Header list of 1hct.pdb file
Complete list - b 23 2 Bytes
HEADER COMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) 02-SEP-94 1HCT
TITLE NMR STRUCTURE OF THE HUMAN SRC SH2 DOMAIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL-PYEEIE-OH;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HUMAN SRC;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: PP60==C-SRC==;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 MOL_ID: 2;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 GENE: NUCLEOTIDE SEQUENCE A;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS HUMAN PP60C-SRC SH2 DOMAIN, COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE)
KEYWDS 2 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 23
AUTHOR R.T.GAMPE JUNIOR,R.X.XU
REVDAT 4 23-FEB-22 1HCT 1 REMARK LINK
REVDAT 3 24-FEB-09 1HCT 1 VERSN
REVDAT 2 01-APR-03 1HCT 1 JRNL
REVDAT 1 15-SEP-95 1HCT 0
JRNL AUTH R.X.XU,J.M.WORD,D.G.DAVIS,M.J.RINK,D.H.WILLARD JR.,
JRNL AUTH 2 R.T.GAMPE JR.
JRNL TITL SOLUTION STRUCTURE OF THE HUMAN PP60C-SRC SH2 DOMAIN
JRNL TITL 2 COMPLEXED WITH A PHOSPHORYLATED TYROSINE PENTAPEPTIDE.
JRNL REF BIOCHEMISTRY V. 34 2107 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7532003
JRNL DOI 10.1021/BI00007A003
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.GILMER,M.RODRIGUEZ,S.JORDAN,R.CROSBY,K.ALLIGOOD,M.GREEN,
REMARK 1 AUTH 2 M.KIMERY,C.WAGNER,D.KINDER,P.CHARIFSON,A.M.HASSELL,
REMARK 1 AUTH 3 D.WILLARD,M.LUTHER,D.RUSNAK,D.D.STERNBACH,M.MEHROTRA,M.PEEL,
REMARK 1 AUTH 4 L.SHAMPINE,R.DAVIS,J.ROBBINS,I.R.PATEL,D.KASSEL,W.BURKHART,
REMARK 1 AUTH 5 M.MOYER,T.BRADSHAW,J.BERMAN
REMARK 1 TITL PEPTIDE INHIBITORS OF SRC SH3-SH2(SLASH)PHOSPHOPROTEIN
REMARK 1 TITL 2 INTERACTIONS
REMARK 1 REF J.BIOL.CHEM. V. 269 31711 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
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-GAMMA1 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 3
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 4
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 1 REFERENCE 5
REMARK 1 AUTH S.K.ANDERSON,C.P.GIBBS,A.TANAKA,H.J.KUNG,D.J.FUGITA
REMARK 1 TITL HUMAN CELLULAR SRC GENE: NUCLEOTIDE SEQUENCE AND DERIVED
REMARK 1 TITL 2 AMINO ACID SEQUENCE OF THE REGION CODING FOR THE
REMARK 1 TITL 3 CARBOXY-TERMINAL TWO-THIRDS OF PP60C-SRC
REMARK 1 REF MOL.CELL.BIOL. V. 5 1122 1985
REMARK 1 REFN ISSN 0270-7306
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: NULL
REMARK 4
REMARK 4 1HCT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173785.
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 : 23
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 1 ALA B 145 45.26 -170.32
REMARK 500 1 GLU B 166 32.87 -89.61
REMARK 500 1 LYS B 181 -165.99 -56.15
REMARK 500 1 ALA B 183 -150.73 -89.27
REMARK 500 1 LYS B 195 -40.64 -146.12
REMARK 500 1 ASN B 198 -169.34 -112.75
REMARK 500 1 TYR B 213 89.59 -179.30
REMARK 500 1 SER B 231 30.21 -89.69
REMARK 500 1 LYS B 232 -41.42 -150.23
REMARK 500 1 THR B 242 -37.68 -133.75
REMARK 500 2 GLU A 102 -176.82 -53.40
REMARK 500 2 ASP B 141 57.47 -149.62
REMARK 500 2 ARG B 169 98.67 -55.36
REMARK 500 2 ASN B 193 56.55 -101.61
REMARK 500 2 ALA B 194 -69.33 -150.08
REMARK 500 2 TYR B 213 137.09 -178.96
REMARK 500 2 THR B 215 -149.46 -134.67
REMARK 500 2 ARG B 217 -27.50 168.12
REMARK 500 2 HIS B 239 139.36 177.47
REMARK 500 2 THR B 242 -37.90 -135.95
REMARK 500 3 ASP B 141 48.18 -177.28
REMARK 500 3 LEU B 163 58.99 -103.09
REMARK 500 3 ALA B 183 -150.58 -89.88
REMARK 500 3 ASN B 193 49.78 -86.79
REMARK 500 3 ALA B 194 -49.18 -132.99
REMARK 500 3 LYS B 195 -67.36 -126.08
REMARK 500 3 TYR B 213 114.90 -178.11
REMARK 500 3 ARG B 217 -39.62 -147.32
REMARK 500 3 SER B 222 141.62 -177.41
REMARK 500 3 HIS B 239 126.78 179.10
REMARK 500 3 THR B 242 -39.24 -138.21
REMARK 500 4 ASP B 141 148.40 65.76
REMARK 500 4 SER B 142 155.16 170.97
REMARK 500 4 ALA B 145 44.18 -150.41
REMARK 500 4 ASN B 164 37.84 -140.15
REMARK 500 4 ALA B 165 30.96 37.12
REMARK 500 4 THR B 180 71.71 -106.68
REMARK 500 4 LYS B 195 -38.18 -137.06
REMARK 500 4 TYR B 213 135.16 -179.06
REMARK 500 4 ARG B 217 -39.83 -148.68
REMARK 500 4 HIS B 239 139.06 178.73
REMARK 500 5 ALA B 165 28.64 38.68
REMARK 500 5 GLU B 166 18.34 -152.80
REMARK 500 5 SER B 177 -81.92 -45.47
REMARK 500 5 GLU B 178 -45.63 83.68
REMARK 500 5 THR B 180 -164.07 -100.51
REMARK 500 5 ASN B 193 53.77 -90.27
REMARK 500 5 ALA B 194 -59.69 -154.63
REMARK 500 5 LYS B 195 -74.15 -97.91
REMARK 500 5 TYR B 213 120.17 -178.42
REMARK 500
REMARK 500 THIS ENTRY HAS 248 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 1 ARG B 155 0.29 SIDE CHAIN
REMARK 500 1 ARG B 156 0.32 SIDE CHAIN
REMARK 500 1 ARG B 160 0.32 SIDE CHAIN
REMARK 500 1 ARG B 169 0.20 SIDE CHAIN
REMARK 500 1 ARG B 175 0.31 SIDE CHAIN
REMARK 500 1 ARG B 205 0.32 SIDE CHAIN
REMARK 500 1 ARG B 217 0.19 SIDE CHAIN
REMARK 500 1 ARG B 240 0.27 SIDE CHAIN
REMARK 500 2 ARG B 155 0.24 SIDE CHAIN
REMARK 500 2 ARG B 156 0.31 SIDE CHAIN
REMARK 500 2 ARG B 160 0.32 SIDE CHAIN
REMARK 500 2 ARG B 169 0.22 SIDE CHAIN
REMARK 500 2 ARG B 175 0.21 SIDE CHAIN
REMARK 500 2 ARG B 205 0.31 SIDE CHAIN
REMARK 500 2 ARG B 217 0.32 SIDE CHAIN
REMARK 500 2 ARG B 240 0.27 SIDE CHAIN
REMARK 500 3 ARG B 155 0.30 SIDE CHAIN
REMARK 500 3 ARG B 156 0.30 SIDE CHAIN
REMARK 500 3 ARG B 160 0.28 SIDE CHAIN
REMARK 500 3 ARG B 169 0.30 SIDE CHAIN
REMARK 500 3 ARG B 175 0.28 SIDE CHAIN
REMARK 500 3 ARG B 205 0.24 SIDE CHAIN
REMARK 500 3 ARG B 217 0.24 SIDE CHAIN
REMARK 500 3 ARG B 240 0.31 SIDE CHAIN
REMARK 500 4 ARG B 155 0.32 SIDE CHAIN
REMARK 500 4 ARG B 156 0.31 SIDE CHAIN
REMARK 500 4 ARG B 160 0.32 SIDE CHAIN
REMARK 500 4 ARG B 169 0.32 SIDE CHAIN
REMARK 500 4 ARG B 175 0.29 SIDE CHAIN
REMARK 500 4 ARG B 205 0.32 SIDE CHAIN
REMARK 500 4 ARG B 217 0.32 SIDE CHAIN
REMARK 500 4 ARG B 240 0.31 SIDE CHAIN
REMARK 500 5 ARG B 155 0.27 SIDE CHAIN
REMARK 500 5 ARG B 156 0.32 SIDE CHAIN
REMARK 500 5 ARG B 160 0.18 SIDE CHAIN
REMARK 500 5 ARG B 169 0.31 SIDE CHAIN
REMARK 500 5 ARG B 175 0.17 SIDE CHAIN
REMARK 500 5 ARG B 205 0.14 SIDE CHAIN
REMARK 500 5 ARG B 217 0.31 SIDE CHAIN
REMARK 500 5 ARG B 240 0.32 SIDE CHAIN
REMARK 500 6 ARG B 155 0.31 SIDE CHAIN
REMARK 500 6 ARG B 156 0.18 SIDE CHAIN
REMARK 500 6 ARG B 160 0.27 SIDE CHAIN
REMARK 500 6 ARG B 169 0.29 SIDE CHAIN
REMARK 500 6 ARG B 175 0.20 SIDE CHAIN
REMARK 500 6 ARG B 205 0.12 SIDE CHAIN
REMARK 500 6 ARG B 217 0.26 SIDE CHAIN
REMARK 500 6 ARG B 240 0.24 SIDE CHAIN
REMARK 500 7 ARG B 155 0.29 SIDE CHAIN
REMARK 500 7 ARG B 156 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 183 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HCS RELATED DB: PDB
DBREF 1HCT B 141 246 UNP P12931 SRC_HUMAN 143 248
DBREF 1HCT A 100 105 PDB 1HCT 1HCT 100 105
SEQRES 1 A 6 ACE PTR GLU GLU ILE GLU
SEQRES 1 B 107 MET ASP SER ILE GLN ALA GLU GLU TRP TYR PHE GLY LYS
SEQRES 2 B 107 ILE THR ARG ARG GLU SER GLU ARG LEU LEU LEU ASN ALA
SEQRES 3 B 107 GLU ASN PRO ARG GLY THR PHE LEU VAL ARG GLU SER GLU
SEQRES 4 B 107 THR THR LYS GLY ALA TYR CYS LEU SER VAL SER ASP PHE
SEQRES 5 B 107 ASP ASN ALA LYS GLY LEU ASN VAL LYS HIS TYR LYS ILE
SEQRES 6 B 107 ARG LYS LEU ASP SER GLY GLY PHE TYR ILE THR SER ARG
SEQRES 7 B 107 THR GLN PHE ASN SER LEU GLN GLN LEU VAL ALA TYR TYR
SEQRES 8 B 107 SER LYS HIS ALA ASP GLY LEU CYS HIS ARG LEU THR THR
SEQRES 9 B 107 VAL CYS PRO
MODRES 1HCT PTR A 101 TYR O-PHOSPHOTYROSINE
HET ACE A 100 6
HET PTR A 101 24
HETNAM ACE ACETYL GROUP
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 ACE C2 H4 O
FORMUL 1 PTR C9 H12 N O6 P
HELIX 1 1 ILE B 143 ALA B 145 5 3
HELIX 2 2 ARG B 155 LEU B 162 1 8
HELIX 3 3 LEU B 223 TYR B 230 1 8
SHEET 1 A 3 PHE B 172 GLU B 176 0
SHEET 2 A 3 TYR B 184 PHE B 191 -1 N SER B 187 O LEU B 173
SHEET 3 A 3 LEU B 197 ILE B 204 -1 N ILE B 204 O TYR B 184
LINK C ACE A 100 N PTR A 101 1555 1555 1.31
LINK C PTR A 101 N GLU A 102 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
MODEL 1
Complete list - b 23 2 Bytes