LEU B 205 108.35
REMARK 500 LEU B 205 PTR B 206 110.95
REMARK 500 PTR B 206 GLN B 207 -138.40
REMARK 500 GLN B 207 GLY B 208 109.61
REMARK 500 GLY B 208 LEU B 209 146.15
REMARK 500 LEU B 209 SER B 210 -64.21
REMARK 500 SER B 210 THR B 211 91.47
REMARK 500 THR B 211 ALA B 212 -93.38
REMARK 500 ALA B 212 THR B 213 -138.62
REMARK 500 THR B 213 LYS B 214 -65.61
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 ARG A 5 0.28 SIDE CHAIN
REMARK 500 ARG A 16 0.19 SIDE CHAIN
REMARK 500 ARG A 17 0.32 SIDE CHAIN
REMARK 500 ARG A 32 0.15 SIDE CHAIN
REMARK 500 ARG A 64 0.25 SIDE CHAIN
REMARK 500 ARG A 69 0.27 SIDE CHAIN
REMARK 500 ARG A 102 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TCE A 1 104 UNP P29353 SHC_HUMAN 480 583
DBREF 1TCE B 201 214 UNP P20963 CD3Z_HUMAN 136 149
SEQADV 1TCE SER A 46 UNP P29353 LEU 525 CONFLICT
SEQADV 1TCE PTR B 206 UNP P20963 TYR 141 MODIFIED RESIDUE
SEQRES 1 A 107 ALA GLU GLN LEU ARG GLY GLU PRO TRP PHE HIS GLY LYS
SEQRES 2 A 107 LEU SER ARG ARG GLU ALA GLU ALA LEU LEU GLN LEU ASN
SEQRES 3 A 107 GLY ASP PHE LEU VAL ARG GLU SER THR THR THR PRO GLY
SEQRES 4 A 107 GLN TYR VAL LEU THR GLY SER GLN SER GLY GLN PRO LYS
SEQRES 5 A 107 HIS LEU LEU LEU VAL ASP PRO GLU GLY VAL VAL ARG THR
SEQRES 6 A 107 LYS ASP HIS ARG PHE GLU SER VAL SER HIS LEU ILE SER
SEQRES 7 A 107 TYR HIS MET ASP ASN HIS LEU PRO ILE ILE SER ALA GLY
SEQRES 8 A 107 SER GLU LEU CYS LEU GLN GLN PRO VAL GLU ARG LYS LEU
SEQRES 9 A 107 LEU GLU HIS
SEQRES 1 B 14 GLY HIS ASP GLY LEU PTR GLN GLY LEU SER THR ALA THR
SEQRES 2 B 14 LYS
MODRES 1TCE PTR B 206 TYR O-PHOSPHOTYROSINE
HET PTR B 206 24
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR C9 H12 N O6 P
HELIX 1 1 GLN A 3 GLY A 6 1 4
HELIX 2 2 ARG A 16 LEU A 22 1 7
HELIX 3 3 VAL A 73 ASN A 83 1 11
SHEET 1 A 3 VAL A 31 GLU A 33 0
SHEET 2 A 3 TYR A 41 SER A 46 -1 N VAL A 42 O ARG A 32
SHEET 3 A 3 PRO A 51 LEU A 55 -1 N LEU A 54 O LEU A 43
LINK C LEU B 205 N PTR B 206 1555 1555 1.31
LINK C PTR B 206 N GLN B 207 1555 1555 1.31
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
Complete list - 2 20 Bytes