Header list of 1p68.pdb file
Complete list - b 23 2 Bytes
HEADER DE NOVO PROTEIN 29-APR-03 1P68
TITLE SOLUTION STRUCTURE OF S-824, A DE NOVO DESIGNED FOUR HELIX BUNDLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DE NOVO DESIGNED PROTEIN S-824;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS PROTEIN, FOUR HELIX BUNDLE, DE NOVO DESIGN, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR Y.WEI,S.KIM,D.FELA,J.BAUM,M.H.HECHT
REVDAT 3 23-FEB-22 1P68 1 REMARK
REVDAT 2 24-FEB-09 1P68 1 VERSN
REVDAT 1 11-NOV-03 1P68 0
JRNL AUTH Y.WEI,S.KIM,D.FELA,J.BAUM,M.H.HECHT
JRNL TITL SOLUTION STRUCTURE OF A DE NOVO PROTEIN FROM A DESIGNED
JRNL TITL 2 COMBINATORIAL LIBRARY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 13270 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 14593201
JRNL DOI 10.1073/PNAS.1835644100
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P68 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000019058.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : 50MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 50MM ACETATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR TECHNIQUES.
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 VAL A 82 H GLU A 86 1.36
REMARK 500 O ILE A 85 H ILE A 89 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 ASN A 22 19.93 -152.97
REMARK 500 1 HIS A 24 -52.42 -178.44
REMARK 500 1 HIS A 74 34.51 -155.38
REMARK 500 1 LEU A 75 90.34 -51.23
REMARK 500 1 GLN A 76 68.30 -65.64
REMARK 500 1 THR A 81 -74.16 -69.03
REMARK 500 2 TYR A 2 40.88 -96.96
REMARK 500 2 ASN A 22 10.84 -146.50
REMARK 500 2 HIS A 24 -51.78 -179.13
REMARK 500 2 VAL A 33 -60.25 -90.01
REMARK 500 2 HIS A 74 32.31 -154.97
REMARK 500 2 LEU A 75 88.31 -52.67
REMARK 500 2 GLN A 76 69.70 -67.97
REMARK 500 2 THR A 81 -74.41 -67.45
REMARK 500 2 LEU A 99 -67.20 -96.10
REMARK 500 3 HIS A 24 58.67 179.56
REMARK 500 3 HIS A 74 28.72 -153.82
REMARK 500 3 LEU A 75 85.30 -49.38
REMARK 500 3 THR A 81 -74.23 -69.93
REMARK 500 4 HIS A 24 47.18 179.04
REMARK 500 4 HIS A 74 26.97 -147.19
REMARK 500 4 LEU A 75 91.95 -49.50
REMARK 500 4 GLN A 76 68.23 -64.54
REMARK 500 4 THR A 81 -74.64 -69.69
REMARK 500 5 ASN A 22 12.63 -146.01
REMARK 500 5 HIS A 24 -51.18 -178.32
REMARK 500 5 HIS A 74 30.08 -156.33
REMARK 500 5 LEU A 75 85.25 -50.70
REMARK 500 5 THR A 81 -73.26 -68.67
REMARK 500 5 LEU A 99 -63.02 -100.81
REMARK 500 5 HIS A 101 33.63 -96.59
REMARK 500 6 HIS A 24 -52.65 -175.97
REMARK 500 6 HIS A 74 36.49 -150.92
REMARK 500 6 LEU A 75 85.35 -67.46
REMARK 500 6 GLN A 76 65.75 -68.03
REMARK 500 7 HIS A 24 -48.66 -175.20
REMARK 500 7 HIS A 74 32.71 -152.15
REMARK 500 7 LEU A 75 83.28 -54.65
REMARK 500 7 THR A 81 -74.40 -69.93
REMARK 500 8 ASN A 22 -20.12 -145.41
REMARK 500 8 HIS A 24 -53.13 -178.86
REMARK 500 8 SER A 53 -168.32 -64.59
REMARK 500 8 LEU A 75 92.08 -51.92
REMARK 500 8 GLN A 76 69.14 -64.30
REMARK 500 8 THR A 81 -74.56 -68.02
REMARK 500 9 TYR A 2 54.61 -99.32
REMARK 500 9 HIS A 24 57.60 179.39
REMARK 500 9 HIS A 74 32.03 -150.90
REMARK 500 9 LEU A 75 82.76 -50.27
REMARK 500 9 THR A 81 -74.15 -69.55
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5687 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGNMENT OF S-824
DBREF 1P68 A 1 102 PDB 1P68 1P68 1 102
SEQRES 1 A 102 MET TYR GLY LYS LEU ASN ASP LEU LEU GLU ASP LEU GLN
SEQRES 2 A 102 GLU VAL LEU LYS ASN LEU HIS LYS ASN TRP HIS GLY GLY
SEQRES 3 A 102 LYS ASP ASN LEU HIS ASP VAL ASP ASN HIS LEU GLN ASN
SEQRES 4 A 102 VAL ILE GLU ASP ILE HIS ASP PHE MET GLN GLY GLY GLY
SEQRES 5 A 102 SER GLY GLY LYS LEU GLN GLU MET MET LYS GLU PHE GLN
SEQRES 6 A 102 GLN VAL LEU ASP GLU LEU ASN ASN HIS LEU GLN GLY GLY
SEQRES 7 A 102 LYS HIS THR VAL HIS HIS ILE GLU GLN ASN ILE LYS GLU
SEQRES 8 A 102 ILE PHE HIS HIS LEU GLU GLU LEU VAL HIS ARG
HELIX 1 1 LYS A 4 LYS A 21 1 18
HELIX 2 2 LEU A 30 ASP A 46 1 17
HELIX 3 3 GLY A 55 MET A 60 1 6
HELIX 4 4 MET A 60 ASN A 73 1 14
HELIX 5 5 GLY A 78 LYS A 90 1 13
HELIX 6 6 GLU A 91 HIS A 101 1 11
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