Header list of 1xf7.pdb file
Complete list - t 20 2 Bytes
HEADER TRANSCRIPTION 14-SEP-04 1XF7
TITLE HIGH RESOLUTION NMR STRUCTURE OF THE WILMS' TUMOR SUPPRESSOR PROTEIN
TITLE 2 (WT1) FINGER 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WILMS' TUMOR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC FINGER 3;
COMPND 5 SYNONYM: WT33; WILMS' TUMOR SUPPRESSOR PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHESIZED BY SOLID-PHASE SYNTHESIS. THE SEQUENCE
SOURCE 4 OCCURS NATURALLY HOMO SAPIENS (HUMAN). THE G28E AND T29K MUTATIONS
SOURCE 5 IMPROVE SAMPLE BEHAVIOR WITHOUT AFFECTING THE STRUCTURE
KEYWDS ZINC FINGER, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR M.J.LACHENMANN,J.E.LADBURY,J.DONG,K.HUANG,P.CAREY,M.A.WEISS
REVDAT 3 20-OCT-21 1XF7 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1XF7 1 VERSN
REVDAT 1 14-DEC-04 1XF7 0
JRNL AUTH M.J.LACHENMANN,J.E.LADBURY,J.DONG,K.HUANG,P.CAREY,M.A.WEISS
JRNL TITL WHY ZINC FINGERS PREFER ZINC: LIGAND-FIELD SYMMETRY AND THE
JRNL TITL 2 HIDDEN THERMODYNAMICS OF METAL ION SELECTIVITY
JRNL REF BIOCHEMISTRY V. 43 13910 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15518539
JRNL DOI 10.1021/BI0491999
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 4.3-5.3, X-PLOR 3.1
REMARK 3 AUTHORS : VARIAN, INC. (VNMR), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XF7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030292.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : 50MM D11-TRIS-HCL, 5.5MM ZNCL2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 5MM WT1-F3[EK]; 5MM WT1-F3[EK]
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY; 2D TOCSY; 3D
REMARK 210 -TOCSY-NOESY; 2D-ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : VXRS; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DGII STANDALONE
REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMULATED
REMARK 210 ANNEALING FOLLOWED BY RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 19 ARG A 23 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 24 ARG A 14 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
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 GLN A 9 64.43 102.39
REMARK 500 1 ARG A 23 24.31 -71.60
REMARK 500 1 GLU A 28 -62.22 -18.67
REMARK 500 2 LYS A 6 38.55 -99.19
REMARK 500 2 THR A 7 -42.62 -131.78
REMARK 500 2 GLN A 9 51.04 85.17
REMARK 500 2 ARG A 23 44.90 -80.91
REMARK 500 2 THR A 26 44.97 -108.21
REMARK 500 3 LYS A 6 41.48 -100.55
REMARK 500 3 THR A 7 -48.38 -135.92
REMARK 500 3 GLN A 9 64.31 69.70
REMARK 500 3 ARG A 23 27.20 -77.07
REMARK 500 3 GLU A 28 -58.36 -123.29
REMARK 500 4 GLN A 9 58.66 97.20
REMARK 500 5 LYS A 6 37.56 -92.26
REMARK 500 5 GLN A 9 55.77 99.41
REMARK 500 5 ARG A 23 39.43 -79.04
REMARK 500 5 THR A 26 59.20 -111.36
REMARK 500 5 GLU A 28 130.59 -1.10
REMARK 500 6 LYS A 6 40.36 -100.05
REMARK 500 6 THR A 7 -47.12 -134.84
REMARK 500 6 ARG A 23 42.19 -82.81
REMARK 500 6 THR A 26 56.04 -114.45
REMARK 500 7 PRO A 2 154.61 -34.35
REMARK 500 7 THR A 7 -38.18 -131.57
REMARK 500 7 GLN A 9 60.17 98.33
REMARK 500 7 ARG A 23 40.29 -90.46
REMARK 500 7 GLU A 28 47.82 -103.32
REMARK 500 8 LYS A 6 34.31 -99.18
REMARK 500 8 GLN A 9 51.74 104.41
REMARK 500 8 ARG A 23 39.02 -82.85
REMARK 500 8 GLU A 28 114.85 -23.91
REMARK 500 9 GLN A 9 52.36 101.58
REMARK 500 9 ARG A 23 43.13 -79.42
REMARK 500 9 THR A 26 54.78 -118.43
REMARK 500 10 GLN A 9 60.87 67.65
REMARK 500 10 ARG A 23 -8.20 -58.69
REMARK 500 10 GLU A 28 51.05 -118.59
REMARK 500 11 LYS A 6 42.97 -106.47
REMARK 500 11 GLN A 9 55.83 89.35
REMARK 500 11 ARG A 23 37.97 -76.93
REMARK 500 11 THR A 26 46.39 114.48
REMARK 500 12 THR A 7 -39.51 -135.08
REMARK 500 12 GLN A 9 61.51 103.48
REMARK 500 13 LYS A 6 33.58 -87.13
REMARK 500 13 GLN A 9 60.27 90.03
REMARK 500 13 GLU A 28 -94.47 -13.98
REMARK 500 14 LYS A 6 40.47 -97.18
REMARK 500 14 THR A 7 -46.98 -131.60
REMARK 500 15 HIS A 25 -50.90 -124.26
REMARK 500
REMARK 500 THIS ENTRY HAS 141 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 1 PRO A 2 3 149.12
REMARK 500 LYS A 1 PRO A 2 6 148.91
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 10 0.28 SIDE CHAIN
REMARK 500 1 ARG A 14 0.32 SIDE CHAIN
REMARK 500 1 ARG A 23 0.23 SIDE CHAIN
REMARK 500 2 ARG A 10 0.29 SIDE CHAIN
REMARK 500 2 ARG A 14 0.17 SIDE CHAIN
REMARK 500 2 ARG A 23 0.20 SIDE CHAIN
REMARK 500 3 ARG A 10 0.27 SIDE CHAIN
REMARK 500 3 ARG A 14 0.27 SIDE CHAIN
REMARK 500 3 ARG A 23 0.28 SIDE CHAIN
REMARK 500 4 ARG A 10 0.31 SIDE CHAIN
REMARK 500 4 ARG A 14 0.26 SIDE CHAIN
REMARK 500 4 ARG A 23 0.30 SIDE CHAIN
REMARK 500 5 ARG A 10 0.30 SIDE CHAIN
REMARK 500 5 ARG A 14 0.12 SIDE CHAIN
REMARK 500 5 ARG A 23 0.27 SIDE CHAIN
REMARK 500 6 ARG A 10 0.15 SIDE CHAIN
REMARK 500 6 ARG A 14 0.27 SIDE CHAIN
REMARK 500 6 ARG A 23 0.32 SIDE CHAIN
REMARK 500 7 ARG A 10 0.25 SIDE CHAIN
REMARK 500 7 ARG A 14 0.30 SIDE CHAIN
REMARK 500 7 ARG A 23 0.27 SIDE CHAIN
REMARK 500 8 ARG A 10 0.23 SIDE CHAIN
REMARK 500 8 ARG A 14 0.30 SIDE CHAIN
REMARK 500 8 ARG A 23 0.32 SIDE CHAIN
REMARK 500 9 ARG A 10 0.28 SIDE CHAIN
REMARK 500 9 ARG A 14 0.30 SIDE CHAIN
REMARK 500 9 ARG A 23 0.32 SIDE CHAIN
REMARK 500 10 ARG A 10 0.30 SIDE CHAIN
REMARK 500 10 ARG A 14 0.30 SIDE CHAIN
REMARK 500 10 ARG A 23 0.30 SIDE CHAIN
REMARK 500 11 ARG A 10 0.31 SIDE CHAIN
REMARK 500 11 ARG A 14 0.26 SIDE CHAIN
REMARK 500 11 ARG A 23 0.29 SIDE CHAIN
REMARK 500 12 ARG A 10 0.21 SIDE CHAIN
REMARK 500 12 ARG A 14 0.30 SIDE CHAIN
REMARK 500 12 ARG A 23 0.25 SIDE CHAIN
REMARK 500 13 ARG A 10 0.30 SIDE CHAIN
REMARK 500 13 ARG A 14 0.30 SIDE CHAIN
REMARK 500 13 ARG A 23 0.29 SIDE CHAIN
REMARK 500 14 ARG A 10 0.31 SIDE CHAIN
REMARK 500 14 ARG A 14 0.28 SIDE CHAIN
REMARK 500 14 ARG A 23 0.20 SIDE CHAIN
REMARK 500 15 ARG A 10 0.31 SIDE CHAIN
REMARK 500 15 ARG A 14 0.20 SIDE CHAIN
REMARK 500 15 ARG A 23 0.32 SIDE CHAIN
REMARK 500 16 ARG A 10 0.30 SIDE CHAIN
REMARK 500 16 ARG A 14 0.29 SIDE CHAIN
REMARK 500 16 ARG A 23 0.13 SIDE CHAIN
REMARK 500 17 ARG A 10 0.31 SIDE CHAIN
REMARK 500 17 ARG A 14 0.21 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 117 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 30 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 5 SG
REMARK 620 2 CYS A 8 SG 109.6
REMARK 620 3 HIS A 21 NE2 109.9 110.7
REMARK 620 4 HIS A 25 NE2 108.6 112.6 105.4
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 30
DBREF 1XF7 A 1 29 UNP P19544 WT1_HUMAN 381 409
SEQADV 1XF7 GLU A 28 UNP P19544 LYS 408 ENGINEERED MUTATION
SEQADV 1XF7 LYS A 29 UNP P19544 THR 409 ENGINEERED MUTATION
SEQRES 1 A 29 LYS PRO PHE GLN CYS LYS THR CYS GLN ARG LYS PHE SER
SEQRES 2 A 29 ARG SER ASP HIS LEU LYS THR HIS THR ARG THR HIS THR
SEQRES 3 A 29 GLY GLU LYS
HET ZN A 30 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ARG A 14 ARG A 23 1 10
SHEET 1 A 2 PHE A 3 GLN A 4 0
SHEET 2 A 2 LYS A 11 PHE A 12 -1 O PHE A 12 N PHE A 3
LINK SG CYS A 5 ZN ZN A 30 1555 1555 2.29
LINK SG CYS A 8 ZN ZN A 30 1555 1555 2.30
LINK NE2 HIS A 21 ZN ZN A 30 1555 1555 1.99
LINK NE2 HIS A 25 ZN ZN A 30 1555 1555 2.00
SITE 1 AC1 4 CYS A 5 CYS A 8 HIS A 21 HIS A 25
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 - t 20 2 Bytes