Header list of 1dvw.pdb file
Complete list - 16 20 Bytes
HEADER METAL BINDING PROTEIN 22-JAN-00 1DVW
TITLE NMR STRUCTURE OF 18 RESIDUE PEPTIDE FROM MERP PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 18 RESIDUE PEPTIDE FROM MERP PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: SYNTHETIC
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: 18 RESIDUE SYNTHETIC PEPTIDE
KEYWDS TURN, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR G.VEGLIA,F.PORCELLI,T.M.DE SILVA,A.M.PRANTNER,S.J.OPELLA
REVDAT 4 16-FEB-22 1DVW 1 REMARK LINK
REVDAT 3 24-FEB-09 1DVW 1 VERSN
REVDAT 2 21-JUN-05 1DVW 1 JRNL
REVDAT 1 23-DEC-03 1DVW 0
JRNL AUTH G.VEGLIA,F.PORCELLI,T.M.DE SILVA,A.M.PRANTNER,S.J.OPELLA
JRNL TITL THE STRUCTURE OF THE METAL-BINDING MOTIF GMTCAAC IS SIMILAR
JRNL TITL 2 IN AN 18-RESIDUE LINEAR PEPTIDE AND THE MERCURY BINDING
JRNL TITL 3 PROTEIN MERP
JRNL REF J.AM.CHEM.SOC. V. 122 2389 2000
JRNL REFN ISSN 0002-7863
JRNL DOI 10.1021/JA992908Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.840, X-PLOR 3.840
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 81 RESTRAINTS, 77 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 4 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1DVW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010420.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM PEPTIDE; 20 MM PHOSPHATE
REMARK 210 BUFFER PH=6.5; 1MM DTT.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : HYBRID DISTANCE
REMARK 210 GEOMETRY/SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10
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 LEU A 2 -141.86 50.65
REMARK 500 1 MET A 7 -161.89 56.55
REMARK 500 1 ALA A 10 28.53 46.32
REMARK 500 1 ALA A 11 -55.80 -141.79
REMARK 500 1 VAL A 16 33.19 -90.93
REMARK 500 2 MET A 7 -159.23 46.28
REMARK 500 2 THR A 8 82.25 53.98
REMARK 500 2 ALA A 10 27.97 47.24
REMARK 500 2 ALA A 11 -58.77 -141.39
REMARK 500 2 VAL A 16 31.37 -91.08
REMARK 500 3 MET A 7 -164.02 51.53
REMARK 500 3 THR A 8 75.33 54.07
REMARK 500 3 ALA A 10 28.15 46.44
REMARK 500 3 ALA A 11 -60.03 -140.79
REMARK 500 3 VAL A 16 36.00 -91.14
REMARK 500 4 PRO A 5 65.94 -68.35
REMARK 500 4 THR A 8 92.81 53.03
REMARK 500 4 CYS A 9 58.43 -169.17
REMARK 500 4 ALA A 10 28.35 46.08
REMARK 500 4 ALA A 11 -55.88 -140.66
REMARK 500 4 VAL A 16 33.51 -90.83
REMARK 500 5 PRO A 5 67.71 -69.44
REMARK 500 5 THR A 8 78.55 54.20
REMARK 500 5 CYS A 9 60.48 -152.99
REMARK 500 5 ALA A 10 27.73 46.01
REMARK 500 5 ALA A 11 -55.55 -138.61
REMARK 500 5 VAL A 16 36.12 -90.46
REMARK 500 6 LEU A 2 115.00 62.78
REMARK 500 6 ALA A 3 75.07 51.73
REMARK 500 6 MET A 7 -138.77 60.58
REMARK 500 6 THR A 8 76.67 60.66
REMARK 500 6 CYS A 9 47.04 -148.14
REMARK 500 6 ALA A 10 27.02 47.22
REMARK 500 6 ALA A 11 -53.43 -138.48
REMARK 500 6 VAL A 16 32.77 -90.82
REMARK 500 7 MET A 7 -165.53 -169.42
REMARK 500 7 THR A 8 97.61 49.18
REMARK 500 7 CYS A 9 64.90 -162.49
REMARK 500 7 ALA A 10 27.68 46.55
REMARK 500 7 ALA A 11 -61.71 -142.17
REMARK 500 7 THR A 15 -70.26 -73.26
REMARK 500 7 VAL A 16 31.64 -90.82
REMARK 500 8 LEU A 2 -178.60 56.17
REMARK 500 8 MET A 7 -157.42 52.59
REMARK 500 8 THR A 8 81.70 52.32
REMARK 500 8 CYS A 9 61.89 -153.60
REMARK 500 8 ALA A 10 28.64 46.03
REMARK 500 8 ALA A 11 -53.83 -141.61
REMARK 500 8 CYS A 12 37.41 -141.44
REMARK 500 8 VAL A 16 37.37 -90.93
REMARK 500
REMARK 500 THIS ENTRY HAS 65 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 HG A 20 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 8 N
REMARK 620 2 CYS A 9 N 62.5
REMARK 620 3 CYS A 9 SG 120.5 65.6
REMARK 620 4 CYS A 12 N 103.3 84.3 98.5
REMARK 620 5 CYS A 12 SG 78.5 128.4 160.9 72.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 20
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AFI RELATED DB: PDB
REMARK 900 RELATED ID: 1AFJ RELATED DB: PDB
DBREF 1DVW A 1 18 UNP P04129 MERP_SHIFL 25 42
SEQRES 1 A 18 THR LEU ALA VAL PRO GLY MET THR CYS ALA ALA CYS PRO
SEQRES 2 A 18 ILE THR VAL LYS LYS
HET HG A 20 1
HETNAM HG MERCURY (II) ION
FORMUL 2 HG HG 2+
LINK N THR A 8 HG HG A 20 1555 1555 2.82
LINK N CYS A 9 HG HG A 20 1555 1555 3.02
LINK SG CYS A 9 HG HG A 20 1555 1555 2.32
LINK N CYS A 12 HG HG A 20 1555 1555 3.09
LINK SG CYS A 12 HG HG A 20 1555 1555 2.33
SITE 1 AC1 4 MET A 7 THR A 8 CYS A 9 CYS A 12
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