Header list of 4znf.pdb file
Complete list - r 16 2 Bytes
HEADER ZINC FINGER DNA BINDING DOMAIN 09-JUL-90 4ZNF
TITLE HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF A SINGLE ZINC FINGER
TITLE 2 FROM A HUMAN ENHANCER BINDING PROTEIN IN SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS ZINC FINGER DNA BINDING DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 41
AUTHOR A.M.GRONENBORN,G.M.CLORE,J.G.OMICHINSKI
REVDAT 4 16-MAR-22 4ZNF 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 4ZNF 1 VERSN
REVDAT 2 08-MAR-05 4ZNF 1 TITLE KEYWDS EXPDTA HETATM
REVDAT 1 15-JAN-92 4ZNF 0
JRNL AUTH J.G.OMICHINSKI,G.M.CLORE,E.APPELLA,K.SAKAGUCHI,
JRNL AUTH 2 A.M.GRONENBORN
JRNL TITL HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF A SINGLE ZINC
JRNL TITL 2 FINGER FROM A HUMAN ENHANCER BINDING PROTEIN IN SOLUTION.
JRNL REF BIOCHEMISTRY V. 29 9324 1990
JRNL REFN ISSN 0006-2960
JRNL PMID 2248949
JRNL DOI 10.1021/BI00492A004
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:
REMARK 3 THE 3D STRUCTURE OF THE ZINC FINGER IN SOLUTION
REMARK 3 BY NMR IS BASED ON 487 APPROXIMATE INTERPROTON DISTANCE
REMARK 3 RESTRAINTS AND 63 TORSION ANGLE RESTRAINTS DERIVED FROM
REMARK 3 NOE AND COUPLING CONSTANT MEASUREMENTS. THE STRUCTURES
REMARK 3 ARE CALCULATED USING THE HYBRID METRIC MATRIX DISTANCE
REMARK 3 GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD DESCRIBED
REMARK 3 BY M. NILGES, G. M. CLORE, AND A. M. GRONENBORN (1988)
REMARK 3 FEBS LETT 229, 317.
REMARK 3
REMARK 3 THIS ENTRY REPRESENTS 41 MODELS OF THE ZINC FINGER OF
REMARK 3 HUMAN ENHANCER BINDING PROTEIN. THE RESTRAINED MINIMIZED
REMARK 3 AVERAGE STRUCTURE (SA)$R DERIVED BY RESTRAINED LEAST
REMARK 3 SQUARE REFINEMENT OF THE MEAN STRUCTURE OBTAINED BY
REMARK 3 AVERAGING THE COORDINATES OF THE FINAL 41 SA STRUCTURES
REMARK 3 BEST FITTED TO EACH OTHER CAN BE FOUND IN PDB ENTRY 3ZNF.
REMARK 4
REMARK 4 4ZNF 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_1000179661.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : 41
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 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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 HIS A 4 CG HIS A 4 ND1 -0.116
REMARK 500 1 HIS A 27 CG HIS A 27 CD2 0.057
REMARK 500 1 HIS A 27 CG HIS A 27 ND1 -0.095
REMARK 500 2 HIS A 4 CG HIS A 4 ND1 -0.117
REMARK 500 2 HIS A 21 CG HIS A 21 ND1 -0.091
REMARK 500 2 HIS A 27 CG HIS A 27 ND1 -0.097
REMARK 500 3 HIS A 4 CG HIS A 4 ND1 -0.116
REMARK 500 3 HIS A 27 CG HIS A 27 ND1 -0.098
REMARK 500 4 HIS A 4 CG HIS A 4 ND1 -0.113
REMARK 500 4 HIS A 21 CG HIS A 21 ND1 -0.093
REMARK 500 4 HIS A 27 CG HIS A 27 CD2 0.058
REMARK 500 4 HIS A 27 CG HIS A 27 ND1 -0.096
REMARK 500 5 HIS A 4 CG HIS A 4 ND1 -0.119
REMARK 500 5 HIS A 27 CG HIS A 27 CD2 0.054
REMARK 500 5 HIS A 27 CG HIS A 27 ND1 -0.097
REMARK 500 6 HIS A 4 CG HIS A 4 ND1 -0.115
REMARK 500 6 HIS A 21 CG HIS A 21 ND1 -0.090
REMARK 500 6 HIS A 27 CG HIS A 27 CD2 0.057
REMARK 500 6 HIS A 27 CG HIS A 27 ND1 -0.101
REMARK 500 7 HIS A 4 CG HIS A 4 ND1 -0.115
REMARK 500 7 HIS A 27 CG HIS A 27 CD2 0.059
REMARK 500 7 HIS A 27 CG HIS A 27 ND1 -0.101
REMARK 500 8 HIS A 4 CG HIS A 4 ND1 -0.118
REMARK 500 8 HIS A 21 CG HIS A 21 ND1 -0.090
REMARK 500 8 HIS A 27 CG HIS A 27 CD2 0.055
REMARK 500 8 HIS A 27 CG HIS A 27 ND1 -0.100
REMARK 500 9 HIS A 4 CG HIS A 4 ND1 -0.116
REMARK 500 9 HIS A 27 CG HIS A 27 CD2 0.060
REMARK 500 9 HIS A 27 CG HIS A 27 ND1 -0.099
REMARK 500 10 HIS A 4 CG HIS A 4 ND1 -0.115
REMARK 500 10 HIS A 21 CG HIS A 21 ND1 -0.090
REMARK 500 10 HIS A 27 CG HIS A 27 CD2 0.060
REMARK 500 10 HIS A 27 CG HIS A 27 ND1 -0.099
REMARK 500 11 HIS A 4 CG HIS A 4 ND1 -0.113
REMARK 500 11 HIS A 21 CG HIS A 21 ND1 -0.092
REMARK 500 11 HIS A 27 CG HIS A 27 CD2 0.056
REMARK 500 11 HIS A 27 CG HIS A 27 ND1 -0.098
REMARK 500 12 HIS A 4 CG HIS A 4 ND1 -0.115
REMARK 500 12 HIS A 27 CG HIS A 27 CD2 0.063
REMARK 500 12 HIS A 27 CG HIS A 27 ND1 -0.100
REMARK 500 13 HIS A 4 CG HIS A 4 ND1 -0.116
REMARK 500 13 HIS A 21 CG HIS A 21 ND1 -0.091
REMARK 500 13 HIS A 27 CG HIS A 27 CD2 0.055
REMARK 500 13 HIS A 27 CG HIS A 27 ND1 -0.098
REMARK 500 14 HIS A 4 CG HIS A 4 ND1 -0.115
REMARK 500 14 HIS A 27 CG HIS A 27 ND1 -0.099
REMARK 500 15 HIS A 4 CG HIS A 4 ND1 -0.117
REMARK 500 15 HIS A 21 CG HIS A 21 ND1 -0.091
REMARK 500 15 HIS A 27 CG HIS A 27 CD2 0.061
REMARK 500 15 HIS A 27 CG HIS A 27 ND1 -0.101
REMARK 500
REMARK 500 THIS ENTRY HAS 130 BOND DEVIATIONS.
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 PRO A 2 37.04 -69.01
REMARK 500 1 TYR A 7 -75.55 -157.59
REMARK 500 1 CYS A 8 -157.45 -58.80
REMARK 500 1 PHE A 12 -163.39 -124.86
REMARK 500 1 ALA A 26 -90.26 -63.53
REMARK 500 1 HIS A 27 71.33 -175.51
REMARK 500 1 SER A 28 73.70 -152.15
REMARK 500 2 PRO A 2 7.32 -66.10
REMARK 500 2 CYS A 5 164.59 -47.88
REMARK 500 2 TYR A 7 -74.36 -160.94
REMARK 500 2 CYS A 8 -164.44 -61.10
REMARK 500 2 PHE A 10 69.06 -68.98
REMARK 500 2 ALA A 26 -89.25 -50.26
REMARK 500 2 HIS A 27 66.41 -175.43
REMARK 500 2 SER A 28 83.34 -169.28
REMARK 500 3 PRO A 2 30.52 -67.36
REMARK 500 3 CYS A 5 156.69 -48.07
REMARK 500 3 TYR A 7 -77.17 -161.07
REMARK 500 3 CYS A 8 -159.76 -57.79
REMARK 500 3 PHE A 10 92.76 -67.93
REMARK 500 3 PHE A 12 -154.59 -102.81
REMARK 500 3 LYS A 25 39.57 -76.93
REMARK 500 3 ALA A 26 -87.07 -64.05
REMARK 500 3 HIS A 27 81.55 -172.80
REMARK 500 3 SER A 28 95.66 -171.03
REMARK 500 4 PRO A 2 24.53 -65.00
REMARK 500 4 TYR A 7 -74.55 -156.25
REMARK 500 4 CYS A 8 -157.51 -61.36
REMARK 500 4 PHE A 10 92.11 -67.96
REMARK 500 4 LYS A 20 -19.13 -46.35
REMARK 500 4 LYS A 25 25.08 -73.21
REMARK 500 4 ALA A 26 -87.79 -52.20
REMARK 500 4 HIS A 27 76.16 -170.70
REMARK 500 4 SER A 28 87.85 -170.33
REMARK 500 5 TYR A 7 -74.38 -159.71
REMARK 500 5 CYS A 8 -170.25 -58.36
REMARK 500 5 PHE A 12 -164.45 -128.97
REMARK 500 5 SER A 24 -161.53 -64.24
REMARK 500 5 LYS A 25 57.38 -104.53
REMARK 500 5 ALA A 26 -84.34 -80.36
REMARK 500 5 HIS A 27 69.97 -175.16
REMARK 500 6 TYR A 7 -75.47 -160.60
REMARK 500 6 CYS A 8 -168.52 -57.09
REMARK 500 6 PHE A 10 88.50 -66.74
REMARK 500 6 ALA A 26 -87.54 -46.67
REMARK 500 6 HIS A 27 66.93 -173.54
REMARK 500 6 SER A 28 90.21 -171.36
REMARK 500 7 PRO A 2 27.39 -66.30
REMARK 500 7 CYS A 5 167.12 -49.92
REMARK 500 7 TYR A 7 -72.53 -159.06
REMARK 500
REMARK 500 THIS ENTRY HAS 353 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 1 0.26 SIDE CHAIN
REMARK 500 2 ARG A 1 0.30 SIDE CHAIN
REMARK 500 3 ARG A 1 0.20 SIDE CHAIN
REMARK 500 4 ARG A 1 0.30 SIDE CHAIN
REMARK 500 5 ARG A 1 0.28 SIDE CHAIN
REMARK 500 6 ARG A 1 0.21 SIDE CHAIN
REMARK 500 7 ARG A 1 0.19 SIDE CHAIN
REMARK 500 8 ARG A 1 0.31 SIDE CHAIN
REMARK 500 9 ARG A 1 0.20 SIDE CHAIN
REMARK 500 11 ARG A 1 0.10 SIDE CHAIN
REMARK 500 12 ARG A 1 0.31 SIDE CHAIN
REMARK 500 13 ARG A 1 0.32 SIDE CHAIN
REMARK 500 14 ARG A 1 0.22 SIDE CHAIN
REMARK 500 15 ARG A 1 0.24 SIDE CHAIN
REMARK 500 16 ARG A 1 0.08 SIDE CHAIN
REMARK 500 17 ARG A 1 0.32 SIDE CHAIN
REMARK 500 18 ARG A 1 0.21 SIDE CHAIN
REMARK 500 19 ARG A 1 0.31 SIDE CHAIN
REMARK 500 20 ARG A 1 0.24 SIDE CHAIN
REMARK 500 21 ARG A 1 0.29 SIDE CHAIN
REMARK 500 22 ARG A 1 0.31 SIDE CHAIN
REMARK 500 23 ARG A 1 0.09 SIDE CHAIN
REMARK 500 24 ARG A 1 0.20 SIDE CHAIN
REMARK 500 25 ARG A 1 0.15 SIDE CHAIN
REMARK 500 26 ARG A 1 0.27 SIDE CHAIN
REMARK 500 27 ARG A 1 0.19 SIDE CHAIN
REMARK 500 28 ARG A 1 0.26 SIDE CHAIN
REMARK 500 29 ARG A 1 0.27 SIDE CHAIN
REMARK 500 30 ARG A 1 0.12 SIDE CHAIN
REMARK 500 31 ARG A 1 0.13 SIDE CHAIN
REMARK 500 32 ARG A 1 0.29 SIDE CHAIN
REMARK 500 33 ARG A 1 0.27 SIDE CHAIN
REMARK 500 34 ARG A 1 0.25 SIDE CHAIN
REMARK 500 35 ARG A 1 0.11 SIDE CHAIN
REMARK 500 36 ARG A 1 0.12 SIDE CHAIN
REMARK 500 37 ARG A 1 0.15 SIDE CHAIN
REMARK 500 38 ARG A 1 0.09 SIDE CHAIN
REMARK 500 39 ARG A 1 0.18 SIDE CHAIN
REMARK 500 40 ARG A 1 0.17 SIDE CHAIN
REMARK 500 41 ARG A 1 0.23 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 31 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 5 SG
REMARK 620 2 CYS A 8 SG 111.9
REMARK 620 3 HIS A 21 NE2 111.2 110.5
REMARK 620 4 HIS A 27 NE2 111.9 97.5 113.1
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 31
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZNF RELATED DB: PDB
DBREF 4ZNF A 1 30 UNP P15822 ZEP1_HUMAN 2113 2142
SEQADV 4ZNF SER A 6 UNP P15822 THR 2118 CONFLICT
SEQRES 1 A 30 ARG PRO TYR HIS CYS SER TYR CYS ASN PHE SER PHE LYS
SEQRES 2 A 30 THR LYS GLY ASN LEU THR LYS HIS MET LYS SER LYS ALA
SEQRES 3 A 30 HIS SER LYS LYS
HET ZN A 31 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 THR A 14 SER A 24 1 11
LINK SG CYS A 5 ZN ZN A 31 1555 1555 2.30
LINK SG CYS A 8 ZN ZN A 31 1555 1555 2.31
LINK NE2 HIS A 21 ZN ZN A 31 1555 1555 2.01
LINK NE2 HIS A 27 ZN ZN A 31 1555 1555 2.02
SITE 1 AC1 4 CYS A 5 CYS A 8 HIS A 21 HIS A 27
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 - r 16 2 Bytes