Header list of 1oy2.pdb file
Complete list - 23 20 Bytes
HEADER SIGNALING PROTEIN 03-APR-03 1OY2
TITLE COUPLING OF FOLDING AND BINDING IN THE PTB DOMAIN OF THE SIGNALING
TITLE 2 PROTEIN SHC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHC TRANSFORMING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PTB DOMAIN;
COMPND 5 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: SHC;
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: PET15B
KEYWDS FREE PROTEIN, STRUCTURE DISORDER, BETA SANDWICH, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR A.FAROOQ,L.ZENG,K.S.YAN,K.S.RAVICHANDRAN,M.-M.ZHOU
REVDAT 3 23-FEB-22 1OY2 1 REMARK
REVDAT 2 24-FEB-09 1OY2 1 VERSN
REVDAT 1 06-APR-04 1OY2 0
JRNL AUTH A.FAROOQ,L.ZENG,K.S.YAN,K.S.RAVICHANDRAN,M.-M.ZHOU
JRNL TITL COUPLING OF FOLDING AND BINDING IN THE PTB DOMAIN OF THE
JRNL TITL 2 SIGNALING PROTEIN SHC
JRNL REF STRUCTURE V. 11 905 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 12906822
JRNL DOI 10.1016/S0969-2126(03)00134-5
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, ARIA
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OY2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018789.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 200MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5MM SHC PTB DOMAIN, 50MM
REMARK 210 SODIUM PHOSPHATE, 20MM DTT-D10
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; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR, X-PLOR, ARIA, NMRVIEW
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 LYS A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 GLY A 6
REMARK 465 GLY A 7
REMARK 465 GLY A 8
REMARK 465 GLY A 9
REMARK 465 ARG A 10
REMARK 465 ARG A 11
REMARK 465 THR A 12
REMARK 465 ARG A 13
REMARK 465 VAL A 14
REMARK 465 GLU A 15
REMARK 465 GLY A 16
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 GLN A 18 158.06 63.13
REMARK 500 GLU A 22 37.04 -166.70
REMARK 500 THR A 25 60.52 -152.59
REMARK 500 ASN A 32 66.19 170.10
REMARK 500 LEU A 39 -62.45 67.88
REMARK 500 HIS A 40 -81.87 -151.71
REMARK 500 GLN A 64 161.39 -45.25
REMARK 500 SER A 65 -68.42 -172.97
REMARK 500 ARG A 67 82.42 -67.07
REMARK 500 ALA A 68 -163.15 -124.66
REMARK 500 ASP A 70 84.48 -171.29
REMARK 500 THR A 73 31.24 -168.95
REMARK 500 VAL A 89 78.81 -119.12
REMARK 500 LYS A 93 102.72 56.98
REMARK 500 THR A 96 -164.92 -125.48
REMARK 500 ARG A 98 -82.65 61.47
REMARK 500 LYS A 100 93.23 -179.59
REMARK 500 ARG A 104 152.60 60.65
REMARK 500 SER A 107 170.72 74.83
REMARK 500 LEU A 110 157.93 64.06
REMARK 500 ARG A 112 138.59 -179.98
REMARK 500 LYS A 116 99.73 -42.06
REMARK 500 PHE A 117 54.04 70.95
REMARK 500 THR A 128 106.37 -54.42
REMARK 500 SER A 130 115.07 -175.33
REMARK 500 ALA A 135 107.27 -55.41
REMARK 500 LYS A 139 62.65 72.91
REMARK 500 GLN A 140 -170.05 -177.28
REMARK 500 SER A 149 -53.98 171.60
REMARK 500 SER A 151 -67.64 -168.78
REMARK 500 ASP A 157 58.05 -170.55
REMARK 500 THR A 160 67.75 179.45
REMARK 500 ALA A 161 -70.88 67.04
REMARK 500 GLU A 162 45.71 -148.14
REMARK 500 ASP A 170 95.57 -177.69
REMARK 500 ASN A 173 49.14 78.45
REMARK 500 GLN A 174 103.48 52.97
REMARK 500 ARG A 175 -61.57 -133.25
REMARK 500 SER A 192 103.59 74.36
REMARK 500 THR A 193 -52.75 -166.47
REMARK 500 GLN A 196 134.02 175.50
REMARK 500 ALA A 197 102.61 -57.35
REMARK 500 PHE A 198 -157.00 -83.10
REMARK 500 GLU A 199 49.75 80.49
REMARK 500 LEU A 200 106.42 179.06
REMARK 500 GLN A 204 173.96 52.92
REMARK 500 LEU A 206 25.61 49.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1N3H RELATED DB: PDB
REMARK 900 FREE PROTEIN STRUCTURE (RESIDUES 111-317)
REMARK 900 RELATED ID: 1SHC RELATED DB: PDB
REMARK 900 PROTEIN (RESIDUES 127-317) COMPLEXED TO TRKA PHOSPHOPEPTIDE
DBREF 1OY2 A 1 207 UNP P29353 SHC1_HUMAN 111 317
SEQRES 1 A 207 MET ASN LYS LEU SER GLY GLY GLY GLY ARG ARG THR ARG
SEQRES 2 A 207 VAL GLU GLY GLY GLN LEU GLY GLY GLU GLU TRP THR ARG
SEQRES 3 A 207 HIS GLY SER PHE VAL ASN LYS PRO THR ARG GLY TRP LEU
SEQRES 4 A 207 HIS PRO ASN ASP LYS VAL MET GLY PRO GLY VAL SER TYR
SEQRES 5 A 207 LEU VAL ARG TYR MET GLY CYS VAL GLU VAL LEU GLN SER
SEQRES 6 A 207 MET ARG ALA LEU ASP PHE ASN THR ARG THR GLN VAL THR
SEQRES 7 A 207 ARG GLU ALA ILE SER LEU VAL CYS GLU ALA VAL PRO GLY
SEQRES 8 A 207 ALA LYS GLY ALA THR ARG ARG ARG LYS PRO CYS SER ARG
SEQRES 9 A 207 PRO LEU SER SER ILE LEU GLY ARG SER ASN LEU LYS PHE
SEQRES 10 A 207 ALA GLY MET PRO ILE THR LEU THR VAL SER THR SER SER
SEQRES 11 A 207 LEU ASN LEU MET ALA ALA ASP CYS LYS GLN ILE ILE ALA
SEQRES 12 A 207 ASN HIS HIS MET GLN SER ILE SER PHE ALA SER GLY GLY
SEQRES 13 A 207 ASP PRO ASP THR ALA GLU TYR VAL ALA TYR VAL ALA LYS
SEQRES 14 A 207 ASP PRO VAL ASN GLN ARG ALA CYS HIS ILE LEU GLU CYS
SEQRES 15 A 207 PRO GLU GLY LEU ALA GLN ASP VAL ILE SER THR ILE GLY
SEQRES 16 A 207 GLN ALA PHE GLU LEU ARG PHE LYS GLN TYR LEU ARG
HELIX 1 1 ASN A 42 GLY A 47 1 6
HELIX 2 2 THR A 73 VAL A 89 1 17
HELIX 3 3 PRO A 90 LYS A 93 5 4
HELIX 4 4 LEU A 186 ILE A 191 1 6
SHEET 1 A 4 SER A 130 MET A 134 0
SHEET 2 A 4 MET A 120 SER A 127 -1 N THR A 123 O MET A 134
SHEET 3 A 4 VAL A 50 GLU A 61 -1 N VAL A 50 O VAL A 126
SHEET 4 A 4 ARG A 112 ASN A 114 -1 O ARG A 112 N GLU A 61
SHEET 1 B 5 SER A 130 MET A 134 0
SHEET 2 B 5 MET A 120 SER A 127 -1 N THR A 123 O MET A 134
SHEET 3 B 5 VAL A 50 GLU A 61 -1 N VAL A 50 O VAL A 126
SHEET 4 B 5 ALA A 176 GLU A 181 -1 O CYS A 177 N VAL A 60
SHEET 5 B 5 VAL A 164 ALA A 165 -1 N VAL A 164 O LEU A 180
CISPEP 1 ARG A 104 PRO A 105 0 0.80
CISPEP 2 ASP A 157 PRO A 158 0 1.76
CISPEP 3 ASP A 170 PRO A 171 0 0.51
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 - 23 20 Bytes