Header list of 1n3k.pdb file
Complete list - b 23 2 Bytes
HEADER APOPTOSIS 28-OCT-02 1N3K
TITLE SOLUTION STRUCTURE OF PHOSPHOPROTEIN ENRICHED IN ASTROCYTES 15 KDA
TITLE 2 (PEA-15)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASTROCYTIC PHOSPHOPROTEIN PEA-15;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHOSPHOPROTEIN ENRICHED IN ASTROCYTES 15 KDA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS;
SOURCE 3 ORGANISM_COMMON: CHINESE HAMSTER;
SOURCE 4 ORGANISM_TAXID: 10029;
SOURCE 5 GENE: PEA15;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE-9
KEYWDS DEATH EFFECTOR DOMAIN, SIX HELIX BUNDLE, APOPTOSIS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.M.HILL,H.VAIDYANATHAN,J.W.RAMOS,M.H.GINSBERG,M.H.WERNER
REVDAT 3 23-FEB-22 1N3K 1 REMARK
REVDAT 2 24-FEB-09 1N3K 1 VERSN
REVDAT 1 14-JAN-03 1N3K 0
JRNL AUTH J.M.HILL,H.VAIDYANATHAN,J.W.RAMOS,M.H.GINSBERG,M.H.WERNER
JRNL TITL RECOGNITION OF ERK MAP KINASE BY PEA-15 REVEALS A COMMON
JRNL TITL 2 DOCKING SITE WITHIN THE DEATH DOMAIN AND DEATH EFFECTOR
JRNL TITL 3 DOMAIN
JRNL REF EMBO J. V. 21 6494 2002
JRNL REFN ISSN 0261-4189
JRNL PMID 12456656
JRNL DOI 10.1093/EMBOJ/CDF641
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843, X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2937 NMR-DERIVED RESTRAINTS, INCLUDING 2522 NOES, 308 DIHEDRAL
REMARK 3 ANGLE RESTRAINTS (121 PHI, 95 PSI, 84 CHI1 AND 8 CHI2) AND 107
REMARK 3 3J(NH-HA) COUPLING CONSTANTS
REMARK 4
REMARK 4 1N3K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017474.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 10MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN U-15N,13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : VARIOUS DOUBLE AND TRIPLE
REMARK 210 RESONANCE EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
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: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O CYS A 27 H ILE A 31 1.55
REMARK 500 O GLU A 21 HG SER A 25 1.56
REMARK 500 O PHE A 46 H GLU A 50 1.57
REMARK 500 O TRP A 45 H LEU A 49 1.57
REMARK 500 O THR A 77 H ASP A 81 1.58
REMARK 500 O LEU A 20 H LYS A 24 1.59
REMARK 500 O VAL A 86 H SER A 90 1.60
REMARK 500
REMARK 500 REMARK: NULL
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 THR A 100 -83.88 -97.60
REMARK 500 1 ALA A 105 -59.34 -146.88
REMARK 500 1 PRO A 125 75.71 -103.46
REMARK 500 1 PRO A 127 40.22 -83.19
REMARK 500 2 ASN A 53 34.91 -92.35
REMARK 500 2 ASP A 93 -72.66 -108.97
REMARK 500 2 LEU A 95 -74.05 -78.98
REMARK 500 2 THR A 100 -86.42 -97.31
REMARK 500 2 LEU A 123 -70.92 -86.21
REMARK 500 2 PRO A 125 71.93 -102.71
REMARK 500 3 ASN A 53 36.68 -95.10
REMARK 500 3 GLU A 91 91.80 -68.38
REMARK 500 3 THR A 100 -118.76 -92.31
REMARK 500 3 ILE A 102 77.46 -118.17
REMARK 500 3 ALA A 105 -63.77 -146.79
REMARK 500 3 PRO A 125 70.18 -102.30
REMARK 500 4 ASN A 53 34.45 -93.31
REMARK 500 4 GLU A 91 96.00 -68.89
REMARK 500 4 THR A 100 -113.49 -84.46
REMARK 500 4 ALA A 105 -56.94 -141.59
REMARK 500 4 ARG A 113 38.59 -94.21
REMARK 500 4 PRO A 125 72.71 -102.31
REMARK 500 5 ASN A 53 35.29 -92.36
REMARK 500 5 GLU A 91 86.03 -68.97
REMARK 500 5 ASP A 93 -80.69 -110.94
REMARK 500 5 THR A 100 -85.79 -89.12
REMARK 500 5 ILE A 102 59.40 -148.19
REMARK 500 5 ALA A 105 -66.84 -146.63
REMARK 500 5 TYR A 108 150.05 -49.62
REMARK 500 6 ASN A 53 35.60 -92.98
REMARK 500 6 GLU A 91 88.34 -69.05
REMARK 500 6 ASP A 96 43.61 -92.18
REMARK 500 6 THR A 100 -119.00 -83.54
REMARK 500 6 ALA A 105 -60.38 -145.71
REMARK 500 7 ASN A 53 30.35 -92.20
REMARK 500 7 THR A 100 -83.37 -95.61
REMARK 500 7 ALA A 105 -59.91 -134.20
REMARK 500 8 ASN A 53 33.53 -91.83
REMARK 500 8 THR A 100 -86.38 -94.46
REMARK 500 8 PRO A 125 74.01 -102.27
REMARK 500 9 ASN A 53 33.00 -92.04
REMARK 500 9 GLU A 91 89.73 -69.62
REMARK 500 9 LEU A 95 -76.36 -73.11
REMARK 500 9 THR A 100 -88.69 -97.97
REMARK 500 9 PRO A 125 67.28 -103.63
REMARK 500 10 ASN A 53 34.61 -93.15
REMARK 500 10 GLU A 91 88.27 -69.39
REMARK 500 10 ASP A 93 -81.77 -95.99
REMARK 500 10 THR A 100 -89.45 -97.74
REMARK 500 10 ALA A 105 -61.72 -138.37
REMARK 500
REMARK 500 THIS ENTRY HAS 93 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1N3K A 1 130 UNP Q9Z297 PEA15_CRIGR 1 130
SEQRES 1 A 130 MET ALA GLU TYR GLY THR LEU LEU GLN ASP LEU THR ASN
SEQRES 2 A 130 ASN ILE THR LEU GLU ASP LEU GLU GLN LEU LYS SER ALA
SEQRES 3 A 130 CYS LYS GLU ASP ILE PRO SER GLU LYS SER GLU GLU ILE
SEQRES 4 A 130 THR THR GLY SER ALA TRP PHE SER PHE LEU GLU SER HIS
SEQRES 5 A 130 ASN LYS LEU ASP LYS ASP ASN LEU SER TYR ILE GLU HIS
SEQRES 6 A 130 ILE PHE GLU ILE SER ARG ARG PRO ASP LEU LEU THR MET
SEQRES 7 A 130 VAL VAL ASP TYR ARG THR ARG VAL LEU LYS ILE SER GLU
SEQRES 8 A 130 GLU ASP GLU LEU ASP THR LYS LEU THR ARG ILE PRO SER
SEQRES 9 A 130 ALA LYS LYS TYR LYS ASP ILE ILE ARG GLN PRO SER GLU
SEQRES 10 A 130 GLU GLU ILE ILE LYS LEU ALA PRO PRO PRO LYS LYS ALA
HELIX 1 1 MET A 1 ILE A 15 1 15
HELIX 2 2 THR A 16 LYS A 28 1 13
HELIX 3 3 PRO A 32 GLU A 37 1 6
HELIX 4 4 THR A 41 HIS A 52 1 12
HELIX 5 5 LEU A 60 SER A 70 1 11
HELIX 6 6 ARG A 72 SER A 90 1 19
HELIX 7 7 GLU A 119 ALA A 124 5 6
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