Header list of 1sx1.pdb file
Complete list - 2 20 Bytes
HEADER PROTEIN TRANSPORT 30-MAR-04 1SX1
TITLE SOLUTION NMR STRUCTURE AND X-RAY ABSORPTION ANALYSIS OF THE C-TERMINAL
TITLE 2 ZINC-BINDING DOMAIN OF THE SECA ATPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SECA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL ZINC BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SOLID PHASE PEPTIDE SYNTHESIS, N-TERMINALLY
SOURCE 4 ACETYLATED. THE SEQUENCE OF THIS PEPTIDE NATURALLY EXISTS IN
SOURCE 5 ESCHERICHIA COLI.
KEYWDS ZINC, METAL ION, TETRAHEDRAL COORDINATION, NO SECONDARY STRUCTURE,
KEYWDS 2 STRUCTURAL ZINC COORDINATION, PROTEIN TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.R.DEMPSEY,M.WRONA,J.M.MOULIN,G.B.GLOOR,F.JALILEHVAND,G.LAJOIE,
AUTHOR 2 G.S.SHAW,B.H.SHILTON
REVDAT 4 02-MAR-22 1SX1 1 REMARK LINK
REVDAT 3 24-FEB-09 1SX1 1 VERSN
REVDAT 2 10-AUG-04 1SX1 1 JRNL
REVDAT 1 06-JUL-04 1SX1 0
JRNL AUTH B.R.DEMPSEY,M.WRONA,J.M.MOULIN,G.B.GLOOR,F.JALILEHVAND,
JRNL AUTH 2 G.LAJOIE,G.S.SHAW,B.H.SHILTON
JRNL TITL SOLUTION NMR STRUCTURE AND X-RAY ABSORPTION ANALYSIS OF THE
JRNL TITL 2 C-TERMINAL ZINC-BINDING DOMAIN OF THE SECA ATPASE.
JRNL REF BIOCHEMISTRY V. 43 9361 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15260479
JRNL DOI 10.1021/BI0493057
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER ET AL. (CNS), BRUNGER ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES BASED ON 317 RESTRAINTS, 274
REMARK 3 ARE NOE-DERIVED DISTANCE RESTRAINTS, 33 ARE DIHEDRAL ANGLE
REMARK 3 RESTRAINTS, AND 10 ARE RESTRAINTS FOR THE TETRAHEDRAL
REMARK 3 COORDINATION OF ZINC BY 3CYS AND 1 HIS.
REMARK 4
REMARK 4 1SX1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022056.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 7.0; 7.0
REMARK 210 IONIC STRENGTH : 50MM NACL, 5MM NAN3, 3.4MM
REMARK 210 ZNCL2; 50MM NACL, 5MM NAN3, 7MM
REMARK 210 ZNCL2
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.7MM SECA ZINC BINDING DOMAIN
REMARK 210 NA; 20MM DEUTERATED PIPES BUFFER,
REMARK 210 50MM NACL, 5MM NAN3, 0.5MM TCEP,
REMARK 210 3.4MM ZNCL2, 90% H2O, 10% D2O;
REMARK 210 3.5MM SECA ZINC BINDING DOMAIN
REMARK 210 NA; 20MM DEUTERATED PIPES BUFFER,
REMARK 210 50MM NACL, 5MM NAN3, 0.5MM TCEP,
REMARK 210 7MM ZNCL2, 90% H2O, 10% D2O;
REMARK 210 1.7MM SECA ZINC BINDING DOMAIN
REMARK 210 NA; 20MM DEUTERATED PIPES BUFFER,
REMARK 210 50MM NACL, 5MM NAN3, 0.5MM TCEP,
REMARK 210 3.4MM ZNCL2, 100% D2O; 3.5MM
REMARK 210 SECA ZINC BINDING DOMAIN NA;
REMARK 210 20MM DEUTERATED PIPES BUFFER,
REMARK 210 50MM NACL, 5MM NAN3, 0.5MM TCEP,
REMARK 210 7MM ZNCL2, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, VNMR 6.1C,
REMARK 210 PIPP/STAPP 4.3.3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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:
REMARK 210 THIS STRUCTURE WAS DETERMINED USING STANDARD TWO-DIMENSIONAL 1H
REMARK 210 NMR TECHNIQUES.
REMARK 210 THIS SET OF STRUCTURES IS THE CALCULATION OF THE FINAL FOLD OF THE
REMARK 210 DOMAIN USING RESTRAINTS FOR ZINC COORDINATION BASED ON EXAFS DATA
REMARK 210 FOR THIS DOMAIN.
REMARK 210 A SECOND SET OF STRUCTURES HAS BEEN DEPOSITED THAT SHOWS THE
REMARK 210 CALCULATION OF THE INITIAL FOLD OF THE ZBD WITHOUT USING ZINC
REMARK 210 RESTRAINTS.
REMARK 210
REMARK 210 FOR REMARK 500: THE BOND LENGTH IS SPECIFICED BY CNS AND NOT A
REMARK 210 PROBLEM WITH THE STRUCTURE REFINEMENT.
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: 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 ARG A 4 -29.54 -37.12
REMARK 500 1 CYS A 8 134.67 -38.66
REMARK 500 1 CYS A 19 -120.52 -107.19
REMARK 500 2 ARG A 4 -33.08 -34.72
REMARK 500 2 CYS A 8 133.72 -34.57
REMARK 500 2 CYS A 19 -119.73 -119.05
REMARK 500 3 ARG A 4 -29.77 -36.79
REMARK 500 3 CYS A 8 134.14 -38.77
REMARK 500 3 CYS A 19 -119.96 -104.54
REMARK 500 4 CYS A 8 135.11 -38.04
REMARK 500 4 CYS A 19 -120.05 -113.65
REMARK 500 5 CYS A 19 -120.34 -150.08
REMARK 500 6 CYS A 19 -120.28 -150.20
REMARK 500 7 CYS A 8 135.25 -38.67
REMARK 500 7 CYS A 19 -120.10 -121.96
REMARK 500 8 CYS A 8 134.78 -38.67
REMARK 500 8 TYR A 16 -70.08 -47.82
REMARK 500 8 CYS A 19 -75.66 -150.14
REMARK 500 9 CYS A 19 -112.56 -98.86
REMARK 500 10 CYS A 8 135.62 -37.67
REMARK 500 10 CYS A 19 -85.78 -107.04
REMARK 500 11 ARG A 4 -31.97 -34.99
REMARK 500 11 CYS A 8 134.31 -36.52
REMARK 500 11 CYS A 19 -120.15 -102.31
REMARK 500 12 ARG A 4 -30.08 -36.64
REMARK 500 12 CYS A 8 135.71 -38.41
REMARK 500 12 CYS A 19 -78.73 -150.02
REMARK 500 12 HIS A 20 -86.14 -105.64
REMARK 500 13 ARG A 4 -30.48 -36.52
REMARK 500 13 ASN A 5 0.32 -69.96
REMARK 500 13 CYS A 8 133.74 -39.48
REMARK 500 13 CYS A 19 -120.07 -111.62
REMARK 500 14 ARG A 4 -30.36 -36.51
REMARK 500 14 CYS A 19 -80.54 -150.39
REMARK 500 14 HIS A 20 -88.34 -105.72
REMARK 500 15 CYS A 8 135.32 -38.88
REMARK 500 15 CYS A 19 -120.03 -149.97
REMARK 500 16 ARG A 4 -29.94 -36.92
REMARK 500 16 CYS A 8 134.64 -39.08
REMARK 500 16 CYS A 19 -74.85 -150.22
REMARK 500 17 CYS A 8 135.24 -39.20
REMARK 500 17 CYS A 19 -120.71 -91.88
REMARK 500 18 ARG A 4 -30.52 -35.71
REMARK 500 18 CYS A 8 135.19 -37.75
REMARK 500 18 CYS A 19 -80.98 -110.04
REMARK 500 19 CYS A 19 -120.13 -99.85
REMARK 500 20 CYS A 19 -120.60 -150.36
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 23 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 8 SG
REMARK 620 2 CYS A 10 SG 99.3
REMARK 620 3 CYS A 19 SG 111.9 111.7
REMARK 620 4 HIS A 20 ND1 100.9 119.9 111.7
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 23
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SX0 RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE AND X-RAY ABSORPTION ANALYSIS OF THE C-
REMARK 900 TERMINAL ZINC-BINDING DOMAIN OF THE SECA ATPASE
DBREF 1SX1 A 1 22 PDB 1SX1 1SX1 1 22
SEQRES 1 A 22 LYS VAL GLY ARG ASN ASP PRO CYS PRO CYS GLY SER GLY
SEQRES 2 A 22 LYS LYS TYR LYS GLN CYS HIS GLY ARG
HET ZN A 23 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
LINK SG CYS A 8 ZN ZN A 23 1555 1555 2.36
LINK SG CYS A 10 ZN ZN A 23 1555 1555 2.36
LINK SG CYS A 19 ZN ZN A 23 1555 1555 2.36
LINK ND1 HIS A 20 ZN ZN A 23 1555 1555 2.04
SITE 1 AC1 4 CYS A 8 CYS A 10 CYS A 19 HIS A 20
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 - 2 20 Bytes