Header list of 1shc.pdb file
Complete list - 2 20 Bytes
HEADER COMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) 27-MAR-96 1SHC
TITLE SHC PTB DOMAIN COMPLEXED WITH A TRKA RECEPTOR PHOSPHOPEPTIDE, NMR,
TITLE 2 MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PTB DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TRKA RECEPTOR PHOSPHOPEPTIDE;
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: PTB DOMAIN OF SHC;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 EXPRESSION_SYSTEM_GENE: PTB DOMAIN OF SHC;
SOURCE 12 MOL_ID: 2
KEYWDS COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE), PHOSPHOTYROSINE BINDING DOMAIN
KEYWDS 2 (PTB), COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) COMPLEX
EXPDTA SOLUTION NMR
AUTHOR M.-M.ZHOU,K.S.RAVICHANDRAN,E.T.OLEJNICZAK,A.M.PETROS,R.P.MEADOWS,
AUTHOR 2 M.SATTLER,J.E.HARLAN,W.S.WADE,S.J.BURAKOFF,S.W.FESIK
REVDAT 3 02-MAR-22 1SHC 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1SHC 1 VERSN
REVDAT 1 15-MAY-97 1SHC 0
JRNL AUTH M.M.ZHOU,K.S.RAVICHANDRAN,E.F.OLEJNICZAK,A.M.PETROS,
JRNL AUTH 2 R.P.MEADOWS,M.SATTLER,J.E.HARLAN,W.S.WADE,S.J.BURAKOFF,
JRNL AUTH 3 S.W.FESIK
JRNL TITL STRUCTURE AND LIGAND RECOGNITION OF THE PHOSPHOTYROSINE
JRNL TITL 2 BINDING DOMAIN OF SHC.
JRNL REF NATURE V. 378 584 1995
JRNL REFN ISSN 0028-0836
JRNL PMID 8524391
JRNL DOI 10.1038/378584A0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.M.ZHOU,B.HUANG,E.T.OLEJNICZAK,R.P.MEADOWS,S.B.SHUKER,
REMARK 1 AUTH 2 M.MIYAZAKI,T.TRUB,S.E.SHOELSON,S.W.FESIK
REMARK 1 TITL STRUCTURAL BASIS FOR IL-4 RECEPTOR PHOSPHOPEPTIDE
REMARK 1 TITL 2 RECOGNITION BY THE IRS-1 PTB DOMAIN
REMARK 1 REF NAT.STRUCT.BIOL. V. 3 388 1996
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.TRUB,W.E.CHOI,G.WOLF,E.OTTINGER,Y.CHEN,M.WEISS,
REMARK 1 AUTH 2 S.E.SHOELSON
REMARK 1 TITL SPECIFICITY OF THE PTB DOMAIN OF SHC FOR BETA TURN-FORMING
REMARK 1 TITL 2 PENTAPEPTIDE MOTIFS AMINO-TERMINAL TO PHOSPHOTYROSINE
REMARK 1 REF J.BIOL.CHEM. V. 270 18205 1995
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH W.M.KAVANAUGH,L.T.WILLIAMS
REMARK 1 TITL AN ALTERNATIVE TO SH2 DOMAINS FOR BINDING
REMARK 1 TITL 2 TYROSINE-PHOSPHORYLATED PROTEINS
REMARK 1 REF SCIENCE V. 266 1862 1994
REMARK 1 REFN ISSN 0036-8075
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 WERE USED DURING REFINEMENT: PARALLHDG.PRO IN X-PLOR.
REMARK 4
REMARK 4 1SHC 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_1000176371.
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 HIS A 15 -37.51 179.71
REMARK 500 MET A 16 -79.38 -54.61
REMARK 500 GLN A 18 -159.82 41.05
REMARK 500 LEU A 19 -179.58 58.00
REMARK 500 GLU A 22 29.87 -162.16
REMARK 500 TRP A 24 50.31 35.87
REMARK 500 THR A 25 60.58 -162.02
REMARK 500 HIS A 27 -169.59 -68.64
REMARK 500 PHE A 30 -88.72 38.46
REMARK 500 VAL A 31 -49.86 82.93
REMARK 500 THR A 35 -100.22 -60.67
REMARK 500 ARG A 36 -34.61 173.83
REMARK 500 TRP A 38 -166.37 54.34
REMARK 500 VAL A 50 174.79 -58.21
REMARK 500 SER A 51 93.61 -167.33
REMARK 500 LEU A 63 28.36 -140.71
REMARK 500 SER A 65 -172.84 -62.97
REMARK 500 LEU A 69 -73.11 -117.64
REMARK 500 ASP A 70 108.89 59.02
REMARK 500 GLU A 87 -68.06 -100.38
REMARK 500 PRO A 90 155.49 -44.97
REMARK 500 ALA A 92 -164.40 -72.85
REMARK 500 ALA A 95 39.62 177.44
REMARK 500 ARG A 98 36.95 -167.32
REMARK 500 ARG A 99 86.35 56.00
REMARK 500 PRO A 101 -83.74 -70.32
REMARK 500 CYS A 102 157.50 62.98
REMARK 500 SER A 103 -157.72 -65.30
REMARK 500 ARG A 104 67.13 -161.75
REMARK 500 PRO A 105 93.81 -48.15
REMARK 500 LEU A 106 125.52 -172.85
REMARK 500 SER A 107 -62.84 -105.09
REMARK 500 ILE A 109 83.19 -154.31
REMARK 500 LEU A 110 -168.69 173.70
REMARK 500 ARG A 112 140.81 175.65
REMARK 500 LEU A 115 53.19 -96.20
REMARK 500 THR A 128 94.96 -65.26
REMARK 500 SER A 129 36.53 73.49
REMARK 500 SER A 130 70.95 -152.04
REMARK 500 ASP A 137 -69.01 -104.89
REMARK 500 LYS A 139 70.89 54.23
REMARK 500 GLN A 140 -158.45 -142.18
REMARK 500 ILE A 142 92.61 -66.46
REMARK 500 ALA A 143 122.87 62.71
REMARK 500 HIS A 145 53.23 -157.46
REMARK 500 MET A 147 67.18 -168.44
REMARK 500 GLN A 148 -41.19 -158.63
REMARK 500 SER A 149 -87.95 -104.27
REMARK 500 ILE A 150 -154.13 50.89
REMARK 500 SER A 151 -52.93 -176.60
REMARK 500
REMARK 500 THIS ENTRY HAS 65 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 ARG A 26 0.23 SIDE CHAIN
REMARK 500 ARG A 36 0.24 SIDE CHAIN
REMARK 500 ARG A 55 0.19 SIDE CHAIN
REMARK 500 ARG A 67 0.29 SIDE CHAIN
REMARK 500 ARG A 74 0.19 SIDE CHAIN
REMARK 500 ARG A 79 0.32 SIDE CHAIN
REMARK 500 ARG A 97 0.32 SIDE CHAIN
REMARK 500 ARG A 98 0.25 SIDE CHAIN
REMARK 500 ARG A 99 0.23 SIDE CHAIN
REMARK 500 ARG A 104 0.30 SIDE CHAIN
REMARK 500 ARG A 112 0.32 SIDE CHAIN
REMARK 500 ARG A 175 0.19 SIDE CHAIN
REMARK 500 ARG A 201 0.30 SIDE CHAIN
REMARK 500 ARG A 207 0.18 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1SHC A 13 207 UNP P29353 SHC_HUMAN 126 317
DBREF 1SHC B 483 494 UNP P04629 NTRK1_HUMAN 489 500
SEQADV 1SHC MET A 16 UNP P29353 GLY 126 CONFLICT
SEQADV 1SHC PTR B 490 UNP P04629 TYR 496 MODIFIED RESIDUE
SEQRES 1 A 195 GLY SER HIS MET GLY GLN LEU GLY GLY GLU GLU TRP THR
SEQRES 2 A 195 ARG HIS GLY SER PHE VAL ASN LYS PRO THR ARG GLY TRP
SEQRES 3 A 195 LEU HIS PRO ASN ASP LYS VAL MET GLY PRO GLY VAL SER
SEQRES 4 A 195 TYR LEU VAL ARG TYR MET GLY CYS VAL GLU VAL LEU GLN
SEQRES 5 A 195 SER MET ARG ALA LEU ASP PHE ASN THR ARG THR GLN VAL
SEQRES 6 A 195 THR ARG GLU ALA ILE SER LEU VAL CYS GLU ALA VAL PRO
SEQRES 7 A 195 GLY ALA LYS GLY ALA THR ARG ARG ARG LYS PRO CYS SER
SEQRES 8 A 195 ARG PRO LEU SER SER ILE LEU GLY ARG SER ASN LEU LYS
SEQRES 9 A 195 PHE ALA GLY MET PRO ILE THR LEU THR VAL SER THR SER
SEQRES 10 A 195 SER LEU ASN LEU MET ALA ALA ASP CYS LYS GLN ILE ILE
SEQRES 11 A 195 ALA ASN HIS HIS MET GLN SER ILE SER PHE ALA SER GLY
SEQRES 12 A 195 GLY ASP PRO ASP THR ALA GLU TYR VAL ALA TYR VAL ALA
SEQRES 13 A 195 LYS ASP PRO VAL ASN GLN ARG ALA CYS HIS ILE LEU GLU
SEQRES 14 A 195 CYS PRO GLU GLY LEU ALA GLN ASP VAL ILE SER THR ILE
SEQRES 15 A 195 GLY GLN ALA PHE GLU LEU ARG PHE LYS GLN TYR LEU ARG
SEQRES 1 B 12 HIS ILE ILE GLU ASN PRO GLN PTR PHE SER ASP ALA
MODRES 1SHC PTR B 490 TYR O-PHOSPHOTYROSINE
HET PTR B 490 25
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR C9 H12 N O6 P
HELIX 1 1 HIS A 40 MET A 46 1 7
HELIX 2 2 THR A 73 ALA A 88 1 16
HELIX 3 3 ALA A 187 GLU A 199 1 13
SHEET 1 A 5 GLY A 111 ASN A 114 0
SHEET 2 A 5 CYS A 59 VAL A 62 -1 N GLU A 61 O ARG A 112
SHEET 3 A 5 ALA A 176 LEU A 180 -1 N CYS A 177 O VAL A 60
SHEET 4 A 5 VAL A 164 ALA A 168 -1 N ALA A 168 O ALA A 176
SHEET 5 A 5 PHE A 152 SER A 154 -1 N SER A 154 O ALA A 165
SHEET 1 B 4 GLN A 140 ILE A 142 0
SHEET 2 B 4 SER A 130 ALA A 135 -1 N ALA A 135 O GLN A 140
SHEET 3 B 4 ALA A 118 SER A 127 -1 N SER A 127 O SER A 130
SHEET 4 B 4 VAL A 50 MET A 57 -1 N TYR A 56 O GLY A 119
LINK C GLN B 489 N PTR B 490 1555 1555 1.30
LINK C PTR B 490 N PHE B 491 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