Header list of 1liq.pdb file
Complete list - 23 20 Bytes
HEADER PROTEIN BINDING 18-APR-02 1LIQ
TITLE NON-NATIVE SOLUTION STRUCTURE OF A FRAGMENT OF THE CH1 DOMAIN OF CBP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CREB BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-27;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS
KEYWDS ZINC FINGER, PROTEIN DESIGN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.K.SHARPE,J.M.MATTHEWS,A.H.Y.KWAN,A.NEWTON,D.A.GELL,M.CROSSLEY,
AUTHOR 2 J.P.MACKAY
REVDAT 3 23-FEB-22 1LIQ 1 REMARK LINK
REVDAT 2 24-FEB-09 1LIQ 1 VERSN
REVDAT 1 29-MAY-02 1LIQ 0
JRNL AUTH B.K.SHARPE,J.M.MATTHEWS,A.H.Y.KWAN,A.NEWTON,D.A.GELL,
JRNL AUTH 2 M.CROSSLEY,J.P.MACKAY
JRNL TITL A NEW ZINC BINDING FOLD UNDERLINES THE VERSATILITY OF ZINC
JRNL TITL 2 BINDING MODULES IN PROTEIN EVOLUTION
JRNL REF STRUCTURE V. 10 639 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 12015147
JRNL DOI 10.1016/S0969-2126(02)00757-8
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), BRUNGER ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 275 UMAMBIGUOUS NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 31 SETS OF AMBIGUOUS NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS AND 110 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1LIQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015972.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 275
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4MM CBP(376-402), 0.6MM TCEP,
REMARK 210 0.6MM ZNSO4, 95% H2O, 10% D2O;
REMARK 210 0.4MM CBP(376-402), 0.6MM TCEP,
REMARK 210 0.6MM ZNSO4, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY; E
REMARK 210 -COSY
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 : 50
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 THR A 12 -81.14 -134.31
REMARK 500 1 LYS A 14 22.24 80.44
REMARK 500 1 ASN A 15 76.29 -65.19
REMARK 500 1 ALA A 25 36.65 -174.81
REMARK 500 2 THR A 12 -94.23 -145.20
REMARK 500 2 ASN A 15 76.00 -68.70
REMARK 500 2 ALA A 25 76.53 84.32
REMARK 500 3 THR A 12 -81.21 -133.30
REMARK 500 3 LYS A 14 21.66 80.33
REMARK 500 3 ASN A 15 76.10 -66.04
REMARK 500 3 GLN A 24 134.29 -171.75
REMARK 500 3 ALA A 25 37.53 -167.32
REMARK 500 4 THR A 12 -80.46 -133.60
REMARK 500 4 LYS A 14 22.37 80.13
REMARK 500 4 ASN A 15 76.21 -66.45
REMARK 500 4 CYS A 23 67.76 -114.73
REMARK 500 4 ALA A 25 144.57 -176.09
REMARK 500 5 THR A 12 -81.99 -133.47
REMARK 500 5 ASN A 15 75.53 -67.16
REMARK 500 5 ALA A 25 134.31 84.30
REMARK 500 6 THR A 12 -94.71 -142.22
REMARK 500 6 ASN A 15 75.45 -68.17
REMARK 500 6 ALA A 25 98.26 84.27
REMARK 500 7 THR A 12 -81.07 -126.38
REMARK 500 7 LYS A 14 22.39 81.73
REMARK 500 7 ASN A 15 75.71 -65.96
REMARK 500 7 ALA A 25 77.83 -176.63
REMARK 500 8 THR A 12 -80.93 -131.98
REMARK 500 8 LYS A 14 20.33 81.13
REMARK 500 8 ASN A 15 75.45 -66.84
REMARK 500 8 HIS A 22 -19.46 -142.91
REMARK 500 8 ALA A 25 119.26 -173.98
REMARK 500 9 THR A 12 -81.94 -131.83
REMARK 500 9 LYS A 14 21.25 81.20
REMARK 500 9 ASN A 15 75.63 -66.63
REMARK 500 9 ALA A 25 35.72 84.34
REMARK 500 10 THR A 12 -94.56 -142.76
REMARK 500 10 ASN A 15 75.50 -68.21
REMARK 500 10 GLN A 24 -169.60 46.25
REMARK 500 10 ALA A 25 76.75 84.29
REMARK 500 11 PRO A 8 44.91 -86.78
REMARK 500 11 HIS A 9 -46.84 -139.56
REMARK 500 11 ARG A 11 84.90 -68.15
REMARK 500 11 THR A 12 -83.09 -131.94
REMARK 500 11 ASN A 15 74.99 -67.41
REMARK 500 11 ALA A 25 85.57 84.30
REMARK 500 12 PRO A 8 44.92 -86.83
REMARK 500 12 HIS A 9 -46.99 -139.72
REMARK 500 12 THR A 12 -81.46 -131.22
REMARK 500 12 LYS A 14 21.33 81.35
REMARK 500
REMARK 500 THIS ENTRY HAS 89 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 28 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 5 SG
REMARK 620 2 CYS A 10 SG 104.4
REMARK 620 3 HIS A 19 ND1 109.7 114.3
REMARK 620 4 CYS A 23 SG 104.8 122.0 101.0
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 28
DBREF 1LIQ A 1 27 UNP Q92793 CBP_HUMAN 376 402
SEQRES 1 A 27 GLU VAL ARG ALA CYS SER LEU PRO HIS CYS ARG THR MET
SEQRES 2 A 27 LYS ASN VAL LEU ASN HIS MET THR HIS CYS GLN ALA GLY
SEQRES 3 A 27 LYS
HET ZN A 28 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 GLU A 1 CYS A 5 5 5
HELIX 2 2 ASN A 15 THR A 21 1 7
LINK SG CYS A 5 ZN ZN A 28 1555 1555 2.28
LINK SG CYS A 10 ZN ZN A 28 1555 1555 2.29
LINK ND1 HIS A 19 ZN ZN A 28 1555 1555 2.00
LINK SG CYS A 23 ZN ZN A 28 1555 1555 2.31
SITE 1 AC1 6 CYS A 5 LEU A 7 CYS A 10 HIS A 19
SITE 2 AC1 6 HIS A 22 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 - 23 20 Bytes