Header list of 1ak8.pdb file
Complete list - b 16 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 29-MAY-97 1AK8
TITLE NMR SOLUTION STRUCTURE OF CERIUM-LOADED CALMODULIN AMINO-TERMINAL
TITLE 2 DOMAIN (CE2-TR1C), 23 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, TR1C;
COMPND 5 SYNONYM: CALMODULIN CERIUM TR1C-DOMAIN, RESIDUES 1 - 75;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: CERIUM-LOADED N-TERMINAL DOMAIN OF VERTEBRATE
COMPND 8 CALMODULIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: TESTIS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SG20043;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PLCB1
KEYWDS CERIUM-LOADED, CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 23
AUTHOR D.BENTROP,I.BERTINI,M.A.CREMONINI,S.FORSEN,C.LUCHINAT,A.MALMENDAL
REVDAT 4 16-FEB-22 1AK8 1 REMARK
REVDAT 3 24-FEB-09 1AK8 1 VERSN
REVDAT 2 01-SEP-99 1AK8 1 JRNL
REVDAT 1 17-SEP-97 1AK8 0
JRNL AUTH D.BENTROP,I.BERTINI,M.A.CREMONINI,S.FORSEN,C.LUCHINAT,
JRNL AUTH 2 A.MALMENDAL
JRNL TITL SOLUTION STRUCTURE OF THE PARAMAGNETIC COMPLEX OF THE
JRNL TITL 2 N-TERMINAL DOMAIN OF CALMODULIN WITH TWO CE3+ IONS BY 1H
JRNL TITL 3 NMR.
JRNL REF BIOCHEMISTRY V. 36 11605 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9305950
JRNL DOI 10.1021/BI971022+
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PSEUDYANA
REMARK 3 AUTHORS : CREMONINI
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE CALCULATIONS WERE
REMARK 3 PERFORMED ACCORDING TO A RECENTLY INTRODUCED TORSION ANGLE
REMARK 3 DYNAMICS (TAD) APPROACH USING THE DYANA PROGRAM PACKAGE (GUNTERT
REMARK 3 ET AL., 1996). PSEUDOCONTACT SHIFTS WERE INTRODUCED AS
REMARK 3 CONSTRAINTS USING THE NEWLY DEVELOPED PSEUDYANA MODULE (BANCI ET
REMARK 3 AL., 1997). THE OVERALL STRATEGY OF STRUCTURE COMPUTATION
REMARK 3 COMPRISED THE FOLLOWING SUBSEQUENT STEPS:
REMARK 4
REMARK 4 1AK8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170919.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; CLEAN-TOCSY; DQF-COSY; 1D
REMARK 210 NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 300 MHZ
REMARK 210 SPECTROMETER MODEL : DRX 500; AC-P 300
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, PSEUDYANA
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 23
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 LOWEST TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 H ILE A 27 O ILE A 63 1.49
REMARK 500 O THR A 34 H ARG A 37 1.57
REMARK 500 O LEU A 4 HG1 THR A 5 1.59
REMARK 500 ND2 ASN A 60 CE CE A 77 2.09
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 GLN A 3 142.88 179.55
REMARK 500 1 LEU A 4 -170.80 -56.70
REMARK 500 1 THR A 5 -152.82 59.07
REMARK 500 1 THR A 28 -154.32 -79.55
REMARK 500 1 THR A 34 -68.90 -96.06
REMARK 500 1 ASN A 42 72.09 177.27
REMARK 500 1 ASP A 64 -169.27 -103.40
REMARK 500 1 ARG A 74 -91.67 -42.79
REMARK 500 2 ALA A 1 135.78 177.49
REMARK 500 2 ASP A 2 104.94 172.21
REMARK 500 2 GLN A 3 127.22 -176.60
REMARK 500 2 THR A 28 -151.96 -72.23
REMARK 500 2 THR A 34 -61.10 -94.87
REMARK 500 2 LEU A 39 -77.94 -100.81
REMARK 500 2 ASN A 42 73.39 -167.12
REMARK 500 2 ASP A 64 -169.70 -112.32
REMARK 500 2 ARG A 74 59.26 -109.52
REMARK 500 3 ALA A 1 103.21 164.69
REMARK 500 3 ASP A 2 29.14 -162.34
REMARK 500 3 GLN A 3 119.01 -166.42
REMARK 500 3 LEU A 4 178.40 -53.94
REMARK 500 3 THR A 28 -152.30 -82.80
REMARK 500 3 LEU A 39 -46.33 -146.44
REMARK 500 3 ASN A 42 64.66 177.61
REMARK 500 3 ASP A 64 -167.38 -108.53
REMARK 500 3 LEU A 69 -38.34 -39.74
REMARK 500 4 ALA A 1 -99.96 -118.68
REMARK 500 4 ASP A 2 108.01 169.27
REMARK 500 4 GLN A 3 126.19 175.47
REMARK 500 4 GLU A 7 -39.35 -39.65
REMARK 500 4 THR A 28 -151.35 -80.18
REMARK 500 4 LEU A 39 24.39 -154.73
REMARK 500 4 ASN A 42 65.23 176.36
REMARK 500 5 ALA A 1 79.71 165.05
REMARK 500 5 ASP A 2 46.83 179.37
REMARK 500 5 GLN A 3 118.52 -161.61
REMARK 500 5 ASP A 22 -85.31 -114.03
REMARK 500 5 THR A 28 -150.60 -78.10
REMARK 500 5 LEU A 39 -47.51 -138.07
REMARK 500 5 ASN A 42 68.43 176.41
REMARK 500 5 ASP A 56 89.45 -155.07
REMARK 500 5 ASP A 64 -168.11 -111.75
REMARK 500 5 ARG A 74 63.03 -113.88
REMARK 500 6 ALA A 1 49.40 -176.61
REMARK 500 6 THR A 5 161.76 50.97
REMARK 500 6 GLU A 6 -54.73 68.63
REMARK 500 6 ALA A 10 -37.34 -38.71
REMARK 500 6 THR A 28 -152.32 -88.37
REMARK 500 6 ASN A 42 68.75 170.47
REMARK 500 6 THR A 44 161.20 -44.64
REMARK 500
REMARK 500 THIS ENTRY HAS 201 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: EF1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: EF-HAND METAL BINDING LOOP CE BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: EF2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: EF-HAND METAL BINDING LOOP CE BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CE A 76
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CE A 77
DBREF 1AK8 A 1 75 UNP P62157 CALM_BOVIN 1 75
SEQRES 1 A 76 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 A 76 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 A 76 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 A 76 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 A 76 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 A 76 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS
HET CE A 76 1
HET CE A 77 1
HETNAM CE CERIUM (III) ION
FORMUL 2 CE 2(CE 3+)
HELIX 1 1 THR A 5 PHE A 19 5 15
HELIX 2 2 LYS A 30 LEU A 39 1 10
HELIX 3 3 GLU A 45 GLU A 54 1 10
HELIX 4 4 PHE A 65 ALA A 73 1 9
SITE 1 EF1 12 ASP A 20 LYS A 21 ASP A 22 GLY A 23
SITE 2 EF1 12 ASP A 24 GLY A 25 THR A 26 ILE A 27
SITE 3 EF1 12 THR A 28 THR A 29 LYS A 30 GLU A 31
SITE 1 EF2 12 ASP A 56 ALA A 57 ASP A 58 GLY A 59
SITE 2 EF2 12 ASN A 60 GLY A 61 THR A 62 ILE A 63
SITE 3 EF2 12 ASP A 64 PHE A 65 PRO A 66 GLU A 67
SITE 1 AC1 5 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 5 GLU A 31
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 ASP A 64 GLU A 67
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 - b 16 2 Bytes