Header list of 1fmh.pdb file
Complete list - v 3 2 Bytes
HEADER TRANSCRIPTION 17-AUG-00 1FMH
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 FRAGMENT: LEUCINE ZIPPER ACIDIC CHAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GENERAL CONTROL PROTEIN GCN4;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: LEUCINE ZIPPER BASIC CHAIN;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: 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, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR D.N.MARTI,I.JELESAROV,H.R.BOSSHARD
REVDAT 3 03-NOV-21 1FMH 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1FMH 1 VERSN
REVDAT 1 01-NOV-00 1FMH 0
JRNL AUTH D.N.MARTI,I.JELESAROV,H.R.BOSSHARD
JRNL TITL INTERHELICAL ION PAIRING IN COILED COILS: SOLUTION STRUCTURE
JRNL TITL 2 OF A HETERODIMERIC LEUCINE ZIPPER AND DETERMINATION OF PKA
JRNL TITL 3 VALUES OF GLU SIDE CHAINS.
JRNL REF BIOCHEMISTRY V. 39 12804 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 11041845
JRNL DOI 10.1021/BI001242E
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.JELESAROV,H.R.BOSSHARD
REMARK 1 TITL THERMODYNAMIC CHARACTERIZATION OF THE COUPLED FOLDING AND
REMARK 1 TITL 2 ASSOCIATION OF HETERODIMERIC COILED COILS (LEUCINE ZIPPERS)
REMARK 1 REF J.MOL.BIOL. V. 263 344 1996
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1996.0579
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.DURR,I.JELESAROV,H.R.BOSSHARD
REMARK 1 TITL EXTREMELY FAST FOLDING OF A VERY STABLE LEUCINE ZIPPER WITH
REMARK 1 TITL 2 A STRENGTHENED HYDROPHOBIC CORE AND LACKING ELECTROSTATIC
REMARK 1 TITL 3 INTERACTIONS BETWEEN HELICES
REMARK 1 REF BIOCHEMISTRY V. 38 870 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI981891E
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES WERE CALCULATED ON THE BASIS
REMARK 3 OF 1494 NOE DERIVED DISTANCE CONSTRAINTS AND 52 PHI ANGLE
REMARK 3 RESTRAINTS
REMARK 4
REMARK 4 1FMH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011714.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.65
REMARK 210 IONIC STRENGTH : 10 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.1 MM AB ZIPPER; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, X-PLOR 3.851
REMARK 210 METHOD USED : 1. DISTANCE
REMARK 210 GEOMETRY/REGULARIZATION, 2.
REMARK 210 SIMULATED ANNEALING, 3.
REMARK 210 MOLECULAR DYNAMICS SIMULATION
REMARK 210 INCLUDING 8 ANGSTROMS WATER SHELL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
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 : 14
REMARK 210
REMARK 210 REMARK: STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR
REMARK 210 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 HB3 GLU A 1 HG3 GLN A 4 1.25
REMARK 500 OE2 GLU A 8 HZ3 LYS B 13 1.58
REMARK 500 OE2 GLU A 13 HH21 ARG B 8 1.59
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 CYS A 30 -73.09 -114.91
REMARK 500 1 CYS B 30 46.63 -149.41
REMARK 500 2 CYS B 30 -66.82 -137.04
REMARK 500 3 CYS B 30 -66.52 -147.28
REMARK 500 5 CYS A 30 -70.74 -142.84
REMARK 500 5 CYS B 30 -76.17 -163.54
REMARK 500 6 CYS B 30 -59.27 -137.64
REMARK 500 7 CYS A 30 52.32 -107.71
REMARK 500 8 CYS B 30 -62.37 -140.15
REMARK 500 11 CYS B 30 -73.08 -131.60
REMARK 500 15 CYS B 30 -63.06 -129.13
REMARK 500 16 CYS B 30 49.99 -140.35
REMARK 500 17 CYS B 30 -46.81 -142.01
REMARK 500 21 CYS B 30 -70.63 -155.45
REMARK 500 23 CYS B 30 -63.94 -134.72
REMARK 500 24 CYS B 30 -81.50 -136.33
REMARK 500 25 CYS B 30 -63.25 -136.69
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 32
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 B 32
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZTA RELATED DB: PDB
REMARK 900 2ZTA IS GCN4 HOMODIMERIC LEUCINE ZIPPER
REMARK 900 RELATED ID: 1JUN RELATED DB: PDB
REMARK 900 1JUN IS C-JUN HOMODIMERIC LEUCINE ZIPPER
REMARK 900 RELATED ID: 2A93 RELATED DB: PDB
REMARK 900 2A93 IS C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER
DBREF 1FMH A 1 31 UNP P03069 GCN4_YEAST 249 279
DBREF 1FMH B 1 31 UNP P03069 GCN4_YEAST 249 279
SEQADV 1FMH GLU A 1 UNP P03069 ARG 249 ENGINEERED MUTATION
SEQADV 1FMH VAL A 2 UNP P03069 MET 250 ENGINEERED MUTATION
SEQADV 1FMH ALA A 3 UNP P03069 LYS 251 ENGINEERED MUTATION
SEQADV 1FMH LYS A 7 UNP P03069 ASP 255 ENGINEERED MUTATION
SEQADV 1FMH GLU A 8 UNP P03069 LYS 256 ENGINEERED MUTATION
SEQADV 1FMH ALA A 10 UNP P03069 GLU 258 ENGINEERED MUTATION
SEQADV 1FMH GLN A 11 UNP P03069 GLU 259 ENGINEERED MUTATION
SEQADV 1FMH ALA A 12 UNP P03069 LEU 260 ENGINEERED MUTATION
SEQADV 1FMH GLU A 13 UNP P03069 LEU 261 ENGINEERED MUTATION
SEQADV 1FMH ALA A 14 UNP P03069 SER 262 ENGINEERED MUTATION
SEQADV 1FMH GLU A 15 UNP P03069 LYS 263 ENGINEERED MUTATION
SEQADV 1FMH GLN A 18 UNP P03069 HIS 266 ENGINEERED MUTATION
SEQADV 1FMH GLN A 21 UNP P03069 ASN 269 ENGINEERED MUTATION
SEQADV 1FMH GLN A 25 UNP P03069 ARG 273 ENGINEERED MUTATION
SEQADV 1FMH GLU A 27 UNP P03069 LYS 275 ENGINEERED MUTATION
SEQADV 1FMH HIS A 28 UNP P03069 LYS 276 ENGINEERED MUTATION
SEQADV 1FMH GLU A 29 UNP P03069 LEU 277 ENGINEERED MUTATION
SEQADV 1FMH CYS A 30 UNP P03069 VAL 278 ENGINEERED MUTATION
SEQADV 1FMH GLU B 1 UNP P03069 ARG 249 ENGINEERED MUTATION
SEQADV 1FMH VAL B 2 UNP P03069 MET 250 ENGINEERED MUTATION
SEQADV 1FMH GLN B 3 UNP P03069 LYS 251 ENGINEERED MUTATION
SEQADV 1FMH ALA B 4 UNP P03069 GLN 252 ENGINEERED MUTATION
SEQADV 1FMH LYS B 6 UNP P03069 GLU 254 ENGINEERED MUTATION
SEQADV 1FMH LYS B 7 UNP P03069 ASP 255 ENGINEERED MUTATION
SEQADV 1FMH ARG B 8 UNP P03069 LYS 256 ENGINEERED MUTATION
SEQADV 1FMH GLN B 10 UNP P03069 GLU 258 ENGINEERED MUTATION
SEQADV 1FMH ALA B 11 UNP P03069 GLU 259 ENGINEERED MUTATION
SEQADV 1FMH LYS B 13 UNP P03069 LEU 261 ENGINEERED MUTATION
SEQADV 1FMH ALA B 14 UNP P03069 SER 262 ENGINEERED MUTATION
SEQADV 1FMH ARG B 15 UNP P03069 LYS 263 ENGINEERED MUTATION
SEQADV 1FMH ALA B 18 UNP P03069 HIS 266 ENGINEERED MUTATION
SEQADV 1FMH ALA B 19 UNP P03069 LEU 267 ENGINEERED MUTATION
SEQADV 1FMH LYS B 20 UNP P03069 GLU 268 ENGINEERED MUTATION
SEQADV 1FMH GLN B 21 UNP P03069 ASN 269 ENGINEERED MUTATION
SEQADV 1FMH LYS B 22 UNP P03069 GLU 270 ENGINEERED MUTATION
SEQADV 1FMH GLN B 24 UNP P03069 ALA 272 ENGINEERED MUTATION
SEQADV 1FMH ALA B 25 UNP P03069 ARG 273 ENGINEERED MUTATION
SEQADV 1FMH ARG B 27 UNP P03069 LYS 275 ENGINEERED MUTATION
SEQADV 1FMH HIS B 28 UNP P03069 LYS 276 ENGINEERED MUTATION
SEQADV 1FMH LYS B 29 UNP P03069 LEU 277 ENGINEERED MUTATION
SEQADV 1FMH CYS B 30 UNP P03069 VAL 278 ENGINEERED MUTATION
SEQRES 1 A 33 ACE GLU VAL ALA GLN LEU GLU LYS GLU VAL ALA GLN ALA
SEQRES 2 A 33 GLU ALA GLU ASN TYR GLN LEU GLU GLN GLU VAL ALA GLN
SEQRES 3 A 33 LEU GLU HIS GLU CYS GLY NH2
SEQRES 1 B 33 ACE GLU VAL GLN ALA LEU LYS LYS ARG VAL GLN ALA LEU
SEQRES 2 B 33 LYS ALA ARG ASN TYR ALA ALA LYS GLN LYS VAL GLN ALA
SEQRES 3 B 33 LEU ARG HIS LYS CYS GLY NH2
HET ACE A 0 6
HET NH2 A 32 3
HET ACE B 0 6
HET NH2 B 32 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 CYS A 30 1 30
HELIX 2 2 GLU B 1 GLY B 31 1 31
SSBOND 1 CYS A 30 CYS B 30 1555 1555 2.03
LINK C ACE A 0 N GLU A 1 1555 1555 1.33
LINK C GLY A 31 N NH2 A 32 1555 1555 1.33
LINK C ACE B 0 N GLU B 1 1555 1555 1.32
LINK C GLY B 31 N NH2 B 32 1555 1555 1.33
SITE 1 AC3 2 CYS A 30 GLY A 31
SITE 1 AC4 2 CYS B 30 GLY B 31
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 - v 3 2 Bytes