Header list of 1nlp.pdb file
Complete list - 23 20 Bytes
HEADER COMPLEX (TRANSFERASE/PEPTIDE) 04-AUG-96 1NLP
TITLE STRUCTURE OF SIGNAL TRANSDUCTION PROTEIN, NMR, MINIMIZED AVERAGE
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-SRC;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 EC: 2.7.1.112;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NL2 (MN8-MN1-PLPPLP);
COMPND 9 CHAIN: N;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: LIGAND NL2 CONTAINS NON-PEPTIDE ELEMENTS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: CHICKEN;
SOURCE 6 EXPRESSION_SYSTEM: GST-FUSION;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;
SOURCE 8 EXPRESSION_SYSTEM_GENE: CHICKEN;
SOURCE 9 MOL_ID: 2
KEYWDS SRC, SH3 DOMAIN, LIGANDS, NON-PEPTIDE ELEMENTS, COMPLEX (TRANSFERASE-
KEYWDS 2 PEPTIDE), COMPLEX (TRANSFERASE-PEPTIDE) COMPLEX
EXPDTA SOLUTION NMR
AUTHOR S.FENG,T.M.KAPOOR,F.SHIRAI,A.P.COMBS,S.L.SCHREIBER
REVDAT 3 23-FEB-22 1NLP 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1NLP 1 VERSN
REVDAT 1 27-JAN-97 1NLP 0
JRNL AUTH S.FENG,T.M.KAPOOR,F.SHIRAI,A.P.COMBS,S.L.SCHREIBER
JRNL TITL MOLECULAR BASIS FOR THE BINDING OF SH3 LIGANDS WITH
JRNL TITL 2 NON-PEPTIDE ELEMENTS IDENTIFIED BY COMBINATORIAL SYNTHESIS.
JRNL REF CHEM.BIOL. V. 3 661 1996
JRNL REFN ISSN 1074-5521
JRNL PMID 8807900
JRNL DOI 10.1016/S1074-5521(96)90134-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.P.COMBS,T.M.KAPOOR,S.FENG,J.K.CHEN,L.F.DAUDE-SNOW,
REMARK 1 AUTH 2 S.L.SCHREIBER
REMARK 1 TITL PROTEIN STRUCTURE-BASED COMBINATORIAL CHEMISTRY: DISCOVERY
REMARK 1 TITL 2 OF NON-PEPTIDE BINDING ELEMENTS TO SRC SH3 DOMAIN
REMARK 1 REF J.AM.CHEM.SOC. V. 118 287 1996
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.FENG,C.KASAHARA,R.J.RICKLES,S.L.SCHREIBER
REMARK 1 TITL SPECIFIC INTERACTIONS OUTSIDE THE PROLINE-RICH CORE OF TWO
REMARK 1 TITL 2 CLASSES OF SRC HOMOLOGY 3 LIGANDS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 92 12408 1995
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.YU,J.K.CHEN,S.FENG,D.C.DALGARNO,A.W.BRAUER,S.L.SCHREIBER
REMARK 1 TITL STRUCTURAL BASIS FOR THE BINDING OF PROLINE-RICH PEPTIDES TO
REMARK 1 TITL 2 SH3 DOMAINS
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 76 933 1994
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 4
REMARK 1 AUTH S.FENG,J.K.CHEN,H.YU,J.A.SIMON,S.L.SCHREIBER
REMARK 1 TITL TWO BINDING ORIENTATIONS FOR PEPTIDES TO THE SRC SH3 DOMAIN:
REMARK 1 TITL 2 DEVELOPMENT OF A GENERAL MODEL FOR SH3-LIGAND INTERACTIONS
REMARK 1 REF SCIENCE V. 266 1241 1994
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 5
REMARK 1 AUTH H.YU,M.K.ROSEN,T.B.SHIN,C.SEIDEL-DUGAN,J.S.BRUGGE,
REMARK 1 AUTH 2 S.L.SCHREIBER
REMARK 1 TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN OF SRC AND
REMARK 1 TITL 2 IDENTIFICATION OF ITS LIGAND-BINDING SITE
REMARK 1 REF SCIENCE V. 258 1665 1992
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NLP 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_1000175328.
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 : MINIMIZED AVERAGE
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: C, N
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 GLY C 1
REMARK 465 SER C 2
REMARK 465 HIS C 3
REMARK 465 MET C 4
REMARK 465 GLY C 5
REMARK 465 GLY C 6
REMARK 465 VAL C 7
REMARK 465 THR C 8
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 LEU C 13 -31.34 -38.76
REMARK 500 VAL C 35 -74.78 -113.38
REMARK 500 TYR C 55 174.75 -50.15
REMARK 500 LEU N 79 150.85 -43.00
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NLP C 1 64 UNP P00525 SRC_AVISR 77 140
DBREF 1NLP N 72 81 PDB 1NLP 1NLP 72 81
SEQADV 1NLP SER C 2 UNP P00525 ALA 78 CONFLICT
SEQADV 1NLP HIS C 3 UNP P00525 LEU 79 CONFLICT
SEQADV 1NLP MET C 4 UNP P00525 ALA 80 CONFLICT
SEQRES 1 C 64 GLY SER HIS MET GLY GLY VAL THR THR PHE VAL ALA LEU
SEQRES 2 C 64 TYR ASP TYR GLU SER ARG THR GLU THR ASP LEU SER PHE
SEQRES 3 C 64 LYS LYS GLY GLU ARG LEU GLN ILE VAL ASN ASN THR GLU
SEQRES 4 C 64 GLY ASP TRP TRP LEU ALA HIS SER LEU THR THR GLY GLN
SEQRES 5 C 64 THR GLY TYR ILE PRO SER ASN TYR VAL ALA PRO SER
SEQRES 1 N 10 ACE MN8 MN1 PRO LEU PRO PRO LEU PRO NH2
HET ACE N 72 6
HET MN8 N 73 36
HET MN1 N 74 17
HET NH2 N 81 3
HETNAM ACE ACETYL GROUP
HETNAM MN8 2-(4-CARCOXY-5-ISOPROPYLTHIAZOLYL)BENZOPIPERIDINE
HETNAM MN1 4-CARBOXYPIPERIDINE
HETNAM NH2 AMINO GROUP
FORMUL 2 ACE C2 H4 O
FORMUL 2 MN8 C16 H18 N2 O2 S
FORMUL 2 MN1 C6 H11 N O2
FORMUL 2 NH2 H2 N
HELIX 1 1 SER C 58 TYR C 60 5 3
SHEET 1 A 3 GLN C 52 PRO C 57 0
SHEET 2 A 3 TRP C 42 SER C 47 -1 N SER C 47 O GLN C 52
SHEET 3 A 3 LEU C 32 ASN C 36 -1 N ASN C 36 O LEU C 44
LINK C ACE N 72 N11 MN8 N 73 1555 1555 1.31
LINK C1 MN8 N 73 N1 MN1 N 74 1555 1555 1.32
LINK C MN1 N 74 N PRO N 75 1555 1555 1.31
LINK C PRO N 80 N NH2 N 81 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 - 23 20 Bytes