Header list of 1n65.pdb file
Complete list - t 27 2 Bytes
HEADER METAL BINDING PROTEIN 08-NOV-02 1N65
TITLE FAMILY OF NMR SOLUTION STRUCTURES OF CA CE CALBINDIN D9K IN
TITLE 2 DENATURATING CONDITIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VITAMIN D-DEPENDENT CALCIUM-BINDING PROTEIN, INTESTINAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CABP, CALBINDIN D9K;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: CALB3 OR S100D;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CALCIUM BINDING PROTEINS, NMR SOLUTION STRUCTURE, PARAMAGNETISM-BASED
KEYWDS 2 CONSTRAINTS, DENATURATING AGENTS, GUANIDINIUM CHLORIDE, METAL
KEYWDS 3 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.JIMENEZ,L.POGGI,M.PICCIOLI
REVDAT 3 27-OCT-21 1N65 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1N65 1 VERSN
REVDAT 1 18-NOV-03 1N65 0
JRNL AUTH B.JIMENEZ,L.POGGI,M.PICCIOLI
JRNL TITL MONITORING THE EARLY STEPS OF UNFOLDING OF DICALCIUM AND
JRNL TITL 2 MONO-CE(3+)-SUBSTITUTED FORMS OF P43M CALBINDIN D(9K).
JRNL REF BIOCHEMISTRY V. 42 13066 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14596622
JRNL DOI 10.1021/BI034638+
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PARAMAGNETIC-DYANA 1.0, PSEUDYANA 3.1
REMARK 3 AUTHORS : BARBIERI R., BERTINI I., CAVALLARO G., LEE Y.-M.,
REMARK 3 LUCHINAT C., ROSATO A. (PARAMAGNETIC-DYANA),
REMARK 3 L.BANCI,I.BERTINI,M.A.CREMONINI,G.GORI SAVELLINI,
REMARK 3 C.LUCHINAT,K.WUTHRICH AND P.GUNTERT (PSEUDYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N65 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017566.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 2M GUANIDINIUM CHLORIDE
REMARK 210 (GMDHCL); PURE WATER
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : UNIFORM LABELING WITH 15N,
REMARK 210 H2O/D20 90/10; UNIFORM LABELING
REMARK 210 WITH 15N, H2O/D20 90/10
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-15N HSQC; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ; 700 MHZ; 600
REMARK 210 MHZ; 400 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TAD SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NOESY CONSTRAINTS WERE OBTAINED ON THE NATIVE FORM OF THE
REMARK 210 PROTEIN, WHILE PARAMAGNETIC CONSTRAINTS WERE COLLECTED IN THE
REMARK 210 PRESENCE OF 2M GUANIDINIUM CHLORIDE
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 ND2 ASN A 56 CE CE A 76 0.33
REMARK 500 HD22 ASN A 56 CE CE A 76 0.93
REMARK 500 HD21 ASN A 56 CE CE A 76 1.07
REMARK 500 CG ASN A 56 CE CE A 76 1.47
REMARK 500 O LEU A 49 H LEU A 53 1.52
REMARK 500 H LEU A 23 O VAL A 61 1.52
REMARK 500 O GLU A 11 H ALA A 15 1.55
REMARK 500 O SER A 24 H LEU A 28 1.56
REMARK 500 O GLU A 5 H ILE A 9 1.57
REMARK 500 O PHE A 66 H LEU A 69 1.58
REMARK 500 O PHE A 63 H GLN A 67 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 19 175.44 -49.63
REMARK 500 1 ASP A 54 93.36 -64.13
REMARK 500 1 LYS A 55 55.97 -112.68
REMARK 500 1 ASP A 58 -50.99 -162.20
REMARK 500 1 GLU A 60 144.49 -177.87
REMARK 500 2 ASP A 19 175.44 -49.63
REMARK 500 2 ASP A 54 93.36 -64.13
REMARK 500 2 LYS A 55 55.97 -112.68
REMARK 500 2 ASP A 58 -50.99 -162.20
REMARK 500 2 GLU A 60 144.49 -177.87
REMARK 500 3 ASP A 19 176.46 -52.31
REMARK 500 3 ASP A 58 16.07 59.77
REMARK 500 3 GLU A 60 158.29 170.39
REMARK 500 4 ASP A 19 176.46 -52.31
REMARK 500 4 ASP A 58 16.07 59.77
REMARK 500 4 GLU A 60 158.29 170.39
REMARK 500 5 ASP A 19 164.34 -45.47
REMARK 500 5 ASP A 54 -163.18 -74.97
REMARK 500 5 LYS A 55 72.66 80.66
REMARK 500 5 ASN A 56 57.16 176.47
REMARK 500 5 ASP A 58 -58.00 -149.44
REMARK 500 6 ASP A 19 164.34 -45.47
REMARK 500 6 ASP A 54 -163.18 -74.97
REMARK 500 6 LYS A 55 72.66 80.66
REMARK 500 6 ASN A 56 57.16 176.47
REMARK 500 6 ASP A 58 -58.00 -149.44
REMARK 500 7 ASP A 19 165.90 -46.86
REMARK 500 7 ASN A 56 -58.82 -154.72
REMARK 500 8 ASP A 19 165.90 -46.86
REMARK 500 8 ASN A 56 -58.82 -154.72
REMARK 500 9 ASP A 19 160.32 -43.92
REMARK 500 9 LYS A 55 70.10 -117.12
REMARK 500 9 ASN A 56 -55.27 -147.99
REMARK 500 9 ASP A 58 -56.54 -157.22
REMARK 500 10 ASP A 19 160.32 -43.92
REMARK 500 10 LYS A 55 70.10 -117.12
REMARK 500 10 ASN A 56 -55.27 -147.99
REMARK 500 10 ASP A 58 -56.54 -157.22
REMARK 500 11 ASP A 19 157.20 -41.10
REMARK 500 11 LYS A 55 95.94 85.05
REMARK 500 11 ASN A 56 -50.73 174.07
REMARK 500 11 ASP A 58 -58.98 -150.13
REMARK 500 11 SER A 62 152.83 -48.57
REMARK 500 12 ASP A 19 157.20 -41.10
REMARK 500 12 LYS A 55 95.94 85.05
REMARK 500 12 ASN A 56 -50.73 174.07
REMARK 500 12 ASP A 58 -58.98 -150.13
REMARK 500 12 SER A 62 152.83 -48.57
REMARK 500 13 ASP A 19 163.80 -46.28
REMARK 500 13 ASP A 54 99.38 -68.77
REMARK 500
REMARK 500 THIS ENTRY HAS 88 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CE A 76
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KSM RELATED DB: PDB
REMARK 900 RELATED ID: 1KQV RELATED DB: PDB
DBREF 1N65 A 1 75 UNP P02633 S100G_BOVIN 4 78
SEQADV 1N65 MET A 43 UNP P02633 PRO 46 ENGINEERED MUTATION
SEQRES 1 A 75 LYS SER PRO GLU GLU LEU LYS GLY ILE PHE GLU LYS TYR
SEQRES 2 A 75 ALA ALA LYS GLU GLY ASP PRO ASN GLN LEU SER LYS GLU
SEQRES 3 A 75 GLU LEU LYS LEU LEU LEU GLN THR GLU PHE PRO SER LEU
SEQRES 4 A 75 LEU LYS GLY MET SER THR LEU ASP GLU LEU PHE GLU GLU
SEQRES 5 A 75 LEU ASP LYS ASN GLY ASP GLY GLU VAL SER PHE GLU GLU
SEQRES 6 A 75 PHE GLN VAL LEU VAL LYS LYS ILE SER GLN
HET CE A 76 1
HETNAM CE CERIUM (III) ION
FORMUL 2 CE CE 3+
HELIX 1 1 SER A 2 ALA A 15 1 14
HELIX 2 2 SER A 24 GLU A 35 1 12
HELIX 3 3 PRO A 37 GLY A 42 1 6
HELIX 4 4 THR A 45 ASP A 54 1 10
HELIX 5 5 PHE A 63 GLN A 75 1 13
SHEET 1 A 2 GLN A 22 LEU A 23 0
SHEET 2 A 2 VAL A 61 SER A 62 -1 O VAL A 61 N LEU A 23
SITE 1 AC1 5 ASP A 54 ASN A 56 ASP A 58 GLU A 60
SITE 2 AC1 5 GLU A 65
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 - t 27 2 Bytes