Header list of 2bye.pdb file
Complete list - g 9 2 Bytes
HEADER LIPASE 01-AUG-05 2BYE
TITLE NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EPSILON RA 1 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE C, EPSILON 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RA1 DOMAIN, RESIDUES 2006-2114;
COMPND 5 SYNONYM: PHOSPHOLIPASE C EPSILON;
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTRIEX4
KEYWDS PHOSPHOLIPASE C EPSILON, RAS ASSOCIATION DOMAIN, UBIQUITIN SUPERFOLD,
KEYWDS 2 LIPASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.D.BUNNEY,R.HARRIS,N.L.GANDARILLAS,M.B.JOSEPHS,S.M.ROE,H.F.PATERSON,
AUTHOR 2 F.RODRIGUES-LIMA,D.ESPOSITO,P.GIESCHIK,L.H.PEARL,P.C.DRISCOLL,
AUTHOR 3 M.KATAN
REVDAT 5 14-JUN-23 2BYE 1 REMARK
REVDAT 4 15-JAN-20 2BYE 1 REMARK
REVDAT 3 24-JAN-18 2BYE 1 SOURCE
REVDAT 2 24-FEB-09 2BYE 1 VERSN
REVDAT 1 22-FEB-06 2BYE 0
JRNL AUTH T.D.BUNNEY,R.HARRIS,N.L.GANDARILLAS,M.B.JOSEPHS,S.M.ROE,
JRNL AUTH 2 S.C.SORLI,H.F.PATERSON,F.RODRIGUES-LIMA,D.ESPOSITO,
JRNL AUTH 3 C.P.PONTING,P.GIERSCHIK,L.H.PEARL,P.C.DRISCOLL,M.KATAN
JRNL TITL STRUCTURAL AND MECHANISTIC INSIGHTS INTO RAS ASSOCIATION
JRNL TITL 2 DOMAINS OF PHOSPHOLIPASE C EPSILON.
JRNL REF MOL.CELL V. 21 495 2006
JRNL REFN ISSN 1097-2765
JRNL PMID 16483931
JRNL DOI 10.1016/J.MOLCEL.2006.01.008
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH
REMARK 3 AUTHORS : C.D. SCHWIETERS, J.J. KUSZEWSKI, N. TJ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: AB INITIO SIMULATED ANNEALING PROTOCOL
REMARK 3 WITH CARTESIAN MOLECULAR DYNAMICS AND TORSION ANGLE DYNAMICS
REMARK 3 SIMULATED ANNEALING. A FINAL STEP OF RESTRAINED MOLECULAR
REMARK 3 DYNAMICS WITH EXPLICIT INCLUSION OF SOLVENT.
REMARK 4
REMARK 4 2BYE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1290025136.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 275
REMARK 210 PRESSURE : 1.0 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER. 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : C13-NOESY; 15N-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG, CNS, XPLOR-NIH
REMARK 210 METHOD USED : RESTRAINED SIMULATED ANNEALING,
REMARK 210 WATER REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY STRUCTURE WITH NO
REMARK 210 RESTRAINT VIOLATIONS
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 ON 13C, 15N-LABELED PROTEIN.
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 HG13 VAL A 104 HE2 LYS A 106 1.22
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 43 99.82 -36.58
REMARK 500 1 GLU A 45 -12.00 72.53
REMARK 500 1 GLN A 46 -95.36 -68.17
REMARK 500 1 ILE A 48 15.32 55.93
REMARK 500 1 PRO A 50 -161.03 -56.85
REMARK 500 1 THR A 53 -156.49 -110.35
REMARK 500 1 ASP A 54 23.68 -75.87
REMARK 500 1 LYS A 68 -89.47 66.28
REMARK 500 1 CYS A 71 92.07 60.81
REMARK 500 1 GLN A 108 32.43 -78.32
REMARK 500 2 GLU A 3 80.17 -67.17
REMARK 500 2 LYS A 5 -47.80 -174.97
REMARK 500 2 GLN A 46 -97.53 -69.93
REMARK 500 2 ILE A 48 -43.19 96.14
REMARK 500 2 LYS A 49 109.84 -54.08
REMARK 500 2 PRO A 50 -150.39 -76.31
REMARK 500 2 VAL A 51 77.99 -118.41
REMARK 500 2 THR A 53 -151.37 -112.42
REMARK 500 2 ASP A 54 7.40 -60.61
REMARK 500 2 LYS A 66 17.50 -140.17
REMARK 500 2 GLU A 67 -169.08 63.75
REMARK 500 2 LYS A 68 -46.30 72.06
REMARK 500 2 CYS A 71 103.82 -166.40
REMARK 500 2 GLN A 74 88.39 70.72
REMARK 500 2 TRP A 93 -58.14 70.71
REMARK 500 2 GLU A 97 -61.63 -134.00
REMARK 500 3 GLU A 3 91.73 -55.20
REMARK 500 3 ARG A 4 -71.73 -148.97
REMARK 500 3 LYS A 5 35.41 -154.92
REMARK 500 3 GLN A 46 -96.26 -68.79
REMARK 500 3 ILE A 48 -47.79 78.32
REMARK 500 3 PRO A 50 -146.04 -64.14
REMARK 500 3 THR A 53 -148.20 -117.37
REMARK 500 3 ASP A 54 12.15 -62.91
REMARK 500 3 GLU A 67 -164.73 60.80
REMARK 500 3 LYS A 68 -76.31 73.45
REMARK 500 3 GLU A 70 82.71 36.06
REMARK 500 3 TRP A 93 -57.85 71.71
REMARK 500 3 GLU A 97 -167.18 -124.16
REMARK 500 3 GLN A 108 27.56 -77.40
REMARK 500 4 GLU A 2 73.51 63.08
REMARK 500 4 ARG A 4 -75.54 -142.09
REMARK 500 4 LYS A 5 26.21 -149.40
REMARK 500 4 GLN A 46 -86.49 -70.78
REMARK 500 4 ILE A 48 -51.56 74.05
REMARK 500 4 PRO A 50 -147.51 -59.78
REMARK 500 4 THR A 53 -146.73 -119.19
REMARK 500 4 ASP A 54 16.90 -66.21
REMARK 500 4 GLU A 67 -158.24 59.23
REMARK 500 4 LYS A 68 -79.07 74.83
REMARK 500
REMARK 500 THIS ENTRY HAS 283 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BYF RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EPSILON RA 2 DOMAIN
REMARK 900 RELATED ID: 6624 RELATED DB: BMRB
DBREF 2BYE A 1 1 PDB 2BYE 2BYE 1 1
DBREF 2BYE A 2 110 UNP Q5VWL5 Q5VWL5_HUMAN 2006 2114
SEQRES 1 A 110 GLY GLU GLU ARG LYS CYS LEU GLN THR HIS ARG VAL THR
SEQRES 2 A 110 VAL HIS GLY VAL PRO GLY PRO GLU PRO PHE THR VAL PHE
SEQRES 3 A 110 THR ILE ASN GLY GLY THR LYS ALA LYS GLN LEU LEU GLN
SEQRES 4 A 110 GLN ILE LEU THR ASN GLU GLN ASP ILE LYS PRO VAL THR
SEQRES 5 A 110 THR ASP TYR PHE LEU MET GLU GLU LYS TYR PHE ILE SER
SEQRES 6 A 110 LYS GLU LYS ASN GLU CYS ARG LYS GLN PRO PHE GLN ARG
SEQRES 7 A 110 ALA ILE GLY PRO GLU GLU GLU ILE MET GLN ILE LEU SER
SEQRES 8 A 110 SER TRP PHE PRO GLU GLU GLY TYR MET GLY ARG ILE VAL
SEQRES 9 A 110 LEU LYS THR GLN GLN GLU
HELIX 1 1 LYS A 33 THR A 43 1 11
HELIX 2 2 GLU A 85 TRP A 93 1 9
SHEET 1 AA 2 ARG A 11 VAL A 14 0
SHEET 2 AA 2 THR A 24 THR A 27 -1 O THR A 24 N VAL A 14
SHEET 1 AB 3 GLN A 77 ILE A 80 0
SHEET 2 AB 3 TYR A 55 GLU A 60 -1 O LEU A 57 N ILE A 80
SHEET 3 AB 3 ILE A 103 THR A 107 -1 O VAL A 104 N MET A 58
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 - g 9 2 Bytes