Header list of 1gnf.pdb file
Complete list - v 29 2 Bytes
HEADER TRANSCRIPTION REGULATION 12-OCT-98 1GNF
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER OF MURINE GATA-1,
TITLE 2 NMR, 25 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION FACTOR GATA-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL ZINC FINGER;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 CELL_LINE: BL21;
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_PLASMID: PGEX-2T
KEYWDS ZINC FINGER, TRANSCRIPTION REGULATION
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR K.KOWALSKI,R.CZOLIJ,G.F.KING,M.CROSSLEY,J.P.MACKAY
REVDAT 3 29-NOV-17 1GNF 1 REMARK HELIX
REVDAT 2 24-FEB-09 1GNF 1 VERSN
REVDAT 1 08-JUN-99 1GNF 0
JRNL AUTH K.KOWALSKI,R.CZOLIJ,G.F.KING,M.CROSSLEY,J.P.MACKAY
JRNL TITL THE SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER OF
JRNL TITL 2 GATA-1 REVEALS A SPECIFIC BINDING FACE FOR THE
JRNL TITL 3 TRANSCRIPTIONAL CO-FACTOR FOG.
JRNL REF J.BIOMOL.NMR V. 13 249 1999
JRNL REFN ISSN 0925-2738
JRNL PMID 10212985
JRNL DOI 10.1023/A:1008309602929
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1GNF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173632.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 5.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 95% H2O:5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY; DQFCOSY; NOESY; ECOSY;
REMARK 210 HSQC; TOCSY-HSQC; NOESY-HSQC; J-
REMARK 210 MODULATED HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600; DRX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA 2.12, X-PLOR 3.843
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST RESIDUAL RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HOMONUCLEAR 1H, AND
REMARK 210 HETERONUCLEAR 1H/15N NMR SPECTROSCOPY
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 ASP A 218 H GLY A 221 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 GLU A 200 -80.18 -48.09
REMARK 500 1 ALA A 201 -160.60 -68.24
REMARK 500 1 ASN A 206 -60.85 -91.95
REMARK 500 1 ALA A 209 106.51 -50.24
REMARK 500 1 ASP A 218 -160.61 -122.24
REMARK 500 1 HIS A 222 -163.82 -79.51
REMARK 500 1 ASN A 226 -72.68 174.10
REMARK 500 1 PRO A 240 -73.63 -73.12
REMARK 500 1 LEU A 241 -169.49 66.71
REMARK 500 2 SER A 199 71.22 42.63
REMARK 500 2 GLU A 200 -78.09 -53.68
REMARK 500 2 ALA A 201 169.20 -49.87
REMARK 500 2 CYS A 204 108.18 -49.26
REMARK 500 2 LEU A 214 137.15 65.90
REMARK 500 2 ASP A 218 -160.11 -124.68
REMARK 500 2 HIS A 222 -166.71 -71.76
REMARK 500 2 ASN A 226 -81.67 167.78
REMARK 500 2 PRO A 240 -164.84 -74.11
REMARK 500 3 SER A 199 40.03 -173.74
REMARK 500 3 PRO A 213 -155.18 -69.90
REMARK 500 3 LEU A 214 118.69 -37.32
REMARK 500 3 ASP A 218 -162.88 -128.02
REMARK 500 3 HIS A 222 -166.70 -74.73
REMARK 500 3 LEU A 224 173.99 -55.44
REMARK 500 3 ASN A 226 -76.15 168.08
REMARK 500 3 LEU A 241 -164.03 -117.36
REMARK 500 4 SER A 199 27.14 46.78
REMARK 500 4 ARG A 216 124.94 -175.78
REMARK 500 4 ASP A 218 -157.71 -127.56
REMARK 500 4 LEU A 224 173.21 -53.33
REMARK 500 4 ASN A 226 -56.68 69.87
REMARK 500 4 MET A 234 -61.88 -93.72
REMARK 500 4 LEU A 241 -97.60 -108.95
REMARK 500 4 ILE A 242 -76.11 -93.93
REMARK 500 5 SER A 199 27.97 -143.55
REMARK 500 5 GLU A 200 -78.00 -53.94
REMARK 500 5 ALA A 211 72.17 -111.02
REMARK 500 5 LEU A 214 119.03 69.02
REMARK 500 5 ARG A 216 121.51 63.44
REMARK 500 5 ASP A 218 -163.93 -126.14
REMARK 500 5 CYS A 225 42.71 -100.66
REMARK 500 5 ASN A 226 -56.93 67.94
REMARK 500 5 GLN A 237 -164.23 -79.55
REMARK 500 5 LEU A 241 -126.94 -142.77
REMARK 500 6 SER A 199 25.12 47.22
REMARK 500 6 ASN A 206 -61.42 -91.77
REMARK 500 6 LEU A 214 140.52 -172.18
REMARK 500 6 TRP A 215 -72.11 -98.27
REMARK 500 6 ARG A 216 126.40 61.38
REMARK 500 6 ASP A 218 -163.16 -123.67
REMARK 500
REMARK 500 THIS ENTRY HAS 214 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 202 0.31 SIDE CHAIN
REMARK 500 1 ARG A 216 0.32 SIDE CHAIN
REMARK 500 1 ARG A 217 0.25 SIDE CHAIN
REMARK 500 1 ARG A 219 0.29 SIDE CHAIN
REMARK 500 1 ARG A 239 0.23 SIDE CHAIN
REMARK 500 2 ARG A 202 0.21 SIDE CHAIN
REMARK 500 2 ARG A 216 0.19 SIDE CHAIN
REMARK 500 2 ARG A 217 0.26 SIDE CHAIN
REMARK 500 2 ARG A 219 0.31 SIDE CHAIN
REMARK 500 2 ARG A 239 0.14 SIDE CHAIN
REMARK 500 2 ARG A 243 0.20 SIDE CHAIN
REMARK 500 3 ARG A 202 0.25 SIDE CHAIN
REMARK 500 3 ARG A 216 0.32 SIDE CHAIN
REMARK 500 3 ARG A 217 0.11 SIDE CHAIN
REMARK 500 3 ARG A 219 0.25 SIDE CHAIN
REMARK 500 3 ARG A 239 0.20 SIDE CHAIN
REMARK 500 3 ARG A 243 0.31 SIDE CHAIN
REMARK 500 4 ARG A 202 0.30 SIDE CHAIN
REMARK 500 4 ARG A 216 0.31 SIDE CHAIN
REMARK 500 4 ARG A 217 0.31 SIDE CHAIN
REMARK 500 4 ARG A 219 0.29 SIDE CHAIN
REMARK 500 4 ARG A 239 0.21 SIDE CHAIN
REMARK 500 4 ARG A 243 0.32 SIDE CHAIN
REMARK 500 5 ARG A 202 0.30 SIDE CHAIN
REMARK 500 5 ARG A 216 0.31 SIDE CHAIN
REMARK 500 5 ARG A 217 0.19 SIDE CHAIN
REMARK 500 5 ARG A 219 0.15 SIDE CHAIN
REMARK 500 5 ARG A 239 0.15 SIDE CHAIN
REMARK 500 5 ARG A 243 0.23 SIDE CHAIN
REMARK 500 6 ARG A 216 0.13 SIDE CHAIN
REMARK 500 6 ARG A 217 0.31 SIDE CHAIN
REMARK 500 6 ARG A 219 0.19 SIDE CHAIN
REMARK 500 6 ARG A 239 0.22 SIDE CHAIN
REMARK 500 6 ARG A 243 0.31 SIDE CHAIN
REMARK 500 7 ARG A 202 0.29 SIDE CHAIN
REMARK 500 7 ARG A 216 0.20 SIDE CHAIN
REMARK 500 7 ARG A 217 0.31 SIDE CHAIN
REMARK 500 7 ARG A 219 0.31 SIDE CHAIN
REMARK 500 7 ARG A 239 0.31 SIDE CHAIN
REMARK 500 7 ARG A 243 0.22 SIDE CHAIN
REMARK 500 8 ARG A 202 0.29 SIDE CHAIN
REMARK 500 8 ARG A 216 0.32 SIDE CHAIN
REMARK 500 8 ARG A 217 0.32 SIDE CHAIN
REMARK 500 8 ARG A 219 0.32 SIDE CHAIN
REMARK 500 8 ARG A 239 0.14 SIDE CHAIN
REMARK 500 8 ARG A 243 0.21 SIDE CHAIN
REMARK 500 9 ARG A 202 0.28 SIDE CHAIN
REMARK 500 9 ARG A 216 0.24 SIDE CHAIN
REMARK 500 9 ARG A 217 0.20 SIDE CHAIN
REMARK 500 9 ARG A 219 0.17 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 143 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 244 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 204 SG
REMARK 620 2 CYS A 207 SG 109.6
REMARK 620 3 CYS A 225 SG 109.1 109.4
REMARK 620 4 CYS A 228 SG 109.0 110.7 109.0
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 244
DBREF 1GNF A 198 243 UNP P17679 GATA1_MOUSE 198 243
SEQADV 1GNF GLY A 198 UNP P17679 PRO 198 CLONING ARTIFACT
SEQADV 1GNF SER A 199 UNP P17679 CYS 199 CLONING ARTIFACT
SEQRES 1 A 46 GLY SER GLU ALA ARG GLU CYS VAL ASN CYS GLY ALA THR
SEQRES 2 A 46 ALA THR PRO LEU TRP ARG ARG ASP ARG THR GLY HIS TYR
SEQRES 3 A 46 LEU CYS ASN ALA CYS GLY LEU TYR HIS LYS MET ASN GLY
SEQRES 4 A 46 GLN ASN ARG PRO LEU ILE ARG
HET ZN A 244 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 H1 ASN A 226 ASN A 235 1 10
LINK ZN ZN A 244 SG CYS A 204 1555 1555 2.30
LINK ZN ZN A 244 SG CYS A 207 1555 1555 2.31
LINK ZN ZN A 244 SG CYS A 225 1555 1555 2.30
LINK ZN ZN A 244 SG CYS A 228 1555 1555 2.30
SITE 1 AC1 4 CYS A 204 CYS A 207 CYS A 225 CYS A 228
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 29 2 Bytes