Header list of 1w4m.pdb file
Complete list - r 25 2 Bytes
HEADER SIGNAL TRANSDUCTION 26-JUL-04 1W4M
TITLE STRUCTURE OF THE HUMAN PLECKSTRIN DEP DOMAIN BY
TITLE 2 MULTIDIMENSIONAL NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLECKSTRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HUMAN DEP DOMAIN, RESIDUES 121-223;
COMPND 5 SYNONYM: HUMAN PLECKSTRIN DEP DOMAIN, PLATELET P47 PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET9D, PETM30
KEYWDS SIGNAL TRANSDUCTION, DEP DOMAIN, HUMAN PLECKSTRIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR C.CIVERA,B.SIMON,G.STIER,M.SATTLER,M.J.MACIAS
REVDAT 3 24-FEB-09 1W4M 1 VERSN
REVDAT 2 04-MAY-05 1W4M 1 JRNL
REVDAT 1 15-DEC-04 1W4M 0
JRNL AUTH C.CIVERA,B.SIMON,G.STIER,M.SATTLER,M.J.MACIAS
JRNL TITL STRUCTURE AND DYNAMICS OF THE HUMAN PLECKSTRIN DEP
JRNL TITL 2 DOMAIN: DISTINCT MOLECULAR FEATURES OF A NOVEL DEP
JRNL TITL 3 DOMAIN SUBFAMILY
JRNL REF PROTEINS: STRUCT.,FUNCT., V. 58 354 2005
JRNL REF 2 GENET.
JRNL REFN ISSN 0887-3585
JRNL PMID 15573383
JRNL DOI 10.1002/PROT.20320
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,
REMARK 3 RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1W4M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUL-04.
REMARK 100 THE PDBE ID CODE IS EBI-20067.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295.0
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 30MM
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 20MM PHOSPHATE BUFFER,
REMARK 210 30MM NACL, 3MM
REMARK 210 DITHIOTHREITOL (DTT), 0.
REMARK 210 03% (W/V) NAN3 IN 90% H2O
REMARK 210 / 10% D2O OR 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D HOMONUCLEAR TOCSY AND
REMARK 210 NOESY , 1H-15N-HSQC, HNCA,
REMARK 210 CBCANH, CBCACONH, HNCO,
REMARK 210 HCCCONH, CCONH, HCCH-TOCSY,
REMARK 210 HBHACONH, HBCBCCDHD,
REMARK 210 HBCBCCDCEHE3D , 13C-EDITED
REMARK 210 TOCSY, 1H-15N-HNHA , IPAP
REMARK 210 1H-15N-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA CNS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NONE
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO A 1
REMARK 465 GLU A 2
REMARK 465 THR A 3
REMARK 465 ILE A 4
REMARK 465 PRO A 100
REMARK 465 ASP A 101
REMARK 465 SER A 102
REMARK 465 GLY A 103
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 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 ASP A 15 -169.43 -66.91
REMARK 500 1 THR A 16 -87.37 -82.64
REMARK 500 1 ILE A 20 -176.13 -65.00
REMARK 500 1 GLU A 22 103.32 -57.52
REMARK 500 1 LYS A 27 -86.93 -128.50
REMARK 500 1 ARG A 52 -57.05 -123.89
REMARK 500 1 ASP A 91 40.62 -86.11
REMARK 500 2 ASP A 15 -173.79 -60.77
REMARK 500 2 THR A 16 -86.83 -85.52
REMARK 500 2 GLU A 22 105.16 -54.79
REMARK 500 2 LYS A 27 -92.71 -88.46
REMARK 500 2 ASP A 28 -67.45 -120.17
REMARK 500 2 ARG A 52 -54.92 -125.92
REMARK 500 2 PRO A 72 105.81 -59.94
REMARK 500 2 ALA A 85 34.96 -90.44
REMARK 500 2 ASP A 91 43.10 -85.32
REMARK 500 3 ASP A 15 -174.76 -63.56
REMARK 500 3 THR A 16 -85.05 -85.61
REMARK 500 3 ILE A 20 -179.19 -62.66
REMARK 500 3 GLU A 22 101.19 -50.92
REMARK 500 3 LYS A 27 -82.34 -109.57
REMARK 500 3 ASN A 48 -157.97 -115.53
REMARK 500 3 ARG A 52 -55.83 -124.82
REMARK 500 3 ASP A 91 37.16 -97.74
REMARK 500 4 ASP A 15 -178.34 -63.26
REMARK 500 4 THR A 16 -82.60 -85.06
REMARK 500 4 ILE A 20 -177.40 -65.96
REMARK 500 4 GLU A 22 105.13 -56.14
REMARK 500 4 LYS A 27 -128.20 -103.78
REMARK 500 4 ASP A 28 -72.01 -84.51
REMARK 500 4 ASN A 48 -162.49 -113.44
REMARK 500 4 ARG A 52 -55.00 -129.53
REMARK 500 4 ALA A 85 40.01 -92.75
REMARK 500 4 PRO A 88 -77.96 -67.25
REMARK 500 4 ASP A 91 36.92 -90.15
REMARK 500 5 ASP A 15 -171.20 -66.63
REMARK 500 5 THR A 16 -86.72 -83.79
REMARK 500 5 ILE A 20 -169.14 -66.52
REMARK 500 5 LYS A 21 -155.22 -79.45
REMARK 500 5 GLU A 22 93.99 -168.94
REMARK 500 5 LYS A 27 -165.00 -127.35
REMARK 500 5 ASN A 48 -163.03 -104.31
REMARK 500 5 SER A 50 -70.48 -70.37
REMARK 500 5 ARG A 52 -56.84 -125.24
REMARK 500 5 PRO A 72 150.80 -48.08
REMARK 500 5 ALA A 85 55.32 -111.17
REMARK 500 5 PRO A 88 42.43 -96.43
REMARK 500 5 ASP A 91 39.51 -86.72
REMARK 500 6 ASP A 15 -170.92 -66.69
REMARK 500 6 THR A 16 -85.56 -88.71
REMARK 500 6 ILE A 20 -169.07 -66.82
REMARK 500 6 LYS A 21 -153.83 -80.41
REMARK 500 6 GLU A 22 82.53 -169.97
REMARK 500 6 LYS A 27 -88.57 -78.48
REMARK 500 6 ASP A 28 -54.10 -120.24
REMARK 500 6 ARG A 52 -55.01 -122.57
REMARK 500 7 ASP A 15 -174.84 -64.35
REMARK 500 7 THR A 16 -87.63 -84.03
REMARK 500 7 ILE A 20 34.46 -78.14
REMARK 500 7 LYS A 21 95.45 49.54
REMARK 500 7 LYS A 27 -143.89 -77.25
REMARK 500 7 ASN A 48 -157.71 -94.88
REMARK 500 7 ARG A 52 -54.61 -129.90
REMARK 500 7 ASP A 91 33.55 -87.34
REMARK 500 8 ASP A 15 -173.25 -61.78
REMARK 500 8 THR A 16 -84.56 -87.94
REMARK 500 8 ILE A 20 -177.71 -62.37
REMARK 500 8 GLU A 22 107.72 -50.26
REMARK 500 8 LYS A 27 -85.31 -118.82
REMARK 500 8 ASP A 28 -70.53 -109.09
REMARK 500 8 ASN A 48 -169.36 -100.49
REMARK 500 8 ARG A 52 -56.78 -126.36
REMARK 500 9 ASP A 15 -170.69 -66.56
REMARK 500 9 THR A 16 -87.25 -89.97
REMARK 500 9 ILE A 20 -175.24 -69.84
REMARK 500 9 GLU A 22 104.93 -55.03
REMARK 500 9 LYS A 27 -81.90 -95.04
REMARK 500 9 ASP A 28 -62.74 -120.09
REMARK 500 9 ARG A 52 -55.36 -122.12
REMARK 500 10 ASN A 24 98.53 -63.41
REMARK 500 10 LYS A 27 -87.53 -113.29
REMARK 500 10 ASP A 28 -73.41 -112.01
REMARK 500 10 ASN A 33 98.18 -68.14
REMARK 500 10 HIS A 34 75.99 60.03
REMARK 500 10 ARG A 52 -55.87 -120.59
REMARK 500 10 ALA A 85 30.06 -81.86
REMARK 500 10 ASP A 91 30.71 -86.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PLS RELATED DB: PDB
REMARK 900 PLECKSTRIN (N-TERMINAL PLECKSTRIN HOMOLOGY
REMARK 900 DOMAIN) MUTANT WITH LEU GLU (HIS)6 ADDED
REMARK 900 TO THE C TERMINUS (INS(G105-LEHHHHHH))
REMARK 900 (NMR, 25 STRUCTURES)
DBREF 1W4M A 1 103 UNP P08567 PLEK_HUMAN 121 223
SEQRES 1 A 103 PRO GLU THR ILE ASP LEU GLY ALA LEU TYR LEU SER MET
SEQRES 2 A 103 LYS ASP THR GLU LYS GLY ILE LYS GLU LEU ASN LEU GLU
SEQRES 3 A 103 LYS ASP LYS LYS ILE PHE ASN HIS CYS PHE THR GLY ASN
SEQRES 4 A 103 CYS VAL ILE ASP TRP LEU VAL SER ASN GLN SER VAL ARG
SEQRES 5 A 103 ASN ARG GLN GLU GLY LEU MET ILE ALA SER SER LEU LEU
SEQRES 6 A 103 ASN GLU GLY TYR LEU GLN PRO ALA GLY ASP MET SER LYS
SEQRES 7 A 103 SER ALA VAL ASP GLY THR ALA GLU ASN PRO PHE LEU ASP
SEQRES 8 A 103 ASN PRO ASP ALA PHE TYR TYR PHE PRO ASP SER GLY
HELIX 1 1 ASP A 5 LYS A 14 1 10
HELIX 2 2 GLY A 38 ASN A 48 1 11
HELIX 3 3 ASN A 53 GLY A 68 1 16
HELIX 4 4 GLY A 74 VAL A 81 1 8
SHEET 1 AA 2 LEU A 25 GLU A 26 0
SHEET 2 AA 2 ILE A 31 PHE A 32 -1 O PHE A 32 N LEU A 25
SHEET 1 AB 3 CYS A 35 THR A 37 0
SHEET 2 AB 3 PHE A 96 TYR A 98 -1 O TYR A 97 N PHE A 36
SHEET 3 AB 3 GLN A 71 ALA A 73 -1 O GLN A 71 N TYR A 98
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 - r 25 2 Bytes