Header list of 1wo5.pdb file
Complete list - 10 20 Bytes
HEADER TRANSFERASE 12-AUG-04 1WO5
TITLE SOLUTION STRUCTURE OF DESIGNED FUNCTIONAL FINGER 2 (DFF2): DESIGNED
TITLE 2 MUTANT BASED ON NON-NATIVE CHANCE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CREB BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CBP;
COMPND 5 EC: 2.3.1.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE
SOURCE 4 OF THE PEPTIDE IS NATURALLY IN HOMO SAPIENS (HUMAN).
KEYWDS ZINC FINGER, PROTEIN DESIGN, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.K.SHARPE,C.K.LIEW,J.A.WILCE,M.CROSSLEY,J.M.MATTHEWS,J.P.MACKAY
REVDAT 3 10-NOV-21 1WO5 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1WO5 1 VERSN
REVDAT 1 08-MAR-05 1WO5 0
JRNL AUTH B.K.SHARPE,C.K.LIEW,A.H.KWAN,J.A.WILCE,M.CROSSLEY,
JRNL AUTH 2 J.M.MATTHEWS,J.P.MACKAY
JRNL TITL ASSESSMENT OF THE ROBUSTNESS OF A SERENDIPITOUS ZINC BINDING
JRNL TITL 2 FOLD: MUTAGENESIS AND PROTEIN GRAFTING
JRNL REF STRUCTURE V. 13 257 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 15698569
JRNL DOI 10.1016/J.STR.2004.12.007
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 196
REMARK 3 UNAMBIGUOUS NOE-DERIVED DISTANCE RESTRAINTS AND 101 DIHEDRAL
REMARK 3 ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1WO5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000023803.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 275
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.3MM DFF2, 0.5MM TCEP, 1MM
REMARK 210 ZNSO4, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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: 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 PHE A 6 31.31 -98.21
REMARK 500 1 LYS A 8 -74.97 -95.10
REMARK 500 1 ALA A 12 35.27 -85.67
REMARK 500 1 CYS A 23 30.86 -144.97
REMARK 500 1 ALA A 24 -169.24 -79.76
REMARK 500 2 VAL A 9 49.61 -91.91
REMARK 500 2 CYS A 10 -66.20 -156.49
REMARK 500 2 VAL A 16 -65.30 -105.12
REMARK 500 3 VAL A 2 51.05 -91.21
REMARK 500 3 ALA A 12 35.14 -85.60
REMARK 500 4 VAL A 2 51.18 -90.99
REMARK 500 4 CYS A 10 -66.80 -95.04
REMARK 500 4 ALA A 12 35.14 -85.63
REMARK 500 4 VAL A 16 -63.35 -97.82
REMARK 500 4 CYS A 23 34.68 -143.55
REMARK 500 4 ALA A 24 171.57 -58.73
REMARK 500 5 CYS A 10 -66.98 -95.13
REMARK 500 6 VAL A 2 46.93 -94.01
REMARK 500 6 VAL A 9 51.52 -90.47
REMARK 500 6 CYS A 10 -57.08 -158.61
REMARK 500 6 ALA A 12 35.17 -85.70
REMARK 500 6 CYS A 23 30.98 -143.57
REMARK 500 7 VAL A 2 48.17 -92.94
REMARK 500 7 CYS A 10 -61.99 -93.17
REMARK 500 7 ALA A 12 35.17 -85.65
REMARK 500 7 CYS A 23 32.86 -143.61
REMARK 500 8 VAL A 2 49.67 -92.06
REMARK 500 8 CYS A 10 -53.22 -162.51
REMARK 500 8 ALA A 12 35.10 -85.61
REMARK 500 8 CYS A 23 31.02 -143.62
REMARK 500 9 VAL A 2 40.52 -96.75
REMARK 500 9 CYS A 10 -66.69 -90.33
REMARK 500 9 ALA A 12 35.28 -85.70
REMARK 500 9 CYS A 23 30.99 -143.60
REMARK 500 10 VAL A 2 47.04 -94.72
REMARK 500 10 ALA A 12 35.18 -85.74
REMARK 500 11 VAL A 2 52.41 -95.07
REMARK 500 11 ALA A 12 35.18 -85.62
REMARK 500 12 VAL A 2 43.11 -96.07
REMARK 500 12 ALA A 12 35.09 -85.59
REMARK 500 13 VAL A 2 41.24 -96.28
REMARK 500 13 ALA A 12 35.12 -85.69
REMARK 500 13 CYS A 23 32.22 -143.65
REMARK 500 14 CYS A 10 -65.07 -93.77
REMARK 500 14 ALA A 12 35.28 -85.62
REMARK 500 14 CYS A 23 31.19 -143.59
REMARK 500 15 VAL A 9 40.20 -96.96
REMARK 500 15 CYS A 10 -57.10 -145.20
REMARK 500 15 ALA A 12 35.09 -85.65
REMARK 500 16 VAL A 9 45.89 -94.40
REMARK 500
REMARK 500 THIS ENTRY HAS 77 RAMACHANDRAN OUTLIERS.
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 26 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 5 SG
REMARK 620 2 CYS A 10 SG 106.4
REMARK 620 3 HIS A 19 ND1 111.7 116.3
REMARK 620 4 CYS A 23 SG 109.0 112.5 100.9
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 26
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LIQ RELATED DB: PDB
REMARK 900 WILD-TYPE SEQUENCE OF NON-NATIVE CHANCE DOMAIN
REMARK 900 RELATED ID: 1WO3 RELATED DB: PDB
REMARK 900 MINIMAL MUTANT 1 (MM1): MULTIPLE ALANINE MUTANT OF CHANCE
REMARK 900 RELATED ID: 1WO4 RELATED DB: PDB
REMARK 900 MINIMAL MUTANT 2 (MM2): MULTIPLE ALANINE MUTANT OF CHANCE
REMARK 900 RELATED ID: 1WO6 RELATED DB: PDB
REMARK 900 DESIGNED FUNCTIONAL FINGER 5 (DFF5)
REMARK 900 RELATED ID: 1WO7 RELATED DB: PDB
REMARK 900 DESIGNED FUNCTIONAL FINGER 7 (DFF7)
DBREF 1WO5 A 1 25 UNP Q92793 CBP_HUMAN 376 400
SEQADV 1WO5 ARG A 1 UNP Q92793 GLU 376 ENGINEERED MUTATION
SEQADV 1WO5 ILE A 3 UNP Q92793 ARG 378 ENGINEERED MUTATION
SEQADV 1WO5 PHE A 6 UNP Q92793 SER 381 ENGINEERED MUTATION
SEQADV 1WO5 LYS A 8 UNP Q92793 PRO 383 ENGINEERED MUTATION
SEQADV 1WO5 VAL A 9 UNP Q92793 HIS 384 ENGINEERED MUTATION
SEQADV 1WO5 ALA A 11 UNP Q92793 ARG 386 ENGINEERED MUTATION
SEQADV 1WO5 ALA A 12 UNP Q92793 THR 387 ENGINEERED MUTATION
SEQADV 1WO5 ALA A 13 UNP Q92793 MET 388 ENGINEERED MUTATION
SEQADV 1WO5 ALA A 14 UNP Q92793 LYS 389 ENGINEERED MUTATION
SEQADV 1WO5 ALA A 17 UNP Q92793 LEU 392 ENGINEERED MUTATION
SEQADV 1WO5 ALA A 18 UNP Q92793 ASN 393 ENGINEERED MUTATION
SEQADV 1WO5 ALA A 24 UNP Q92793 GLN 399 ENGINEERED MUTATION
SEQADV 1WO5 LYS A 25 UNP Q92793 ALA 400 ENGINEERED MUTATION
SEQRES 1 A 25 ARG VAL ILE ALA CYS PHE LEU LYS VAL CYS ALA ALA ALA
SEQRES 2 A 25 ALA ASN VAL ALA ALA HIS MET THR HIS CYS ALA LYS
HET ZN A 26 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 CYS A 10 ALA A 14 5 5
HELIX 2 2 ASN A 15 MET A 20 1 6
HELIX 3 3 THR A 21 CYS A 23 5 3
LINK SG CYS A 5 ZN ZN A 26 1555 1555 2.31
LINK SG CYS A 10 ZN ZN A 26 1555 1555 2.30
LINK ND1 HIS A 19 ZN ZN A 26 1555 1555 2.01
LINK SG CYS A 23 ZN ZN A 26 1555 1555 2.31
SITE 1 AC1 4 CYS A 5 CYS A 10 HIS A 19 CYS A 23
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 - 10 20 Bytes