Header list of 1m36.pdb file
Complete list - 23 20 Bytes
HEADER DNA BINDING PROTEIN 27-JUN-02 1M36
TITLE SOLUTION STRUCTURE OF A CCHC ZINC FINGER FROM MOZ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOCYTIC LEUKEMIA ZINC FINGER PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 3-33;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MOZ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS ZINC FINGER, ACETYL TRANSFERASE, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.H.Y.KWAN,D.A.GELL,C.K.LIEW,J.P.MACKAY
REVDAT 3 23-FEB-22 1M36 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1M36 1 VERSN
REVDAT 1 27-JAN-04 1M36 0
JRNL AUTH A.H.Y.KWAN,D.A.GELL,C.K.LIEW,J.P.MACKAY
JRNL TITL SOLUTION STRUCTURE OF A CCHC ZINC FINGER FROM MOZ
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, DYANA 1.5
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT ET AL (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE CALCULATIONS WERE PERFORMED
REMARK 3 USING THE PACKAGE ARIA 1.1 (AMBIGUOUS RESTRAINTS IN ITERATIVE
REMARK 3 ASSIGNMENT). FINAL STRUCTURES ARE BASED ON 832 UNAMBIGUOUS NOE-
REMARK 3 DERIVED DISTANCE CONSTRAINTS, 1 SET OF AMBIGUOUS NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS AND 19 ADDITIONAL DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1M36 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016539.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM MOZ PROTEIN (533-563), 1MM
REMARK 210 TCEP, 0.7MM ZNSO4, 95% H2O, 5%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
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 : XEASY 1.3.13, ARIA 1.1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D NMR
REMARK 210 HOMONUCLEAR 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
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 LEU A 14 72.29 62.94
REMARK 500 2 ARG A 3 -80.15 -170.56
REMARK 500 2 LEU A 7 -145.59 -82.31
REMARK 500 2 CYS A 10 -156.33 -73.65
REMARK 500 2 LEU A 14 74.33 57.42
REMARK 500 3 LEU A 14 67.18 69.15
REMARK 500 4 LEU A 7 -154.03 -83.88
REMARK 500 5 PRO A 5 -178.04 -68.74
REMARK 500 5 LEU A 7 -144.52 -103.58
REMARK 500 6 SER A 2 43.92 -89.49
REMARK 500 6 PRO A 5 -73.97 -67.20
REMARK 500 6 GLU A 11 -7.64 75.31
REMARK 500 7 LEU A 7 -153.15 -86.31
REMARK 500 7 GLU A 11 -4.95 73.75
REMARK 500 7 CYS A 30 36.12 -84.36
REMARK 500 8 PRO A 5 -153.32 -87.72
REMARK 500 9 LEU A 7 -148.61 -76.54
REMARK 500 9 TRP A 32 -72.37 -81.78
REMARK 500 10 LEU A 4 135.07 71.49
REMARK 500 10 LEU A 7 -149.95 -122.32
REMARK 500 11 PRO A 5 -77.55 -69.08
REMARK 500 11 LEU A 7 -149.24 -84.84
REMARK 500 12 PRO A 5 -92.11 -75.64
REMARK 500 12 LEU A 7 -156.31 -135.88
REMARK 500 12 TRP A 32 -156.17 -105.36
REMARK 500 13 PRO A 5 -87.46 -62.91
REMARK 500 13 LEU A 7 -136.33 -140.47
REMARK 500 13 GLU A 11 -20.76 80.15
REMARK 500 13 TRP A 32 -69.95 -99.63
REMARK 500 14 ARG A 3 -83.39 -93.58
REMARK 500 14 LEU A 7 -171.70 -68.97
REMARK 500 14 GLU A 11 -1.36 70.61
REMARK 500 14 LYS A 28 -23.94 73.40
REMARK 500 14 CYS A 30 100.56 -54.86
REMARK 500 14 TRP A 32 -85.34 -95.74
REMARK 500 15 LEU A 4 155.60 70.12
REMARK 500 15 LEU A 7 -164.70 64.38
REMARK 500 15 LYS A 28 -11.65 171.15
REMARK 500 15 TRP A 32 -102.04 -119.65
REMARK 500 16 LEU A 7 -167.42 -76.51
REMARK 500 16 GLU A 11 -14.88 72.62
REMARK 500 16 LYS A 28 -52.71 76.08
REMARK 500 17 LYS A 6 64.20 61.90
REMARK 500 17 LEU A 7 -142.72 62.53
REMARK 500 17 GLU A 11 -10.36 77.59
REMARK 500 17 TRP A 32 -73.58 -94.36
REMARK 500 18 LEU A 4 81.82 58.44
REMARK 500 18 PRO A 5 -151.49 -74.32
REMARK 500 18 LEU A 7 -166.31 -116.15
REMARK 500 19 ARG A 3 -72.17 72.10
REMARK 500
REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 34 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 10 SG
REMARK 620 2 CYS A 13 SG 108.8
REMARK 620 3 HIS A 26 NE2 109.6 110.5
REMARK 620 4 CYS A 30 SG 110.6 108.7 108.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 34
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FY7 RELATED DB: PDB
REMARK 900 1FY7 CONTAINS ESA1 (YEAST HOMOLOGUE OF MOZ) HISTONE
REMARK 900 ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A
DBREF 1M36 A 3 33 UNP Q92794 MYST3_HUMAN 533 563
SEQADV 1M36 GLY A 1 UNP Q92794 CLONING ARTIFACT
SEQADV 1M36 SER A 2 UNP Q92794 CLONING ARTIFACT
SEQRES 1 A 33 GLY SER ARG LEU PRO LYS LEU TYR LEU CYS GLU PHE CYS
SEQRES 2 A 33 LEU LYS TYR MET LYS SER ARG THR ILE LEU GLN GLN HIS
SEQRES 3 A 33 MET LYS LYS CYS GLY TRP PHE
HET ZN A 34 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 SER A 19 CYS A 30 1 12
SHEET 1 A 2 TYR A 8 LEU A 9 0
SHEET 2 A 2 TYR A 16 MET A 17 -1 O MET A 17 N TYR A 8
LINK SG CYS A 10 ZN ZN A 34 1555 1555 2.30
LINK SG CYS A 13 ZN ZN A 34 1555 1555 2.29
LINK NE2 HIS A 26 ZN ZN A 34 1555 1555 1.97
LINK SG CYS A 30 ZN ZN A 34 1555 1555 2.31
SITE 1 AC1 4 CYS A 10 CYS A 13 HIS A 26 CYS A 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
Complete list - 23 20 Bytes