Header list of 1g25.pdb file
Complete list - b 23 2 Bytes
HEADER METAL BINDING PROTEIN 17-OCT-00 1G25
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN TFIIH MAT1
TITLE 2 SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CDK-ACTIVATING KINASE ASSEMBLY FACTOR MAT1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: RING FINGER PROTEIN MAT1;
COMPND 6 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: MAT1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 LAMBDA (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T2
KEYWDS RING FINGER (C3HC4), METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR V.GERVAIS,E.WASIELEWSKI,D.BUSSO,A.POTERSZMAN,J.M.EGLY,J.C.THIERRY,
AUTHOR 2 B.KIEFFER
REVDAT 4 23-FEB-22 1G25 1 REMARK LINK
REVDAT 3 24-FEB-09 1G25 1 VERSN
REVDAT 2 04-FEB-03 1G25 1 JRNL REMARK
REVDAT 1 01-NOV-00 1G25 0
JRNL AUTH V.GERVAIS,D.BUSSO,E.WASIELEWSKI,A.POTERSZMAN,J.M.EGLY,
JRNL AUTH 2 J.C.THIERRY,B.KIEFFER
JRNL TITL SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN
JRNL TITL 2 TFIIH MAT1 SUBUNIT: NEW INSIGHTS INTO THE RING FINGER FAMILY
JRNL REF J.BIOL.CHEM. V. 276 7457 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11056162
JRNL DOI 10.1074/JBC.M007963200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8, X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 988 RESTRAINTS, 897 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 72
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,11 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS AND 8 DISTANCE RESTRAINTS FROM THE ZINC BINDING.
REMARK 4
REMARK 4 1G25 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012139.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 290; 283
REMARK 210 PH : 7.5; 7.5; 7.5
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL
REMARK 210 PRESSURE : AMBIANT; AMBIANT; AMBIANT
REMARK 210 SAMPLE CONTENTS : 2 MM MAT1; 20 MM TRIS-HCL PH
REMARK 210 7.5; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_NOESY; DQF-COSY; 2D_TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 1.3, XEASY 1.3.13
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 57
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
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 O CYS A 34 H LEU A 38 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 ASP A 2 -63.51 -128.61
REMARK 500 1 ASP A 3 -147.41 60.30
REMARK 500 1 CYS A 6 160.48 -32.44
REMARK 500 1 ARG A 8 -71.01 -59.98
REMARK 500 1 CYS A 9 46.45 -93.44
REMARK 500 1 LYS A 10 93.77 -35.50
REMARK 500 1 THR A 11 -43.51 -176.11
REMARK 500 1 THR A 12 -109.61 -47.08
REMARK 500 1 LYS A 13 -38.07 -26.81
REMARK 500 1 PRO A 17 39.65 -97.84
REMARK 500 1 SER A 18 56.60 -164.20
REMARK 500 1 LEU A 19 -143.93 -138.29
REMARK 500 1 LYS A 20 159.06 178.66
REMARK 500 1 VAL A 25 -74.30 -33.34
REMARK 500 1 HIS A 28 -98.86 -130.57
REMARK 500 1 THR A 29 134.21 -179.34
REMARK 500 1 CYS A 31 172.08 -44.86
REMARK 500 1 ALA A 43 107.78 65.35
REMARK 500 1 GLU A 48 -57.41 -141.58
REMARK 500 1 LYS A 55 88.56 170.77
REMARK 500 1 SER A 56 -121.00 59.08
REMARK 500 1 ASN A 57 102.63 79.28
REMARK 500 1 LEU A 62 -40.48 -175.41
REMARK 500 1 GLU A 64 90.11 59.74
REMARK 500 2 ASP A 3 -93.38 -37.00
REMARK 500 2 CYS A 6 130.97 -30.98
REMARK 500 2 CYS A 9 48.95 -99.88
REMARK 500 2 LYS A 10 93.61 -31.38
REMARK 500 2 THR A 11 -38.75 -178.86
REMARK 500 2 THR A 12 -100.58 -48.27
REMARK 500 2 LYS A 13 -27.50 -36.09
REMARK 500 2 LYS A 20 -153.81 -145.97
REMARK 500 2 VAL A 25 -99.86 22.33
REMARK 500 2 HIS A 28 -100.66 -102.27
REMARK 500 2 THR A 29 128.08 171.60
REMARK 500 2 CYS A 31 171.34 -48.80
REMARK 500 2 CYS A 34 -71.07 -80.35
REMARK 500 2 ALA A 43 -145.35 68.23
REMARK 500 2 ASN A 45 -179.45 72.20
REMARK 500 2 ARG A 54 62.34 -178.10
REMARK 500 2 LYS A 55 49.86 173.56
REMARK 500 2 LEU A 62 113.70 -174.52
REMARK 500 2 GLU A 64 59.37 -94.24
REMARK 500 3 ASP A 2 -95.80 43.33
REMARK 500 3 ASP A 3 -153.33 38.71
REMARK 500 3 CYS A 9 50.54 -99.34
REMARK 500 3 LYS A 10 85.83 -27.32
REMARK 500 3 THR A 11 -52.80 -174.84
REMARK 500 3 ARG A 15 -78.48 -88.45
REMARK 500 3 SER A 18 67.71 -118.34
REMARK 500
REMARK 500 THIS ENTRY HAS 421 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 8 0.12 SIDE CHAIN
REMARK 500 1 ARG A 15 0.32 SIDE CHAIN
REMARK 500 1 ARG A 41 0.20 SIDE CHAIN
REMARK 500 1 ARG A 54 0.27 SIDE CHAIN
REMARK 500 1 ARG A 59 0.24 SIDE CHAIN
REMARK 500 2 ARG A 8 0.26 SIDE CHAIN
REMARK 500 2 ARG A 15 0.32 SIDE CHAIN
REMARK 500 2 ARG A 41 0.23 SIDE CHAIN
REMARK 500 2 ARG A 54 0.20 SIDE CHAIN
REMARK 500 2 ARG A 59 0.31 SIDE CHAIN
REMARK 500 3 ARG A 8 0.25 SIDE CHAIN
REMARK 500 3 ARG A 15 0.28 SIDE CHAIN
REMARK 500 3 ARG A 41 0.32 SIDE CHAIN
REMARK 500 3 ARG A 54 0.25 SIDE CHAIN
REMARK 500 3 ARG A 59 0.11 SIDE CHAIN
REMARK 500 4 ARG A 8 0.23 SIDE CHAIN
REMARK 500 4 ARG A 15 0.25 SIDE CHAIN
REMARK 500 4 ARG A 54 0.32 SIDE CHAIN
REMARK 500 4 ARG A 59 0.15 SIDE CHAIN
REMARK 500 5 ARG A 8 0.27 SIDE CHAIN
REMARK 500 5 ARG A 15 0.32 SIDE CHAIN
REMARK 500 5 ARG A 41 0.14 SIDE CHAIN
REMARK 500 5 ARG A 54 0.17 SIDE CHAIN
REMARK 500 5 ARG A 59 0.11 SIDE CHAIN
REMARK 500 6 ARG A 8 0.19 SIDE CHAIN
REMARK 500 6 ARG A 15 0.23 SIDE CHAIN
REMARK 500 6 ARG A 41 0.32 SIDE CHAIN
REMARK 500 6 ARG A 54 0.29 SIDE CHAIN
REMARK 500 6 ARG A 59 0.27 SIDE CHAIN
REMARK 500 7 ARG A 8 0.29 SIDE CHAIN
REMARK 500 7 ARG A 15 0.22 SIDE CHAIN
REMARK 500 7 ARG A 41 0.20 SIDE CHAIN
REMARK 500 7 ARG A 54 0.26 SIDE CHAIN
REMARK 500 7 ARG A 59 0.31 SIDE CHAIN
REMARK 500 8 ARG A 8 0.31 SIDE CHAIN
REMARK 500 8 ARG A 15 0.32 SIDE CHAIN
REMARK 500 8 ARG A 41 0.15 SIDE CHAIN
REMARK 500 8 ARG A 54 0.22 SIDE CHAIN
REMARK 500 8 ARG A 59 0.20 SIDE CHAIN
REMARK 500 9 ARG A 8 0.26 SIDE CHAIN
REMARK 500 9 ARG A 15 0.12 SIDE CHAIN
REMARK 500 9 ARG A 41 0.28 SIDE CHAIN
REMARK 500 9 ARG A 54 0.23 SIDE CHAIN
REMARK 500 9 ARG A 59 0.32 SIDE CHAIN
REMARK 500 10 ARG A 8 0.32 SIDE CHAIN
REMARK 500 10 ARG A 15 0.32 SIDE CHAIN
REMARK 500 10 ARG A 41 0.29 SIDE CHAIN
REMARK 500 10 ARG A 54 0.20 SIDE CHAIN
REMARK 500 10 ARG A 59 0.15 SIDE CHAIN
REMARK 500 11 ARG A 8 0.22 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 97 PLANE DEVIATIONS.
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 66 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 6 SG
REMARK 620 2 CYS A 9 SG 111.9
REMARK 620 3 CYS A 31 SG 106.9 111.1
REMARK 620 4 CYS A 34 SG 108.1 109.6 109.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 67 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 26 SG
REMARK 620 2 HIS A 28 ND1 110.2
REMARK 620 3 CYS A 46 SG 108.9 111.1
REMARK 620 4 CYS A 49 SG 111.1 108.6 107.0
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 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 67
DBREF 1G25 A 1 65 UNP P51948 MAT1_HUMAN 1 65
SEQRES 1 A 65 MET ASP ASP GLN GLY CYS PRO ARG CYS LYS THR THR LYS
SEQRES 2 A 65 TYR ARG ASN PRO SER LEU LYS LEU MET VAL ASN VAL CYS
SEQRES 3 A 65 GLY HIS THR LEU CYS GLU SER CYS VAL ASP LEU LEU PHE
SEQRES 4 A 65 VAL ARG GLY ALA GLY ASN CYS PRO GLU CYS GLY THR PRO
SEQRES 5 A 65 LEU ARG LYS SER ASN PHE ARG VAL GLN LEU PHE GLU ASP
HET ZN A 66 1
HET ZN A 67 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 THR A 11 ASN A 16 1 6
HELIX 2 2 GLU A 32 ARG A 41 1 10
SHEET 1 A 3 LEU A 30 CYS A 31 0
SHEET 2 A 3 LEU A 21 VAL A 23 -1 N MET A 22 O LEU A 30
SHEET 3 A 3 ARG A 59 GLN A 61 -1 N ARG A 59 O VAL A 23
LINK SG CYS A 6 ZN ZN A 66 1555 1555 2.28
LINK SG CYS A 9 ZN ZN A 66 1555 1555 2.32
LINK SG CYS A 26 ZN ZN A 67 1555 1555 2.30
LINK ND1 HIS A 28 ZN ZN A 67 1555 1555 2.00
LINK SG CYS A 31 ZN ZN A 66 1555 1555 2.29
LINK SG CYS A 34 ZN ZN A 66 1555 1555 2.29
LINK SG CYS A 46 ZN ZN A 67 1555 1555 2.29
LINK SG CYS A 49 ZN ZN A 67 1555 1555 2.30
SITE 1 AC1 5 CYS A 6 CYS A 9 CYS A 31 SER A 33
SITE 2 AC1 5 CYS A 34
SITE 1 AC2 4 CYS A 26 HIS A 28 CYS A 46 CYS A 49
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