Header list of 1u2u.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION 20-JUL-04 1U2U
TITLE NMR SOLUTION STRUCTURE OF A DESIGNED HETERODIMERIC LEUCINE ZIPPER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENERAL CONTROL PROTEIN GCN4;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: GENERAL CONTROL PROTEIN GCN4;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHETIC PEPTIDE BASED ON THE SEQUENCE OF THE
SOURCE 4 LEUCINE ZIPPER DOMAIN IN GCN4 (BAKER'S YEAST);
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 OTHER_DETAILS: SYNTHETIC PEPTIDE BASED ON THE SEQUENCE OF THE
SOURCE 8 LEUCINE ZIPPER DOMAIN IN GCN4 (BAKER'S YEAST)
KEYWDS COILED COIL, LEUCINE ZIPPER, INTER-HELICAL ION PAIRING, ELECTROSTATIC
KEYWDS 2 INTERACTIONS, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 27
AUTHOR D.N.MARTI,H.R.BOSSHARD
REVDAT 3 02-MAR-22 1U2U 1 REMARK LINK
REVDAT 2 24-FEB-09 1U2U 1 VERSN
REVDAT 1 05-OCT-04 1U2U 0
JRNL AUTH D.N.MARTI,H.R.BOSSHARD
JRNL TITL INVERSE ELECTROSTATIC EFFECT: ELECTROSTATIC REPULSION IN THE
JRNL TITL 2 UNFOLDED STATE STABILIZES A LEUCINE ZIPPER.
JRNL REF BIOCHEMISTRY V. 43 12436 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15449933
JRNL DOI 10.1021/BI048771T
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.N.MARTI,H.R.BOSSHARD
REMARK 1 TITL ELECTROSTATIC INTERACTIONS IN LEUCINE ZIPPERS: THERMODYNAMIC
REMARK 1 TITL 2 ANALYSIS OF THE CONTRIBUTIONS OF GLU AND HIS RESIDUES AND
REMARK 1 TITL 3 THE EFFECT OF MUTATING SALT BRIDGES
REMARK 1 REF J.MOL.BIOL. V. 330 621 2003
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 12842476
REMARK 1 DOI 10.1016/S0022-2836(03)00623-5
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.N.MARTI,I.JELESAROV,H.R.BOSSHARD
REMARK 1 TITL INTERHELICAL ION PAIRING IN COILED COILS: SOLUTION STRUCTURE
REMARK 1 TITL 2 OF A HETERODIMERIC LEUCINE ZIPPER AND DETERMINATION OF PKA
REMARK 1 TITL 3 VALUES OF GLU SIDE CHAINS
REMARK 1 REF BIOCHEMISTRY V. 39 12804 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 11041845
REMARK 1 DOI 10.1021/BI001242E
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES WERE CALCULATED ON THE BASIS
REMARK 3 OF 1246 NOE DERIVED DISTANCE CONSTRAINTS AND 44 PHI ANGLE
REMARK 3 RESTRAINTS
REMARK 4
REMARK 4 1U2U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023174.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310.00
REMARK 210 PH : 5.7
REMARK 210 IONIC STRENGTH : 10MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.6MM, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY; 2D
REMARK 210 1H-15N HSQC; 2D 1H-13C HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, CNS 1.1, PROCHECK
REMARK 210 3.4.4, WHAT IF 19991018
REMARK 210 METHOD USED : DISTANCE GEOMETRY/
REMARK 210 REGULARIZATION, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210 SIMULATION IN VACUO
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 27
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, LOW
REMARK 210 DEVIATION OF EXPERIMENTAL PKA
REMARK 210 VALUES FROM PKA DERIVED BY
REMARK 210 CONTINUUM ELECTROSTATICS
REMARK 210 CALCULATIONS ON STRUCTURES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 25
REMARK 210
REMARK 210 REMARK: STRUCTURE WAS DETERMINED USING STANDARD 2D NMR 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 B 2 H ALA B 4 0.77
REMARK 500 O LEU B 19 H VAL B 23 1.53
REMARK 500 O LEU A 19 H VAL A 23 1.57
REMARK 500 O VAL B 2 N ALA B 4 1.71
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 GLU A 27 59.35 -90.00
REMARK 500 1 VAL B 2 118.82 -26.46
REMARK 500 1 GLN B 3 28.62 -27.82
REMARK 500 2 VAL B 2 -87.94 -44.38
REMARK 500 2 LEU B 12 -50.09 -120.46
REMARK 500 3 GLN B 3 -69.46 -92.62
REMARK 500 3 HIS B 28 -75.31 -90.02
REMARK 500 4 GLU A 27 58.98 -90.01
REMARK 500 4 GLN B 3 -63.94 -92.27
REMARK 500 5 GLU A 27 46.14 -90.32
REMARK 500 5 VAL B 2 -88.99 -33.12
REMARK 500 5 HIS B 28 -75.48 -70.80
REMARK 500 6 GLU A 6 -75.63 -60.83
REMARK 500 6 GLN A 11 -73.39 -63.90
REMARK 500 6 GLU A 13 -35.37 -39.37
REMARK 500 6 GLU A 27 59.59 -90.20
REMARK 500 6 VAL B 2 -81.38 -38.58
REMARK 500 6 LEU B 12 -79.21 -95.19
REMARK 500 7 VAL B 2 -90.76 -44.27
REMARK 500 7 LYS B 29 51.47 -90.04
REMARK 500 8 LEU A 26 -71.85 -52.86
REMARK 500 8 GLN B 3 -67.88 -91.90
REMARK 500 8 ALA B 4 -14.80 -48.82
REMARK 500 9 LEU A 19 -50.69 -127.15
REMARK 500 9 GLU A 27 50.81 -90.17
REMARK 500 9 GLN B 3 -66.46 -91.72
REMARK 500 9 ALA B 4 -17.90 -48.08
REMARK 500 9 LYS B 20 -30.63 -39.90
REMARK 500 10 VAL B 2 -73.41 -43.63
REMARK 500 11 GLU A 27 52.29 -90.06
REMARK 500 11 VAL B 2 -85.82 -39.64
REMARK 500 12 GLU A 27 51.85 -90.05
REMARK 500 12 VAL B 2 -91.03 -46.54
REMARK 500 13 VAL A 2 -62.45 -29.93
REMARK 500 13 GLU A 27 43.62 -90.34
REMARK 500 13 VAL B 2 -86.96 -37.47
REMARK 500 14 LEU A 26 -76.85 -62.46
REMARK 500 14 VAL B 2 -87.16 -38.72
REMARK 500 15 GLU A 27 52.87 -90.09
REMARK 500 15 VAL B 2 -82.14 -40.08
REMARK 500 15 ASN B 16 -33.51 -38.90
REMARK 500 16 HIS A 28 -91.77 -78.34
REMARK 500 16 VAL B 2 -80.88 -33.02
REMARK 500 16 LYS B 29 108.33 -55.73
REMARK 500 17 GLU A 27 50.39 -90.19
REMARK 500 17 VAL B 2 -17.68 -49.19
REMARK 500 17 GLN B 3 -71.05 -93.94
REMARK 500 17 LYS B 6 -70.55 -89.78
REMARK 500 17 LYS B 20 -31.20 -39.17
REMARK 500 18 GLN A 11 -73.90 -65.24
REMARK 500
REMARK 500 THIS ENTRY HAS 77 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 B 31
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FMH RELATED DB: PDB
REMARK 900 DISULFIDE-LINKED DESIGNED HETERODIMERIC LEUCINE ZIPPER
REMARK 900 RELATED ID: 2ZTA RELATED DB: PDB
REMARK 900 GCN4 HOMODIMERIC LEUCINE ZIPPER
REMARK 900 RELATED ID: 1JUN RELATED DB: PDB
REMARK 900 C-JUN HOMODIMERIC LEUCINE ZIPPER
REMARK 900 RELATED ID: 2A93 RELATED DB: PDB
REMARK 900 C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER
DBREF 1U2U A 0 31 PDB 1U2U 1U2U 0 31
DBREF 1U2U B 0 31 PDB 1U2U 1U2U 0 31
SEQRES 1 A 32 ACE GLU VAL ALA GLN LEU GLU LYS GLU VAL ALA GLN LEU
SEQRES 2 A 32 GLU ALA GLU ASN TYR GLN LEU GLU GLN GLU VAL ALA GLN
SEQRES 3 A 32 LEU GLU HIS GLU GLY NH2
SEQRES 1 B 32 ACE GLU VAL GLN ALA LEU LYS LYS ARG VAL GLN ALA LEU
SEQRES 2 B 32 LYS ALA ARG ASN TYR ALA LEU LYS GLN LYS VAL GLN ALA
SEQRES 3 B 32 LEU ARG HIS LYS GLY NH2
HET ACE A 0 6
HET NH2 A 31 3
HET ACE B 0 6
HET NH2 B 31 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE 2(C2 H4 O)
FORMUL 1 NH2 2(H2 N)
HELIX 1 1 GLU A 1 GLU A 27 1 27
HELIX 2 2 LEU B 5 GLN B 10 1 6
HELIX 3 3 LEU B 12 LYS B 29 1 18
LINK C ACE A 0 N GLU A 1 1555 1555 1.33
LINK C GLY A 30 N NH2 A 31 1555 1555 1.33
LINK C ACE B 0 N GLU B 1 1555 1555 1.34
LINK C GLY B 30 N NH2 B 31 1555 1555 1.33
SITE 1 AC3 2 GLU A 29 GLY A 30
SITE 1 AC4 1 GLY B 30
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
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