Header list of 1fre.pdb file
Complete list - 23 202 Bytes
HEADER ZINC-BINDING PROTEIN 31-JAN-96 1FRE
TITLE XNF7 BBOX, DEVELOPMENTAL PROTEIN, PH 7.5, 30 C, WITH ZINC, NMR, 1
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR FACTOR XNF7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BBOX;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355
KEYWDS ZINC-BINDING PROTEIN, XNF7, BBOX, DEVELOPMENT, MID-BLASTULA-
KEYWDS 2 TRANSITION
EXPDTA SOLUTION NMR
AUTHOR K.L.B.BORDEN,P.S.FREEMONT
REVDAT 4 23-FEB-22 1FRE 1 REMARK LINK
REVDAT 3 24-FEB-09 1FRE 1 VERSN
REVDAT 2 01-APR-03 1FRE 1 JRNL
REVDAT 1 12-FEB-97 1FRE 0
JRNL AUTH K.L.BORDEN,J.M.LALLY,S.R.MARTIN,N.J.O'REILLY,L.D.ETKIN,
JRNL AUTH 2 P.S.FREEMONT
JRNL TITL NOVEL TOPOLOGY OF A ZINC-BINDING DOMAIN FROM A PROTEIN
JRNL TITL 2 INVOLVED IN REGULATING EARLY XENOPUS DEVELOPMENT.
JRNL REF EMBO J. V. 14 5947 1995
JRNL REFN ISSN 0261-4189
JRNL PMID 8846787
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.S.FREEMONT
REMARK 1 TITL THE RING FINGER. A NOVEL PROTEIN SEQUENCE MOTIF RELATED TO
REMARK 1 TITL 2 THE ZINC FINGER
REMARK 1 REF ANN.N.Y.ACAD.SCI. V. 684 174 1993
REMARK 1 REFN ISSN 0077-8923
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.A.REDDY,M.KLOC,L.ETKIN
REMARK 1 TITL THE CLONING AND CHARACTERIZATION OF A MATERNALLY EXPRESSED
REMARK 1 TITL 2 NOVEL ZINC FINGER NUCLEAR PHOSPHOPROTEIN (XNF7) IN XENOPUS
REMARK 1 TITL 3 LAEVIS
REMARK 1 REF DEV.BIOL. V. 148 107 1991
REMARK 1 REFN ISSN 0012-1606
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FRE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173382.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 ARG A 1
REMARK 465 PRO A 2
REMARK 465 LEU A 3
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 LEU A 15 O LEU A 40 2.19
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 LYS A 5 -80.53 -66.69
REMARK 500 CYS A 6 68.44 14.25
REMARK 500 GLU A 8 97.00 39.46
REMARK 500 HIS A 9 -63.45 179.00
REMARK 500 GLU A 11 45.86 -84.50
REMARK 500 ARG A 12 -14.00 161.53
REMARK 500 LEU A 15 -144.76 -166.76
REMARK 500 CYS A 17 -87.42 -128.65
REMARK 500 LYS A 18 161.58 60.87
REMARK 500 ASP A 20 47.32 179.13
REMARK 500 SER A 24 115.58 58.78
REMARK 500 CYS A 25 -158.67 -137.73
REMARK 500 CYS A 28 34.97 -172.38
REMARK 500 ARG A 29 -0.08 78.64
REMARK 500 ASP A 30 -40.54 -157.46
REMARK 500 SER A 31 57.32 79.13
REMARK 500 ALA A 35 -77.15 77.01
REMARK 500 SER A 36 20.75 -152.79
REMARK 500 HIS A 37 -92.48 -49.77
REMARK 500 ASN A 38 154.38 174.18
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 ARG A 12 0.28 SIDE CHAIN
REMARK 500 ARG A 29 0.28 SIDE CHAIN
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 43 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 6 SG
REMARK 620 2 HIS A 9 CD2 90.3
REMARK 620 3 HIS A 9 NE2 95.6 40.9
REMARK 620 4 CYS A 28 SG 97.6 151.0 110.3
REMARK 620 5 HIS A 34 CD2 85.3 108.1 148.8 100.4
REMARK 620 6 HIS A 34 NE2 121.7 92.0 121.8 107.1 39.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZINC BINDING SITE 1.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 43
DBREF 1FRE A 1 42 UNP Q92021 NF7B_XENLA 219 260
SEQRES 1 A 42 ARG PRO LEU GLU LYS CYS SER GLU HIS ASP GLU ARG LEU
SEQRES 2 A 42 LYS LEU TYR CYS LYS ASP ASP GLY THR LEU SER CYS VAL
SEQRES 3 A 42 ILE CYS ARG ASP SER LEU LYS HIS ALA SER HIS ASN PHE
SEQRES 4 A 42 LEU PRO ILE
HET ZN A 43 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 H1 ILE A 27 SER A 31 1HELICAL TURN 5
SHEET 1 S1 1 LEU A 13 LYS A 18 0
SHEET 1 S2 1 ASN A 38 PRO A 41 0
LINK SG CYS A 6 ZN ZN A 43 1555 1555 2.32
LINK CD2 HIS A 9 ZN ZN A 43 1555 1555 1.90
LINK NE2 HIS A 9 ZN ZN A 43 1555 1555 2.04
LINK SG CYS A 28 ZN ZN A 43 1555 1555 2.30
LINK CD2 HIS A 34 ZN ZN A 43 1555 1555 2.18
LINK NE2 HIS A 34 ZN ZN A 43 1555 1555 1.53
SITE 1 ZN1 5 CYS A 6 HIS A 9 CYS A 28 HIS A 34
SITE 2 ZN1 5 ZN A 43
SITE 1 AC1 5 CYS A 6 HIS A 9 LEU A 13 CYS A 28
SITE 2 AC1 5 HIS A 34
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
Complete list - 23 202 Bytes