Header list of 1kqv.pdb file
Complete list - t 27 2 Bytes
HEADER METAL BINDING PROTEIN 08-JAN-02 1KQV
TITLE FAMILY OF NMR SOLUTION STRUCTURES OF CA LN CALBINDIN D9K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VITAMIN D-DEPENDENT CALCIUM-BINDING PROTEIN;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CALCIUM BINDING PROTEINS, NMR SOLUTION STRUCTURE, PARAMAGNETISM-BASED
KEYWDS 2 CONSTRAINTS, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR I.BERTINI,A.DONAIRE,B.JIMENEZ,C.LUCHINAT,G.PARIGI,M.PICCIOLI,L.POGGI
REVDAT 3 27-OCT-21 1KQV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1KQV 1 VERSN
REVDAT 1 16-JAN-02 1KQV 0
JRNL AUTH I.BERTINI,A.DONAIRE,B.JIMENEZ,C.LUCHINAT,G.PARIGI,
JRNL AUTH 2 M.PICCIOLI,L.POGGI
JRNL TITL PARAMAGNETISM-BASED VERSUS CLASSICAL CONSTRAINTS: AN
JRNL TITL 2 ANALYSIS OF THE SOLUTION STRUCTURE OF CA LN CALBINDIN D9K.
JRNL REF J.BIOMOL.NMR V. 21 85 2001
JRNL REFN ISSN 0925-2738
JRNL PMID 11727989
JRNL DOI 10.1023/A:1012422402545
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PSEUDYANA 3.1, PSEUDYANA 3.1
REMARK 3 AUTHORS : BANCI, L., BERTINI, I., CREMONINI, M.A., GORI
REMARK 3 SAVELLINI, G., LUCHINAT, C., WUTHRICH, K. AND
REMARK 3 GUNTERT, P. (PSEUDYANA), BANCI, L., BERTINI, I.,
REMARK 3 CREMONINI, M.A., GORI SAVELLINI, G., LUCHINAT, C.,
REMARK 3 WUTHRICH, K. AND GUNTERT, P. (PSEUDYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KQV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015246.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 283
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : WATER SOLUTION; WATER SOLUTION
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 2.0 MM CA LN CB
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 HNCA; HNCO; HNHB; IR-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ; 700
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCURE WAS DETERMINED USING BOTH STANDARD AND
REMARK 210 TAILORED NMR EXPERIMENTS IN ORDER TO DETECT PARAMAGNETIC SIGNALS.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-30
REMARK 465 RES C SSSEQI
REMARK 465 MET A -3
REMARK 465 SER A -2
REMARK 465 ALA A -1
REMARK 465 LYS A 0
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 O LEU A 46 H PHE A 50 1.53
REMARK 500 O SER A 24 H LEU A 28 1.56
REMARK 500 O GLU A 48 H GLU A 52 1.59
REMARK 500 O LEU A 28 H LEU A 32 1.59
REMARK 500 OD2 ASP A 58 LA LA A 105 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 SER A 2 176.32 -59.96
REMARK 500 1 ASP A 58 -57.11 -134.46
REMARK 500 1 VAL A 61 52.46 -102.23
REMARK 500 1 SER A 62 165.55 -43.26
REMARK 500 2 PHE A 36 89.77 -151.46
REMARK 500 3 SER A 2 175.15 -59.92
REMARK 500 3 PHE A 36 88.75 -151.17
REMARK 500 4 PHE A 36 89.38 -151.55
REMARK 500 4 ASP A 58 -54.55 -131.35
REMARK 500 4 VAL A 61 51.12 -101.77
REMARK 500 4 SER A 62 164.41 -46.04
REMARK 500 5 SER A 2 174.77 -59.90
REMARK 500 5 ASP A 58 -68.82 -142.37
REMARK 500 5 SER A 62 172.06 -46.35
REMARK 500 6 PHE A 36 89.27 -151.57
REMARK 500 6 LYS A 55 -42.40 -168.46
REMARK 500 6 ASP A 58 -52.58 -137.40
REMARK 500 6 VAL A 61 52.40 -97.07
REMARK 500 6 SER A 62 165.88 -47.08
REMARK 500 7 SER A 2 173.97 -59.86
REMARK 500 7 PHE A 36 89.20 -151.80
REMARK 500 7 ASP A 58 -55.82 -131.56
REMARK 500 7 VAL A 61 58.79 -103.83
REMARK 500 8 ASP A 58 -58.63 -134.50
REMARK 500 8 VAL A 61 57.78 -97.38
REMARK 500 8 SER A 62 166.34 -48.79
REMARK 500 9 SER A 2 175.18 -59.98
REMARK 500 9 PHE A 36 88.98 -151.47
REMARK 500 9 ASP A 58 -56.42 -129.60
REMARK 500 9 VAL A 61 62.58 -102.98
REMARK 500 9 SER A 62 179.81 -49.25
REMARK 500 10 PHE A 36 88.78 -151.27
REMARK 500 10 ASP A 58 -48.53 -133.36
REMARK 500 10 VAL A 61 59.21 -100.47
REMARK 500 10 SER A 62 173.02 -48.77
REMARK 500 11 PHE A 36 89.02 -151.45
REMARK 500 11 THR A 45 170.08 -59.94
REMARK 500 11 ASP A 54 74.02 -68.17
REMARK 500 12 PHE A 36 89.09 -151.65
REMARK 500 12 ASP A 58 -51.73 -134.91
REMARK 500 13 LYS A 41 57.60 -94.56
REMARK 500 13 LYS A 55 -37.36 -178.36
REMARK 500 13 ASP A 58 -51.52 -135.68
REMARK 500 13 VAL A 61 53.32 -98.51
REMARK 500 13 SER A 62 164.86 -46.19
REMARK 500 14 PHE A 36 89.13 -151.55
REMARK 500 14 THR A 45 170.08 -59.90
REMARK 500 14 ASP A 54 68.83 -69.84
REMARK 500 14 ASP A 58 -52.62 -124.56
REMARK 500 14 VAL A 61 48.37 -100.86
REMARK 500
REMARK 500 THIS ENTRY HAS 117 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 LA A 105
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K31 RELATED DB: PDB
REMARK 900 1K31 IS THE AVERAGE NMR SOLUTION STRUCTURE OF CA LN CALBINDIN D9K
DBREF 1KQV A -3 75 UNP P02633 S100G_BOVIN 0 78
SEQADV 1KQV MET A 43 UNP P02633 PRO 46 ENGINEERED MUTATION
SEQRES 1 A 79 MET SER ALA LYS LYS SER PRO GLU GLU LEU LYS GLY ILE
SEQRES 2 A 79 PHE GLU LYS TYR ALA ALA LYS GLU GLY ASP PRO ASN GLN
SEQRES 3 A 79 LEU SER LYS GLU GLU LEU LYS LEU LEU LEU GLN THR GLU
SEQRES 4 A 79 PHE PRO SER LEU LEU LYS GLY MET SER THR LEU ASP GLU
SEQRES 5 A 79 LEU PHE GLU GLU LEU ASP LYS ASN GLY ASP GLY GLU VAL
SEQRES 6 A 79 SER PHE GLU GLU PHE GLN VAL LEU VAL LYS LYS ILE SER
SEQRES 7 A 79 GLN
HET LA A 105 1
HETNAM LA LANTHANUM (III) ION
FORMUL 2 LA LA 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 SER A 62 ILE A 73 1 12
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