Header list of 7znf.pdb file
Complete list - 16 20 Bytes
HEADER ZINC FINGER DNA BINDING DOMAIN 22-AUG-91 7ZNF
TITLE ALTERNATING ZINC FINGERS IN THE HUMAN MALE ASSOCIATED PROTEIN ZFY: 2D
TITLE 2 NMR STRUCTURE OF AN EVEN FINGER AND IMPLICATIONS FOR "JUMPING-LINKER"
TITLE 3 DNA RECOGNITION
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 12
AUTHOR M.KOCHOYAN,H.T.KEUTMANN,M.A.WEISS
REVDAT 3 16-MAR-22 7ZNF 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 7ZNF 1 VERSN
REVDAT 1 31-JAN-94 7ZNF 0
JRNL AUTH M.KOCHOYAN,T.F.HAVEL,D.T.NGUYEN,C.E.DAHL,H.T.KEUTMANN,
JRNL AUTH 2 M.A.WEISS
JRNL TITL ALTERNATING ZINC FINGERS IN THE HUMAN MALE ASSOCIATED
JRNL TITL 2 PROTEIN ZFY: 2D NMR STRUCTURE OF AN EVEN FINGER AND
JRNL TITL 3 IMPLICATIONS FOR "JUMPING-LINKER" DNA RECOGNITION.
JRNL REF BIOCHEMISTRY V. 30 3371 1991
JRNL REFN ISSN 0006-2960
JRNL PMID 1849423
JRNL DOI 10.1021/BI00228A004
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.KOCHOYAN,H.T.KEUTMANN,M.A.WEISS
REMARK 1 TITL ALTERNATING ZINC FINGERS IN THE HUMAN MALE ASSOCIATED
REMARK 1 TITL 2 PROTEIN ZFY: REFINEMENT OF THE NMR STRUCTURE OF AN EVEN
REMARK 1 TITL 3 FINGER BY SELECTIVE DEUTERIUM LABELING AND IMPLICATIONS FOR
REMARK 1 TITL 4 DNA RECOGNITION
REMARK 1 REF BIOCHEMISTRY V. 30 7063 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.KOCHOYAN,H.T.KEUTMANN,M.A.WEISS
REMARK 1 TITL ARCHITECTURAL RULES OF THE ZINC-FINGER MOTIF: COMPARATIVE
REMARK 1 TITL 2 TWO-DIMENSIONAL NMR STUDIES OF NATIVE AND "AROMATIC-SWAP"
REMARK 1 TITL 3 DOMAINS DEFINE A "WEAKLY POLAR SWITCH"
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 88 8455 1991
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : HAVEL (DGII), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7ZNF 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_1000179952.
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 : 12
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: 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 4 HIS A 26 NE2 HIS A 26 CD2 -0.068
REMARK 500 9 HIS A 21 NE2 HIS A 21 CD2 -0.066
REMARK 500 9 HIS A 26 NE2 HIS A 26 CD2 -0.066
REMARK 500 12 HIS A 21 NE2 HIS A 21 CD2 -0.066
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 CYS A 8 -164.82 -120.79
REMARK 500 1 ALA A 13 76.46 -113.32
REMARK 500 1 ASP A 14 175.60 121.98
REMARK 500 1 HIS A 21 -56.20 -25.49
REMARK 500 1 THR A 24 -50.93 -125.85
REMARK 500 1 HIS A 26 55.19 -113.85
REMARK 500 1 SER A 27 68.16 -103.92
REMARK 500 1 GLU A 29 26.94 40.24
REMARK 500 2 CYS A 8 -160.64 -123.22
REMARK 500 2 GLU A 9 64.56 -118.61
REMARK 500 2 HIS A 26 -50.91 -120.40
REMARK 500 2 SER A 27 121.29 -10.72
REMARK 500 2 LYS A 28 67.73 -110.49
REMARK 500 3 GLN A 4 -167.10 -127.57
REMARK 500 3 TYR A 7 -53.38 -131.33
REMARK 500 3 CYS A 8 -157.18 -121.66
REMARK 500 3 PHE A 12 -62.87 -125.99
REMARK 500 3 ALA A 13 -39.11 105.21
REMARK 500 3 LYS A 23 -28.54 -37.40
REMARK 500 3 SER A 27 -69.79 -136.81
REMARK 500 3 GLU A 29 -66.73 9.06
REMARK 500 4 THR A 2 101.04 11.58
REMARK 500 4 TYR A 7 -51.67 -130.46
REMARK 500 4 CYS A 8 -166.44 -117.42
REMARK 500 4 GLU A 9 54.52 -116.61
REMARK 500 4 THR A 24 -40.67 -132.91
REMARK 500 4 HIS A 26 67.20 -112.87
REMARK 500 4 LYS A 28 -29.62 -39.59
REMARK 500 4 GLU A 29 66.21 -105.32
REMARK 500 5 TYR A 7 -57.15 -128.76
REMARK 500 5 CYS A 8 -158.10 -126.58
REMARK 500 5 GLU A 9 75.09 -118.47
REMARK 500 5 SER A 15 -50.74 -24.92
REMARK 500 5 SER A 16 -36.93 -38.69
REMARK 500 5 HIS A 26 60.61 -112.11
REMARK 500 5 SER A 27 45.17 -106.52
REMARK 500 6 THR A 2 -57.01 -123.62
REMARK 500 6 TYR A 7 -55.63 -131.60
REMARK 500 6 CYS A 8 -160.97 -120.38
REMARK 500 6 GLU A 9 69.49 -119.87
REMARK 500 6 SER A 15 -50.56 -21.26
REMARK 500 6 LYS A 23 35.82 -88.87
REMARK 500 6 THR A 24 -54.95 -138.67
REMARK 500 6 HIS A 26 44.39 -99.38
REMARK 500 7 TYR A 7 -51.88 -135.53
REMARK 500 7 CYS A 8 -160.24 -116.08
REMARK 500 7 GLU A 9 64.38 -113.97
REMARK 500 7 LYS A 23 35.26 -88.39
REMARK 500 7 THR A 24 -50.41 -134.82
REMARK 500 7 HIS A 26 56.43 -103.76
REMARK 500
REMARK 500 THIS ENTRY HAS 100 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 11 0.31 SIDE CHAIN
REMARK 500 2 ARG A 11 0.30 SIDE CHAIN
REMARK 500 3 ARG A 11 0.31 SIDE CHAIN
REMARK 500 4 ARG A 11 0.30 SIDE CHAIN
REMARK 500 5 ARG A 11 0.32 SIDE CHAIN
REMARK 500 6 ARG A 11 0.29 SIDE CHAIN
REMARK 500 7 ARG A 11 0.19 SIDE CHAIN
REMARK 500 8 ARG A 11 0.30 SIDE CHAIN
REMARK 500 9 ARG A 11 0.29 SIDE CHAIN
REMARK 500 10 ARG A 11 0.20 SIDE CHAIN
REMARK 500 11 ARG A 11 0.31 SIDE CHAIN
REMARK 500 12 ARG A 11 0.30 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 111.0
REMARK 620 3 HIS A 21 NE2 112.8 110.7
REMARK 620 4 HIS A 26 NE2 110.6 109.5 101.9
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
DBREF 7ZNF A 1 29 UNP P08048 ZFY_HUMAN 570 598
SEQADV 7ZNF THR A 2 UNP P08048 PRO 571 CONFLICT
SEQADV 7ZNF LYS A 10 UNP P08048 TYR 579 CONFLICT
SEQADV 7ZNF PHE A 12 UNP P08048 SER 581 CONFLICT
SEQRES 1 A 30 LYS THR TYR GLN CYS GLN TYR CYS GLU LYS ARG PHE ALA
SEQRES 2 A 30 ASP SER SER ASN LEU LYS THR HIS ILE LYS THR LYS HIS
SEQRES 3 A 30 SER LYS GLU LYS
HET ZN A 31 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 H1 SER A 15 HIS A 26 1SEE REMARK 4 12
SHEET 1 B1 2 THR A 2 GLN A 6 0
SHEET 2 B1 2 CYS A 8 ALA A 13 -1 N PHE A 12 O TYR A 3
LINK SG CYS A 5 ZN ZN A 31 1555 1555 2.29
LINK SG CYS A 8 ZN ZN A 31 1555 1555 2.29
LINK NE2 HIS A 21 ZN ZN A 31 1555 1555 1.99
LINK NE2 HIS A 26 ZN ZN A 31 1555 1555 1.98
SITE 1 AC1 4 CYS A 5 CYS A 8 HIS A 21 HIS A 26
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 - 16 20 Bytes