Header list of 1lxf.pdb file
Complete list - b 23 2 Bytes
HEADER METAL BINDING PROTEIN, PROTEIN BINDING 05-JUN-02 1LXF
TITLE STRUCTURE OF THE REGULATORY N-DOMAIN OF HUMAN CARDIAC TROPONIN C IN
TITLE 2 COMPLEX WITH HUMAN CARDIAC TROPONIN-I(147-163) AND BEPRIDIL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C, SLOW SKELETAL AND CARDIAC MUSCLES;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: REGULATORY N DOMAIN (RESIDUES 1-89);
COMPND 5 SYNONYM: CARDIAC TROPONIN C, TN-C;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TROPONIN I, CARDIAC MUSCLE;
COMPND 9 CHAIN: I;
COMPND 10 FRAGMENT: SWITCH PEPTIDE (RESIDUES 147-163);
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TNNC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-(DE3PLYSS);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-3A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THE SEQUENCE OF THE PROTEIN IS NATURALLY FOUND IN
SOURCE 14 HOMO SAPIENS. THE PROTEIN WAS CHEMICALLY SYNTHESIZED.
KEYWDS MUSCLE, CARDIAC TROPONIN C-DRUG INTERACTION, BEPRIDIL, CARDIAC
KEYWDS 2 TROPONIN I-DRUG INTERACTION, METAL BINDING PROTEIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR X.WANG,M.X.LI,B.D.SYKES
REVDAT 3 23-FEB-22 1LXF 1 REMARK LINK
REVDAT 2 24-FEB-09 1LXF 1 VERSN
REVDAT 1 11-DEC-02 1LXF 0
JRNL AUTH X.WANG,M.X.LI,B.D.SYKES
JRNL TITL STRUCTURE OF THE REGULATORY N-DOMAIN OF HUMAN CARDIAC
JRNL TITL 2 TROPONIN C IN COMPLEX WITH HUMAN CARDIAC TROPONIN I147-163
JRNL TITL 3 AND BEPRIDIL.
JRNL REF J.BIOL.CHEM. V. 277 31124 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12060657
JRNL DOI 10.1074/JBC.M203896200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, X-PLOR 3.85
REMARK 3 AUTHORS : DELAGLIO, FRANK (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 1169 NOE RESTRAINTS, 88
REMARK 3 DIHEDRAL ANGLE RESTRAINTS USED FOR THE REFINEMENT OF CNTNC, 30
REMARK 3 NOE RESTRAINTS USED BETWEEN CNTNC AND CTNI147-163, 28 NOE
REMARK 3 RESTRAINTS USED BETWEEN CNTNC AND BEPRIDIL, 24 INTRAMOLECULAR
REMARK 3 NOE RESTRAINTS AND 12 DIHEDRAL ANGLE RESTRAINTS USED WITHIN
REMARK 3 CTNI147-163.
REMARK 4
REMARK 4 1LXF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016377.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM CNTNC, 3MM CTNI147-163,
REMARK 210 1.5MM BEPRIDIL, 5MM DTT, 100MM
REMARK 210 KCL, 10MM IMDZ, TRACE AMOUNT OF
REMARK 210 NAN3, 50UM DSS, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_DIPSI; HCCH-TOCSY; 3D_
REMARK 210 13C,15N-SEPARATED-NOESY;
REMARK 210 CBCACONNH; HNCACB; 2D_13C, 15N-
REMARK 210 FILTERED NOESY; 2D_13C, 15N-
REMARK 210 FILTERED DIPSI; 3D_13C, 15N-
REMARK 210 FILTERED, EDITED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY INOVA; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I
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 O LYS C 17 H LYS C 21 1.50
REMARK 500 O LEU C 57 H MET C 60 1.55
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 GLU C 15 -75.59 -70.18
REMARK 500 1 ASP C 33 -91.86 -110.76
REMARK 500 1 ASP C 73 -165.18 -61.22
REMARK 500 1 ASP C 75 -77.35 -87.38
REMARK 500 1 PHE C 77 -74.22 -54.72
REMARK 500 1 ASP C 87 65.59 164.48
REMARK 500 1 ALA I 150 -52.47 83.79
REMARK 500 2 ASP C 2 -44.22 173.89
REMARK 500 2 ASP C 33 -90.24 -118.88
REMARK 500 2 LYS C 43 -74.36 -41.11
REMARK 500 2 ASN C 51 79.97 -114.56
REMARK 500 2 ASP C 73 -172.11 -55.04
REMARK 500 2 ASP C 75 -77.51 -89.24
REMARK 500 3 ASP C 2 -35.58 167.16
REMARK 500 3 GLU C 15 -72.28 -80.21
REMARK 500 3 ALA C 22 -70.68 -40.79
REMARK 500 3 ASP C 33 -81.27 -168.59
REMARK 500 3 ASP C 65 63.46 -67.99
REMARK 500 3 ASP C 73 -170.65 -55.52
REMARK 500 3 ASP C 75 -74.76 -110.72
REMARK 500 3 PHE C 77 -71.48 -59.35
REMARK 500 3 MET C 80 -39.24 -37.50
REMARK 500 3 ASP C 88 130.82 -37.41
REMARK 500 3 ALA I 150 -35.14 164.73
REMARK 500 3 LEU I 157 64.94 -118.59
REMARK 500 3 LEU I 158 64.00 -105.70
REMARK 500 3 ARG I 161 38.20 -146.27
REMARK 500 4 LEU C 12 152.96 -42.98
REMARK 500 4 GLU C 15 -74.72 -58.44
REMARK 500 4 GLU C 19 -39.01 -37.72
REMARK 500 4 ASP C 33 -83.08 -120.18
REMARK 500 4 LEU C 48 43.26 -108.64
REMARK 500 4 ASP C 73 -177.66 -48.96
REMARK 500 4 PHE C 77 -77.37 -37.87
REMARK 500 4 LEU C 78 -72.21 -34.08
REMARK 500 4 ASP C 87 53.45 -157.61
REMARK 500 4 ASP C 88 99.16 -41.76
REMARK 500 4 SER I 149 -70.87 -69.11
REMARK 500 4 ALA I 150 -28.47 157.41
REMARK 500 4 ALA I 160 -50.65 84.22
REMARK 500 4 ARG I 161 -44.86 -162.00
REMARK 500 5 ILE C 4 -31.89 -39.96
REMARK 500 5 GLU C 14 -34.64 -38.69
REMARK 500 5 ASN C 18 -72.69 -62.23
REMARK 500 5 GLU C 19 -30.02 -38.82
REMARK 500 5 ILE C 26 -67.93 -108.48
REMARK 500 5 ASP C 33 -76.45 -129.87
REMARK 500 5 THR C 38 -31.05 -38.82
REMARK 500 5 LEU C 48 -85.27 -96.90
REMARK 500 5 ASP C 75 -82.02 -81.23
REMARK 500
REMARK 500 THIS ENTRY HAS 380 RAMACHANDRAN OUTLIERS.
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 CA C 93 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL C 64 O
REMARK 620 2 ASP C 65 OD1 90.2
REMARK 620 3 ASP C 67 OD1 106.9 108.6
REMARK 620 4 SER C 69 OG 164.1 78.7 66.7
REMARK 620 5 THR C 71 O 109.1 54.2 139.6 73.7
REMARK 620 6 GLU C 76 OE2 78.2 133.2 118.2 117.7 86.9
REMARK 620 7 GLU C 76 OE1 45.8 91.9 147.0 144.8 73.4 48.3
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 93
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEP C 92
DBREF 1LXF C 1 89 UNP P63316 TNNC1_HUMAN 1 89
DBREF 1LXF I 147 163 UNP P19429 TNNI3_HUMAN 148 164
SEQRES 1 C 89 MET ASP ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR
SEQRES 2 C 89 GLU GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE
SEQRES 3 C 89 PHE VAL LEU GLY ALA GLU ASP GLY CYS ILE SER THR LYS
SEQRES 4 C 89 GLU LEU GLY LYS VAL MET ARG MET LEU GLY GLN ASN PRO
SEQRES 5 C 89 THR PRO GLU GLU LEU GLN GLU MET ILE ASP GLU VAL ASP
SEQRES 6 C 89 GLU ASP GLY SER GLY THR VAL ASP PHE ASP GLU PHE LEU
SEQRES 7 C 89 VAL MET MET VAL ARG CYS MET LYS ASP ASP SER
SEQRES 1 I 17 ARG ILE SER ALA ASP ALA MET MET GLN ALA LEU LEU GLY
SEQRES 2 I 17 ALA ARG ALA LYS
HET CA C 93 1
HET BEP C 92 61
HETNAM CA CALCIUM ION
HETNAM BEP 1-ISOBUTOXY-2-PYRROLIDINO-3[N-BENZYLANILINO] PROPANE
HETSYN BEP BEPRIDIL
FORMUL 3 CA CA 2+
FORMUL 4 BEP C24 H34 N2 O
HELIX 1 1 ASP C 2 LEU C 12 1 11
HELIX 2 2 THR C 13 VAL C 28 1 16
HELIX 3 3 SER C 37 LEU C 48 1 12
HELIX 4 4 THR C 53 ASP C 65 1 13
HELIX 5 5 ASP C 73 LYS C 86 1 14
HELIX 6 6 ALA I 150 LEU I 157 1 8
LINK O VAL C 64 CA CA C 93 1555 1555 3.28
LINK OD1 ASP C 65 CA CA C 93 1555 1555 2.78
LINK OD1 ASP C 67 CA CA C 93 1555 1555 2.72
LINK OG SER C 69 CA CA C 93 1555 1555 2.21
LINK O THR C 71 CA CA C 93 1555 1555 2.79
LINK OE2 GLU C 76 CA CA C 93 1555 1555 2.45
LINK OE1 GLU C 76 CA CA C 93 1555 1555 2.77
SITE 1 AC1 6 VAL C 64 ASP C 65 ASP C 67 SER C 69
SITE 2 AC1 6 THR C 71 GLU C 76
SITE 1 AC2 13 PHE C 27 LEU C 41 MET C 45 LEU C 48
SITE 2 AC2 13 MET C 60 ILE C 61 VAL C 72 PHE C 77
SITE 3 AC2 13 MET C 80 MET C 81 CYS C 84 ILE I 148
SITE 4 AC2 13 MET I 153
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 23 2 Bytes