Header list of 1kfz.pdb file
Complete list - t 27 2 Bytes
HEADER SIGNALING PROTEIN 24-NOV-01 1KFZ
TITLE SOLUTION STRUCTURE OF C-TERMINAL SEM-5 SH3 DOMAIN (ENSEMBLE OF 16
TITLE 2 STRUCTURES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEX MUSCLE ABNORMAL PROTEIN 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL SH3 DOMAIN (RESIDUES 155-214);
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;
SOURCE 3 ORGANISM_TAXID: 6239;
SOURCE 4 GENE: SEM-5;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET19B
KEYWDS ALL BETA PROTEIN, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR J.C.FERREON,D.E.VOLK,B.A.LUXON,D.GORENSTEIN,V.J.HILSER
REVDAT 4 27-OCT-21 1KFZ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1KFZ 1 VERSN
REVDAT 2 04-NOV-03 1KFZ 3 ATOM
REVDAT 1 20-MAY-03 1KFZ 0
JRNL AUTH J.C.FERREON,D.E.VOLK,B.A.LUXON,D.GORENSTEIN,V.J.HILSER
JRNL TITL SOLUTION STRUCTURE, DYNAMICS AND THERMODYNAMICS OF THE
JRNL TITL 2 NATIVE STATE ENSEMBLE OF SEM-5 C-TERMINAL SH3 DOMAIN
JRNL REF BIOCHEMISTRY V. 42 5582 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12741814
JRNL DOI 10.1021/BI030005J
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX V.98, CNS 1.0
REMARK 3 AUTHORS : MSI (FELIX), BRUNGER, ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KFZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014916.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.8
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM SEM-5 SH3 DOMAIN, BOTH 15N,
REMARK 210 AND 15N,13C LABELED, 50 MM
REMARK 210 SODIUM ACETATE BUFFER, 10 MM
REMARK 210 CACL2, 100 MM NACL, PH 4.8, 90%
REMARK 210 H2O, 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-NOESY-HSQC; 3D 13C-NOESY
REMARK 210 -HSQC; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 1.0, CNS 1.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
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 : 2
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: 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 PHE A 163 140.20 -170.12
REMARK 500 1 LYS A 176 -168.95 -115.65
REMARK 500 1 ASN A 185 -171.73 -175.16
REMARK 500 1 LYS A 186 51.84 -151.39
REMARK 500 1 ASN A 198 -67.70 170.94
REMARK 500 1 TYR A 211 -62.59 -106.26
REMARK 500 1 SER A 213 178.17 -54.96
REMARK 500 2 MET A 154 -77.51 -133.48
REMARK 500 2 PHE A 163 139.49 -170.16
REMARK 500 2 ASN A 166 78.43 -109.92
REMARK 500 2 LYS A 176 -168.19 -116.15
REMARK 500 2 VAL A 180 93.46 -69.59
REMARK 500 2 ASN A 197 64.86 66.03
REMARK 500 2 ASN A 198 11.81 82.69
REMARK 500 2 TYR A 211 -68.59 -101.45
REMARK 500 3 MET A 154 -80.59 62.60
REMARK 500 3 VAL A 180 96.07 -69.68
REMARK 500 3 ASN A 197 -62.60 76.23
REMARK 500 3 ASN A 198 29.62 -164.61
REMARK 500 3 PRO A 204 108.67 -59.82
REMARK 500 3 TYR A 211 -65.67 -98.88
REMARK 500 3 ASN A 212 74.47 61.77
REMARK 500 4 MET A 154 117.98 62.24
REMARK 500 4 PHE A 163 140.24 -170.28
REMARK 500 4 LEU A 196 59.53 -116.96
REMARK 500 4 ASN A 197 65.98 67.93
REMARK 500 4 ASN A 198 10.85 83.30
REMARK 500 4 ALA A 209 114.65 -161.49
REMARK 500 4 TYR A 211 -68.71 -99.94
REMARK 500 4 ASN A 212 74.58 61.75
REMARK 500 5 MET A 154 -77.26 -85.38
REMARK 500 5 ASN A 166 78.59 -109.67
REMARK 500 5 VAL A 180 94.70 -69.70
REMARK 500 5 ASN A 185 174.65 179.75
REMARK 500 5 ASN A 197 -60.03 76.59
REMARK 500 5 ASN A 198 -40.38 -143.08
REMARK 500 5 PHE A 203 149.45 -170.09
REMARK 500 5 ALA A 209 111.98 -163.24
REMARK 500 5 TYR A 211 -66.15 -93.25
REMARK 500 5 SER A 213 80.61 -64.77
REMARK 500 6 PHE A 163 -164.23 -170.05
REMARK 500 6 ASN A 197 -59.87 76.61
REMARK 500 6 ASN A 198 -38.76 -150.29
REMARK 500 6 TYR A 211 -68.82 -96.35
REMARK 500 6 ASN A 212 74.61 61.73
REMARK 500 7 GLU A 155 112.84 -166.08
REMARK 500 7 PHE A 163 140.16 -170.25
REMARK 500 7 LEU A 196 86.04 -69.99
REMARK 500 7 ASN A 197 -59.73 77.68
REMARK 500 7 ASN A 198 -39.82 -146.33
REMARK 500
REMARK 500 THIS ENTRY HAS 128 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K76 RELATED DB: PDB
REMARK 900 1K76 IS THE SOLUTION STRUCTURE OF C-TERMINAL SEM-5 SH3 DOMAIN
REMARK 900 (MINIMIZED AVERAGE STRUCTURE).
DBREF 1KFZ A 155 214 UNP P29355 SEM5_CAEEL 155 214
SEQADV 1KFZ HIS A 153 UNP P29355 CLONING ARTIFACT
SEQADV 1KFZ MET A 154 UNP P29355 CLONING ARTIFACT
SEQADV 1KFZ ALA A 209 UNP P29355 CYS 209 ENGINEERED MUTATION
SEQRES 1 A 62 HIS MET GLU THR LYS PHE VAL GLN ALA LEU PHE ASP PHE
SEQRES 2 A 62 ASN PRO GLN GLU SER GLY GLU LEU ALA PHE LYS ARG GLY
SEQRES 3 A 62 ASP VAL ILE THR LEU ILE ASN LYS ASP ASP PRO ASN TRP
SEQRES 4 A 62 TRP GLU GLY GLN LEU ASN ASN ARG ARG GLY ILE PHE PRO
SEQRES 5 A 62 SER ASN TYR VAL ALA PRO TYR ASN SER ASN
SHEET 1 A 5 ARG A 199 PRO A 204 0
SHEET 2 A 5 TRP A 191 LEU A 196 -1 N TRP A 192 O PHE A 203
SHEET 3 A 5 VAL A 180 ASN A 185 -1 N THR A 182 O GLN A 195
SHEET 4 A 5 LYS A 157 ALA A 161 -1 N VAL A 159 O ILE A 181
SHEET 5 A 5 VAL A 208 PRO A 210 -1 O ALA A 209 N GLN A 160
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 - t 27 2 Bytes