Header list of 1f70.pdb file
Complete list - 16 20 Bytes
HEADER TRANSPORT PROTEIN 24-JUN-00 1F70
TITLE REFINED SOLUTION STRUCTURE OF CALMODULIN N-TERMINAL DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PTNCO12
KEYWDS CALCIUM BINDING, EF HANDS, FOUR-HELIX BUNDLE, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR J.CHOU,S.LI,A.BAX
REVDAT 5 16-FEB-22 1F70 1 REMARK
REVDAT 4 24-FEB-09 1F70 1 VERSN
REVDAT 3 01-APR-03 1F70 1 JRNL
REVDAT 2 04-APR-01 1F70 1 JRNL
REVDAT 1 22-SEP-00 1F70 0
JRNL AUTH J.J.CHOU,S.LI,A.BAX
JRNL TITL STUDY OF CONFORMATIONAL REARRANGEMENT AND REFINEMENT OF
JRNL TITL 2 STRUCTURAL HOMOLOGY MODELS BY THE USE OF HETERONUCLEAR
JRNL TITL 3 DIPOLAR COUPLINGS.
JRNL REF J.BIOMOL.NMR V. 18 217 2000
JRNL REFN ISSN 0925-2738
JRNL PMID 11142512
JRNL DOI 10.1023/A:1026563923774
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.84
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F70 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011321.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM CALMODULIN U-15N,13C; 5 MM
REMARK 210 HEPE BUFFER, 100 MM KCL; 1 MM
REMARK 210 CALMODULIN U-15N,13C; 5 MM HEPE
REMARK 210 BUFFER, 100 MM KCL; 21 MG/ML
REMARK 210 FILAMENTOUS PHAGE PF1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D IPAP-HSQC (NO H1 DECOUPLING);
REMARK 210 3D CT-(H)CA(CO)NH (NO H1
REMARK 210 DECOUPLING); 3D HNCO (NO CA
REMARK 210 DECOUPLING)
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.8, NMRDRAW 1.8
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS REFINED USING PREVIOUS NMR RESTRAINTS
REMARK 210 AND NEWLY MEASURED DIPOLAR COUPLINGS
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 OD2 ASP A 56 H GLY A 61 1.55
REMARK 500 OD2 ASP A 20 H GLY A 25 1.59
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 ASP A 2 83.10 -58.51
REMARK 500 2 ASP A 2 83.97 -173.54
REMARK 500 3 ASP A 2 83.10 -58.51
REMARK 500 4 ASP A 2 83.67 -58.64
REMARK 500 5 ASP A 2 83.81 -169.67
REMARK 500 6 ASP A 2 83.81 -169.67
REMARK 500 8 ASP A 2 83.11 -58.51
REMARK 500 10 ASP A 2 83.46 -58.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CFC RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF FULL-LENGTH CALMODULIN WITHOUT DIPOLAR COUPLING
REMARK 900 REFINEMENT
REMARK 900 RELATED ID: 1DMO RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF FULL-LENGTH CALMODULIN WITHOUT DIPOLAR COUPLING
REMARK 900 REFINEMENT
REMARK 900 RELATED ID: 1F71 RELATED DB: PDB
REMARK 900 C-TERMINAL DOMAIN OF CALMODULIN REFINED WITH DIPOLAR COUPLINGS
DBREF 1F70 A 2 76 UNP P62155 CALM_XENLA 2 76
SEQRES 1 A 76 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 76 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 76 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 76 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 76 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 76 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET
HELIX 1 1 THR A 5 PHE A 19 1 15
HELIX 2 2 GLU A 31 GLY A 40 1 10
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 PHE A 65 MET A 76 1 12
SHEET 1 A 2 THR A 26 THR A 28 0
SHEET 2 A 2 THR A 62 ASP A 64 -1 N ILE A 63 O ILE A 27
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